P81274 · GPSM2_HUMAN
- ProteinG-protein-signaling modulator 2
- GeneGPSM2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids684 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in mitotic spindle pole organization via its interaction with NUMA1 (PubMed:11781568, PubMed:15632202, PubMed:21816348).
Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed:22327364).
Plays a role in metaphase spindle orientation (PubMed:22327364).
Also plays an important role in asymmetric cell divisions (PubMed:21816348).
Has guanine nucleotide dissociation inhibitor (GDI) activity towards G(i) alpha proteins, such as GNAI1 and GNAI3, and thereby regulates their activity (By similarity).
Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed:22327364).
Plays a role in metaphase spindle orientation (PubMed:22327364).
Also plays an important role in asymmetric cell divisions (PubMed:21816348).
Has guanine nucleotide dissociation inhibitor (GDI) activity towards G(i) alpha proteins, such as GNAI1 and GNAI3, and thereby regulates their activity (By similarity).
Miscellaneous
Dysfunction of LGN is associated with the phenotype of multiple micronuclei due to chromosomal mis-segregation and defect in cell division through mis-localization of mitotic spindle regulator protein NUMA1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 608 | GDP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 613 | GDP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 642 | GDP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 647 | GDP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R |
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameG-protein-signaling modulator 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP81274
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes in the cytoplasm during interphase and at cell cortex during metaphase (PubMed:11781568, PubMed:15632202, PubMed:22074847).
Colocalizes with NUMA1 to mitotic spindle poles (PubMed:11781568, PubMed:21816348).
Localized at the central and lateral cell cortex regions in a RanGTP-dependent manner (PubMed:22327364).
In horizontally retinal progenitor dividing cells, localized to the lateral cortical region. In vertically retinal progenitor dividing cells, localized at the polar cortical region (By similarity).
Colocalizes with NUMA1 to mitotic spindle poles (PubMed:11781568, PubMed:21816348).
Localized at the central and lateral cell cortex regions in a RanGTP-dependent manner (PubMed:22327364).
In horizontally retinal progenitor dividing cells, localized to the lateral cortical region. In vertically retinal progenitor dividing cells, localized at the polar cortical region (By similarity).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Chudley-McCullough syndrome (CMCS)
- Note
- DescriptionAn autosomal recessive neurologic disorder characterized by early-onset sensorineural deafness and specific brain anomalies on MRI, including hypoplasia of the corpus callosum, enlarged cysterna magna with mild focal cerebellar dysplasia, and nodular heterotopia. Some patients have hydrocephalus. Psychomotor development is normal.
- See alsoMIM:604213
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 228 | Abolishes location at mitotic spindle poles; when associated with A-243. | ||||
Sequence: R → A | ||||||
Mutagenesis | 228 | Strongly reduces interaction with INSC. Abolishes interaction with INSC; when associated with R-290. | ||||
Sequence: R → E | ||||||
Mutagenesis | 243 | Abolishes location at mitotic spindle poles; when associated with A-228. | ||||
Sequence: R → A | ||||||
Mutagenesis | 290 | Abolishes interaction with INSC; when associated with E-228. | ||||
Sequence: N → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 753 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000106358 | 1-684 | UniProt | G-protein-signaling modulator 2 | |||
Sequence: MEENLISMREDHSFHVRYRMEASCLELALEGERLCKSGDCRAGVSFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLHDYAKALEYHHHDLTLARTIGDQLGEAKASGNLGNTLKVLGNFDEAIVCCQRHLDISRELNDKVGEARALYNLGNVYHAKGKSFGCPGPQDVGEFPEEVRDALQAAVDFYEENLSLVTALGDRAAQGRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEFGDKAAERRAYSNLGNAYIFLGEFETASEYYKKTLLLARQLKDRAVEAQSCYSLGNTYTLLQDYEKAIDYHLKHLAIAQELNDRIGEGRACWSLGNAYTALGNHDQAMHFAEKHLEISREVGDKSGELTARLNLSDLQMVLGLSYSTNNSIMSENTEIDSSLNGVRPKLGRRHSMENMELMKLTPEKVQNWNSEILAKQKPLIAKPSAKLLFVNRLKGKKYKTNSSTKVLQDASNSIDHRIPNSQRKISADTIGDEGFFDLLSRFQSNRMDDQRCCLQEKNCHTASTTTSSTPPKMMLKTSSVPVVSPNTDEFLDLLASSQSRRLDDQRASFSNLPGLRLTQNSQSVLSHLMTNDNKEADEDFFDILVKCQGSRLDDQRCAPPPATTKGPTVPDEDFFSLILRSQGKRMDEQRVLLQRDQNRDTDFGLKDFLQNNALLEFKNSGKKSADH | |||||||
Modified residue | 132 | UniProt | Phosphoserine; by PKG | ||||
Sequence: S | |||||||
Modified residue | 352 | UniProt | Phosphoserine; by PKG | ||||
Sequence: S | |||||||
Modified residue | 408 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 483 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 483 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 486 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 501 | UniProt | Phosphoserine; by PKC | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 526 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 541 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 541 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 565 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 607 | UniProt | Phosphoserine; by PKG | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the dynein-dynactin complex; this interaction is inhibited in a PLK1-dependent manner (PubMed:22327364).
Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (PubMed:26766442).
Interacts with LLGL2 (PubMed:15632202).
Interacts (via TPR repeat region) with INSC/inscuteable (PubMed:16458856, PubMed:22074847).
Interacts (via TPR repeat region) with NUMA1 (via C-terminus); this interaction is direct, inhibited in a PLK1-dependent manner, prevents the binding of NUMA1 with SPAG5 and promotes spindle pole organization (PubMed:11781568, PubMed:22327364, PubMed:27462074).
INSC and NUMA1 compete for the same binding site, but INSC has higher affinity and can displace NUMA1 (in vitro) (PubMed:22074847).
Interacts with GNAI2 (PubMed:8973305).
Interacts (via GoLoco domains) with the GDP-bound form of GNAI1 and GNAI3; has much lower affinity for the GTP-bound form. Interaction with GDP-bound GNAI3 strongly enhances the affinity for NUMA1 (By similarity).
Interacts (via TPR repeat region) with FRMPD1 (PubMed:22074847).
INSC and FRMPD1 compete for the same binding site, but INSC has higher affinity and can displace FRMPD1 (in vitro) (By similarity).
Interacts (via TPR repeat region) with FRMPD4 (PubMed:22074847, PubMed:25664792).
Identified in a complex with INSC and F2RL2/Par3 (PubMed:16458856).
Interacts with TASOR (By similarity).
Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (PubMed:26766442).
Interacts with LLGL2 (PubMed:15632202).
Interacts (via TPR repeat region) with INSC/inscuteable (PubMed:16458856, PubMed:22074847).
Interacts (via TPR repeat region) with NUMA1 (via C-terminus); this interaction is direct, inhibited in a PLK1-dependent manner, prevents the binding of NUMA1 with SPAG5 and promotes spindle pole organization (PubMed:11781568, PubMed:22327364, PubMed:27462074).
INSC and NUMA1 compete for the same binding site, but INSC has higher affinity and can displace NUMA1 (in vitro) (PubMed:22074847).
Interacts with GNAI2 (PubMed:8973305).
Interacts (via GoLoco domains) with the GDP-bound form of GNAI1 and GNAI3; has much lower affinity for the GTP-bound form. Interaction with GDP-bound GNAI3 strongly enhances the affinity for NUMA1 (By similarity).
Interacts (via TPR repeat region) with FRMPD1 (PubMed:22074847).
INSC and FRMPD1 compete for the same binding site, but INSC has higher affinity and can displace FRMPD1 (in vitro) (By similarity).
Interacts (via TPR repeat region) with FRMPD4 (PubMed:22074847, PubMed:25664792).
Identified in a complex with INSC and F2RL2/Par3 (PubMed:16458856).
Interacts with TASOR (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P81274 | ARHGEF40 Q8TER5-2 | 3 | EBI-618655, EBI-10275150 | |
BINARY | P81274 | GAS2L1 Q99501 | 3 | EBI-618655, EBI-10981762 | |
BINARY | P81274 | GNAI1 P63096 | 3 | EBI-618655, EBI-618639 | |
BINARY | P81274 | GNAI3 P08754 | 3 | EBI-618655, EBI-357563 | |
BINARY | P81274 | GPSM2 P81274 | 7 | EBI-618655, EBI-618655 | |
BINARY | P81274 | INSC Q1MX18 | 4 | EBI-618655, EBI-12081118 | |
BINARY | P81274 | LRRC8E Q6NSJ5 | 3 | EBI-618655, EBI-8647013 | |
BINARY | P81274 | NUMA1 Q14980 | 6 | EBI-618655, EBI-521611 | |
BINARY | P81274 | WHRN Q9P202 | 3 | EBI-618655, EBI-310886 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 22-357 | Important for interaction with NUMA1; INSC and FRMPD1 | ||||
Sequence: ASCLELALEGERLCKSGDCRAGVSFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLHDYAKALEYHHHDLTLARTIGDQLGEAKASGNLGNTLKVLGNFDEAIVCCQRHLDISRELNDKVGEARALYNLGNVYHAKGKSFGCPGPQDVGEFPEEVRDALQAAVDFYEENLSLVTALGDRAAQGRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEFGDKAAERRAYSNLGNAYIFLGEFETASEYYKKTLLLARQLKDRAVEAQSCYSLGNTYTLLQDYEKAIDYHLKHLAIAQELNDRIGEGRACWSLGNAYTALGNHDQAMHFAEKHLEISREVGD | ||||||
Repeat | 24-57 | TPR 1 | ||||
Sequence: CLELALEGERLCKSGDCRAGVSFFEAAVQVGTED | ||||||
Repeat | 62-95 | TPR 2 | ||||
Sequence: SAIYSQLGNAYFYLHDYAKALEYHHHDLTLARTI | ||||||
Repeat | 102-135 | TPR 3 | ||||
Sequence: AKASGNLGNTLKVLGNFDEAIVCCQRHLDISREL | ||||||
Repeat | 142-184 | TPR 4 | ||||
Sequence: ARALYNLGNVYHAKGKSFGCPGPQDVGEFPEEVRDALQAAVDF | ||||||
Repeat | 202-235 | TPR 5 | ||||
Sequence: GRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEF | ||||||
Repeat | 242-275 | TPR 6 | ||||
Sequence: RRAYSNLGNAYIFLGEFETASEYYKKTLLLARQL | ||||||
Repeat | 282-315 | TPR 7 | ||||
Sequence: AQSCYSLGNTYTLLQDYEKAIDYHLKHLAIAQEL | ||||||
Repeat | 322-355 | TPR 8 | ||||
Sequence: GRACWSLGNAYTALGNHDQAMHFAEKHLEISREV | ||||||
Domain | 489-511 | GoLoco 1 | ||||
Sequence: DEGFFDLLSRFQSNRMDDQRCCL | ||||||
Domain | 544-566 | GoLoco 2 | ||||
Sequence: TDEFLDLLASSQSRRLDDQRASF | ||||||
Domain | 594-616 | GoLoco 3 | ||||
Sequence: DEDFFDILVKCQGSRLDDQRCAP | ||||||
Domain | 628-650 | GoLoco 4 | ||||
Sequence: DEDFFSLILRSQGKRMDEQRVLL |
Sequence similarities
Belongs to the GPSM family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length684
- Mass (Da)76,662
- Last updated2010-04-20 v3
- ChecksumD007A4765F57CB90
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B0QZC9 | B0QZC9_HUMAN | GPSM2 | 52 | ||
B0QZD0 | B0QZD0_HUMAN | GPSM2 | 75 | ||
A0A2R8Y896 | A0A2R8Y896_HUMAN | GPSM2 | 83 | ||
A0A2R8Y6E3 | A0A2R8Y6E3_HUMAN | GPSM2 | 311 | ||
A0A2R8Y673 | A0A2R8Y673_HUMAN | GPSM2 | 93 | ||
A0A6Q8PFD2 | A0A6Q8PFD2_HUMAN | GPSM2 | 519 | ||
A0A6Q8PGU2 | A0A6Q8PGU2_HUMAN | GPSM2 | 465 | ||
A0A6Q8PGW7 | A0A6Q8PGW7_HUMAN | GPSM2 | 625 | ||
A0A6Q8PGS6 | A0A6Q8PGS6_HUMAN | GPSM2 | 384 | ||
A0A6Q8PF02 | A0A6Q8PF02_HUMAN | GPSM2 | 701 | ||
A0A2R8YCX1 | A0A2R8YCX1_HUMAN | GPSM2 | 228 | ||
Q5T1N9 | Q5T1N9_HUMAN | GPSM2 | 213 | ||
H0Y4A4 | H0Y4A4_HUMAN | GPSM2 | 627 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 400 | in Ref. 1; AAB40385 | ||||
Sequence: R → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U54999 EMBL· GenBank· DDBJ | AAB40385.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB445462 EMBL· GenBank· DDBJ | BAH84760.1 EMBL· GenBank· DDBJ | mRNA | ||
AL449266 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471122 EMBL· GenBank· DDBJ | EAW56340.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC027732 EMBL· GenBank· DDBJ | AAH27732.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY136740 EMBL· GenBank· DDBJ | AAN01266.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456786 EMBL· GenBank· DDBJ | CAG33067.1 EMBL· GenBank· DDBJ | mRNA |