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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei608 – 6081GDP; shared with dimeric partnerCombined sources1 Publication
Binding sitei613 – 6131GDP; shared with dimeric partnerCombined sources1 Publication
Binding sitei642 – 6421GDP; shared with dimeric partnerCombined sources1 Publication
Binding sitei647 – 6471GDP; shared with dimeric partnerCombined sources1 Publication

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
  • regulation of catalytic activity Source: GOC
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
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi210 – 2101N → F: Nearly abolishes interaction with NUMA1. 1 Publication
Mutagenesisi228 – 2281R → A: Abolishes interaction with NUMA1; when associated with A-243. Abolishes interaction with FRMPD1; when associated with A-243. 2 Publications
Mutagenesisi243 – 2431R → A: Abolishes interaction with NUMA1; when associated with A-228. Abolishes interaction with FRMPD1; when associated with A-228. 2 Publications
Mutagenesisi254 – 2541F → E: Abolishes interaction with INSC. 1 Publication
Mutagenesisi290 – 2901N → E: Abolishes interaction with INSC. 1 Publication
Mutagenesisi601 – 6011L → E: Disrupts one GNAI3 binding site. 1 Publication
Mutagenesisi635 – 6351I → E: Disrupts one GNAI3 binding site. 1 Publication
Mutagenesisi642 – 6421R → 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 Publication
Mutagenesisi647 – 6471R → A: Reduces affinity for GDP-bound GNAI3 500-fold; when associated with A-642. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 679679G-protein-signaling modulator 2PRO_0000106359Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei408 – 4081PhosphoserineCombined sources
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei487 – 4871PhosphothreonineBy similarity
Modified residuei540 – 5401PhosphoserineBy similarity
Modified residuei564 – 5641PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VDU0.
PaxDbiQ8VDU0.
PRIDEiQ8VDU0.

PTM databases

iPTMnetiQ8VDU0.
PhosphoSiteiQ8VDU0.

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

BgeeiQ8VDU0.
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 interaction.
DIPiDIP-60164N.
IntActiQ8VDU0. 4 interactions.
MINTiMINT-4096561.
STRINGi10090.ENSMUSP00000029482.

Structurei

Secondary structure

1
679
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3615Combined sources
Helixi40 – 5314Combined sources
Helixi58 – 7417Combined sources
Helixi78 – 9518Combined sources
Helixi98 – 11417Combined sources
Helixi118 – 13417Combined sources
Helixi138 – 15720Combined sources
Beta strandi159 – 1635Combined sources
Helixi172 – 19524Combined sources
Helixi198 – 21417Combined sources
Helixi218 – 23518Combined sources
Helixi238 – 25417Combined sources
Helixi258 – 27417Combined sources
Helixi278 – 29417Combined sources
Helixi298 – 31417Combined sources
Helixi318 – 33518Combined sources
Helixi338 – 35215Combined sources
Helixi598 – 6014Combined sources
Turni617 – 6193Combined sources
Helixi632 – 64615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 22-648.
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
Domaini490 – 51223GoLoco 1PROSITE-ProRule annotationAdd
BLAST
Domaini543 – 56523GoLoco 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 FRMPD12 PublicationsAdd
BLAST

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.
OrthoDBiEOG7WHH8W.
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.
[Graphical view]
SMARTiSM00390. GoLoco. 4 hits.
SM00028. TPR. 6 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 AAH21308.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL87447.1 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
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. Positions 22-648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217976. 1 interaction.
DIPiDIP-60164N.
IntActiQ8VDU0. 4 interactions.
MINTiMINT-4096561.
STRINGi10090.ENSMUSP00000029482.

PTM databases

iPTMnetiQ8VDU0.
PhosphoSiteiQ8VDU0.

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.
OrthoDBiEOG7WHH8W.
PhylomeDBiQ8VDU0.
TreeFamiTF328344.

Miscellaneous databases

NextBioi344635.
PROiQ8VDU0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDU0.
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.
[Graphical view]
SMARTiSM00390. GoLoco. 4 hits.
SM00028. TPR. 6 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. "A mouse homologue of Drosophila pins can asymmetrically localize and substitute for pins function in Drosophila neuroblasts."
    Yu F., Morin X., Kaushik R., Bahri S., Yang X., Chia W.
    J. Cell Sci. 116:887-896(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  2. "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].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-640.
    Strain: C57BL/6J.
    Tissue: Aorta and Vein.
  4. "Asymmetric cell divisions promote stratification and differentiation of mammalian skin."
    Lechler T., Fuchs E.
    Nature 437:275-280(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INSC AND F2RL2.
    Strain: CD-1.
    Tissue: Epidermis.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung and Spleen.
  7. "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: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 198-357 IN COMPLEXES WITH NUMA1 AND INSC, INTERACTION WITH NUMA1 AND INSC, MUTAGENESIS OF ASN-210; ARG-228; ARG-243; PHE-254 AND ASN-290.
  8. "Crystal structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from Galphai."
    Jia M., Li J., Zhu J., Wen W., Zhang M., Wang W.
    J. Biol. Chem. 287:36766-36776(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 594-618 AND 628-652 IN COMPLEXES WITH GNAI1; GNAI3 AND GDP, INTERACTION WITH GNAI1 AND GNAI3, DOMAIN, MUTAGENESIS OF LEU-601; ILE-635; ARG-642 AND ARG-647.
  9. "Structural and biochemical characterization of the interaction between LGN and Frmpd1."
    Pan Z., Shang Y., Jia M., Zhang L., Xia C., Zhang M., Wang W., Wen W.
    J. Mol. Biol. 425:1039-1049(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 22-357 IN COMPLEX WITH FRMPD1, INTERACTION WITH FRMPD1 AND NUMA1, MUTAGENESIS OF ARG-228 AND ARG-243.
  10. "An autoinhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs."
    Pan Z., Zhu J., Shang Y., Wei Z., Jia M., Xia C., Wen W., Wang W., Zhang M.
    Structure 21:1007-1017(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 96-357 AND 593-651 IN COMPLEXES WITH GNAI1 AND GNAI3, INTERACTION WITH NUMA1; GNAI1 AND GNAI3, DOMAIN.

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: April 13, 2016
This is version 121 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.