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Protein

E3 ubiquitin-protein ligase ZNRF3

Gene

ZNRF3

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

Functioni

E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone.1 Publication

Enzyme regulationi

Negatively regulated by R-spondin proteins such as RSPO1: interaction with RSPO1 induces the indirect association between ZNRF3 and LGR4, promoting membrane clearance of ZNRF3.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri293 – 33442RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • frizzled binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • canonical Wnt signaling pathway Source: Ensembl
  • negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  • negative regulation of non-canonical Wnt signaling pathway Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • stem cell proliferation Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
  • Wnt receptor catabolic process Source: UniProtKB
  • Wnt signaling pathway, planar cell polarity pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-4641263. Regulation of FZD by ubiquitination.
SIGNORiQ9ULT6.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase ZNRF3 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 203
Zinc/RING finger protein 3
Gene namesi
Name:ZNRF3
Synonyms:KIAA1133, RNF203
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:18126. ZNRF3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini56 – 219164ExtracellularSequence analysisAdd
BLAST
Transmembranei220 – 24021HelicalSequence analysisAdd
BLAST
Topological domaini241 – 936696CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031P → A: Abolishes interaction with RSPO1 and prevents subsequent membrane clearance. 1 Publication

Organism-specific databases

PharmGKBiPA134983897.

Polymorphism and mutation databases

BioMutaiZNRF3.
DMDMi126253847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5555Sequence analysisAdd
BLAST
Chaini56 – 936881E3 ubiquitin-protein ligase ZNRF3PRO_0000277806Add
BLAST

Proteomic databases

EPDiQ9ULT6.
PaxDbiQ9ULT6.
PeptideAtlasiQ9ULT6.
PRIDEiQ9ULT6.

PTM databases

iPTMnetiQ9ULT6.
PhosphoSiteiQ9ULT6.

Expressioni

Gene expression databases

BgeeiQ9ULT6.
CleanExiHS_ZNRF3.
ExpressionAtlasiQ9ULT6. baseline and differential.
GenevisibleiQ9ULT6. HS.

Organism-specific databases

HPAiHPA036703.

Interactioni

Subunit structurei

Interacts with LRP6, FZD4, FZD5, FZD6 and FZD8. Interacts with RSPO1; interaction promotes indirect interaction with LGR4 and membrane clearance of ZNRF3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RSPO1Q2MKA73EBI-949772,EBI-10045219

GO - Molecular functioni

  • frizzled binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123905. 11 interactions.
DIPiDIP-50030N.
IntActiQ9ULT6. 4 interactions.
MINTiMINT-2877014.
STRINGi9606.ENSP00000443824.

Structurei

3D structure databases

ProteinModelPortaliQ9ULT6.
SMRiQ9ULT6. Positions 56-207, 292-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ZNRF3 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri293 – 33442RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000155811.
HOVERGENiHBG082538.
InParanoidiQ9ULT6.
KOiK16273.
OMAiCYTEDYS.
OrthoDBiEOG7P5T06.
PhylomeDBiQ9ULT6.
TreeFamiTF317074.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ULT6-1) [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
MRPRSGGRPG ATGRRRRRLR RRPRGLRCSR LPPPPPLPLL LGLLLAAAGP
60 70 80 90 100
GAARAKETAF VEVVLFESSP SGDYTTYTTG LTGRFSRAGA TLSAEGEIVQ
110 120 130 140 150
MHPLGLCNNN DEEDLYEYGW VGVVKLEQPE LDPKPCLTVL GKAKRAVQRG
160 170 180 190 200
ATAVIFDVSE NPEAIDQLNQ GSEDPLKRPV VYVKGADAIK LMNIVNKQKV
210 220 230 240 250
ARARIQHRPP RQPTEYFDMG IFLAFFVVVS LVCLILLVKI KLKQRRSQNS
260 270 280 290 300
MNRLAVQALE KMETRKFNSK SKGRREGSCG ALDTLSSSST SDCAICLEKY
310 320 330 340 350
IDGEELRVIP CTHRFHRKCV DPWLLQHHTC PHCRHNIIEQ KGNPSAVCVE
360 370 380 390 400
TSNLSRGRQQ RVTLPVHYPG RVHRTNAIPA YPTRTSMDSH GNPVTLLTMD
410 420 430 440 450
RHGEQSLYSP QTPAYIRSYP PLHLDHSLAA HRCGLEHRAY SPAHPFRRPK
460 470 480 490 500
LSGRSFSKAA CFSQYETMYQ HYYFQGLSYP EQEGQSPPSL APRGPARAFP
510 520 530 540 550
PSGSGSLLFP TVVHVAPPSH LESGSTSSFS CYHGHRSVCS GYLADCPGSD
560 570 580 590 600
SSSSSSSGQC HCSSSDSVVD CTEVSNQGVY GSCSTFRSSL SSDYDPFIYR
610 620 630 640 650
SRSPCRASEA GGSGSSGRGP ALCFEGSPPP EELPAVHSHG AGRGEPWPGP
660 670 680 690 700
ASPSGDQVST CSLEMNYSSN SSLEHRGPNS STSEVGLEAS PGAAPDLRRT
710 720 730 740 750
WKGGHELPSC ACCCEPQPSP AGPSAGAAGS STLFLGPHLY EGSGPAGGEP
760 770 780 790 800
QSGSSQGLYG LHPDHLPRTD GVKYEGLPCC FYEEKQVARG GGGGSGCYTE
810 820 830 840 850
DYSVSVQYTL TEEPPPGCYP GARDLSQRIP IIPEDVDCDL GLPSDCQGTH
860 870 880 890 900
SLGSWGGTRG PDTPRPHRGL GATREEERAL CCQARALLRP GCPPEEAGAV
910 920 930
RANFPSALQD TQESSTTATE AAGPRSHSAD SSSPGA
Length:936
Mass (Da):100,574
Last modified:February 20, 2007 - v3
Checksum:iEE68B810BD3C9C74
GO
Isoform 2 (identifier: Q9ULT6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Note: No experimental confirmation available.
Show »
Length:836
Mass (Da):89,908
Checksum:iFFA1207940602B17
GO

Sequence cautioni

The sequence CAG30283.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. CuratedVSP_044043Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096397 mRNA. Translation: BAG53280.1.
Z95113, AL021393 Genomic DNA. Translation: CAI17901.1.
AL021393, Z95113 Genomic DNA. Translation: CAI17992.1.
AL031596 Genomic DNA. No translation available.
AB051436 mRNA. Translation: BAB33319.1.
CR456397 mRNA. Translation: CAG30283.1. Different initiation.
BC021570 mRNA. Translation: AAH21570.1.
BC069019 mRNA. Translation: AAH69019.1.
BC094857 mRNA. Translation: AAH94857.1.
CCDSiCCDS42999.1. [Q9ULT6-2]
CCDS56225.1. [Q9ULT6-1]
RefSeqiNP_001193927.1. NM_001206998.1. [Q9ULT6-1]
NP_115549.2. NM_032173.3. [Q9ULT6-2]
XP_005261830.1. XM_005261773.2. [Q9ULT6-2]
XP_011528742.1. XM_011530440.1. [Q9ULT6-2]
XP_011528743.1. XM_011530441.1. [Q9ULT6-2]
UniGeneiHs.604200.
Hs.655242.
Hs.732114.

Genome annotation databases

EnsembliENST00000402174; ENSP00000384456; ENSG00000183579. [Q9ULT6-2]
ENST00000406323; ENSP00000384553; ENSG00000183579. [Q9ULT6-2]
ENST00000544604; ENSP00000443824; ENSG00000183579. [Q9ULT6-1]
GeneIDi84133.
KEGGihsa:84133.
UCSCiuc003aeg.4. human. [Q9ULT6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096397 mRNA. Translation: BAG53280.1.
Z95113, AL021393 Genomic DNA. Translation: CAI17901.1.
AL021393, Z95113 Genomic DNA. Translation: CAI17992.1.
AL031596 Genomic DNA. No translation available.
AB051436 mRNA. Translation: BAB33319.1.
CR456397 mRNA. Translation: CAG30283.1. Different initiation.
BC021570 mRNA. Translation: AAH21570.1.
BC069019 mRNA. Translation: AAH69019.1.
BC094857 mRNA. Translation: AAH94857.1.
CCDSiCCDS42999.1. [Q9ULT6-2]
CCDS56225.1. [Q9ULT6-1]
RefSeqiNP_001193927.1. NM_001206998.1. [Q9ULT6-1]
NP_115549.2. NM_032173.3. [Q9ULT6-2]
XP_005261830.1. XM_005261773.2. [Q9ULT6-2]
XP_011528742.1. XM_011530440.1. [Q9ULT6-2]
XP_011528743.1. XM_011530441.1. [Q9ULT6-2]
UniGeneiHs.604200.
Hs.655242.
Hs.732114.

3D structure databases

ProteinModelPortaliQ9ULT6.
SMRiQ9ULT6. Positions 56-207, 292-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123905. 11 interactions.
DIPiDIP-50030N.
IntActiQ9ULT6. 4 interactions.
MINTiMINT-2877014.
STRINGi9606.ENSP00000443824.

PTM databases

iPTMnetiQ9ULT6.
PhosphoSiteiQ9ULT6.

Polymorphism and mutation databases

BioMutaiZNRF3.
DMDMi126253847.

Proteomic databases

EPDiQ9ULT6.
PaxDbiQ9ULT6.
PeptideAtlasiQ9ULT6.
PRIDEiQ9ULT6.

Protocols and materials databases

DNASUi84133.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000402174; ENSP00000384456; ENSG00000183579. [Q9ULT6-2]
ENST00000406323; ENSP00000384553; ENSG00000183579. [Q9ULT6-2]
ENST00000544604; ENSP00000443824; ENSG00000183579. [Q9ULT6-1]
GeneIDi84133.
KEGGihsa:84133.
UCSCiuc003aeg.4. human. [Q9ULT6-1]

Organism-specific databases

CTDi84133.
GeneCardsiZNRF3.
HGNCiHGNC:18126. ZNRF3.
HPAiHPA036703.
MIMi612062. gene.
neXtProtiNX_Q9ULT6.
PharmGKBiPA134983897.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000155811.
HOVERGENiHBG082538.
InParanoidiQ9ULT6.
KOiK16273.
OMAiCYTEDYS.
OrthoDBiEOG7P5T06.
PhylomeDBiQ9ULT6.
TreeFamiTF317074.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-4641263. Regulation of FZD by ubiquitination.
SIGNORiQ9ULT6.

Miscellaneous databases

ChiTaRSiZNRF3. human.
GenomeRNAii84133.
PROiQ9ULT6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULT6.
CleanExiHS_ZNRF3.
ExpressionAtlasiQ9ULT6. baseline and differential.
GenevisibleiQ9ULT6. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-936 (ISOFORM 1).
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 77-936 (ISOFORM 1).
  6. "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] OF 284-936.
    Tissue: Brain and Muscle.
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH FZD4; FZD5; FZD6; FZD8; LRP6 AND RSPO1, MUTAGENESIS OF PRO-103.

Entry informationi

Entry nameiZNRF3_HUMAN
AccessioniPrimary (citable) accession number: Q9ULT6
Secondary accession number(s): B3KU18
, Q6ICH1, Q6NTF8, Q8WU18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: July 6, 2016
This is version 119 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.