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Q9Y653

- GPR56_HUMAN

UniProt

Q9Y653 - GPR56_HUMAN

Protein

G-protein coupled receptor 56

Gene

GPR56

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      Previous versions | rss
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    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. Isoforms show differences in receptor signaling, specifically in serum response element (SRE) transcriptional activation upon overexpression. Overexpression inhibits melanoma tumor growth and metastasis and, during melanoma progression, regulates VEGFA production and angiogenesis through PRKCA; unprocessed GPR56 is inhibiting and GPR56 NT is activating angiogenesis. 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.1 Publication

    Sites

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

    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. brain development Source: GDB
    3. cell adhesion Source: GDB
    4. cell-cell signaling Source: ProtInc
    5. cerebral cortex radial glia guided migration Source: UniProtKB
    6. G-protein coupled receptor signaling pathway Source: GDB
    7. layer formation in cerebral cortex Source: UniProtKB
    8. negative regulation of cell proliferation Source: UniProtKB
    9. negative regulation of neuron migration Source: UniProtKB
    10. neuropeptide signaling pathway Source: InterPro
    11. positive regulation of cell adhesion Source: UniProtKB
    12. positive regulation of Rho protein signal transduction Source: UniProtKB
    13. protein kinase C signaling Source: UniProtKB
    14. Rho protein signal transduction Source: UniProtKB
    15. 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):
    Protein TM7XN1
    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:TM7LN4, TM7XN1
    ORF Names:UNQ540/PRO1083
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:4512. GPR56.

    Subcellular locationi

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

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. glial limiting end-foot Source: UniProtKB
    3. integral component of membrane Source: GDB
    4. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Polymicrogyria, bilateral frontoparietal (BFPP) [MIM:606854]: A malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination, most severe in the frontoparietal regions. BFPP clinical manifestations include developmental and psychomotor delay, cerebellar and pyramidal signs, truncal ataxia, seizures, hyperreflexia. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → Q in BFPP; abolishes interaction with COL3A1. 1 Publication
    VAR_069581
    Natural varianti38 – 381R → W in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. 2 Publications
    VAR_026242
    Natural varianti88 – 881Y → C in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. 1 Publication
    VAR_026243
    Natural varianti91 – 911C → S in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. 1 Publication
    VAR_026244
    Natural varianti346 – 3461C → S in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization. 1 Publication
    VAR_026245
    Natural varianti349 – 3491W → S in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization. 1 Publication
    VAR_069582
    Natural varianti496 – 4961E → K in BFPP; reduces cell surface localization. 1 Publication
    VAR_069583
    Natural varianti565 – 5651R → W in BFPP; reduces cell surface localization. 2 Publications
    VAR_026246
    Natural varianti640 – 6401L → R in BFPP; reduces cell surface localization. 1 Publication
    VAR_069584
    Polymicrogyria, bilateral perisylvian, autosomal recessive (BPPR) [MIM:615752]: A form of polymicrogyria, a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. BPPR is characterized by strikingly restricted polymicrogyria limited to the cortex surrounding the Sylvian fissure. Affected individuals have intellectual and language difficulty and seizures, but no motor disability. Polymicrogyria is a heterogeneous disorder, considered to be the result of post-migratory abnormal cortical organization.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. Homozygous deletion of 1 of 2 tandem 15-bp repeats located 144 bp upstream of the GPR56 non-coding exon 1m transcription start site, results in impaired perisylvian GPR56 expression and disruption of perisylvian gyri (PubMed:24531968).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi381 – 3811H → S: Abolishes cleavage. 1 Publication
    Mutagenesisi383 – 3831T → G: Abolishes cleavage. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi606854. phenotype.
    615752. phenotype.
    Orphaneti101070. Bilateral frontoparietal polymicrogyria.
    98889. Bilateral perisylvian polymicrogyria.
    PharmGKBiPA28901.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 693668G-protein coupled receptor 56PRO_0000012880Add
    BLAST
    Chaini26 – ?382357GPR56 N-terminal fragmentPRO_0000423086Add
    BLAST
    Chaini?383 – 693311GPR56 C-terminal fragmentPRO_0000423087Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Autoproteolytically cleaved into 2 fragments; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked. Shedding to yield the secreted GPR56 N-terminal fragment seems to involve metalloprotease(s).1 Publication
    N-glycosylated. Contains sialic acid residues.1 Publication
    Ubiquitinated. Undergoes polyubiquitination upon activation.1 Publication

    Keywords - PTMi

    Glycoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y653.
    PaxDbiQ9Y653.
    PRIDEiQ9Y653.

    PTM databases

    PhosphoSiteiQ9Y653.

    Expressioni

    Tissue specificityi

    Widely distributed with highest levels found in thyroid gland, brain and heart. Expressed in a great number of tumor cells. Expression is down-regulated in different tumors from highly metastatic cells.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y653.
    BgeeiQ9Y653.
    CleanExiHS_GPR56.
    GenevestigatoriQ9Y653.

    Organism-specific databases

    HPAiHPA046065.

    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. Interacts with TGM2; TGM2 probably is not a GPR56 ligand and the interaction is reported conflictingly (PubMed:16757564, PubMed:21349848). 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 GNA11.5 Publications

    Protein-protein interaction databases

    BioGridi114704. 3 interactions.
    IntActiQ9Y653. 2 interactions.
    STRINGi9606.ENSP00000369018.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y653.
    SMRiQ9Y653. Positions 445-658.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 402377ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini424 – 44825CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini470 – 4767ExtracellularSequence Analysis
    Topological domaini498 – 51821CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini540 – 57637ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini598 – 60912CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini631 – 6366ExtracellularSequence Analysis
    Topological domaini658 – 69336CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei403 – 42321Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei449 – 46921Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei477 – 49721Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei519 – 53921Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei577 – 59721Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei610 – 63021Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei637 – 65721Helical; 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.
    HOVERGENiHBG051814.
    InParanoidiQ9Y653.
    KOiK08450.
    OMAiWGFPIFL.
    OrthoDBiEOG7XPZ55.
    PhylomeDBiQ9Y653.
    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]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y653-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTPQSLLQTT LFLLSLLFLV QGAHGRGHRE DFRFCSQRNQ THRSSLHYKP    50
    TPDLRISIEN SEEALTVHAP FPAAHPASRS FPDPRGLYHF CLYWNRHAGR 100
    LHLLYGKRDF LLSDKASSLL CFQHQEESLA QGPPLLATSV TSWWSPQNIS 150
    LPSAASFTFS FHSPPHTAAH NASVDMCELK RDLQLLSQFL KHPQKASRRP 200
    SAAPASQQLQ SLESKLTSVR FMGDMVSFEE DRINATVWKL QPTAGLQDLH 250
    IHSRQEEEQS EIMEYSVLLP RTLFQRTKGR SGEAEKRLLL VDFSSQALFQ 300
    DKNSSQVLGE KVLGIVVQNT KVANLTEPVV LTFQHQLQPK NVTLQCVFWV 350
    EDPTLSSPGH WSSAGCETVR RETQTSCFCN HLTYFAVLMV SSVEVDAVHK 400
    HYLSLLSYVG CVVSALACLV TIAAYLCSRV PLPCRRKPRD YTIKVHMNLL 450
    LAVFLLDTSF LLSEPVALTG SEAGCRASAI FLHFSLLTCL SWMGLEGYNL 500
    YRLVVEVFGT YVPGYLLKLS AMGWGFPIFL VTLVALVDVD NYGPIILAVH 550
    RTPEGVIYPS MCWIRDSLVS YITNLGLFSL VFLFNMAMLA TMVVQILRLR 600
    PHTQKWSHVL TLLGLSLVLG LPWALIFFSF ASGTFQLVVL YLFSIITSFQ 650
    GFLIFIWYWS MRLQARGGPS PLKSNSDSAR LPISSGSTSS SRI 693
    Length:693
    Mass (Da):77,738
    Last modified:March 15, 2004 - v2
    Checksum:i801C8E62666A5155
    GO
    Isoform 2 (identifier: Q9Y653-2) [UniParc]FASTAAdd to Basket

    Also known as: S1

    The sequence of this isoform differs from the canonical sequence as follows:
         429-434: Missing.

    Show »
    Length:687
    Mass (Da):77,072
    Checksum:iBB8712796ED1B99B
    GO
    Isoform 3 (identifier: Q9Y653-3) [UniParc]FASTAAdd to Basket

    Also known as: S2

    The sequence of this isoform differs from the canonical sequence as follows:
         21-21: Q → QASASS
         429-434: Missing.

    Show »
    Length:692
    Mass (Da):77,476
    Checksum:i62A00681FE932B65
    GO
    Isoform 4 (identifier: Q9Y653-4) [UniParc]FASTAAdd to Basket

    Also known as: S3

    The sequence of this isoform differs from the canonical sequence as follows:
         38-207: Missing.

    Show »
    Length:523
    Mass (Da):58,655
    Checksum:iC4CB64E369DDC33C
    GO
    Isoform 5 (identifier: Q9Y653-5) [UniParc]FASTAAdd to Basket

    Also known as: S4

    The sequence of this isoform differs from the canonical sequence as follows:
         1-175: Missing.

    Note: Has no predictable signal peptide.

    Show »
    Length:518
    Mass (Da):58,042
    Checksum:i7CFB3855CAED164C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti329 – 3291V → A(PubMed:17974005)Curated
    Sequence conflicti561 – 5611M → R in BAD18684. (PubMed:14702039)Curated
    Sequence conflicti678 – 6781S → C in AAD30545. (PubMed:10049584)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → Q in BFPP; abolishes interaction with COL3A1. 1 Publication
    VAR_069581
    Natural varianti38 – 381R → W in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. 2 Publications
    VAR_026242
    Natural varianti88 – 881Y → C in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. 1 Publication
    VAR_026243
    Natural varianti91 – 911C → S in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. 1 Publication
    VAR_026244
    Natural varianti281 – 2811S → R.3 Publications
    Corresponds to variant rs1801257 [ dbSNP | Ensembl ].
    VAR_017910
    Natural varianti306 – 3061Q → H.6 Publications
    Corresponds to variant rs1801255 [ dbSNP | Ensembl ].
    VAR_017911
    Natural varianti346 – 3461C → S in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization. 1 Publication
    VAR_026245
    Natural varianti349 – 3491W → S in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization. 1 Publication
    VAR_069582
    Natural varianti493 – 4931M → T.
    Corresponds to variant rs17379472 [ dbSNP | Ensembl ].
    VAR_049457
    Natural varianti496 – 4961E → K in BFPP; reduces cell surface localization. 1 Publication
    VAR_069583
    Natural varianti527 – 5271P → L.
    Corresponds to variant rs16958679 [ dbSNP | Ensembl ].
    VAR_049458
    Natural varianti565 – 5651R → W in BFPP; reduces cell surface localization. 2 Publications
    VAR_026246
    Natural varianti640 – 6401L → R in BFPP; reduces cell surface localization. 1 Publication
    VAR_069584

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 175175Missing in isoform 5. 1 PublicationVSP_047554Add
    BLAST
    Alternative sequencei21 – 211Q → QASASS in isoform 3. 1 PublicationVSP_047555
    Alternative sequencei38 – 207170Missing in isoform 4. 1 PublicationVSP_047556Add
    BLAST
    Alternative sequencei429 – 4346Missing in isoform 2 and isoform 3. 2 PublicationsVSP_035068

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106858 mRNA. Translation: AAD30545.1.
    AJ011001 mRNA. Translation: CAB37294.1.
    EU432119 mRNA. Translation: ABY87918.1.
    AY358400 mRNA. Translation: AAQ88766.1.
    AK131550 mRNA. Translation: BAD18684.1.
    AK299110 mRNA. Translation: BAG61166.1.
    AB065909 Genomic DNA. Translation: BAC06124.1.
    BT007311 mRNA. Translation: AAP35975.1.
    CR936747 mRNA. No translation available.
    AC018552 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW82939.1.
    CH471092 Genomic DNA. Translation: EAW82940.1.
    BC008770 mRNA. Translation: AAH08770.1.
    CCDSiCCDS32460.1. [Q9Y653-1]
    CCDS32461.1. [Q9Y653-2]
    RefSeqiNP_001139242.1. NM_001145770.2. [Q9Y653-2]
    NP_001139243.1. NM_001145771.2. [Q9Y653-1]
    NP_001139244.1. NM_001145772.2. [Q9Y653-2]
    NP_001139245.1. NM_001145773.2. [Q9Y653-3]
    NP_001139246.1. NM_001145774.2. [Q9Y653-2]
    NP_001277071.1. NM_001290142.1. [Q9Y653-4]
    NP_001277072.1. NM_001290143.1. [Q9Y653-5]
    NP_005673.3. NM_005682.6. [Q9Y653-1]
    NP_958932.1. NM_201524.3. [Q9Y653-2]
    NP_958933.1. NM_201525.3. [Q9Y653-2]
    XP_005256303.1. XM_005256246.1. [Q9Y653-1]
    XP_005256304.1. XM_005256247.1. [Q9Y653-1]
    XP_005256305.1. XM_005256248.1. [Q9Y653-1]
    XP_005256306.1. XM_005256249.1. [Q9Y653-1]
    XP_005256308.1. XM_005256251.2. [Q9Y653-1]
    XP_005256309.1. XM_005256252.1. [Q9Y653-1]
    XP_005256310.1. XM_005256253.2. [Q9Y653-1]
    XP_005256311.1. XM_005256254.1. [Q9Y653-1]
    XP_005256312.1. XM_005256255.1. [Q9Y653-2]
    XP_006721405.1. XM_006721342.1. [Q9Y653-1]
    XP_006721406.1. XM_006721343.1. [Q9Y653-1]
    XP_006721407.1. XM_006721344.1. [Q9Y653-1]
    XP_006721408.1. XM_006721345.1. [Q9Y653-1]
    XP_006721409.1. XM_006721346.1. [Q9Y653-1]
    XP_006721410.1. XM_006721347.1. [Q9Y653-3]
    UniGeneiHs.513633.

    Genome annotation databases

    EnsembliENST00000388813; ENSP00000373465; ENSG00000205336. [Q9Y653-2]
    ENST00000456916; ENSP00000398034; ENSG00000205336. [Q9Y653-1]
    ENST00000540164; ENSP00000444911; ENSG00000205336. [Q9Y653-2]
    ENST00000562558; ENSP00000456620; ENSG00000205336. [Q9Y653-2]
    ENST00000562631; ENSP00000455351; ENSG00000205336. [Q9Y653-2]
    ENST00000567835; ENSP00000456794; ENSG00000205336. [Q9Y653-1]
    ENST00000568908; ENSP00000457456; ENSG00000205336. [Q9Y653-2]
    ENST00000568909; ENSP00000455215; ENSG00000205336. [Q9Y653-1]
    GeneIDi9289.
    KEGGihsa:9289.
    UCSCiuc002ema.1. human. [Q9Y653-1]
    uc002emc.2. human. [Q9Y653-2]

    Polymorphism databases

    DMDMi45476992.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106858 mRNA. Translation: AAD30545.1 .
    AJ011001 mRNA. Translation: CAB37294.1 .
    EU432119 mRNA. Translation: ABY87918.1 .
    AY358400 mRNA. Translation: AAQ88766.1 .
    AK131550 mRNA. Translation: BAD18684.1 .
    AK299110 mRNA. Translation: BAG61166.1 .
    AB065909 Genomic DNA. Translation: BAC06124.1 .
    BT007311 mRNA. Translation: AAP35975.1 .
    CR936747 mRNA. No translation available.
    AC018552 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW82939.1 .
    CH471092 Genomic DNA. Translation: EAW82940.1 .
    BC008770 mRNA. Translation: AAH08770.1 .
    CCDSi CCDS32460.1. [Q9Y653-1 ]
    CCDS32461.1. [Q9Y653-2 ]
    RefSeqi NP_001139242.1. NM_001145770.2. [Q9Y653-2 ]
    NP_001139243.1. NM_001145771.2. [Q9Y653-1 ]
    NP_001139244.1. NM_001145772.2. [Q9Y653-2 ]
    NP_001139245.1. NM_001145773.2. [Q9Y653-3 ]
    NP_001139246.1. NM_001145774.2. [Q9Y653-2 ]
    NP_001277071.1. NM_001290142.1. [Q9Y653-4 ]
    NP_001277072.1. NM_001290143.1. [Q9Y653-5 ]
    NP_005673.3. NM_005682.6. [Q9Y653-1 ]
    NP_958932.1. NM_201524.3. [Q9Y653-2 ]
    NP_958933.1. NM_201525.3. [Q9Y653-2 ]
    XP_005256303.1. XM_005256246.1. [Q9Y653-1 ]
    XP_005256304.1. XM_005256247.1. [Q9Y653-1 ]
    XP_005256305.1. XM_005256248.1. [Q9Y653-1 ]
    XP_005256306.1. XM_005256249.1. [Q9Y653-1 ]
    XP_005256308.1. XM_005256251.2. [Q9Y653-1 ]
    XP_005256309.1. XM_005256252.1. [Q9Y653-1 ]
    XP_005256310.1. XM_005256253.2. [Q9Y653-1 ]
    XP_005256311.1. XM_005256254.1. [Q9Y653-1 ]
    XP_005256312.1. XM_005256255.1. [Q9Y653-2 ]
    XP_006721405.1. XM_006721342.1. [Q9Y653-1 ]
    XP_006721406.1. XM_006721343.1. [Q9Y653-1 ]
    XP_006721407.1. XM_006721344.1. [Q9Y653-1 ]
    XP_006721408.1. XM_006721345.1. [Q9Y653-1 ]
    XP_006721409.1. XM_006721346.1. [Q9Y653-1 ]
    XP_006721410.1. XM_006721347.1. [Q9Y653-3 ]
    UniGenei Hs.513633.

    3D structure databases

    ProteinModelPortali Q9Y653.
    SMRi Q9Y653. Positions 445-658.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114704. 3 interactions.
    IntActi Q9Y653. 2 interactions.
    STRINGi 9606.ENSP00000369018.

    Protein family/group databases

    MEROPSi S63.011.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q9Y653.

    Polymorphism databases

    DMDMi 45476992.

    Proteomic databases

    MaxQBi Q9Y653.
    PaxDbi Q9Y653.
    PRIDEi Q9Y653.

    Protocols and materials databases

    DNASUi 9289.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000388813 ; ENSP00000373465 ; ENSG00000205336 . [Q9Y653-2 ]
    ENST00000456916 ; ENSP00000398034 ; ENSG00000205336 . [Q9Y653-1 ]
    ENST00000540164 ; ENSP00000444911 ; ENSG00000205336 . [Q9Y653-2 ]
    ENST00000562558 ; ENSP00000456620 ; ENSG00000205336 . [Q9Y653-2 ]
    ENST00000562631 ; ENSP00000455351 ; ENSG00000205336 . [Q9Y653-2 ]
    ENST00000567835 ; ENSP00000456794 ; ENSG00000205336 . [Q9Y653-1 ]
    ENST00000568908 ; ENSP00000457456 ; ENSG00000205336 . [Q9Y653-2 ]
    ENST00000568909 ; ENSP00000455215 ; ENSG00000205336 . [Q9Y653-1 ]
    GeneIDi 9289.
    KEGGi hsa:9289.
    UCSCi uc002ema.1. human. [Q9Y653-1 ]
    uc002emc.2. human. [Q9Y653-2 ]

    Organism-specific databases

    CTDi 9289.
    GeneCardsi GC16P057653.
    GeneReviewsi GPR56.
    HGNCi HGNC:4512. GPR56.
    HPAi HPA046065.
    MIMi 604110. gene.
    606854. phenotype.
    615752. phenotype.
    neXtProti NX_Q9Y653.
    Orphaneti 101070. Bilateral frontoparietal polymicrogyria.
    98889. Bilateral perisylvian polymicrogyria.
    PharmGKBi PA28901.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290113.
    HOVERGENi HBG051814.
    InParanoidi Q9Y653.
    KOi K08450.
    OMAi WGFPIFL.
    OrthoDBi EOG7XPZ55.
    PhylomeDBi Q9Y653.
    TreeFami TF321769.

    Miscellaneous databases

    ChiTaRSi GPR56. human.
    GenomeRNAii 9289.
    NextBioi 34805.
    PROi Q9Y653.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y653.
    Bgeei Q9Y653.
    CleanExi HS_GPR56.
    Genevestigatori Q9Y653.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-281 AND HIS-306.
    2. "TM7XN1, a novel human EGF-TM7 like protein, detected with mRNA differential display using human melanoma cell lines with different metastatic potential."
      Zendman A.J.W., Cornelissen I.M.H.A., Weidle U.H., Ruiter D.J., van Muijen G.N.P.
      FEBS Lett. 446:292-298(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ARG-281 AND HIS-306.
    3. Kaighin V.A., Martin A.L., Aronstam R.S.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANTS ARG-281 AND HIS-306.
      Tissue: Prostate.
    6. "Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
      Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-306.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT HIS-306.
      Tissue: Colon carcinoma.
    9. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORM 1), VARIANT HIS-306.
      Tissue: Placenta.
    12. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-40.
    13. "Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: central role of CD81 in facilitating GPR56-Galpha q/11 association."
      Little K.D., Hemler M.E., Stipp C.S.
      Mol. Biol. Cell 15:2375-2387(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD81; CD9 AND GNA11.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "GPR56, an atypical G protein-coupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis."
      Xu L., Begum S., Hearn J.D., Hynes R.O.
      Proc. Natl. Acad. Sci. U.S.A. 103:9023-9028(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TGM2.
    16. "Splicing variants of the orphan G-protein-coupled receptor GPR56 regulate the activity of transcription factors associated with tumorigenesis."
      Kim J.E., Han J.M., Park C.R., Shin K.J., Ahn C., Seong J.Y., Hwang J.I.
      J. Cancer Res. Clin. Oncol. 136:47-53(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 3; 4 AND 5).
    17. "GPR56 Regulates VEGF production and angiogenesis during melanoma progression."
      Yang L., Chen G., Mohanty S., Scott G., Fazal F., Rahman A., Begum S., Hynes R.O., Xu L.
      Cancer Res. 71:5558-5568(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TGM2.
    18. "Disease-associated GPR56 mutations cause bilateral frontoparietal polymicrogyria via multiple mechanisms."
      Chiang N.Y., Hsiao C.C., Huang Y.S., Chen H.Y., Hsieh I.J., Chang G.W., Lin H.H.
      J. Biol. Chem. 286:14215-14225(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION (GPR56 N-TERMINAL FRAGMENT), GLYCOSYLATION, CHARACTERIZATION OF VARIANTS BFPP TRP-38; CYS-88; SER-91; SER-346; SER-349; TRP-565 AND ARG-640, MUTAGENESIS OF THR-383.
    19. "The N terminus of the adhesion G protein-coupled receptor GPR56 controls receptor signaling activity."
      Paavola K.J., Stephenson J.R., Ritter S.L., Alter S.P., Hall R.A.
      J. Biol. Chem. 286:28914-28921(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION, UBIQUITINATION.
    20. "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis."
      Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., Sudhof T.C., Brunger A.T.
      EMBO J. 31:1364-1378(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF HIS-381 AND THR-383.
    21. "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, CHARACTERIZATION OF VARIANTS BFPP GLN-38; TRP-38; CYS-88 AND SER-91.
    22. Cited for: FUNCTION, INVOLVEMENT IN BPPR.
    23. Cited for: VARIANTS BFPP TRP-38; CYS-88; SER-91; SER-346 AND TRP-565.
    24. Cited for: VARIANTS BFPP GLN-38; TRP-38; SER-349; TRP-565 AND ARG-640.
    25. "A novel GPR56 mutation causes bilateral frontoparietal polymicrogyria."
      Luo R., Yang H.M., Jin Z., Halley D.J., Chang B.S., MacPherson L., Brueton L., Piao X.
      Pediatr. Neurol. 45:49-53(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BFPP LYS-496, CHARACTERIZATION OF VARIANT BFPP LYS-496.

    Entry informationi

    Entry nameiGPR56_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y653
    Secondary accession number(s): A6NIT7
    , A6NJV9, B0M0K4, B4DR54, O95966, Q6ZMP1, Q8NGB3, Q96HB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3