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Q8VDU0

- GPSM2_MOUSE

UniProt

Q8VDU0 - GPSM2_MOUSE

Protein

G-protein-signaling modulator 2

Gene

Gpsm2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    Plays an important role in spindle pole orientation By similarity. Interacts and contributes to the functional activity of G(i) alpha proteins. Acts to stabilize the apical complex during neuroblast divisions.By similarity

    GO - Molecular functioni

    1. GTPase regulator activity Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. establishment of mitotic spindle orientation Source: MGI
    2. lung epithelial cell differentiation Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G-protein-signaling modulator 2
    Alternative name(s):
    Pins homolog
    Gene namesi
    Name:Gpsm2
    Synonyms:Lgn, Pins
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1923373. Gpsm2.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcell cortex By similarity
    Note: Localizes in the cytoplasm in the interphase and at cell periphery in the metaphase.By similarity

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. cell cortex Source: UniProtKB-SubCell
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    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 – 4081Phosphoserine1 Publication
    Modified residuei484 – 4841PhosphoserineBy similarity
    Modified residuei487 – 4871PhosphothreonineBy similarity
    Modified residuei540 – 5401PhosphoserineBy similarity
    Modified residuei564 – 5641Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8VDU0.
    PRIDEiQ8VDU0.

    PTM databases

    PhosphoSiteiQ8VDU0.

    Expressioni

    Tissue specificityi

    Expressed in many tissues, but its expression is enriched in the ventricular zone of the developing central nervous systems.

    Gene expression databases

    ArrayExpressiQ8VDU0.
    BgeeiQ8VDU0.
    GenevestigatoriQ8VDU0.

    Interactioni

    Subunit structurei

    Interacts with LLGL2 By similarity. Interacts with INSC/inscuteable and F2RL2.By similarity1 Publication

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi217976. 1 interaction.
    DIPiDIP-60164N.
    IntActiQ8VDU0. 3 interactions.
    MINTiMINT-4096561.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 20-648.
    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

    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

    eggNOGiCOG0457.
    GeneTreeiENSGT00530000063126.
    HOGENOMiHOG000231543.
    HOVERGENiHBG051823.
    InParanoidiQ8VDU0.
    KOiK15837.
    OMAiEYYEANL.
    OrthoDBiEOG7WHH8W.
    PhylomeDBiQ8VDU0.
    TreeFamiTF328344.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR003109. GoLoco_motif.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF02188. GoLoco. 4 hits.
    PF00515. TPR_1. 2 hits.
    PF13176. TPR_7. 1 hit.
    [Graphical view]
    SMARTiSM00390. GoLoco. 4 hits.
    SM00028. TPR. 6 hits.
    [Graphical view]
    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

    MEGNLISMRE DHSFHVRYRM EASCLELALE GERLCKSGDC RAGVSFFEAA    50
    VQVGTEDLKT LSAIYSQLGN AYFYLHDYAK ALEYHHHDLT LARTIGDQLG 100
    EAKASGNLGN TLKVLGNFDE AIVCCQRHLD ISRELNDKVG EARALYNLGN 150
    VYHAKGKSFG CPGPQDTGEF PEDVRNALQA AVDLYEENLS LVTALGDRAA 200
    QGRAFGNLGN THYLLGNFRD AVIAHEQRLL IAKEFGDKAA ERRAYSNLGN 250
    AYIFLGEFET ASEYYKKTLL LARQLKDRAV EAQSCYSLGN TYTLLQDYEK 300
    AIDYHLKHLA IAQELKDRIG EGRACWSLGN AYTALGNHDQ AMHFAEKHLE 350
    ISREVGDKSG ELTARLNLSD LQMVLGLSYS TNNSMMSENI EIDGSLHGAG 400
    AKLGRRHSME NLELMKLTPE KVPNWNSEIL AKQKPLIAKP SAKLLFVNRL 450
    KGKKYKSGSA CTKVLQDASN SVDHRAPRSQ KKISSDTIGD EGFFDLLRRF 500
    QSNRMDDQRC HLQGNCRTTS TAAASATPKL MKAPSVSVVS PNTDEFLDLL 550
    ASSQSRRLDD QRASFSNLPG LRLTKGNSPS VLERLMTNDK KEPDEDFFDI 600
    LVKCQGSRLD DQRCAPPSAA TKGPTVPDED FFSLILRSQA KRMDEQRVLL 650
    QRDPNRDSEF GLKELLQNNA LLEFKHSGK 679
    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.
    The sequence AAL87447.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY081187 mRNA. Translation: AAL87447.1 . Different initiation.
    BC021308 mRNA. Translation: AAH21308.1 . Different initiation.
    AK040996 mRNA. Translation: BAC30775.1 .
    CCDSi CCDS51048.1.
    RefSeqi NP_083798.2. NM_029522.2.
    UniGenei Mm.226941.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RO2 X-ray 2.30 A 22-357 [» ]
    3RO3 X-ray 1.10 A 198-357 [» ]
    4G2V X-ray 2.40 A 22-357 [» ]
    4G5O X-ray 2.90 E/F/G/H 628-653 [» ]
    4G5Q X-ray 2.90 E/F/G/H 628-652 [» ]
    4G5R X-ray 3.48 E/F/G/Z 628-652 [» ]
    4G5S X-ray 3.62 E/F/G/Z 594-618 [» ]
    4JHR X-ray 2.80 A/B 96-357 [» ]
    A/B 593-651 [» ]
    ProteinModelPortali Q8VDU0.
    SMRi Q8VDU0. Positions 20-648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 217976. 1 interaction.
    DIPi DIP-60164N.
    IntActi Q8VDU0. 3 interactions.
    MINTi MINT-4096561.

    PTM databases

    PhosphoSitei Q8VDU0.

    Proteomic databases

    PaxDbi Q8VDU0.
    PRIDEi Q8VDU0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029482 ; ENSMUSP00000029482 ; ENSMUSG00000027883 .
    GeneIDi 76123.
    KEGGi mmu:76123.
    UCSCi uc008qzo.2. mouse.

    Organism-specific databases

    CTDi 29899.
    MGIi MGI:1923373. Gpsm2.

    Phylogenomic databases

    eggNOGi COG0457.
    GeneTreei ENSGT00530000063126.
    HOGENOMi HOG000231543.
    HOVERGENi HBG051823.
    InParanoidi Q8VDU0.
    KOi K15837.
    OMAi EYYEANL.
    OrthoDBi EOG7WHH8W.
    PhylomeDBi Q8VDU0.
    TreeFami TF328344.

    Miscellaneous databases

    NextBioi 344635.
    PROi Q8VDU0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VDU0.
    Bgeei Q8VDU0.
    Genevestigatori Q8VDU0.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR003109. GoLoco_motif.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF02188. GoLoco. 4 hits.
    PF00515. TPR_1. 2 hits.
    PF13176. TPR_7. 1 hit.
    [Graphical view ]
    SMARTi SM00390. GoLoco. 4 hits.
    SM00028. TPR. 6 hits.
    [Graphical view ]
    PROSITEi PS50877. GOLOCO. 4 hits.
    PS50005. TPR. 6 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
      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].

    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: October 1, 2014
    This is version 106 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

    External Data

    Dasty 3