Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8K209

- GPR56_MOUSE

UniProt

Q8K209 - GPR56_MOUSE

Protein

G-protein coupled receptor 56

Gene

Gpr56

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in cell adhesion and probably in cell-cell interactions. Regulates the migration of neural precursor cells. Receptor for collagen III/Col3a1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial basemant membrane integrity and in cortical lamination. Binding to the Col3a1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to Gna13 and possibly Gna12. Required for normal cortical development and regulation of neuroprogenitor cells proliferation.5 Publications

    Enzyme regulationi

    GPR56 NT is proposed to inhibit receptor signaling; its interactions with extracellular ligands and /or homophilic GPR56 NT interactions may relieve the inhibition.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei382 – 3832Cleavage; by autocatalysisBy similarity

    GO - Molecular functioni

    1. collagen binding Source: UniProtKB
    2. extracellular matrix binding Source: UniProtKB
    3. G-protein coupled receptor activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. cell adhesion Source: UniProtKB-KW
    3. cerebral cortex radial glia guided migration Source: UniProtKB
    4. layer formation in cerebral cortex Source: UniProtKB
    5. negative regulation of cell proliferation Source: UniProtKB
    6. negative regulation of neuron migration Source: UniProtKB
    7. neuropeptide signaling pathway Source: InterPro
    8. positive regulation of cell adhesion Source: UniProtKB
    9. positive regulation of Rho protein signal transduction Source: UniProtKB
    10. protein kinase C signaling Source: UniProtKB
    11. Rho protein signal transduction Source: UniProtKB
    12. vascular endothelial growth factor production Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Cell adhesion, Differentiation, Neurogenesis

    Protein family/group databases

    MEROPSiS63.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G-protein coupled receptor 56
    Alternative name(s):
    Serpentine receptor cyt28
    Cleaved into the following 2 chains:
    GPR56 N-terminal fragment
    Short name:
    GPR56 NT
    Short name:
    GPR56(N)
    Alternative name(s):
    GPR56 extracellular subunit
    GPR56 subunit alpha
    GPR56 C-terminal fragment
    Short name:
    GPR56 CT
    Short name:
    GPR56(C)
    Alternative name(s):
    GPR56 seven-transmembrane subunit
    Short name:
    GPR56 7TM
    GPR56 subunit beta
    Gene namesi
    Name:Gpr56
    Synonyms:Cyt28
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1340051. Gpr56.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. glial limiting end-foot Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Cobblestone-like cortical malformation with defective pial basement membrane (BM), abnormal anchorage of radial glial endfeet, mislocalized Cajal-Retzius cells and neuronal overmigration. Severe malformation of the rostral cerebellum that develops perinatally. Granule cells from the rostral region show loss of adhesion to extracellular matrix molecules of the pial basement membrane. In GPR56 knockout mice, neurons overmigrate through breached pial basement membrane or undermigrate forming irregular cortical layers.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381R → Q or W: Reduced cell surface localization. 1 Publication
    Mutagenesisi88 – 881Y → C: Reduced cell surface localization. 1 Publication
    Mutagenesisi91 – 911C → S: Reduced cell surface localization. 1 Publication
    Mutagenesisi346 – 3461C → S: Abolishes proteolytic cleavage and cell surface localization. 1 Publication
    Mutagenesisi349 – 3491W → S: Abolishes proteolytic cleavage and cell surface localization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 687662G-protein coupled receptor 56PRO_0000012882Add
    BLAST
    Chaini26 – ?382357GPR56 N-terminal fragmentPRO_0000423090Add
    BLAST
    Chaini?383 – 687305GPR56 C-terminal fragmentPRO_0000423091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi39 – 391N-linked (GlcNAc...)1 Publication
    Glycosylationi148 – 1481N-linked (GlcNAc...)1 Publication
    Glycosylationi171 – 1711N-linked (GlcNAc...)1 Publication
    Glycosylationi234 – 2341N-linked (GlcNAc...)1 Publication
    Glycosylationi303 – 3031N-linked (GlcNAc...)1 Publication
    Glycosylationi324 – 3241N-linked (GlcNAc...)1 Publication
    Glycosylationi341 – 3411N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Autoproteolytically cleaved into 2 fragments; the large extracellular N-terminal fragment and the membroune-bound C-terminal fragment predominantly remain associated and non-covalently linked.1 Publication
    N-glycosylated. Th secreted GPR56 N-terminal fragment is heavily glycosylated.1 Publication
    Ubiquitinated. Undergoes polyubiquitination upon activation By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8K209.
    PaxDbiQ8K209.
    PRIDEiQ8K209.

    PTM databases

    PhosphoSiteiQ8K209.

    Expressioni

    Tissue specificityi

    Expressed in neural progenitor cells in fetal forbrain. Expressed in migrating neurons. Expressed in radial glial endfeet (at protein level).1 Publication

    Gene expression databases

    BgeeiQ8K209.
    CleanExiMM_GPR56.
    GenevestigatoriQ8K209.

    Interactioni

    Subunit structurei

    Predominantly non-covalently linked heterodimer of the N-terminal and the C-terminal fragment. GPR56 NT self-associates in a trans-trans manner; the homophilic interaction enhances receptor signaling. GPR56 CT interacts with ARRB2; the interaction is impaired by GPR56 NT. Part of a GPCR-tetraspanin complex at least consisting of GPR56, CD81, eventually CD9, and GNA11 in which CD81 is enhancing the association of GPR56 with GNA11 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8K209. 1 interaction.
    STRINGi10090.ENSMUSP00000090959.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K209.
    SMRiQ8K209. Positions 439-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 402377ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini424 – 44219CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini464 – 4718ExtracellularSequence Analysis
    Topological domaini493 – 51220CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini534 – 57037ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini592 – 60312CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini625 – 6306ExtracellularSequence Analysis
    Topological domaini652 – 68736CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei403 – 42321Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei443 – 46321Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei472 – 49221Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei513 – 53321Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei571 – 59121Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei604 – 62421Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei631 – 65121Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini343 – 39452GPSPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GPS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG290113.
    GeneTreeiENSGT00750000117610.
    HOGENOMiHOG000015136.
    HOVERGENiHBG051814.
    InParanoidiQ8K209.
    KOiK08450.
    OMAiWGFPIFL.
    OrthoDBiEOG7XPZ55.
    PhylomeDBiQ8K209.
    TreeFamiTF321769.

    Family and domain databases

    InterProiIPR017981. GPCR_2-like.
    IPR003910. GPCR_2_orphan_rcpt_GPR56.
    IPR000832. GPCR_2_secretin-like.
    IPR000203. GPS.
    [Graphical view]
    PfamiPF00002. 7tm_2. 1 hit.
    PF01825. GPS. 1 hit.
    [Graphical view]
    PRINTSiPR00249. GPCRSECRETIN.
    PR01422. GPR56ORPHANR.
    SMARTiSM00303. GPS. 1 hit.
    [Graphical view]
    PROSITEiPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    PS50221. GPS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8K209-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVQVLRQMV YFLLSLFSLV QGAHSGSPRE DFRFCGQRNQ TQQSTLHYDQ    50
    SSEPHIFVWN TEETLTIRAP FLAAPDIPRF FPEPRGLYHF CLYWSRHTGR 100
    LHLRYGKHDY LLSSQASRLL CFQKQEQSLK QGAPLIATSV SSWQIPQNTS 150
    LPGAPSFIFS FHNAPHKVSH NASVDMCDLK KELQQLSRYL QHPQKAAKRP 200
    TAAFISQQLQ SLESKLTSVS FLGDTLSFEE DRVNATVWKL PPTAGLEDLH 250
    IHSQKEEEQS EVQAYSLLLP RAVFQQTRGR RRDDAKRLLV VDFSSQALFQ 300
    DKNSSQVLGE KVLGIVVQNT KVTNLSDPVV LTFQHQPQPK NVTLQCVFWV 350
    EDPASSSTGS WSSAGCETVS RDTQTSCLCN HLTYFAVLMV SSTEVEATHK 400
    HYLTLLSYVG CVISALACVF TIAAYLCSRR KSRDYTIKVH MNLLSAVFLL 450
    DVSFLLSEPV ALTGSEAACR TSAMFLHFSL LACLSWMGLE GYNLYRLVVE 500
    VFGTYVPGYL LKLSIVGWGF PVFLVTLVAL VDVNNYGPII LAVRRTPERV 550
    TYPSMCWIRD SLVSYVTNLG LFSLVFLFNL AMLATMVVQI LRLRPHSQNW 600
    PHVLTLLGLS LVLGLPWALV FFSFASGTFQ LVILYLFSII TSFQGFLIFL 650
    WYWSMRFQAQ GGPSPLKNNS DSAKLPISSG STSSSRI 687
    Length:687
    Mass (Da):77,255
    Last modified:October 1, 2002 - v1
    Checksum:iB5315D70B66C9A9A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti643 – 6431F → Y in AAF00617. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF166382 mRNA. Translation: AAF00617.1.
    AK087268 mRNA. Translation: BAC39835.1.
    AK133678 mRNA. Translation: BAE21780.1.
    AK141886 mRNA. Translation: BAE24871.1.
    AK141894 mRNA. Translation: BAE24874.1.
    AK167547 mRNA. Translation: BAE39613.1.
    BC034678 mRNA. Translation: AAH34678.1.
    CCDSiCCDS22553.1.
    RefSeqiNP_001185823.1. NM_001198894.1.
    NP_061370.2. NM_018882.3.
    XP_006530755.1. XM_006530692.1.
    XP_006530756.1. XM_006530693.1.
    XP_006530757.1. XM_006530694.1.
    XP_006530758.1. XM_006530695.1.
    XP_006530759.1. XM_006530696.1.
    XP_006530760.1. XM_006530697.1.
    UniGeneiMm.290834.

    Genome annotation databases

    EnsembliENSMUST00000093271; ENSMUSP00000090959; ENSMUSG00000031785.
    ENSMUST00000179619; ENSMUSP00000137520; ENSMUSG00000031785.
    GeneIDi14766.
    KEGGimmu:14766.
    UCSCiuc009mxl.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF166382 mRNA. Translation: AAF00617.1 .
    AK087268 mRNA. Translation: BAC39835.1 .
    AK133678 mRNA. Translation: BAE21780.1 .
    AK141886 mRNA. Translation: BAE24871.1 .
    AK141894 mRNA. Translation: BAE24874.1 .
    AK167547 mRNA. Translation: BAE39613.1 .
    BC034678 mRNA. Translation: AAH34678.1 .
    CCDSi CCDS22553.1.
    RefSeqi NP_001185823.1. NM_001198894.1.
    NP_061370.2. NM_018882.3.
    XP_006530755.1. XM_006530692.1.
    XP_006530756.1. XM_006530693.1.
    XP_006530757.1. XM_006530694.1.
    XP_006530758.1. XM_006530695.1.
    XP_006530759.1. XM_006530696.1.
    XP_006530760.1. XM_006530697.1.
    UniGenei Mm.290834.

    3D structure databases

    ProteinModelPortali Q8K209.
    SMRi Q8K209. Positions 439-660.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8K209. 1 interaction.
    STRINGi 10090.ENSMUSP00000090959.

    Protein family/group databases

    MEROPSi S63.011.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q8K209.

    Proteomic databases

    MaxQBi Q8K209.
    PaxDbi Q8K209.
    PRIDEi Q8K209.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000093271 ; ENSMUSP00000090959 ; ENSMUSG00000031785 .
    ENSMUST00000179619 ; ENSMUSP00000137520 ; ENSMUSG00000031785 .
    GeneIDi 14766.
    KEGGi mmu:14766.
    UCSCi uc009mxl.2. mouse.

    Organism-specific databases

    CTDi 9289.
    MGIi MGI:1340051. Gpr56.

    Phylogenomic databases

    eggNOGi NOG290113.
    GeneTreei ENSGT00750000117610.
    HOGENOMi HOG000015136.
    HOVERGENi HBG051814.
    InParanoidi Q8K209.
    KOi K08450.
    OMAi WGFPIFL.
    OrthoDBi EOG7XPZ55.
    PhylomeDBi Q8K209.
    TreeFami TF321769.

    Miscellaneous databases

    ChiTaRSi GPR56. mouse.
    NextBioi 286855.
    PROi Q8K209.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8K209.
    CleanExi MM_GPR56.
    Genevestigatori Q8K209.

    Family and domain databases

    InterProi IPR017981. GPCR_2-like.
    IPR003910. GPCR_2_orphan_rcpt_GPR56.
    IPR000832. GPCR_2_secretin-like.
    IPR000203. GPS.
    [Graphical view ]
    Pfami PF00002. 7tm_2. 1 hit.
    PF01825. GPS. 1 hit.
    [Graphical view ]
    PRINTSi PR00249. GPCRSECRETIN.
    PR01422. GPR56ORPHANR.
    SMARTi SM00303. GPS. 1 hit.
    [Graphical view ]
    PROSITEi PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    PS50221. GPS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel hematopoietic stem cell regulatory genes."
      Phillips R.L., Ernst R.E., Dosil M., Wesley C.K., Moore K.A., Kingsley P.D., Sykes S., Palis J., Lemischka I.R.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Liver.
    2. "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].
      Strain: C57BL/6J.
      Tissue: Lung, Pituitary, Placenta and Spinal ganglion.
    3. "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].
    4. "Disease-associated mutations affect GPR56 protein trafficking and cell surface expression."
      Jin Z., Tietjen I., Bu L., Liu-Yesucevitz L., Gaur S.K., Walsh C.A., Piao X.
      Hum. Mol. Genet. 16:1972-1985(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ARG-38; ASN-39; TYR-88; CYS-91; ASN-148; ASN-171; ASN-234; ASN-303; ASN-324 AND ASN-341, MUTAGENESIS OF CYS-346 AND TRP-349.
    5. "GPR56 regulates pial basement membrane integrity and cortical lamination."
      Li S., Jin Z., Koirala S., Bu L., Xu L., Hynes R.O., Walsh C.A., Corfas G., Piao X.
      J. Neurosci. 28:5817-5826(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a G alpha 12/13 and Rho pathway."
      Iguchi T., Sakata K., Yoshizaki K., Tago K., Mizuno N., Itoh H.
      J. Biol. Chem. 283:14469-14478(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "GPR56-regulated granule cell adhesion is essential for rostral cerebellar development."
      Koirala S., Jin Z., Piao X., Corfas G.
      J. Neurosci. 29:7439-7449(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AND DISRUPTION PHENOTYPE.
    8. "G protein-coupled receptor 56 and collagen III, a receptor-ligand pair, regulates cortical development and lamination."
      Luo R., Jeong S.J., Jin Z., Strokes N., Li S., Piao X.
      Proc. Natl. Acad. Sci. U.S.A. 108:12925-12930(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, LIGAND-BINDING.
    9. "Disease-associated mutations prevent GPR56-collagen III interaction."
      Luo R., Jin Z., Deng Y., Strokes N., Piao X.
      PLoS ONE 7:E29818-E29818(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND-BINDING, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-38; TYR-88 AND CYS-91.
    10. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiGPR56_MOUSE
    AccessioniPrimary (citable) accession number: Q8K209
    Secondary accession number(s): Q3UR17, Q9QZT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3