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Q2MKA7 (RSPO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
R-spondin-1
Alternative name(s):
Roof plate-specific spondin-1
Short name=hRspo1
Gene names
Name:RSPO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Interacts with the extracellular domain of FZD8 and LRP6. It however does not form a ternary complex with FZD8 and LRP6. Interacts with WNT1. Binds heparin By similarity. Interacts with ZNRF3; promoting indirect interaction between ZNRF3 and LGR4 and membrane clearance of ZNRF3. Interacts with LGR4, LGR5 and LGR6. Identified in a complex composed of RNF43, LGR5 and RSPO1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Secreted By similarity.

Tissue specificity

Abundantly expressed in adrenal glands, ovary, testis, thyroid and trachea but not in bone marrow, spinal cord, stomach, leukocytes colon, small intestine, prostate, thymus and spleen. Ref.2

Domain

The FU repeats are required for activation and stabilization of beta-catenin By similarity.

Involvement in disease

Keratoderma, palmoplantar, with squamous cell carcinoma of skin and sex reversal (PKKSCC) [MIM:610644]: A recessive syndrome characterized by XX (female to male) SRY-independent sex reversal, palmoplantar hyperkeratosis and predisposition to squamous cell carcinoma of the skin.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Miscellaneous

Upon injection into mice, it induces rapid onset of crypt cell proliferation involving beta-catenin stabilization. It also displays efficacy in a model of chemotherapy-induced intestinal mucositis suggesting possible therapeutic application in gastrointestinal diseases.

Sequence similarities

Belongs to the R-spondin family.

Contains 2 FU (furin-like) repeats.

Contains 1 TSP type-1 domain.

Ontologies

Keywords
   Biological processSensory transduction
Wnt signaling pathway
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DiseasePalmoplantar keratoderma
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcanonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

male meiosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of Wnt signaling pathway

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of canonical Wnt signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of non-canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from direct assay Ref.9. Source: UniProt

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

regulation of male germ cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of receptor internalization

Inferred from direct assay PubMed 17804805. Source: BHF-UCL

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-protein coupled receptor binding

Inferred from physical interaction Ref.8. Source: UniProt

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.6Ref.10. Source: UniProtKB

receptor binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q2MKA7-1)

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: Q2MKA7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MRLGLCVVALVLSWTHLTISSRGIKGKRQRRI → MIFRV
Note: No experimental confirmation available.
Isoform 3 (identifier: Q2MKA7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     146-208: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 263243R-spondin-1
PRO_0000234436

Regions

Repeat34 – 8552FU 1
Repeat91 – 13545FU 2
Domain147 – 20761TSP type-1

Amino acid modifications

Glycosylation1371N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 47 Ref.11 Ref.12 Ref.13
Disulfide bond44 ↔ 53 Ref.11 Ref.12 Ref.13
Disulfide bond56 ↔ 75 Ref.11 Ref.12 Ref.13
Disulfide bond79 ↔ 94 Ref.11 Ref.12 Ref.13
Disulfide bond97 ↔ 105 Ref.11 Ref.12 Ref.13
Disulfide bond102 ↔ 111 Ref.11 Ref.12 Ref.13
Disulfide bond114 ↔ 125 Ref.11 Ref.12 Ref.13
Disulfide bond129 ↔ 142 Ref.11 Ref.12 Ref.13
Disulfide bond148 ↔ 190 By similarity
Disulfide bond159 ↔ 166 By similarity
Disulfide bond199 ↔ 206 By similarity

Natural variations

Alternative sequence1 – 3232MRLGL…RQRRI → MIFRV in isoform 2.
VSP_018320
Alternative sequence146 – 20863Missing in isoform 3.
VSP_043265

Experimental info

Mutagenesis661R → A: Strongly reduces activation of Wnt signaling. Ref.11
Mutagenesis661R → W: Reduces activation of Wnt signaling. Ref.11
Mutagenesis701R → C or E: Strongly reduces activation of Wnt signaling. Ref.11
Mutagenesis711Q → E: No effect on activation of Wnt signaling. Ref.11
Mutagenesis711Q → R: Strongly reduces activation of Wnt signaling. Ref.11
Mutagenesis731G → E or R: Strongly reduces activation of Wnt signaling. Ref.11
Mutagenesis871R → A: Nearly abolishes activation of Wnt signaling. Ref.11 Ref.12
Mutagenesis1061F → A: Abolishes activation of Wnt signaling. Abolishes LGR4 binding. Ref.11 Ref.12
Mutagenesis1061F → E: Abolishes activation of Wnt signaling. Ref.11 Ref.12
Mutagenesis1101F → A: Nearly abolishes activation of Wnt signaling. Ref.11 Ref.12
Mutagenesis1101F → E: Abolishes activation of Wnt signaling. Ref.11 Ref.12
Mutagenesis1221K → A: Strongly reduces affinity for LGR4. Ref.12
Mutagenesis1241R → A: Strongly reduces affinity for LGR4. Ref.12
Sequence conflict1501M → V in BAC05263. Ref.3

Secondary structure

......................... 263
Helix Strand Turn

Details...

Sequences

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

Last modified February 7, 2006. Version 1.
Checksum: 43794A881B1C0278

FASTA26328,959
        10         20         30         40         50         60 
MRLGLCVVAL VLSWTHLTIS SRGIKGKRQR RISAEGSQAC AKGCELCSEV NGCLKCSPKL 

        70         80         90        100        110        120 
FILLERNDIR QVGVCLPSCP PGYFDARNPD MNKCIKCKIE HCEACFSHNF CTKCKEGLYL 

       130        140        150        160        170        180 
HKGRCYPACP EGSSAANGTM ECSSPAQCEM SEWSPWGPCS KKQQLCGFRR GSEERTRRVL 

       190        200        210        220        230        240 
HAPVGDHAAC SDTKETRRCT VRRVPCPEGQ KRRKGGQGRR ENANRNLARK ESKEAGAGSR 

       250        260 
RRKGQQQQQQ QGTVGPLTSA GPA 

« Hide

Isoform 2 [UniParc].

Checksum: 8D08802127EC5668
Show »

FASTA23625,975
Isoform 3 [UniParc].

Checksum: D55BBB18F4F86924
Show »

FASTA20021,775

References

« Hide 'large scale' references
[1]"Mitogenic influence of human R-spondin1 on the intestinal epithelium."
Kim K.-A., Kakitani M., Zhao J., Oshima T., Tang T., Binnerts M., Liu Y., Boyle B., Park E., Emtage P., Funk W.D., Tomizuka K.
Science 309:1256-1259(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]"R-spondin1 is essential in sex determination, skin differentiation and malignancy."
Parma P., Radi O., Vidal V., Chaboissier M.C., Dellambra E., Valentini S., Guerra L., Schedl A., Camerino G.
Nat. Genet. 38:1304-1309(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, INVOLVEMENT IN PALMOPLANTAR HYPERKERATOSIS WITH SQUAMOUS CELL CARCINOMA OF SKIN AND SEX REVERSAL.
[3]"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] (ISOFORM 2).
Tissue: Uterus.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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).
[6]"ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive manner."
Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H., Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R., Bouwmeester T., Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C., Cong F.
Nature 485:195-200(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZNRF3.
[7]"LGR4 and LGR5 are R-spondin receptors mediating Wnt/beta-catenin and Wnt/PCP signalling."
Glinka A., Dolde C., Kirsch N., Huang Y.L., Kazanskaya O., Ingelfinger D., Boutros M., Cruciat C.M., Niehrs C.
EMBO Rep. 12:1055-1061(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGR4 AND LGR5.
[8]"Lgr5 homologues associate with Wnt receptors and mediate R-spondin signalling."
de Lau W., Barker N., Low T.Y., Koo B.K., Li V.S., Teunissen H., Kujala P., Haegebarth A., Peters P.J., van de Wetering M., Stange D.E., van Es J.E., Guardavaccaro D., Schasfoort R.B., Mohri Y., Nishimori K., Mohammed S., Heck A.J., Clevers H.
Nature 476:293-297(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGR4; LGR5 AND LGR6.
[9]"LGR6 is a high affinity receptor of R-spondins and potentially functions as a tumor suppressor."
Gong X., Carmon K.S., Lin Q., Thomas A., Yi J., Liu Q.
PLoS ONE 7:E37137-E37137(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGR6.
[10]"R-Spondin potentiates Wnt/beta-catenin signaling through orphan receptors LGR4 and LGR5."
Ruffner H., Sprunger J., Charlat O., Leighton-Davies J., Grosshans B., Salathe A., Zietzling S., Beck V., Therier M., Isken A., Xie Y., Zhang Y., Hao H., Shi X., Liu D., Song Q., Clay I., Hintzen G. expand/collapse author list , Tchorz J., Bouchez L.C., Michaud G., Finan P., Myer V.E., Bouwmeester T., Porter J., Hild M., Bassilana F., Parker C.N., Cong F.
PLoS ONE 7:E40976-E40976(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGR4 AND LGR5.
[11]"Structure of stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5."
Peng W.C., de Lau W., Forneris F., Granneman J.C., Huch M., Clevers H., Gros P.
Cell Rep. 3:1885-1892(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-146 IN COMPLEX WITH LGR5, FUNCTION, INTERACTION WITH LGR5, MUTAGENESIS OF ARG-66; ARG-70; GLN-71; GLY-73; ARG-87; PHE-106 AND PHE-110, DISULFIDE BONDS.
[12]"Structural basis for R-spondin recognition by LGR4/5/6 receptors."
Wang D., Huang B., Zhang S., Yu X., Wu W., Wang X.
Genes Dev. 27:1339-1344(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-128 IN COMPLEX WITH LGR4, FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-87; PHE-106; PHE-110; LYS-122 AND ARG-124, DISULFIDE BONDS.
[13]"The structural basis of R-spondin recognition by LGR5 and RNF43."
Chen P.H., Chen X., Lin Z., Fang D., He X.
Genes Dev. 27:1345-1350(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 35-144 IN COMPLEX WITH LGR5 AND RNF43, SUBUNIT, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ318235 mRNA. Translation: ABC54570.1.
DQ165084 mRNA. Translation: ABA54597.1.
DQ165085 mRNA. Translation: ABA54598.1.
AK098225 mRNA. Translation: BAC05263.1.
AL513220 Genomic DNA. Translation: CAM12882.1.
AL513220 Genomic DNA. Translation: CAM12883.1.
AL513220 Genomic DNA. Translation: CAI15785.1.
BC114966 mRNA. Translation: AAI14967.1.
CCDSCCDS41304.1. [Q2MKA7-1]
CCDS55590.1. [Q2MKA7-3]
CCDS55591.1. [Q2MKA7-2]
RefSeqNP_001033722.1. NM_001038633.3. [Q2MKA7-1]
NP_001229837.1. NM_001242908.1. [Q2MKA7-1]
NP_001229838.1. NM_001242909.1. [Q2MKA7-2]
NP_001229839.1. NM_001242910.1. [Q2MKA7-3]
XP_006710646.1. XM_006710583.1. [Q2MKA7-1]
UniGeneHs.135015.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BSOX-ray2.20A31-146[»]
4BSPX-ray2.00A31-146[»]
4BSRX-ray3.20C/D31-146[»]
4BSSX-ray3.20C/D/G/H31-146[»]
4BSTX-ray4.30C/D31-146[»]
4BSUX-ray3.20C/D/G/H31-146[»]
4CDKX-ray2.80E/F/G/H31-145[»]
4KNGX-ray2.50M/P35-144[»]
4KT1X-ray2.50E39-128[»]
4LI2X-ray3.19B33-144[»]
ProteinModelPortalQ2MKA7.
SMRQ2MKA7. Positions 40-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129926. 7 interactions.
DIPDIP-59895N.
STRING9606.ENSP00000348944.

PTM databases

PhosphoSiteQ2MKA7.

Polymorphism databases

DMDM97189599.

Proteomic databases

PaxDbQ2MKA7.
PRIDEQ2MKA7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356545; ENSP00000348944; ENSG00000169218. [Q2MKA7-1]
ENST00000373059; ENSP00000362150; ENSG00000169218. [Q2MKA7-2]
ENST00000401068; ENSP00000383846; ENSG00000169218. [Q2MKA7-1]
ENST00000401069; ENSP00000383847; ENSG00000169218. [Q2MKA7-1]
ENST00000401070; ENSP00000383848; ENSG00000169218. [Q2MKA7-3]
ENST00000401071; ENSP00000383849; ENSG00000169218. [Q2MKA7-3]
GeneID284654.
KEGGhsa:284654.
UCSCuc001cbl.2. human. [Q2MKA7-1]
uc009vvf.2. human. [Q2MKA7-2]
uc009vvg.2. human. [Q2MKA7-3]

Organism-specific databases

CTD284654.
GeneCardsGC01M038076.
HGNCHGNC:21679. RSPO1.
HPAHPA046154.
MIM609595. gene.
610644. phenotype.
neXtProtNX_Q2MKA7.
Orphanet85112. Palmoplantar keratoderma - XX sex reversal - predisposition to squamous cell carcinoma.
PharmGKBPA142670967.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311831.
HOGENOMHOG000290668.
HOVERGENHBG082751.
InParanoidQ2MKA7.
OMAIEHCEAC.
OrthoDBEOG7X9G7G.
PhylomeDBQ2MKA7.
TreeFamTF331799.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeQ2MKA7.
CleanExHS_RSPO1.
GenevestigatorQ2MKA7.

Family and domain databases

InterProIPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF00090. TSP_1. 1 hit.
[Graphical view]
SMARTSM00261. FU. 2 hits.
SM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEPS50092. TSP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRSPO1. human.
GeneWikiRSPO1.
GenomeRNAi284654.
NextBio95027.
PROQ2MKA7.
SOURCESearch...

Entry information

Entry nameRSPO1_HUMAN
AccessionPrimary (citable) accession number: Q2MKA7
Secondary accession number(s): A2A420 expand/collapse secondary AC list , Q0H8S6, Q14C72, Q5T0F2, Q8N7L5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 79 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM