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Protein

E3 ubiquitin-protein ligase ZNRF2

Gene

ZNRF2

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

Functioni

May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.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 fingeri199 – 24042RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase ZNRF2 (EC:6.3.2.-)
Alternative name(s):
Protein Ells2
RING finger protein 202
Zinc/RING finger protein 2
Gene namesi
Name:ZNRF2
Synonyms:RNF202
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:22316. ZNRF2.

Subcellular locationi

  • Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Lysosome membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Cell junctionsynapsepresynaptic cell membrane 1 Publication; Peripheral membrane protein 1 Publication

  • Note: Present in presynaptic plasma membranes in neurons.

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: MGI
  • cytoplasmic vesicle membrane Source: MGI
  • endosome membrane Source: UniProtKB-SubCell
  • lysosomal membrane Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • presynaptic membrane Source: UniProtKB-SubCell
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endosome, Lysosome, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134961488.

Polymorphism and mutation databases

BioMutaiZNRF2.
DMDMi74762595.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 242241E3 ubiquitin-protein ligase ZNRF2PRO_0000277803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei25 – 251PhosphoserineBy similarity
Modified residuei82 – 821PhosphoserineCombined sources
Modified residuei89 – 891PhosphoserineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineCombined sources
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei145 – 1451PhosphoserineBy similarity
Modified residuei151 – 1511PhosphoserineCombined sources

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ8NHG8.
MaxQBiQ8NHG8.
PaxDbiQ8NHG8.
PeptideAtlasiQ8NHG8.
PRIDEiQ8NHG8.

PTM databases

iPTMnetiQ8NHG8.
PhosphoSiteiQ8NHG8.

Expressioni

Tissue specificityi

Highly expressed in the brain, with higher expression during development than in adult. Expressed also in mammary glands, testis, colon and kidney.1 Publication

Gene expression databases

BgeeiQ8NHG8.
CleanExiHS_ZNRF2.
ExpressionAtlasiQ8NHG8. baseline and differential.
GenevisibleiQ8NHG8. HS.

Interactioni

Subunit structurei

Interacts with UBE2N.1 Publication

Protein-protein interaction databases

BioGridi128825. 15 interactions.
IntActiQ8NHG8. 3 interactions.
MINTiMINT-7997475.
STRINGi9606.ENSP00000323879.

Structurei

3D structure databases

ProteinModelPortaliQ8NHG8.
SMRiQ8NHG8. Positions 198-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 405Poly-Gly
Compositional biasi41 – 9757Ala-richAdd
BLAST
Compositional biasi124 – 1274Poly-Gly

Domaini

The RING-type zinc finger domain is required for E3 ligase activity.By similarity

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri199 – 24042RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0801. Eukaryota.
ENOG4111V18. LUCA.
GeneTreeiENSGT00390000013068.
HOGENOMiHOG000285998.
HOVERGENiHBG094200.
InParanoidiQ8NHG8.
KOiK10694.
OMAiPGAHQPS.
OrthoDBiEOG70W3FG.
PhylomeDBiQ8NHG8.
TreeFamiTF317681.

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]

Sequencei

Sequence statusi: Complete.

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

Q8NHG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAKQSGPAA ANGRTRAYSG SDLPSSSSGG ANGTAGGGGG ARAAAAGRFP
60 70 80 90 100
AQVPSAHQPS ASGGAAAAAA APAAPAAPRS RSLGGAVGSV ASGARAAQSP
110 120 130 140 150
FSIPNSSSGP YGSQDSVHSS PEDGGGGRDR PVGGSPGGPR LVIGSLPAHL
160 170 180 190 200
SPHMFGGFKC PVCSKFVSSD EMDLHLVMCL TKPRITYNED VLSKDAGECA
210 220 230 240
ICLEELQQGD TIARLPCLCI YHKGCIDEWF EVNRSCPEHP SD
Length:242
Mass (Da):24,115
Last modified:October 1, 2002 - v1
Checksum:iD02776578A1E9E55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF513707 mRNA. Translation: AAQ08115.1.
AF527533 mRNA. Translation: AAM88868.1.
CCDSiCCDS5426.1.
RefSeqiNP_667339.1. NM_147128.3.
XP_011513519.1. XM_011515217.1.
UniGeneiHs.263912.

Genome annotation databases

EnsembliENST00000323037; ENSP00000323879; ENSG00000180233.
GeneIDi223082.
KEGGihsa:223082.
UCSCiuc003tat.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF513707 mRNA. Translation: AAQ08115.1.
AF527533 mRNA. Translation: AAM88868.1.
CCDSiCCDS5426.1.
RefSeqiNP_667339.1. NM_147128.3.
XP_011513519.1. XM_011515217.1.
UniGeneiHs.263912.

3D structure databases

ProteinModelPortaliQ8NHG8.
SMRiQ8NHG8. Positions 198-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128825. 15 interactions.
IntActiQ8NHG8. 3 interactions.
MINTiMINT-7997475.
STRINGi9606.ENSP00000323879.

PTM databases

iPTMnetiQ8NHG8.
PhosphoSiteiQ8NHG8.

Polymorphism and mutation databases

BioMutaiZNRF2.
DMDMi74762595.

Proteomic databases

EPDiQ8NHG8.
MaxQBiQ8NHG8.
PaxDbiQ8NHG8.
PeptideAtlasiQ8NHG8.
PRIDEiQ8NHG8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323037; ENSP00000323879; ENSG00000180233.
GeneIDi223082.
KEGGihsa:223082.
UCSCiuc003tat.3. human.

Organism-specific databases

CTDi223082.
GeneCardsiZNRF2.
H-InvDBHIX0022149.
HGNCiHGNC:22316. ZNRF2.
MIMi612061. gene.
neXtProtiNX_Q8NHG8.
PharmGKBiPA134961488.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0801. Eukaryota.
ENOG4111V18. LUCA.
GeneTreeiENSGT00390000013068.
HOGENOMiHOG000285998.
HOVERGENiHBG094200.
InParanoidiQ8NHG8.
KOiK10694.
OMAiPGAHQPS.
OrthoDBiEOG70W3FG.
PhylomeDBiQ8NHG8.
TreeFamiTF317681.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GenomeRNAii223082.
NextBioi91710.
PROiQ8NHG8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NHG8.
CleanExiHS_ZNRF2.
ExpressionAtlasiQ8NHG8. baseline and differential.
GenevisibleiQ8NHG8. 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. "ZNRF proteins constitute a family of presynaptic E3 ubiquitin ligases."
    Araki T., Milbrandt J.
    J. Neurosci. 23:9385-9394(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. Guo J.H., Yu L.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation."
    Plans V., Scheper J., Soler M., Loukili N., Okano Y., Thomson T.M.
    J. Cell. Biochem. 97:572-582(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2N.
  5. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-113 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89 AND SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiZNRF2_HUMAN
AccessioniPrimary (citable) accession number: Q8NHG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 115 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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.