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Protein

E3 ubiquitin-protein ligase RNF181

Gene

RNF181

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

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers 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 fingeri76 – 11742RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF181 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 181
Gene namesi
Name:RNF181
ORF Names:HSPC238
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:28037. RNF181.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401586.

Polymorphism and mutation databases

BioMutaiRNF181.
DMDMi74761852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 153153E3 ubiquitin-protein ligase RNF181PRO_0000295174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei153 – 1531PhosphothreonineCombined sources

Post-translational modificationi

Auto-ubiquitinated as part of the enzymatic reaction.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9P0P0.
MaxQBiQ9P0P0.
PaxDbiQ9P0P0.
PRIDEiQ9P0P0.

PTM databases

iPTMnetiQ9P0P0.
PhosphoSiteiQ9P0P0.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in liver and heart and lowest levels in brain and skeletal muscle. Expressed in platelets (at protein level).1 Publication

Gene expression databases

BgeeiQ9P0P0.
CleanExiHS_RNF181.
ExpressionAtlasiQ9P0P0. baseline and differential.
GenevisibleiQ9P0P0. HS.

Organism-specific databases

HPAiHPA046112.

Interactioni

Subunit structurei

Directly interacts with ITGA2B and, as a result, with integrin ITGA2B/ITGB3. There is no evidence that integrin ITGA2B/ITGB3 is an endogenous substrate for RNF181-directed ubiquitination.1 Publication

Protein-protein interaction databases

BioGridi119411. 29 interactions.
IntActiQ9P0P0. 19 interactions.
STRINGi9606.ENSP00000306906.

Structurei

3D structure databases

ProteinModelPortaliQ9P0P0.
SMRiQ9P0P0. Positions 74-120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNF181 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri76 – 11742RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000031081.
HOVERGENiHBG108412.
InParanoidiQ9P0P0.
OMAiDEHNCEP.
PhylomeDBiQ9P0P0.
TreeFamiTF332127.

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.

Q9P0P0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASYFDEHDC EPSDPEQETR TNMLLELARS LFNRMDFEDL GLVVDWDHHL
60 70 80 90 100
PPPAAKTVVE NLPRTVIRGS QAELKCPVCL LEFEEEETAI EMPCHHLFHS
110 120 130 140 150
SCILPWLSKT NSCPLCRYEL PTDDDTYEEH RRDKARKQQQ QHRLENLHGA

MYT
Length:153
Mass (Da):17,909
Last modified:October 1, 2000 - v1
Checksum:iAF0CEC8D438FF0AB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181Y → H.1 Publication
Corresponds to variant rs6643 [ dbSNP | Ensembl ].
VAR_033323

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151072 mRNA. Translation: AAF36158.1.
CR457165 mRNA. Translation: CAG33446.1.
AK222700 mRNA. Translation: BAD96420.1.
AC016753 Genomic DNA. Translation: AAY24343.1.
BC002803 mRNA. Translation: AAH02803.1.
CCDSiCCDS1981.1.
RefSeqiNP_057578.1. NM_016494.3.
UniGeneiHs.356187.

Genome annotation databases

EnsembliENST00000306368; ENSP00000306906; ENSG00000168894.
GeneIDi51255.
KEGGihsa:51255.
UCSCiuc002spv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151072 mRNA. Translation: AAF36158.1.
CR457165 mRNA. Translation: CAG33446.1.
AK222700 mRNA. Translation: BAD96420.1.
AC016753 Genomic DNA. Translation: AAY24343.1.
BC002803 mRNA. Translation: AAH02803.1.
CCDSiCCDS1981.1.
RefSeqiNP_057578.1. NM_016494.3.
UniGeneiHs.356187.

3D structure databases

ProteinModelPortaliQ9P0P0.
SMRiQ9P0P0. Positions 74-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119411. 29 interactions.
IntActiQ9P0P0. 19 interactions.
STRINGi9606.ENSP00000306906.

PTM databases

iPTMnetiQ9P0P0.
PhosphoSiteiQ9P0P0.

Polymorphism and mutation databases

BioMutaiRNF181.
DMDMi74761852.

Proteomic databases

EPDiQ9P0P0.
MaxQBiQ9P0P0.
PaxDbiQ9P0P0.
PRIDEiQ9P0P0.

Protocols and materials databases

DNASUi51255.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306368; ENSP00000306906; ENSG00000168894.
GeneIDi51255.
KEGGihsa:51255.
UCSCiuc002spv.2. human.

Organism-specific databases

CTDi51255.
GeneCardsiRNF181.
HGNCiHGNC:28037. RNF181.
HPAiHPA046112.
MIMi612490. gene.
neXtProtiNX_Q9P0P0.
PharmGKBiPA162401586.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000031081.
HOVERGENiHBG108412.
InParanoidiQ9P0P0.
OMAiDEHNCEP.
PhylomeDBiQ9P0P0.
TreeFamiTF332127.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.

Miscellaneous databases

GenomeRNAii51255.
NextBioi54406.
PROiQ9P0P0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0P0.
CleanExiHS_RNF181.
ExpressionAtlasiQ9P0P0. baseline and differential.
GenevisibleiQ9P0P0. 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. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-118.
    Tissue: Brain.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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].
    Tissue: Placenta.
  6. "RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3."
    Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I., Chubb A.J., Treumann A., Moran N.
    Biochem. Biophys. Res. Commun. 369:1088-1093(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ITGA2B, TISSUE SPECIFICITY, AUTOUBIQUITINATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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 THR-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRN181_HUMAN
AccessioniPrimary (citable) accession number: Q9P0P0
Secondary accession number(s): Q53H81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 1, 2000
Last modified: March 16, 2016
This is version 126 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.