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Protein

G-protein-signaling modulator 2

Gene

GPSM2

Organism
Homo sapiens (Human)
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:15632202, PubMed:21816348). 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).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei608 – 6081GDP; shared with dimeric partnerBy similarity
Binding sitei613 – 6131GDP; shared with dimeric partnerBy similarity
Binding sitei642 – 6421GDP; shared with dimeric partnerBy similarity
Binding sitei647 – 6471GDP; shared with dimeric partnerBy similarity

GO - Molecular functioni

  • GDP-dissociation inhibitor activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • establishment of mitotic spindle orientation Source: Ensembl
  • G-protein coupled receptor signaling pathway Source: ProtInc
  • lung epithelial cell differentiation Source: Ensembl
  • maintenance of centrosome location Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

SIGNORiP81274.

Names & Taxonomyi

Protein namesi
Recommended name:
G-protein-signaling modulator 2
Alternative name(s):
Mosaic protein LGN1 Publication
Gene namesi
Name:GPSM2
Synonyms:LGN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29501. GPSM2.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • cell cortex Source: UniProtKB
  • cytoplasm Source: HPA
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Chudley-McCullough syndrome (CMCS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:604213

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281R → A: Abolishes location at mitotic spindle poles; when associated with A-243. 1 Publication
Mutagenesisi228 – 2281R → E: Strongly reduces interaction with INSC. Abolishes interaction with INSC; when associated with R-290. 1 Publication
Mutagenesisi243 – 2431R → A: Abolishes location at mitotic spindle poles; when associated with A-228. 1 Publication
Mutagenesisi290 – 2901N → R: Abolishes interaction with INSC; when associated with E-228. 1 Publication

Keywords - Diseasei

Deafness

Organism-specific databases

MalaCardsiGPSM2.
MIMi604213. phenotype.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
314597. Chudley-McCullough syndrome.
PharmGKBiPA134993615.

Polymorphism and mutation databases

BioMutaiGPSM2.
DMDMi294862507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 684684G-protein-signaling modulator 2PRO_0000106358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321Phosphoserine; by PKGSequence analysis
Modified residuei352 – 3521Phosphoserine; by PKGSequence analysis
Modified residuei408 – 4081PhosphoserineCombined sources
Modified residuei483 – 4831PhosphoserineCombined sources
Modified residuei486 – 4861PhosphothreonineCombined sources
Modified residuei501 – 5011Phosphoserine; by PKCSequence analysis
Modified residuei541 – 5411PhosphoserineCombined sources
Modified residuei565 – 5651PhosphoserineCombined sources
Modified residuei607 – 6071Phosphoserine; by PKGSequence analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP81274.
MaxQBiP81274.
PaxDbiP81274.
PeptideAtlasiP81274.
PRIDEiP81274.

PTM databases

iPTMnetiP81274.
PhosphoSiteiP81274.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiP81274.
CleanExiHS_GPSM2.
ExpressionAtlasiP81274. baseline and differential.
GenevisibleiP81274. HS.

Organism-specific databases

HPAiCAB018962.
HPA007327.
HPA008408.

Interactioni

Subunit structurei

Interacts with LLGL2 (PubMed:15632202). Interacts (via TPR repeat region) with INSC/inscuteable (PubMed:16458856, PubMed:22074847). Interacts (via TPR repeat region) with NUMA1. 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).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-618655,EBI-618655
GNAI1P630963EBI-618655,EBI-618639
NUMA1Q149806EBI-618655,EBI-521611

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi118949. 13 interactions.
DIPiDIP-399N.
IntActiP81274. 12 interactions.
MINTiMINT-3023522.
STRINGi9606.ENSP00000264126.

Structurei

Secondary structure

1
684
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3613Combined sources
Helixi40 – 5314Combined sources
Helixi58 – 7417Combined sources
Helixi78 – 9417Combined sources
Helixi98 – 11518Combined sources
Helixi118 – 13417Combined sources
Helixi138 – 15821Combined sources
Helixi165 – 1684Combined sources
Helixi172 – 19423Combined sources
Helixi198 – 21518Combined sources
Helixi218 – 23417Combined sources
Helixi238 – 25417Combined sources
Helixi258 – 27215Combined sources
Helixi278 – 29417Combined sources
Helixi298 – 31417Combined sources
Helixi318 – 33417Combined sources
Helixi338 – 35417Combined sources
Helixi358 – 37619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SF4X-ray2.60A/B/C20-421[»]
4WNDX-ray1.50A20-421[»]
4WNEX-ray2.00A20-421[»]
4WNFX-ray2.90A20-421[»]
4WNGX-ray2.11A20-421[»]
5A6CX-ray2.90A/B22-357[»]
ProteinModelPortaliP81274.
SMRiP81274. Positions 20-381, 594-648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati24 – 5734TPR 1Add
BLAST
Repeati62 – 9534TPR 2Add
BLAST
Repeati102 – 13534TPR 3Add
BLAST
Repeati142 – 18443TPR 4Add
BLAST
Repeati202 – 23534TPR 5Add
BLAST
Repeati242 – 27534TPR 6Add
BLAST
Repeati282 – 31534TPR 7Add
BLAST
Repeati322 – 35534TPR 8Add
BLAST
Domaini489 – 51123GoLoco 1PROSITE-ProRule annotationAdd
BLAST
Domaini544 – 56623GoLoco 2PROSITE-ProRule annotationAdd
BLAST
Domaini594 – 61623GoLoco 3PROSITE-ProRule annotationAdd
BLAST
Domaini628 – 65023GoLoco 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 357336Important for interaction with NUMA1; INSC and FRMPD1By similarityAdd
BLAST

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.
InParanoidiP81274.
KOiK15837.
OMAiIMRSQAK.
OrthoDBiEOG7WHH8W.
PhylomeDBiP81274.
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.

P81274-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEENLISMRE 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 CPGPQDVGEF PEEVRDALQA AVDFYEENLS 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 IAQELNDRIG EGRACWSLGN AYTALGNHDQ AMHFAEKHLE
360 370 380 390 400
ISREVGDKSG ELTARLNLSD LQMVLGLSYS TNNSIMSENT EIDSSLNGVR
410 420 430 440 450
PKLGRRHSME NMELMKLTPE KVQNWNSEIL AKQKPLIAKP SAKLLFVNRL
460 470 480 490 500
KGKKYKTNSS TKVLQDASNS IDHRIPNSQR KISADTIGDE GFFDLLSRFQ
510 520 530 540 550
SNRMDDQRCC LQEKNCHTAS TTTSSTPPKM MLKTSSVPVV SPNTDEFLDL
560 570 580 590 600
LASSQSRRLD DQRASFSNLP GLRLTQNSQS VLSHLMTNDN KEADEDFFDI
610 620 630 640 650
LVKCQGSRLD DQRCAPPPAT TKGPTVPDED FFSLILRSQG KRMDEQRVLL
660 670 680
QRDQNRDTDF GLKDFLQNNA LLEFKNSGKK SADH
Length:684
Mass (Da):76,662
Last modified:April 20, 2010 - v3
Checksum:iD007A4765F57CB90
GO

Sequence cautioni

The sequence AAB40385.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH27732.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti400 – 4001R → L in AAB40385 (PubMed:8973305).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54999 mRNA. Translation: AAB40385.1. Different initiation.
AB445462 mRNA. Translation: BAH84760.1.
AL449266 Genomic DNA. Translation: CAI14361.1.
CH471122 Genomic DNA. Translation: EAW56340.1.
BC027732 mRNA. Translation: AAH27732.1. Different initiation.
AY136740 mRNA. Translation: AAN01266.1.
CR456786 mRNA. Translation: CAG33067.1.
CCDSiCCDS792.2.
PIRiJC5334. G02540.
RefSeqiNP_001307967.1. NM_001321038.1.
NP_001307968.1. NM_001321039.1.
NP_037428.3. NM_013296.4.
XP_011539603.1. XM_011541301.1.
XP_011539604.1. XM_011541302.1.
UniGeneiHs.584901.
Hs.658489.

Genome annotation databases

EnsembliENST00000264126; ENSP00000264126; ENSG00000121957.
ENST00000406462; ENSP00000385510; ENSG00000121957.
GeneIDi29899.
KEGGihsa:29899.
UCSCiuc010ovc.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54999 mRNA. Translation: AAB40385.1. Different initiation.
AB445462 mRNA. Translation: BAH84760.1.
AL449266 Genomic DNA. Translation: CAI14361.1.
CH471122 Genomic DNA. Translation: EAW56340.1.
BC027732 mRNA. Translation: AAH27732.1. Different initiation.
AY136740 mRNA. Translation: AAN01266.1.
CR456786 mRNA. Translation: CAG33067.1.
CCDSiCCDS792.2.
PIRiJC5334. G02540.
RefSeqiNP_001307967.1. NM_001321038.1.
NP_001307968.1. NM_001321039.1.
NP_037428.3. NM_013296.4.
XP_011539603.1. XM_011541301.1.
XP_011539604.1. XM_011541302.1.
UniGeneiHs.584901.
Hs.658489.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SF4X-ray2.60A/B/C20-421[»]
4WNDX-ray1.50A20-421[»]
4WNEX-ray2.00A20-421[»]
4WNFX-ray2.90A20-421[»]
4WNGX-ray2.11A20-421[»]
5A6CX-ray2.90A/B22-357[»]
ProteinModelPortaliP81274.
SMRiP81274. Positions 20-381, 594-648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118949. 13 interactions.
DIPiDIP-399N.
IntActiP81274. 12 interactions.
MINTiMINT-3023522.
STRINGi9606.ENSP00000264126.

PTM databases

iPTMnetiP81274.
PhosphoSiteiP81274.

Polymorphism and mutation databases

BioMutaiGPSM2.
DMDMi294862507.

Proteomic databases

EPDiP81274.
MaxQBiP81274.
PaxDbiP81274.
PeptideAtlasiP81274.
PRIDEiP81274.

Protocols and materials databases

DNASUi29899.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264126; ENSP00000264126; ENSG00000121957.
ENST00000406462; ENSP00000385510; ENSG00000121957.
GeneIDi29899.
KEGGihsa:29899.
UCSCiuc010ovc.3. human.

Organism-specific databases

CTDi29899.
GeneCardsiGPSM2.
HGNCiHGNC:29501. GPSM2.
HPAiCAB018962.
HPA007327.
HPA008408.
MalaCardsiGPSM2.
MIMi604213. phenotype.
609245. gene.
neXtProtiNX_P81274.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
314597. Chudley-McCullough syndrome.
PharmGKBiPA134993615.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1130. Eukaryota.
ENOG410XP6N. LUCA.
GeneTreeiENSGT00530000063126.
HOGENOMiHOG000231543.
HOVERGENiHBG051823.
InParanoidiP81274.
KOiK15837.
OMAiIMRSQAK.
OrthoDBiEOG7WHH8W.
PhylomeDBiP81274.
TreeFamiTF328344.

Enzyme and pathway databases

SIGNORiP81274.

Miscellaneous databases

GeneWikiiGPSM2.
GenomeRNAii29899.
PROiP81274.
SOURCEiSearch...

Gene expression databases

BgeeiP81274.
CleanExiHS_GPSM2.
ExpressionAtlasiP81274. baseline and differential.
GenevisibleiP81274. HS.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and cDNA cloning of a novel human mosaic protein, LGN, based on interaction with G alpha i2."
    Mochizuki N., Cho G., Wen B., Insel P.A.
    Gene 181:39-43(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GNAI2.
    Tissue: B-cell.
  2. "Involvement of C0671 overexpression in breast cancer cell growth."
    Katagiri T., Fukukawa C., Nakamura Y.
    Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  6. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-684.
    Tissue: Brain.
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-684.
  8. "Direct binding of Lgl2 to LGN during mitosis and its requirement for normal cell division."
    Yasumi M., Sakisaka T., Hoshino T., Kimura T., Sakamoto Y., Yamanaka T., Ohno S., Takai Y.
    J. Biol. Chem. 280:6761-6765(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LLGL2, SUBCELLULAR LOCATION.
    Tissue: Brain.
  9. "Two forms of human Inscuteable-related protein that links Par3 to the Pins homologues LGN and AGS3."
    Izaki T., Kamakura S., Kohjima M., Sumimoto H.
    Biochem. Biophys. Res. Commun. 341:1001-1006(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INSC, IDENTIFICATION IN A COMPLEX WITH INSC AND F2RL2.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; THR-486 AND SER-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Whole exome sequencing and homozygosity mapping identify mutation in the cell polarity protein GPSM2 as the cause of nonsyndromic hearing loss DFNB82."
    Walsh T., Shahin H., Elkan-Miller T., Lee M.K., Thornton A.M., Roeb W., Abu Rayyan A., Loulus S., Avraham K.B., King M.C., Kanaan M.
    Am. J. Hum. Genet. 87:90-94(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CMCS.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in asymmetric cell division for the Par3/mInsc/LGN and Galphai/LGN/NuMA pathways."
    Zhu J., Wen W., Zheng Z., Shang Y., Wei Z., Xiao Z., Pan Z., Du Q., Wang W., Zhang M.
    Mol. Cell 43:418-431(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-228 AND ARG-243.
  14. Cited for: INVOLVEMENT IN CMCS.
  15. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  16. "Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN)."
    Yuzawa S., Kamakura S., Iwakiri Y., Hayase J., Sumimoto H.
    Proc. Natl. Acad. Sci. U.S.A. 108:19210-19215(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-421 IN COMPLEX WITH INSC, INTERACTION WITH INSC; NUMA1; FRMPD1 AND FRMPD4, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-228 AND ASN-290.
  17. "Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN."
    Takayanagi H., Yuzawa S., Sumimoto H.
    Acta Crystallogr. F 71:175-183(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 20-421 IN COMPLEX WITH FRMPD4, INTERACTION WITH FRMPD4.

Entry informationi

Entry nameiGPSM2_HUMAN
AccessioniPrimary (citable) accession number: P81274
Secondary accession number(s): Q5T1N8, Q6IBL7, Q8N0Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.Curated

Caution

It is uncertain whether Met-1 or Met-8 is the initiator.Curated
Mutations in GPSM2 have been identified in people with profound congenital non-syndromic deafness designated as DFNB82 (PubMed:20602914). Subsequent brain imaging of these individuals has revealed frontal polymicrogyria, abnormal corpus callosum, and gray matter heterotopia, consistent with a diagnosis of Chudley-McCullough syndrome (PubMed:22578326).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.