7QJ5 | pdb_00007qj5

Structure of recombinant human gamma-Tubulin Ring Complex (spokes 1-14)

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
L [auth I]	SCOP2B Superfamily	GCP component repeat-like	8090497	3002440	SCOP2B (2022-06-29)
L [auth I]	SCOP2B Superfamily	GCP component repeat-like	8090499	3002440	SCOP2B (2022-06-29)
N [auth K]	SCOP2B Superfamily	GCP component repeat-like	8090499	3002440	SCOP2B (2022-06-29)
N [auth K]	SCOP2B Superfamily	GCP component repeat-like	8090497	3002440	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth 1]	Tubulin_C	e7qj512	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
A [auth 1]	Tubulin	e7qj511	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
AA [auth X]	Tubulin_C	e7qj5X2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
AA [auth X]	Tubulin	e7qj5X1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
B [auth 2]	Tubulin_C	e7qj521	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
B [auth 2]	Tubulin	e7qj522	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
BA [auth Y]	Tubulin_C	e7qj5Y2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
BA [auth Y]	Tubulin	e7qj5Y1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
CA [auth Z]	Tubulin_C	e7qj5Z2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
CA [auth Z]	Tubulin	e7qj5Z1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
R [auth O]	Tubulin_C	e7qj5O2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
R [auth O]	Tubulin	e7qj5O1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
S [auth P]	Tubulin_C	e7qj5P2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
S [auth P]	Tubulin	e7qj5P1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
T [auth Q]	Tubulin_C	e7qj5Q1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
T [auth Q]	Tubulin	e7qj5Q2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
U [auth R]	Tubulin_C	e7qj5R1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
U [auth R]	Tubulin	e7qj5R2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
V [auth S]	Tubulin_C	e7qj5S1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
V [auth S]	Tubulin	e7qj5S2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
W [auth T]	Tubulin_C	e7qj5T1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
W [auth T]	Tubulin	e7qj5T2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
X [auth U]	Tubulin_C	e7qj5U1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
X [auth U]	Tubulin	e7qj5U2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
Y [auth V]	Tubulin_C	e7qj5V2	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
Y [auth V]	Tubulin	e7qj5V1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
Z [auth W]	Tubulin_C	e7qj5W1	A: a+b three layers	X: Bacillus chorismate mutase-like	H: Tubulin C-terminal domain-like (From Topology)	T: Tubulin C-terminal domain-like	F: Tubulin_C	ECOD (1.6)
Z [auth W]	Tubulin	e7qj5W2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Tubulin nucleotide-binding domain-like	F: Tubulin	ECOD (1.6)
C [auth e]	Actin_1st	e7qj5e1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Actin_1st	ECOD (1.6)
C [auth e]	Actin_2nd	e7qj5e2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: Actin_2nd	ECOD (1.6)
L [auth I]	Spc97_Spc98	e7qj5I1	A: alpha complex topology	X: gamma-tubulin complex protein 4 (GCP4) (From Topology)	H: gamma-tubulin complex protein 4 (GCP4) (From Topology)	T: gamma-tubulin complex protein 4 (GCP4)	F: Spc97_Spc98	ECOD (1.6)
N [auth K]	Spc97_Spc98	e7qj5K1	A: alpha complex topology	X: gamma-tubulin complex protein 4 (GCP4) (From Topology)	H: gamma-tubulin complex protein 4 (GCP4) (From Topology)	T: gamma-tubulin complex protein 4 (GCP4)	F: Spc97_Spc98	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	PF00091	Tubulin/FtsZ family, GTPase domain (Tubulin)	Tubulin/FtsZ family, GTPase domain	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ...	This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.	Domain
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	PF03953	Tubulin C-terminal domain (Tubulin_C)	Tubulin C-terminal domain	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tub ...	This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).	Domain
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	PF17681	Gamma tubulin complex component N-terminal (GCP_N_terminal)	Gamma tubulin complex component N-terminal	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 [2]. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC [3]. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2]. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1[3].	Domain
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	PF12554	Mitotic-spindle organizing gamma-tubulin ring associated (MOZART1)	Mitotic-spindle organizing gamma-tubulin ring associated	-	Family
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	PF04130	Gamma tubulin complex component C-terminal (GCP_C_terminal)	Gamma tubulin complex component C-terminal	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 . Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2].	Domain
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	PF00022	Actin (Actin)	Actin	-	Family
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	PF17681	Gamma tubulin complex component N-terminal (GCP_N_terminal)	Gamma tubulin complex component N-terminal	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 [2]. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC [3]. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2]. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1[3].	Domain
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	PF12554	Mitotic-spindle organizing gamma-tubulin ring associated (MOZART1)	Mitotic-spindle organizing gamma-tubulin ring associated	-	Family
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	PF04130	Gamma tubulin complex component C-terminal (GCP_C_terminal)	Gamma tubulin complex component C-terminal	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 . Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2].	Domain
L [auth I], N [auth K]	PF17681	Gamma tubulin complex component N-terminal (GCP_N_terminal)	Gamma tubulin complex component N-terminal	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 [2]. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC [3]. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2]. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1[3].	Domain
L [auth I], N [auth K]	PF12554	Mitotic-spindle organizing gamma-tubulin ring associated (MOZART1)	Mitotic-spindle organizing gamma-tubulin ring associated	-	Family
L [auth I], N [auth K]	PF04130	Gamma tubulin complex component C-terminal (GCP_C_terminal)	Gamma tubulin complex component C-terminal	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 . Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2].	Domain
GA [auth l], M [auth J]	PF17681	Gamma tubulin complex component N-terminal (GCP_N_terminal)	Gamma tubulin complex component N-terminal	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 [2]. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC [3]. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2]. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1[3].	Domain
GA [auth l], M [auth J]	PF04130	Gamma tubulin complex component C-terminal (GCP_C_terminal)	Gamma tubulin complex component C-terminal	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 . Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2].	Domain
KA [auth c], O [auth L]	PF17681	Gamma tubulin complex component N-terminal (GCP_N_terminal)	Gamma tubulin complex component N-terminal	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 [2]. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC [3]. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2]. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1[3].	Domain
KA [auth c], O [auth L]	PF04130	Gamma tubulin complex component C-terminal (GCP_C_terminal)	Gamma tubulin complex component C-terminal	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthe ...	This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast [1]. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated Swiss:Q9UGJ1 . Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	Tubulin gamma-1 chain	binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding structural constituent of cytoskeleton structural molecule activity identical protein binding protein binding	cellular process cell cycle mitotic cell cycle mitotic nuclear division organelle fission chromosome organization sister chromatid segregation cellular component organization organelle organization nuclear division mitotic cell cycle process mitotic sister chromatid segregation nuclear chromosome segregation cellular component organization or biogenesis cellular process cell cycle mitotic cell cycle mitotic nuclear division organelle fission chromosome organization sister chromatid segregation cellular component organization organelle organization nuclear division mitotic cell cycle process mitotic sister chromatid segregation nuclear chromosome segregation cellular component organization or biogenesis chromosome segregation cell cycle process microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization supramolecular fiber organization cytoskeleton organization sexual reproduction reproductive process meiotic cell cycle meiotic spindle organization meiotic cell cycle process spindle organization mitotic spindle organization microtubule cytoskeleton organization involved in mitosis protein polymerization protein-containing complex organization microtubule polymerization cellular component biogenesis microtubule polymerization or depolymerization cellular component assembly microtubule nucleation protein-containing complex assembly	cellular anatomical structure apical part of cell membrane-bounded organelle condensed nuclear chromosome intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle nuclear chromosome chromosome intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle organelle lumen cellular anatomical structure apical part of cell membrane-bounded organelle condensed nuclear chromosome intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle nuclear chromosome chromosome intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle organelle lumen organelle membraneless organelle condensed chromosome nuclear lumen centrosome microtubule organizing center cytoskeleton microtubule cytoskeleton polymeric cytoskeletal fiber spindle spindle microtubule polar microtubule spindle pole supramolecular fiber microtubule supramolecular polymer supramolecular complex centriole cytoplasm cytosol cell leading edge non-motile cilium cell projection cilium plasma membrane bounded cell projection protein-containing complex gamma-tubulin complex neuron projection endosome intracellular vesicle recycling endosome endomembrane system cytoplasmic vesicle vesicle pericentriolar material cytoplasmic microtubule ciliary basal body mitotic spindle mitotic spindle microtubule
C [auth e]	actin, cytoplasmic 1	-	-	intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton organelle membraneless organelle intracellular membraneless organelle
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	Gamma-tubulin complex component 2	cytoskeletal protein binding protein binding binding gamma-tubulin binding tubulin binding	cellular process cell cycle mitotic cell cycle developmental process multicellular organism development multicellular organismal process head development central nervous system development anatomical structure development animal organ development brain development nervous system development system development cellular component organization cellular process cell cycle mitotic cell cycle developmental process multicellular organism development multicellular organismal process head development central nervous system development anatomical structure development animal organ development brain development nervous system development system development cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly neuron migration cellular developmental process generation of neurons neurogenesis cell differentiation cell migration cell motility sexual reproduction reproductive process meiotic cell cycle organelle assembly membraneless organelle assembly spindle assembly chromosome segregation spindle organization cell cycle process protein polymerization microtubule polymerization microtubule polymerization or depolymerization microtubule nucleation	intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton membrane centrosome microtubule organizing center cytoplasm intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton membrane centrosome microtubule organizing center cytoplasm cytosol polymeric cytoskeletal fiber cytoplasmic microtubule supramolecular fiber microtubule supramolecular polymer supramolecular complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen protein-containing complex gamma-tubulin complex
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	Gamma-tubulin complex component 3	cytoskeletal protein binding protein binding binding gamma-tubulin binding tubulin binding structural constituent of cytoskeleton structural molecule activity	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization sexual reproduction reproductive process fertilization cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization sexual reproduction reproductive process fertilization single fertilization meiotic cell cycle organelle assembly membraneless organelle assembly spindle assembly cellular component biogenesis cellular component assembly chromosome segregation spindle organization cell cycle process protein polymerization protein-containing complex organization microtubule polymerization microtubule polymerization or depolymerization microtubule nucleation protein-containing complex assembly	cellular anatomical structure membrane intracellular organelle centrosome microtubule organizing center intracellular anatomical structure cytoskeleton organelle membraneless organelle intracellular membraneless organelle microtubule cytoskeleton polymeric cytoskeletal fiber spindle spindle microtubule cellular anatomical structure membrane intracellular organelle centrosome microtubule organizing center intracellular anatomical structure cytoskeleton organelle membraneless organelle intracellular membraneless organelle microtubule cytoskeleton polymeric cytoskeletal fiber spindle spindle microtubule polar microtubule spindle pole supramolecular fiber microtubule supramolecular polymer supramolecular complex centriole cytoplasm cytosol protein-containing complex gamma-tubulin complex
DA [auth g], EA [auth i], FA [auth m], H [auth b], HA [auth k], DA [auth g], EA [auth i], FA [auth m], H [auth b], HA [auth k], JA [auth d]	Mitotic-spindle organizing protein 1	-	microtubule cytoskeleton organization membraneless organelle assembly mitotic cell cycle cellular component organization cellular component biogenesis cellular component assembly mitotic sister chromatid segregation cell cycle cellular component organization or biogenesis chromosome segregation microtubule cytoskeleton organization involved in mitosis spindle organization cell cycle process mitotic nuclear division microtubule cytoskeleton organization membraneless organelle assembly mitotic cell cycle cellular component organization cellular component biogenesis cellular component assembly mitotic sister chromatid segregation cell cycle cellular component organization or biogenesis chromosome segregation microtubule cytoskeleton organization involved in mitosis spindle organization cell cycle process mitotic nuclear division organelle assembly organelle fission chromosome organization sister chromatid segregation spindle assembly mitotic spindle organization mitotic spindle assembly organelle organization nuclear division mitotic cell cycle process nuclear chromosome segregation cellular process microtubule-based process cytoskeleton organization protein polymerization protein-containing complex organization microtubule nucleation by microtubule organizing center microtubule polymerization microtubule polymerization or depolymerization microtubule nucleation microtubule nucleation by interphase microtubule organizing center protein-containing complex assembly supramolecular fiber organization gamma-tubulin complex localization localization protein-containing complex localization	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex gamma-tubulin ring complex intracellular membraneless organelle gamma-tubulin complex intracellular organelle microtubule organizing center cytoskeleton organelle membraneless organelle microtubule cytoskeleton cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex gamma-tubulin ring complex intracellular membraneless organelle gamma-tubulin complex intracellular organelle microtubule organizing center cytoskeleton organelle membraneless organelle microtubule cytoskeleton interphase microtubule organizing center spindle centrosome
L [auth I], N [auth K]	Gamma-tubulin complex component 4	cytoskeletal protein binding protein binding binding gamma-tubulin binding tubulin binding structural constituent of cytoskeleton structural molecule activity	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization cellular component biogenesis cellular component assembly protein-containing complex organization cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly sexual reproduction reproductive process meiotic cell cycle organelle assembly membraneless organelle assembly spindle assembly chromosome segregation spindle organization cell cycle process protein polymerization microtubule polymerization microtubule polymerization or depolymerization microtubule nucleation	intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton membrane membrane-bounded organelle endosome intracellular vesicle intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton membrane membrane-bounded organelle endosome intracellular vesicle intracellular membrane-bounded organelle recycling endosome endomembrane system cytoplasmic vesicle cytoplasm vesicle centrosome microtubule organizing center cytosol protein-containing complex gamma-tubulin ring complex gamma-tubulin complex polymeric cytoskeletal fiber supramolecular fiber microtubule supramolecular polymer supramolecular complex
GA [auth l], M [auth J]	Gamma-tubulin complex component 5	cytoskeletal protein binding protein binding binding gamma-tubulin binding tubulin binding microtubule binding	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization sexual reproduction reproductive process meiotic cell cycle cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization sexual reproduction reproductive process meiotic cell cycle organelle assembly membraneless organelle assembly spindle assembly cellular component biogenesis cellular component assembly chromosome segregation spindle organization cell cycle process protein polymerization protein-containing complex organization microtubule polymerization microtubule polymerization or depolymerization microtubule nucleation protein-containing complex assembly	intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton centrosome microtubule organizing center cytoplasm cytosol intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton centrosome microtubule organizing center cytoplasm cytosol protein-containing complex gamma-tubulin ring complex gamma-tubulin complex polymeric cytoskeletal fiber supramolecular fiber microtubule supramolecular polymer supramolecular complex
KA [auth c], O [auth L]	Gamma-tubulin complex component 6	cytoskeletal protein binding protein binding binding gamma-tubulin binding tubulin binding microtubule binding	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization sexual reproduction reproductive process meiotic cell cycle cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cytoplasmic microtubule organization cellular component organization or biogenesis supramolecular fiber organization cytoskeleton organization sexual reproduction reproductive process meiotic cell cycle organelle assembly membraneless organelle assembly spindle assembly cellular component biogenesis cellular component assembly chromosome segregation spindle organization cell cycle process protein polymerization protein-containing complex organization microtubule polymerization microtubule polymerization or depolymerization microtubule nucleation protein-containing complex assembly	intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton membrane centrosome microtubule organizing center cytoplasm intracellular organelle cellular anatomical structure intracellular anatomical structure cytoskeleton spindle organelle membraneless organelle intracellular membraneless organelle spindle pole microtubule cytoskeleton membrane centrosome microtubule organizing center cytoplasm cytosol protein-containing complex gamma-tubulin ring complex gamma-tubulin complex polymeric cytoskeletal fiber supramolecular fiber microtubule supramolecular polymer supramolecular complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR002454	Gamma tubulin	Family
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR017975	Tubulin, conserved site	Conserved Site
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR023123	Tubulin, C-terminal	Homologous Superfamily
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR000217	Tubulin	Family
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily
C [auth e]	IPR020902	Actin/actin-like conserved site	Conserved Site
C [auth e]	IPR004001	Actin, conserved site	Conserved Site
C [auth e]	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
C [auth e]	IPR004000	Actin family	Family
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	IPR040457	Gamma tubulin complex component, C-terminal	Domain
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	IPR042241	Gamma-tubulin complex component, C-terminal domain superfamily	Homologous Superfamily
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	IPR007259	Gamma-tubulin complex component protein	Family
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	IPR041470	Gamma tubulin complex component protein, N-terminal	Domain
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	IPR040457	Gamma tubulin complex component, C-terminal	Domain
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	IPR042241	Gamma-tubulin complex component, C-terminal domain superfamily	Homologous Superfamily
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	IPR007259	Gamma-tubulin complex component protein	Family
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	IPR041470	Gamma tubulin complex component protein, N-terminal	Domain
DA [auth g], EA [auth i], FA [auth m], H [auth b], HA [auth k], DA [auth g], EA [auth i], FA [auth m], H [auth b], HA [auth k], JA [auth d]	IPR022214	Mitotic-spindle organizing protein 1	Family
L [auth I], N [auth K]	IPR040457	Gamma tubulin complex component, C-terminal	Domain
L [auth I], N [auth K]	IPR042241	Gamma-tubulin complex component, C-terminal domain superfamily	Homologous Superfamily
L [auth I], N [auth K]	IPR007259	Gamma-tubulin complex component protein	Family
L [auth I], N [auth K]	IPR041470	Gamma tubulin complex component protein, N-terminal	Domain
GA [auth l], M [auth J]	IPR040457	Gamma tubulin complex component, C-terminal	Domain
GA [auth l], M [auth J]	IPR042241	Gamma-tubulin complex component, C-terminal domain superfamily	Homologous Superfamily
GA [auth l], M [auth J]	IPR007259	Gamma-tubulin complex component protein	Family
GA [auth l], M [auth J]	IPR041470	Gamma tubulin complex component protein, N-terminal	Domain
KA [auth c], O [auth L]	IPR040457	Gamma tubulin complex component, C-terminal	Domain
KA [auth c], O [auth L]	IPR045818	Gamma-tubulin complex component 6, N-terminal	Domain
KA [auth c], O [auth L]	IPR042241	Gamma-tubulin complex component, C-terminal domain superfamily	Homologous Superfamily
KA [auth c], O [auth L]	IPR007259	Gamma-tubulin complex component protein	Family
KA [auth c], O [auth L]	IPR041470	Gamma tubulin complex component protein, N-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], A [auth 1], AA [auth X], B [auth 2], BA [auth Y], CA [auth Z], R [auth O], S [auth P], T [auth Q], U [auth R], V [auth S], W [auth T], X [auth U], Y [auth V], Z [auth W]	Pharos: P23258	complex cortical dysplasia with other brain malformations 4 microcephaly breast cancer Epileptic encephalopathy microlissencephaly ovarian cancer cerebral cortical dysplasia lissencephaly spectrum disorders metabolic syndrome X non-small cell lung carcinoma psoriasis cerebrovascular disorder dermatomyositis lung adenocarcinoma osteosarcoma
D [auth A], F [auth C], J [auth G], MA [auth E], P [auth M]	Pharos: Q9BSJ2	epilepsy ovarian cancer Gaucher disease lissencephaly spectrum disorders
E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], E [auth B], G [auth D], I [auth F], IA [auth a], K [auth H], LA [auth j], NA [auth h], OA [auth f], Q [auth N]	Pharos: Q96CW5	adenoma large cell medulloblastoma oligodendroglioma Primary microcephaly amyotrophic lateral sclerosis malignant mesothelioma osteosarcoma psoriasis atypical teratoid rhabdoid tumor medulloblastoma ovarian cancer tuberculosis
DA [auth g], EA [auth i], FA [auth m], H [auth b], HA [auth k], DA [auth g], EA [auth i], FA [auth m], H [auth b], HA [auth k], JA [auth d]	Pharos: Q08AG7	astrocytic tumor malignant ependymoma pancreatic intraductal papillary-mucinous neoplasm atypical teratoid rhabdoid tumor malignant glioma pilocytic astrocytoma glioblastoma oligodendroglioma subependymal giant cell astrocytoma
L [auth I], N [auth K]	Pharos: Q9UGJ1	intellectual disability microcephaly and chorioretinopathy 3 microcephaly Microcephaly with Chorioretinopathy, Autosomal Recessive subependymal giant cell astrocytoma microcephaly and chorioretinopathy 1
GA [auth l], M [auth J]	Pharos: Q96RT8	malignant mesothelioma tuberculosis osteosarcoma psoriasis
KA [auth c], O [auth L]	Pharos: Q96RT7	microcephaly and chorioretinopathy 1 Microcephaly with Chorioretinopathy, Autosomal Recessive atopic eczema cutaneous melanoma hypertensive disorder microcephaly osteosarcoma progressive supranuclear palsy atypical teratoid rhabdoid tumor endogenous depression intellectual disability Pick disease bipolar disorder glioblastoma large cell medulloblastoma