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Q8K209

- GPR56_MOUSE

UniProt

Q8K209 - GPR56_MOUSE

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Protein

G-protein coupled receptor 56

Gene

Gpr56

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Enzyme regulationi

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. cell adhesion Source: UniProtKB-KW
  3. cerebral cortex radial glia guided migration Source: UniProtKB
  4. layer formation in cerebral cortex Source: UniProtKB
  5. negative regulation of cell proliferation Source: UniProtKB
  6. negative regulation of neuron migration Source: UniProtKB
  7. neuropeptide signaling pathway Source: InterPro
  8. positive regulation of cell adhesion Source: UniProtKB
  9. positive regulation of Rho protein signal transduction Source: UniProtKB
  10. protein kinase C signaling Source: UniProtKB
  11. Rho protein signal transduction Source: UniProtKB
  12. vascular endothelial growth factor production Source: UniProtKB
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):
Serpentine receptor cyt28
Cleaved into the following 2 chains:
GPR56 N-terminal fragment
Short name:
GPR56 NT
Short name:
GPR56(N)
Alternative name(s):
GPR56 extracellular subunit
GPR56 subunit alpha
GPR56 C-terminal fragment
Short name:
GPR56 CT
Short name:
GPR56(C)
Alternative name(s):
GPR56 seven-transmembrane subunit
Short name:
GPR56 7TM
GPR56 subunit beta
Gene namesi
Name:Gpr56
Synonyms:Cyt28
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1340051. Gpr56.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 402377ExtracellularSequence AnalysisAdd
BLAST
Transmembranei403 – 42321Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini424 – 44219CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei443 – 46321Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini464 – 4718ExtracellularSequence Analysis
Transmembranei472 – 49221Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini493 – 51220CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei513 – 53321Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini534 – 57037ExtracellularSequence AnalysisAdd
BLAST
Transmembranei571 – 59121Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini592 – 60312CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei604 – 62421Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini625 – 6306ExtracellularSequence Analysis
Transmembranei631 – 65121Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini652 – 68736CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. glial limiting end-foot Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8K209.
PaxDbiQ8K209.
PRIDEiQ8K209.

PTM databases

PhosphoSiteiQ8K209.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8K209.
CleanExiMM_GPR56.
GenevestigatoriQ8K209.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ8K209. 1 interaction.
STRINGi10090.ENSMUSP00000090959.

Structurei

3D structure databases

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

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

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q8K209-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVQVLRQMV YFLLSLFSLV QGAHSGSPRE DFRFCGQRNQ TQQSTLHYDQ
60 70 80 90 100
SSEPHIFVWN TEETLTIRAP FLAAPDIPRF FPEPRGLYHF CLYWSRHTGR
110 120 130 140 150
LHLRYGKHDY LLSSQASRLL CFQKQEQSLK QGAPLIATSV SSWQIPQNTS
160 170 180 190 200
LPGAPSFIFS FHNAPHKVSH NASVDMCDLK KELQQLSRYL QHPQKAAKRP
210 220 230 240 250
TAAFISQQLQ SLESKLTSVS FLGDTLSFEE DRVNATVWKL PPTAGLEDLH
260 270 280 290 300
IHSQKEEEQS EVQAYSLLLP RAVFQQTRGR RRDDAKRLLV VDFSSQALFQ
310 320 330 340 350
DKNSSQVLGE KVLGIVVQNT KVTNLSDPVV LTFQHQPQPK NVTLQCVFWV
360 370 380 390 400
EDPASSSTGS WSSAGCETVS RDTQTSCLCN HLTYFAVLMV SSTEVEATHK
410 420 430 440 450
HYLTLLSYVG CVISALACVF TIAAYLCSRR KSRDYTIKVH MNLLSAVFLL
460 470 480 490 500
DVSFLLSEPV ALTGSEAACR TSAMFLHFSL LACLSWMGLE GYNLYRLVVE
510 520 530 540 550
VFGTYVPGYL LKLSIVGWGF PVFLVTLVAL VDVNNYGPII LAVRRTPERV
560 570 580 590 600
TYPSMCWIRD SLVSYVTNLG LFSLVFLFNL AMLATMVVQI LRLRPHSQNW
610 620 630 640 650
PHVLTLLGLS LVLGLPWALV FFSFASGTFQ LVILYLFSII TSFQGFLIFL
660 670 680
WYWSMRFQAQ GGPSPLKNNS DSAKLPISSG STSSSRI
Length:687
Mass (Da):77,255
Last modified:October 1, 2002 - v1
Checksum:iB5315D70B66C9A9A
GO

Experimental Info

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

Sequence databases

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

Genome annotation databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

IntActi Q8K209. 1 interaction.
STRINGi 10090.ENSMUSP00000090959.

Protein family/group databases

MEROPSi S63.011.
GPCRDBi Search...

PTM databases

PhosphoSitei Q8K209.

Proteomic databases

MaxQBi Q8K209.
PaxDbi Q8K209.
PRIDEi Q8K209.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 9289.
MGIi MGI:1340051. Gpr56.

Phylogenomic databases

eggNOGi NOG290113.
GeneTreei ENSGT00760000118787.
HOGENOMi HOG000015136.
HOVERGENi HBG051814.
InParanoidi Q8K209.
KOi K08450.
OMAi WGFPIFL.
OrthoDBi EOG7XPZ55.
PhylomeDBi Q8K209.
TreeFami TF321769.

Miscellaneous databases

ChiTaRSi Gpr56. mouse.
NextBioi 286855.
PROi Q8K209.
SOURCEi Search...

Gene expression databases

Bgeei Q8K209.
CleanExi MM_GPR56.
Genevestigatori Q8K209.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel hematopoietic stem cell regulatory genes."
    Phillips R.L., Ernst R.E., Dosil M., Wesley C.K., Moore K.A., Kingsley P.D., Sykes S., Palis J., Lemischka I.R.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung, Pituitary, Placenta and Spinal ganglion.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Disease-associated mutations affect GPR56 protein trafficking and cell surface expression."
    Jin Z., Tietjen I., Bu L., Liu-Yesucevitz L., Gaur S.K., Walsh C.A., Piao X.
    Hum. Mol. Genet. 16:1972-1985(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ARG-38; ASN-39; TYR-88; CYS-91; ASN-148; ASN-171; ASN-234; ASN-303; ASN-324 AND ASN-341, MUTAGENESIS OF CYS-346 AND TRP-349.
  5. "GPR56 regulates pial basement membrane integrity and cortical lamination."
    Li S., Jin Z., Koirala S., Bu L., Xu L., Hynes R.O., Walsh C.A., Corfas G., Piao X.
    J. Neurosci. 28:5817-5826(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a G alpha 12/13 and Rho pathway."
    Iguchi T., Sakata K., Yoshizaki K., Tago K., Mizuno N., Itoh H.
    J. Biol. Chem. 283:14469-14478(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "GPR56-regulated granule cell adhesion is essential for rostral cerebellar development."
    Koirala S., Jin Z., Piao X., Corfas G.
    J. Neurosci. 29:7439-7449(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AND DISRUPTION PHENOTYPE.
  8. "G protein-coupled receptor 56 and collagen III, a receptor-ligand pair, regulates cortical development and lamination."
    Luo R., Jeong S.J., Jin Z., Strokes N., Li S., Piao X.
    Proc. Natl. Acad. Sci. U.S.A. 108:12925-12930(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, LIGAND-BINDING.
  9. "Disease-associated mutations prevent GPR56-collagen III interaction."
    Luo R., Jin Z., Deng Y., Strokes N., Piao X.
    PLoS ONE 7:E29818-E29818(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIGAND-BINDING, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-38; TYR-88 AND CYS-91.
  10. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiGPR56_MOUSE
AccessioniPrimary (citable) accession number: Q8K209
Secondary accession number(s): Q3UR17, Q9QZT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3