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Protein

G-protein-signaling modulator 2

Gene

Gpsm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in mitotic spindle pole organization via its interaction with NUMA1 (PubMed:21816348). Plays an important role in asymmetric cell divisions (PubMed:12571286, PubMed:21816348). Has guanine nucleotide dissociation inhibitor (GDI) activity towards G(i) alpha proteins, such as GNAI1 and GNAI3, and thereby regulates their activity (PubMed:22952234).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei608GDP; shared with dimeric partnerCombined sources1 Publication1
Binding sitei613GDP; shared with dimeric partnerCombined sources1 Publication1
Binding sitei642GDP; shared with dimeric partnerCombined sources1 Publication1
Binding sitei647GDP; shared with dimeric partnerCombined sources1 Publication1

GO - Molecular functioni

  • GDP-dissociation inhibitor activity Source: UniProtKB
  • G-protein alpha-subunit binding Source: UniProtKB
  • identical protein binding Source: MGI
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • establishment of mitotic spindle orientation Source: MGI
  • lung epithelial cell differentiation Source: MGI
  • maintenance of centrosome location Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
G-protein-signaling modulator 2
Alternative name(s):
Pins homolog1 Publication
Gene namesi
Name:Gpsm2
Synonyms:Lgn, Pins1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1923373. Gpsm2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcell cortex By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity

  • Note: Localizes in the cytoplasm during interphase and at cell cortex during metaphase. Colocalizes with NUMA1 to mitotic spindle poles.By similarity

GO - Cellular componenti

  • apical part of cell Source: MGI
  • cell cortex Source: UniProtKB
  • cytoplasm Source: MGI
  • mitotic spindle pole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi210N → F: Nearly abolishes interaction with NUMA1. 1 Publication1
Mutagenesisi228R → A: Abolishes interaction with NUMA1; when associated with A-243. Abolishes interaction with FRMPD1; when associated with A-243. 2 Publications1
Mutagenesisi243R → A: Abolishes interaction with NUMA1; when associated with A-228. Abolishes interaction with FRMPD1; when associated with A-228. 2 Publications1
Mutagenesisi254F → E: Abolishes interaction with INSC. 1 Publication1
Mutagenesisi290N → E: Abolishes interaction with INSC. 1 Publication1
Mutagenesisi601L → E: Disrupts one GNAI3 binding site. 1 Publication1
Mutagenesisi635I → E: Disrupts one GNAI3 binding site. 1 Publication1
Mutagenesisi642R → A or G: Reduces affinity for GDP-bound GNAI3 50-fold. Reduces affinity for GDP-bound GNAI3 500-fold; when associated with A-647. 1 Publication1
Mutagenesisi647R → A: Reduces affinity for GDP-bound GNAI3 500-fold; when associated with A-642. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001063591 – 679G-protein-signaling modulator 2Add BLAST679

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei408PhosphoserineCombined sources1
Modified residuei484PhosphoserineBy similarity1
Modified residuei487PhosphothreonineBy similarity1
Modified residuei540PhosphoserineBy similarity1
Modified residuei564PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VDU0.
PaxDbiQ8VDU0.
PRIDEiQ8VDU0.

PTM databases

iPTMnetiQ8VDU0.
PhosphoSitePlusiQ8VDU0.

Expressioni

Tissue specificityi

Detected in brain and liver (at protein level). Detected in brain, spleen, liver and testis, and at lower levels in heart, lung and kidney. Enriched in the ventricular zone of the developing central nervous systems.1 Publication

Gene expression databases

BgeeiENSMUSG00000027883.
ExpressionAtlasiQ8VDU0. baseline and differential.
GenevisibleiQ8VDU0. MM.

Interactioni

Subunit structurei

Interacts with LLGL2 (By similarity). Interacts (via TPR repeat region) with INSC/inscuteable (PubMed:16094321, PubMed:21816348). Interacts (via TPR repeat region) with NUMA1 (PubMed:21816348, PubMed:23318951, PubMed:23665171). INSC and NUMA1 compete for the same binding site, but INSC has higher affinity and can displace NUMA1 (in vitro) (PubMed:21816348). Interacts with GNAI2 (By similarity). Interacts (via GoLoco domains) with the GDP-bound form of GNAI1 and GNAI3; has much lower affinity for the GTP-bound form (PubMed:22952234, PubMed:23665171). Interaction with GDP-bound GNAI3 strongly enhances the affinity for NUMA1 (PubMed:23665171). Interacts (via TPR repeat region) with FRMPD1 (PubMed:23318951). INSC and FRMPD1 compete for the same binding site, but INSC has higher affinity and can displace FRMPD1 (in vitro) (PubMed:23318951). Interacts (via TPR repeat region) with FRMPD4. Identified in a complex with INSC and F2RL2/Par3 (By similarity).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg1Q626967EBI-7575403,EBI-389325From a different organism.
DLG4P783527EBI-7575403,EBI-80389From a different organism.

GO - Molecular functioni

  • G-protein alpha-subunit binding Source: UniProtKB
  • identical protein binding Source: MGI

Protein-protein interaction databases

BioGridi217976. 1 interactor.
DIPiDIP-60164N.
IntActiQ8VDU0. 4 interactors.
MINTiMINT-4096561.
STRINGi10090.ENSMUSP00000029482.

Structurei

Secondary structure

1679
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 36Combined sources15
Helixi40 – 53Combined sources14
Helixi58 – 74Combined sources17
Helixi78 – 95Combined sources18
Helixi98 – 114Combined sources17
Helixi118 – 134Combined sources17
Helixi138 – 157Combined sources20
Beta strandi159 – 163Combined sources5
Helixi172 – 195Combined sources24
Helixi198 – 214Combined sources17
Helixi218 – 235Combined sources18
Helixi238 – 254Combined sources17
Helixi258 – 274Combined sources17
Helixi278 – 294Combined sources17
Helixi298 – 314Combined sources17
Helixi318 – 335Combined sources18
Helixi338 – 352Combined sources15
Helixi598 – 601Combined sources4
Turni617 – 619Combined sources3
Helixi632 – 646Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RO2X-ray2.30A22-357[»]
3RO3X-ray1.10A198-357[»]
4G2VX-ray2.40A22-357[»]
4G5OX-ray2.90E/F/G/H628-653[»]
4G5QX-ray2.90E/F/G/H628-652[»]
4G5RX-ray3.48E/F/G/Z628-652[»]
4G5SX-ray3.62E/F/G/Z594-618[»]
4JHRX-ray2.80A/B96-357[»]
A/B593-651[»]
ProteinModelPortaliQ8VDU0.
SMRiQ8VDU0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati24 – 57TPR 1Add BLAST34
Repeati62 – 95TPR 2Add BLAST34
Repeati102 – 135TPR 3Add BLAST34
Repeati142 – 184TPR 4Add BLAST43
Repeati202 – 235TPR 5Add BLAST34
Repeati242 – 275TPR 6Add BLAST34
Repeati282 – 315TPR 7Add BLAST34
Repeati322 – 355TPR 8Add BLAST34
Domaini490 – 512GoLoco 1PROSITE-ProRule annotationAdd BLAST23
Domaini543 – 565GoLoco 2PROSITE-ProRule annotationAdd BLAST23
Domaini594 – 616GoLoco 3PROSITE-ProRule annotationAdd BLAST23
Domaini628 – 650GoLoco 4PROSITE-ProRule annotationAdd BLAST23

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 357Important for interaction with NUMA1; INSC and FRMPD12 PublicationsAdd BLAST336

Domaini

Each GoLoco domain can bind one GNAI3 (PubMed:22952234). In the auto-inhibited conformation, the GoLoco domains interact with the TPR repeat region (PubMed:23665171).2 Publications

Sequence similaritiesi

Belongs to the GPSM family.Curated
Contains 4 GoLoco domains.PROSITE-ProRule annotation
Contains 8 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1130. Eukaryota.
ENOG410XP6N. LUCA.
GeneTreeiENSGT00530000063126.
HOGENOMiHOG000231543.
HOVERGENiHBG051823.
InParanoidiQ8VDU0.
KOiK15837.
OMAiIMRSQAK.
OrthoDBiEOG091G04C9.
PhylomeDBiQ8VDU0.
TreeFamiTF328344.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR003109. GoLoco_motif.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF02188. GoLoco. 4 hits.
PF13176. TPR_7. 2 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00390. GoLoco. 4 hits.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50877. GOLOCO. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VDU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGNLISMRE DHSFHVRYRM EASCLELALE GERLCKSGDC RAGVSFFEAA
60 70 80 90 100
VQVGTEDLKT LSAIYSQLGN AYFYLHDYAK ALEYHHHDLT LARTIGDQLG
110 120 130 140 150
EAKASGNLGN TLKVLGNFDE AIVCCQRHLD ISRELNDKVG EARALYNLGN
160 170 180 190 200
VYHAKGKSFG CPGPQDTGEF PEDVRNALQA AVDLYEENLS LVTALGDRAA
210 220 230 240 250
QGRAFGNLGN THYLLGNFRD AVIAHEQRLL IAKEFGDKAA ERRAYSNLGN
260 270 280 290 300
AYIFLGEFET ASEYYKKTLL LARQLKDRAV EAQSCYSLGN TYTLLQDYEK
310 320 330 340 350
AIDYHLKHLA IAQELKDRIG EGRACWSLGN AYTALGNHDQ AMHFAEKHLE
360 370 380 390 400
ISREVGDKSG ELTARLNLSD LQMVLGLSYS TNNSMMSENI EIDGSLHGAG
410 420 430 440 450
AKLGRRHSME NLELMKLTPE KVPNWNSEIL AKQKPLIAKP SAKLLFVNRL
460 470 480 490 500
KGKKYKSGSA CTKVLQDASN SVDHRAPRSQ KKISSDTIGD EGFFDLLRRF
510 520 530 540 550
QSNRMDDQRC HLQGNCRTTS TAAASATPKL MKAPSVSVVS PNTDEFLDLL
560 570 580 590 600
ASSQSRRLDD QRASFSNLPG LRLTKGNSPS VLERLMTNDK KEPDEDFFDI
610 620 630 640 650
LVKCQGSRLD DQRCAPPSAA TKGPTVPDED FFSLILRSQA KRMDEQRVLL
660 670
QRDPNRDSEF GLKELLQNNA LLEFKHSGK
Length:679
Mass (Da):75,591
Last modified:April 20, 2010 - v2
Checksum:i8005F2A52FE66D77
GO

Sequence cautioni

The sequence AAH21308 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL87447 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY081187 mRNA. Translation: AAL87447.1. Different initiation.
BC021308 mRNA. Translation: AAH21308.1. Different initiation.
AK040996 mRNA. Translation: BAC30775.1.
CCDSiCCDS51048.1.
RefSeqiNP_083798.2. NM_029522.2.
UniGeneiMm.226941.

Genome annotation databases

EnsembliENSMUST00000029482; ENSMUSP00000029482; ENSMUSG00000027883.
GeneIDi76123.
KEGGimmu:76123.
UCSCiuc008qzo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY081187 mRNA. Translation: AAL87447.1. Different initiation.
BC021308 mRNA. Translation: AAH21308.1. Different initiation.
AK040996 mRNA. Translation: BAC30775.1.
CCDSiCCDS51048.1.
RefSeqiNP_083798.2. NM_029522.2.
UniGeneiMm.226941.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RO2X-ray2.30A22-357[»]
3RO3X-ray1.10A198-357[»]
4G2VX-ray2.40A22-357[»]
4G5OX-ray2.90E/F/G/H628-653[»]
4G5QX-ray2.90E/F/G/H628-652[»]
4G5RX-ray3.48E/F/G/Z628-652[»]
4G5SX-ray3.62E/F/G/Z594-618[»]
4JHRX-ray2.80A/B96-357[»]
A/B593-651[»]
ProteinModelPortaliQ8VDU0.
SMRiQ8VDU0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217976. 1 interactor.
DIPiDIP-60164N.
IntActiQ8VDU0. 4 interactors.
MINTiMINT-4096561.
STRINGi10090.ENSMUSP00000029482.

PTM databases

iPTMnetiQ8VDU0.
PhosphoSitePlusiQ8VDU0.

Proteomic databases

MaxQBiQ8VDU0.
PaxDbiQ8VDU0.
PRIDEiQ8VDU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029482; ENSMUSP00000029482; ENSMUSG00000027883.
GeneIDi76123.
KEGGimmu:76123.
UCSCiuc008qzo.2. mouse.

Organism-specific databases

CTDi29899.
MGIiMGI:1923373. Gpsm2.

Phylogenomic databases

eggNOGiKOG1130. Eukaryota.
ENOG410XP6N. LUCA.
GeneTreeiENSGT00530000063126.
HOGENOMiHOG000231543.
HOVERGENiHBG051823.
InParanoidiQ8VDU0.
KOiK15837.
OMAiIMRSQAK.
OrthoDBiEOG091G04C9.
PhylomeDBiQ8VDU0.
TreeFamiTF328344.

Miscellaneous databases

PROiQ8VDU0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027883.
ExpressionAtlasiQ8VDU0. baseline and differential.
GenevisibleiQ8VDU0. MM.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR003109. GoLoco_motif.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF02188. GoLoco. 4 hits.
PF13176. TPR_7. 2 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00390. GoLoco. 4 hits.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50877. GOLOCO. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGPSM2_MOUSE
AccessioniPrimary (citable) accession number: Q8VDU0
Secondary accession number(s): Q8BLX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: April 20, 2010
Last modified: November 2, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-8 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.