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Q9Y653 (GPR56_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G-protein coupled receptor 56
Alternative name(s):
Protein TM7XN1

Cleaved into the following 2 chains:

  1. GPR56 N-terminal fragment
    Short name=GPR56 NT
    Short name=GPR56(N)
    Alternative name(s):
    GPR56 extracellular subunit
    GPR56 subunit alpha
  2. 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 names
Name:GPR56
Synonyms:TM7LN4, TM7XN1
ORF Names:UNQ540/PRO1083
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.16 Ref.17 Ref.19

Enzyme regulation

GPR56 NT is proposed to inhibit receptor signaling; its interactions with extracellular ligands and /or homophilic GPR56 NT interactions may relieve the inhibition. Ref.19

Subunit structure

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 (Ref.15, Ref.18). 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. Ref.13 Ref.15 Ref.17 Ref.18 Ref.19

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.18.

GPR56 N-terminal fragment: Secreted Ref.18.

Tissue specificity

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. Ref.15

Post-translational modification

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). Ref.20

N-glycosylated. Contains sialic acid residues. Ref.18

Ubiquitinated. Undergoes polyubiquitination upon activation. Ref.19

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.21 Ref.22 Ref.23 Ref.24

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.

Contains 1 GPS domain.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
G-protein coupled receptor
Receptor
Transducer
   PTMGlycoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement Ref.13. Source: GDB

Rho protein signal transduction

Inferred from direct assay Ref.19. Source: UniProtKB

angiogenesis

Inferred from direct assay Ref.17. Source: UniProtKB

brain development

Inferred from mutant phenotype Ref.22. Source: GDB

cell adhesion

Inferred from direct assay PubMed 15674329. Source: GDB

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

cerebral cortex radial glia guided migration

Inferred from sequence or structural similarity. Source: UniProtKB

layer formation in cerebral cortex

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

neuropeptide signaling pathway

Inferred from electronic annotation. Source: InterPro

positive regulation of Rho protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell adhesion

Inferred from direct assay Ref.18. Source: UniProtKB

protein kinase C signaling

Inferred from direct assay Ref.17. Source: UniProtKB

vascular endothelial growth factor production

Inferred from direct assay Ref.17. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

glial limiting end-foot

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Traceable author statement Ref.13. Source: GDB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionG-protein coupled receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

collagen binding

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y653-1)

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.
Isoform 2 (identifier: Q9Y653-2)

Also known as: S1;

The sequence of this isoform differs from the canonical sequence as follows:
     429-434: Missing.
Isoform 3 (identifier: Q9Y653-3)

Also known as: S2;

The sequence of this isoform differs from the canonical sequence as follows:
     21-21: Q → QASASS
     429-434: Missing.
Isoform 4 (identifier: Q9Y653-4)

Also known as: S3;

The sequence of this isoform differs from the canonical sequence as follows:
     38-207: Missing.
Isoform 5 (identifier: Q9Y653-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.12
Chain26 – 693668G-protein coupled receptor 56
PRO_0000012880
Chain26 – ?382357GPR56 N-terminal fragment
PRO_0000423086
Chain?383 – 693311GPR56 C-terminal fragment
PRO_0000423087

Regions

Topological domain26 – 402377Extracellular Potential
Transmembrane403 – 42321Helical; Name=1; Potential
Topological domain424 – 44825Cytoplasmic Potential
Transmembrane449 – 46921Helical; Name=2; Potential
Topological domain470 – 4767Extracellular Potential
Transmembrane477 – 49721Helical; Name=3; Potential
Topological domain498 – 51821Cytoplasmic Potential
Transmembrane519 – 53921Helical; Name=4; Potential
Topological domain540 – 57637Extracellular Potential
Transmembrane577 – 59721Helical; Name=5; Potential
Topological domain598 – 60912Cytoplasmic Potential
Transmembrane610 – 63021Helical; Name=6; Potential
Topological domain631 – 6366Extracellular Potential
Transmembrane637 – 65721Helical; Name=7; Potential
Topological domain658 – 69336Cytoplasmic Potential
Domain343 – 39452GPS

Sites

Site382 – 3832Cleavage; by autocatalysis Probable

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 175175Missing in isoform 5.
VSP_047554
Alternative sequence211Q → QASASS in isoform 3.
VSP_047555
Alternative sequence38 – 207170Missing in isoform 4.
VSP_047556
Alternative sequence429 – 4346Missing in isoform 2 and isoform 3.
VSP_035068
Natural variant381R → Q in BFPP; abolishes interaction with COL3A1. Ref.21 Ref.23
VAR_069581
Natural variant381R → W in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. Ref.18 Ref.21 Ref.22 Ref.23
VAR_026242
Natural variant881Y → C in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. Ref.18 Ref.21 Ref.22
VAR_026243
Natural variant911C → S in BFPP; abolishes interaction with COL3A1; reduces cell surface localization. Ref.18 Ref.21 Ref.22
VAR_026244
Natural variant2811S → R. Ref.1 Ref.2 Ref.5
Corresponds to variant rs1801257 [ dbSNP | Ensembl ].
VAR_017910
Natural variant3061Q → H. Ref.1 Ref.2 Ref.5 Ref.7 Ref.8 Ref.11
Corresponds to variant rs1801255 [ dbSNP | Ensembl ].
VAR_017911
Natural variant3461C → S in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization. Ref.18 Ref.22
VAR_026245
Natural variant3491W → S in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization. Ref.18 Ref.23
VAR_069582
Natural variant4931M → T.
Corresponds to variant rs17379472 [ dbSNP | Ensembl ].
VAR_049457
Natural variant4961E → K in BFPP; reduces cell surface localization. Ref.24
VAR_069583
Natural variant5271P → L.
Corresponds to variant rs16958679 [ dbSNP | Ensembl ].
VAR_049458
Natural variant5651R → W in BFPP; reduces cell surface localization. Ref.18 Ref.22 Ref.23
VAR_026246
Natural variant6401L → R in BFPP; reduces cell surface localization. Ref.18 Ref.23
VAR_069584

Experimental info

Mutagenesis3811H → S: Abolishes cleavage. Ref.20
Mutagenesis3831T → G: Abolishes cleavage. Ref.18 Ref.20
Sequence conflict3291V → A Ref.8
Sequence conflict5611M → R in BAD18684. Ref.5
Sequence conflict6781S → C in AAD30545. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 801C8E62666A5155

FASTA69377,738
        10         20         30         40         50         60 
MTPQSLLQTT LFLLSLLFLV QGAHGRGHRE DFRFCSQRNQ THRSSLHYKP TPDLRISIEN 

        70         80         90        100        110        120 
SEEALTVHAP FPAAHPASRS FPDPRGLYHF CLYWNRHAGR LHLLYGKRDF LLSDKASSLL 

       130        140        150        160        170        180 
CFQHQEESLA QGPPLLATSV TSWWSPQNIS LPSAASFTFS FHSPPHTAAH NASVDMCELK 

       190        200        210        220        230        240 
RDLQLLSQFL KHPQKASRRP SAAPASQQLQ SLESKLTSVR FMGDMVSFEE DRINATVWKL 

       250        260        270        280        290        300 
QPTAGLQDLH IHSRQEEEQS EIMEYSVLLP RTLFQRTKGR SGEAEKRLLL VDFSSQALFQ 

       310        320        330        340        350        360 
DKNSSQVLGE KVLGIVVQNT KVANLTEPVV LTFQHQLQPK NVTLQCVFWV EDPTLSSPGH 

       370        380        390        400        410        420 
WSSAGCETVR RETQTSCFCN HLTYFAVLMV SSVEVDAVHK HYLSLLSYVG CVVSALACLV 

       430        440        450        460        470        480 
TIAAYLCSRV PLPCRRKPRD YTIKVHMNLL LAVFLLDTSF LLSEPVALTG SEAGCRASAI 

       490        500        510        520        530        540 
FLHFSLLTCL SWMGLEGYNL YRLVVEVFGT YVPGYLLKLS AMGWGFPIFL VTLVALVDVD 

       550        560        570        580        590        600 
NYGPIILAVH RTPEGVIYPS MCWIRDSLVS YITNLGLFSL VFLFNMAMLA TMVVQILRLR 

       610        620        630        640        650        660 
PHTQKWSHVL TLLGLSLVLG LPWALIFFSF ASGTFQLVVL YLFSIITSFQ GFLIFIWYWS 

       670        680        690 
MRLQARGGPS PLKSNSDSAR LPISSGSTSS SRI 

« Hide

Isoform 2 (S1) [UniParc].

Checksum: BB8712796ED1B99B
Show »

FASTA68777,072
Isoform 3 (S2) [UniParc].

Checksum: 62A00681FE932B65
Show »

FASTA69277,476
Isoform 4 (S3) [UniParc].

Checksum: C4CB64E369DDC33C
Show »

FASTA52358,655
Isoform 5 (S4) [UniParc].

Checksum: 7CFB3855CAED164C
Show »

FASTA51858,042

References

« Hide 'large scale' references
[1]"GPR56, a novel secretin-like human G-protein-coupled receptor gene."
Liu M., Parker R.M.C., Darby K., Eyre H.J., Copeland N.G., Crawford J., Gilbert D.J., Sutherland G.R., Jenkins N.A., Herzog H.
Genomics 55:296-305(1999) [PubMed] [Europe PMC] [Abstract]
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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"G protein-coupled receptor-dependent development of human frontal cortex."
Piao X., Hill R.S., Bodell A., Chang B.S., Basel-Vanagaite L., Straussberg R., Dobyns W.B., Qasrawi B., Winter R.M., Innes A.M., Voit T., Ross M.E., Michaud J.L., Descarie J.-C., Barkovich A.J., Walsh C.A.
Science 303:2033-2036(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BFPP TRP-38; CYS-88; SER-91; SER-346 AND TRP-565.
[23]"Genotype-phenotype analysis of human frontoparietal polymicrogyria syndromes."
Piao X., Chang B.S., Bodell A., Woods K., Benzeev B., Topcu M., Guerrini R., Goldberg-Stern H., Sztriha L., Dobyns W.B., Barkovich A.J., Walsh C.A.
Ann. Neurol. 58:680-687(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BFPP GLN-38; TRP-38; SER-349; TRP-565 AND ARG-640.
[24]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32460.1. [Q9Y653-1]
CCDS32461.1. [Q9Y653-2]
RefSeqNP_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]
UniGeneHs.513633.

3D structure databases

ProteinModelPortalQ9Y653.
SMRQ9Y653. Positions 445-658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114704. 2 interactions.
IntActQ9Y653. 2 interactions.
STRING9606.ENSP00000369018.

Protein family/group databases

MEROPSS63.011.
GPCRDBSearch...

PTM databases

PhosphoSiteQ9Y653.

Polymorphism databases

DMDM45476992.

Proteomic databases

MaxQBQ9Y653.
PaxDbQ9Y653.
PRIDEQ9Y653.

Protocols and materials databases

DNASU9289.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379694; ENSP00000369016; ENSG00000205336. [Q9Y653-4]
ENST00000379696; ENSP00000369018; ENSG00000205336. [Q9Y653-1]
ENST00000388812; ENSP00000373464; ENSG00000205336. [Q9Y653-1]
ENST00000388813; ENSP00000373465; ENSG00000205336. [Q9Y653-2]
ENST00000456916; ENSP00000398034; ENSG00000205336. [Q9Y653-1]
ENST00000538815; ENSP00000444415; ENSG00000205336. [Q9Y653-2]
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]
GeneID9289.
KEGGhsa:9289.
UCSCuc002ema.1. human. [Q9Y653-1]
uc002emc.2. human. [Q9Y653-2]

Organism-specific databases

CTD9289.
GeneCardsGC16P057653.
GeneReviewsGPR56.
HGNCHGNC:4512. GPR56.
HPAHPA046065.
MIM604110. gene.
606854. phenotype.
neXtProtNX_Q9Y653.
Orphanet101070. Bilateral frontoparietal polymicrogyria.
98889. Bilateral perisylvian polymicrogyria.
PharmGKBPA28901.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290113.
HOVERGENHBG051814.
InParanoidQ9Y653.
KOK08450.
OMAWGFPIFL.
OrthoDBEOG7XPZ55.
PhylomeDBQ9Y653.
TreeFamTF321769.

Gene expression databases

ArrayExpressQ9Y653.
BgeeQ9Y653.
CleanExHS_GPR56.
GenevestigatorQ9Y653.

Family and domain databases

InterProIPR017981. GPCR_2-like.
IPR003910. GPCR_2_orphan_rcpt_GPR56.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSPR00249. GPCRSECRETIN.
PR01422. GPR56ORPHANR.
SMARTSM00303. GPS. 1 hit.
[Graphical view]
PROSITEPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPR56. human.
GenomeRNAi9289.
NextBio34805.
PROQ9Y653.
SOURCESearch...

Entry information

Entry nameGPR56_HUMAN
AccessionPrimary (citable) accession number: Q9Y653
Secondary accession number(s): A6NIT7 expand/collapse secondary AC list , A6NJV9, B0M0K4, B4DR54, O95966, Q6ZMP1, Q8NGB3, Q96HB4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries