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Q2MKA7

- RSPO1_HUMAN

UniProt

Q2MKA7 - RSPO1_HUMAN

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Protein

R-spondin-1

Gene

RSPO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.8 Publications

GO - Molecular functioni

  1. G-protein coupled receptor binding Source: UniProt
  2. heparin binding Source: UniProtKB-KW
  3. receptor binding Source: UniProtKB

GO - Biological processi

  1. canonical Wnt signaling pathway Source: Ensembl
  2. male meiosis Source: Ensembl
  3. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  4. positive regulation of non-canonical Wnt signaling pathway Source: Ensembl
  5. positive regulation of protein phosphorylation Source: UniProt
  6. positive regulation of Wnt signaling pathway Source: UniProtKB
  7. regulation of gene expression Source: Ensembl
  8. regulation of male germ cell proliferation Source: Ensembl
  9. regulation of receptor internalization Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Wnt signaling pathway

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_200716. regulation of FZD by ubiquitination.

Names & Taxonomyi

Protein namesi
Recommended name:
R-spondin-1
Alternative name(s):
Roof plate-specific spondin-1
Short name:
hRspo1
Gene namesi
Name:RSPO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:21679. RSPO1.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661R → A: Strongly reduces activation of Wnt signaling. 1 Publication
Mutagenesisi66 – 661R → W: Reduces activation of Wnt signaling. 1 Publication
Mutagenesisi70 – 701R → C or E: Strongly reduces activation of Wnt signaling. 1 Publication
Mutagenesisi71 – 711Q → E: No effect on activation of Wnt signaling. 1 Publication
Mutagenesisi71 – 711Q → R: Strongly reduces activation of Wnt signaling. 1 Publication
Mutagenesisi73 – 731G → E or R: Strongly reduces activation of Wnt signaling. 1 Publication
Mutagenesisi87 – 871R → A: Nearly abolishes activation of Wnt signaling. 2 Publications
Mutagenesisi106 – 1061F → A: Abolishes activation of Wnt signaling. Abolishes LGR4 binding. 2 Publications
Mutagenesisi106 – 1061F → E: Abolishes activation of Wnt signaling. 2 Publications
Mutagenesisi110 – 1101F → A: Nearly abolishes activation of Wnt signaling. 2 Publications
Mutagenesisi110 – 1101F → E: Abolishes activation of Wnt signaling. 2 Publications
Mutagenesisi122 – 1221K → A: Strongly reduces affinity for LGR4. 1 Publication
Mutagenesisi124 – 1241R → A: Strongly reduces affinity for LGR4. 1 Publication

Keywords - Diseasei

Palmoplantar keratoderma

Organism-specific databases

MIMi610644. phenotype.
Orphaneti85112. Palmoplantar keratoderma - XX sex reversal - predisposition to squamous cell carcinoma.
PharmGKBiPA142670967.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 263243R-spondin-1PRO_0000234436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 47
Disulfide bondi44 ↔ 53
Disulfide bondi56 ↔ 75
Disulfide bondi79 ↔ 94
Disulfide bondi97 ↔ 105
Disulfide bondi102 ↔ 111
Disulfide bondi114 ↔ 125
Disulfide bondi129 ↔ 142
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi148 ↔ 190PROSITE-ProRule annotation
Disulfide bondi159 ↔ 166PROSITE-ProRule annotation
Disulfide bondi199 ↔ 206PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ2MKA7.
PRIDEiQ2MKA7.

PTM databases

PhosphoSiteiQ2MKA7.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ2MKA7.
CleanExiHS_RSPO1.
GenevestigatoriQ2MKA7.

Organism-specific databases

HPAiHPA046154.

Interactioni

Subunit structurei

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.By similarity8 Publications

Protein-protein interaction databases

BioGridi129926. 16 interactions.
DIPiDIP-59895N.
STRINGi9606.ENSP00000348944.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 485
Turni49 – 513
Beta strandi52 – 565
Beta strandi60 – 678
Beta strandi70 – 789
Beta strandi83 – 875
Beta strandi92 – 965
Beta strandi102 – 1076
Beta strandi110 – 1145
Beta strandi119 – 1213
Beta strandi124 – 1263
Turni131 – 1344
Beta strandi136 – 1416

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ2MKA7.
SMRiQ2MKA7. Positions 40-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati34 – 8552FU 1Add
BLAST
Repeati91 – 13545FU 2Add
BLAST
Domaini147 – 20761TSP type-1PROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the R-spondin family.Curated
Contains 2 FU (furin-like) repeats.Curated
Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG311831.
GeneTreeiENSGT00390000011447.
HOGENOMiHOG000290668.
HOVERGENiHBG082751.
InParanoidiQ2MKA7.
OMAiIEHCEAC.
OrthoDBiEOG7X9G7G.
PhylomeDBiQ2MKA7.
TreeFamiTF331799.

Family and domain databases

InterProiIPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF00090. TSP_1. 1 hit.
[Graphical view]
SMARTiSM00261. FU. 2 hits.
SM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEiPS50092. TSP1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q2MKA7) [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
MRLGLCVVAL VLSWTHLTIS SRGIKGKRQR RISAEGSQAC AKGCELCSEV
60 70 80 90 100
NGCLKCSPKL FILLERNDIR QVGVCLPSCP PGYFDARNPD MNKCIKCKIE
110 120 130 140 150
HCEACFSHNF CTKCKEGLYL HKGRCYPACP EGSSAANGTM ECSSPAQCEM
160 170 180 190 200
SEWSPWGPCS KKQQLCGFRR GSEERTRRVL HAPVGDHAAC SDTKETRRCT
210 220 230 240 250
VRRVPCPEGQ KRRKGGQGRR ENANRNLARK ESKEAGAGSR RRKGQQQQQQ
260
QGTVGPLTSA GPA
Length:263
Mass (Da):28,959
Last modified:February 7, 2006 - v1
Checksum:i43794A881B1C0278
GO
Isoform 2 (identifier: Q2MKA7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MRLGLCVVALVLSWTHLTISSRGIKGKRQRRI → MIFRV

Note: No experimental confirmation available.

Show »
Length:236
Mass (Da):25,975
Checksum:i8D08802127EC5668
GO
Isoform 3 (identifier: Q2MKA7-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:200
Mass (Da):21,775
Checksum:iD55BBB18F4F86924
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501M → V in BAC05263. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232MRLGL…RQRRI → MIFRV in isoform 2. 1 PublicationVSP_018320Add
BLAST
Alternative sequencei146 – 20863Missing in isoform 3. 1 PublicationVSP_043265Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41304.1. [Q2MKA7-1]
CCDS55590.1. [Q2MKA7-3]
CCDS55591.1. [Q2MKA7-2]
RefSeqiNP_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]
UniGeneiHs.135015.

Genome annotation databases

EnsembliENST00000356545; ENSP00000348944; ENSG00000169218. [Q2MKA7-1]
ENST00000401068; ENSP00000383846; ENSG00000169218. [Q2MKA7-1]
ENST00000612451; ENSP00000479832; ENSG00000169218. [Q2MKA7-3]
ENST00000615459; ENSP00000481178; ENSG00000169218. [Q2MKA7-2]
GeneIDi284654.
KEGGihsa:284654.
UCSCiuc001cbl.2. human. [Q2MKA7-1]
uc009vvf.2. human. [Q2MKA7-2]
uc009vvg.2. human. [Q2MKA7-3]

Polymorphism databases

DMDMi97189599.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS41304.1. [Q2MKA7-1 ]
CCDS55590.1. [Q2MKA7-3 ]
CCDS55591.1. [Q2MKA7-2 ]
RefSeqi NP_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 ]
UniGenei Hs.135015.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BSO X-ray 2.20 A 31-146 [» ]
4BSP X-ray 2.00 A 31-146 [» ]
4BSR X-ray 3.20 C/D 31-146 [» ]
4BSS X-ray 3.20 C/D/G/H 31-146 [» ]
4BST X-ray 4.30 C/D 31-146 [» ]
4BSU X-ray 3.20 C/D/G/H 31-146 [» ]
4CDK X-ray 2.80 E/F/G/H 31-145 [» ]
4KNG X-ray 2.50 M/P 35-144 [» ]
4KT1 X-ray 2.50 E 39-128 [» ]
4LI2 X-ray 3.19 B 33-144 [» ]
ProteinModelPortali Q2MKA7.
SMRi Q2MKA7. Positions 40-127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 129926. 16 interactions.
DIPi DIP-59895N.
STRINGi 9606.ENSP00000348944.

PTM databases

PhosphoSitei Q2MKA7.

Polymorphism databases

DMDMi 97189599.

Proteomic databases

PaxDbi Q2MKA7.
PRIDEi Q2MKA7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356545 ; ENSP00000348944 ; ENSG00000169218 . [Q2MKA7-1 ]
ENST00000401068 ; ENSP00000383846 ; ENSG00000169218 . [Q2MKA7-1 ]
ENST00000612451 ; ENSP00000479832 ; ENSG00000169218 . [Q2MKA7-3 ]
ENST00000615459 ; ENSP00000481178 ; ENSG00000169218 . [Q2MKA7-2 ]
GeneIDi 284654.
KEGGi hsa:284654.
UCSCi uc001cbl.2. human. [Q2MKA7-1 ]
uc009vvf.2. human. [Q2MKA7-2 ]
uc009vvg.2. human. [Q2MKA7-3 ]

Organism-specific databases

CTDi 284654.
GeneCardsi GC01M038076.
HGNCi HGNC:21679. RSPO1.
HPAi HPA046154.
MIMi 609595. gene.
610644. phenotype.
neXtProti NX_Q2MKA7.
Orphaneti 85112. Palmoplantar keratoderma - XX sex reversal - predisposition to squamous cell carcinoma.
PharmGKBi PA142670967.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG311831.
GeneTreei ENSGT00390000011447.
HOGENOMi HOG000290668.
HOVERGENi HBG082751.
InParanoidi Q2MKA7.
OMAi IEHCEAC.
OrthoDBi EOG7X9G7G.
PhylomeDBi Q2MKA7.
TreeFami TF331799.

Enzyme and pathway databases

Reactomei REACT_200716. regulation of FZD by ubiquitination.

Miscellaneous databases

ChiTaRSi RSPO1. human.
GeneWikii RSPO1.
GenomeRNAii 284654.
NextBioi 95027.
PROi Q2MKA7.
SOURCEi Search...

Gene expression databases

Bgeei Q2MKA7.
CleanExi HS_RSPO1.
Genevestigatori Q2MKA7.

Family and domain databases

InterProi IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF00090. TSP_1. 1 hit.
[Graphical view ]
SMARTi SM00261. FU. 2 hits.
SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEi PS50092. TSP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiRSPO1_HUMAN
AccessioniPrimary (citable) accession number: Q2MKA7
Secondary accession number(s): A2A420
, Q0H8S6, Q14C72, Q5T0F2, Q8N7L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 7, 2006
Last modified: October 29, 2014
This is version 82 of the entry and version 1 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

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3