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Protein

E3 ubiquitin-protein ligase RNF187

Gene

RNF187

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 coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8.1 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 fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
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 RNF187 (EC:6.3.2.-)
Alternative name(s):
RING domain AP1 coactivator 1
Short name:
RACO-1
RING finger protein 187
Gene namesi
Name:RNF187
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:27146. RNF187.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Predominantly located in the cytoplasm. Shuttles between the cytoplasm and the nucleus.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → A: Loss of protein expression. 1 Publication
Mutagenesisi12 – 121C → A: Increased RNF187 stability and reduced polyubiquitination; when associated with A-15. 1 Publication
Mutagenesisi15 – 151C → A: Increased RNF187 stability and reduced polyubiquitination; when associated with A-12. 1 Publication
Mutagenesisi195 – 1951K → R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but on effect on subcellular location; when associated with R-223 and R-224.
Mutagenesisi223 – 2231K → R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but on effect on subcellular location; when associated with R-195 and R-224.
Mutagenesisi224 – 2241K → R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but on effect on subcellular location; when associated with R-195 and R-223.

Organism-specific databases

PharmGKBiPA142671058.

Polymorphism and mutation databases

DMDMi332278146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235E3 ubiquitin-protein ligase RNF187PRO_0000278241Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei109 – 1091Asymmetric dimethylarginine; by PRMT11 Publication
Cross-linki195 – 195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki223 – 223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki224 – 224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the absence of growth factors and MAP3K1-induced 'Lys-63'-linked polyubiquitination. 'Lys-48'-autoubiquitination leads to degradation by the proteasome, while MAP3K1-induced 'Lys-63'-linked polyubiquitination results in the stabilization of the protein. 'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-223 and Lys-224) and are thus mutually exclusive. Other sites of ubiquitination are not excluded.1 Publication
Arginine methylation by PRMT1 stabilizes RNF187 by facilitating K63-linked ubiquitin chain formation, and enables dimerization, c-Jun interaction and subsequent AP1 target gene expression.2 Publications

Keywords - PTMi

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

MaxQBiQ5TA31.
PaxDbiQ5TA31.
PRIDEiQ5TA31.

PTM databases

iPTMnetiQ5TA31.
PhosphoSiteiQ5TA31.

Expressioni

Gene expression databases

BgeeiQ5TA31.
CleanExiHS_RNF187.
GenevisibleiQ5TA31. HS.

Organism-specific databases

HPAiHPA030098.

Interactioni

Subunit structurei

Homodimer. Interacts with JUN, independently of JUN phosphorylation.2 Publications

Protein-protein interaction databases

BioGridi127223. 15 interactions.
STRINGi9606.ENSP00000306396.

Structurei

3D structure databases

ProteinModelPortaliQ5TA31.
SMRiQ5TA31. Positions 2-52.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410JC6A. Eukaryota.
ENOG4111A5E. LUCA.
HOGENOMiHOG000154159.
HOVERGENiHBG093909.
InParanoidiQ5TA31.
KOiK15709.
OrthoDBiEOG7CK388.
TreeFamiTF351093.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5TA31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPAGPAEA ACALCQRAPR EPVRADCGHR FCRACVVRFW AEEDGPFPCP
60 70 80 90 100
ECADDCWQRA VEPGRPPLSR RLLALEEAAA APARDGPASE AALQLLCRAD
110 120 130 140 150
AGPLCAACRM AAGPEPPEWE PRWRKALRGK ENKGSVEIMR KDLNDARDLH
160 170 180 190 200
GQAESAAAVW KGHVMDRRKK ALTDYKKLRA FFVEEEEHFL QEAEKEEGLP
210 220 230
EDELADPTER FRSLLQAVSE LEKKHRNLGL SMLLQ
Length:235
Mass (Da):26,190
Last modified:May 3, 2011 - v2
Checksum:i6C16442F7419CD25
GO

Sequence cautioni

The sequence AAH12758.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAH12758.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI23328.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL139288 Genomic DNA. Translation: CAI23328.1. Sequence problems.
BC012758 mRNA. Translation: AAH12758.1. Sequence problems.
BC064481 mRNA. Translation: AAH64481.1.
CCDSiCCDS76271.1.
RefSeqiNP_001010858.2. NM_001010858.2.
UniGeneiHs.356377.
Hs.679030.

Genome annotation databases

EnsembliENST00000305943; ENSP00000306396; ENSG00000168159.
GeneIDi149603.
KEGGihsa:149603.
UCSCiuc057qfa.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL139288 Genomic DNA. Translation: CAI23328.1. Sequence problems.
BC012758 mRNA. Translation: AAH12758.1. Sequence problems.
BC064481 mRNA. Translation: AAH64481.1.
CCDSiCCDS76271.1.
RefSeqiNP_001010858.2. NM_001010858.2.
UniGeneiHs.356377.
Hs.679030.

3D structure databases

ProteinModelPortaliQ5TA31.
SMRiQ5TA31. Positions 2-52.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127223. 15 interactions.
STRINGi9606.ENSP00000306396.

PTM databases

iPTMnetiQ5TA31.
PhosphoSiteiQ5TA31.

Polymorphism and mutation databases

DMDMi332278146.

Proteomic databases

MaxQBiQ5TA31.
PaxDbiQ5TA31.
PRIDEiQ5TA31.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305943; ENSP00000306396; ENSG00000168159.
GeneIDi149603.
KEGGihsa:149603.
UCSCiuc057qfa.1. human.

Organism-specific databases

CTDi149603.
GeneCardsiRNF187.
H-InvDBHIX0028697.
HGNCiHGNC:27146. RNF187.
HPAiHPA030098.
MIMi613754. gene.
neXtProtiNX_Q5TA31.
PharmGKBiPA142671058.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JC6A. Eukaryota.
ENOG4111A5E. LUCA.
HOGENOMiHOG000154159.
HOVERGENiHBG093909.
InParanoidiQ5TA31.
KOiK15709.
OrthoDBiEOG7CK388.
TreeFamiTF351093.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF187. human.
GenomeRNAii149603.
NextBioi86195.
PROiQ5TA31.
SOURCEiSearch...

Gene expression databases

BgeeiQ5TA31.
CleanExiHS_RNF187.
GenevisibleiQ5TA31. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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].
    Tissue: Lymph and Uterus.
  3. "Identification of a co-activator that links growth factor signalling to c-Jun/AP-1 activation."
    Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J., Behrens A.
    Nat. Cell Biol. 12:963-972(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH JUN, SUBCELLULAR LOCATION, IDENTIFICATION OF A NON-AUG INITIATOR START CODON, UBIQUITINATION AT LYS-195; LYS-223 AND LYS-224, MUTAGENESIS OF MET-1; CYS-12 AND CYS-15.
  4. "Arginine methylation of the c-Jun coactivator RACO-1 is required for c-Jun/AP-1 activation."
    Davies C.C., Chakraborty A., Diefenbacher M.E., Skehel M., Behrens A.
    EMBO J. 32:1556-1567(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-98 AND ARG-109, SUBUNIT.

Entry informationi

Entry nameiRN187_HUMAN
AccessioniPrimary (citable) accession number: Q5TA31
Secondary accession number(s): A6NL57, Q6P2J7, Q6PJR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 3, 2011
Last modified: March 16, 2016
This is version 82 of the entry and version 2 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

Caution

This sequence initiates at a CTG codon.1 Publication

Keywords - Technical termi

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. 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.