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Q9Y653

- GPR56_HUMAN

UniProt

Q9Y653 - GPR56_HUMAN

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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

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
Complete GO annotation...

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: UniProtKB
  2. glial limiting end-foot Source: UniProtKB
  3. integral component of membrane Source: GDB
  4. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

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

BgeeiQ9Y653.
CleanExiHS_GPR56.
ExpressionAtlasiQ9Y653. baseline and differential.
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.
GeneTreeiENSGT00760000118787.
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) [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

        10         20         30         40         50
MTPQSLLQTT LFLLSLLFLV QGAHGRGHRE DFRFCSQRNQ THRSSLHYKP
60 70 80 90 100
TPDLRISIEN SEEALTVHAP FPAAHPASRS FPDPRGLYHF CLYWNRHAGR
110 120 130 140 150
LHLLYGKRDF LLSDKASSLL CFQHQEESLA QGPPLLATSV TSWWSPQNIS
160 170 180 190 200
LPSAASFTFS FHSPPHTAAH NASVDMCELK RDLQLLSQFL KHPQKASRRP
210 220 230 240 250
SAAPASQQLQ SLESKLTSVR FMGDMVSFEE DRINATVWKL QPTAGLQDLH
260 270 280 290 300
IHSRQEEEQS EIMEYSVLLP RTLFQRTKGR SGEAEKRLLL VDFSSQALFQ
310 320 330 340 350
DKNSSQVLGE KVLGIVVQNT KVANLTEPVV LTFQHQLQPK NVTLQCVFWV
360 370 380 390 400
EDPTLSSPGH WSSAGCETVR RETQTSCFCN HLTYFAVLMV SSVEVDAVHK
410 420 430 440 450
HYLSLLSYVG CVVSALACLV TIAAYLCSRV PLPCRRKPRD YTIKVHMNLL
460 470 480 490 500
LAVFLLDTSF LLSEPVALTG SEAGCRASAI FLHFSLLTCL SWMGLEGYNL
510 520 530 540 550
YRLVVEVFGT YVPGYLLKLS AMGWGFPIFL VTLVALVDVD NYGPIILAVH
560 570 580 590 600
RTPEGVIYPS MCWIRDSLVS YITNLGLFSL VFLFNMAMLA TMVVQILRLR
610 620 630 640 650
PHTQKWSHVL TLLGLSLVLG LPWALIFFSF ASGTFQLVVL YLFSIITSFQ
660 670 680 690
GFLIFIWYWS MRLQARGGPS PLKSNSDSAR LPISSGSTSS SRI
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]
CCDS73893.1. [Q9Y653-3]
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. [Q9Y653-3]
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 ]
CCDS73893.1. [Q9Y653-3 ]
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 . [Q9Y653-3 ]
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.
GeneTreei ENSGT00760000118787.
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

Bgeei Q9Y653.
CleanExi HS_GPR56.
ExpressionAtlasi Q9Y653. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 134 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