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Protein

E3 ubiquitin-protein ligase RNF152

Gene

RNF152

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

Functioni

E3 ubiquitin-protein ligase mediating 'Lys-63'-linked polyubiquitination of RRAGA in response to amino acid starvation. Thereby, regulates mTORC1 signaling and plays a role in the cellular response to amino acid availability (PubMed:25936802). Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation. Induces apoptosis when overexpressed (PubMed:21203937).2 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
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)DescriptionActionsGraphical viewLength
Zinc fingeri12 – 55RING-typePROSITE-ProRule annotationAdd BLAST44

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • small GTPase binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cellular response to amino acid starvation Source: UniProtKB
  • negative regulation of TORC1 signaling Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • protein ubiquitination Source: Reactome

Keywordsi

Molecular functionTransferase
Biological processApoptosis, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-8866654. E3 ubiquitin ligases ubiquitinate target proteins.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF152Curated (EC:2.3.2.271 Publication)
Alternative name(s):
RING finger protein 152Imported
RING-type E3 ubiquitin transferase RNF152Curated
Gene namesi
Name:RNF152Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:26811. RNF152.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei167 – 187HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • integral component of organelle membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: UniProtKB

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000176641.
PharmGKBiPA134984811.

Polymorphism and mutation databases

BioMutaiRNF152.
DMDMi41017760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000561111 – 203E3 ubiquitin-protein ligase RNF152Add BLAST203

Post-translational modificationi

Ubiquitinated. Autoubiquitinated in vitro, leading to its degradation by the proteasome (Probable).1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ8N8N0.
PRIDEiQ8N8N0.

PTM databases

iPTMnetiQ8N8N0.
PhosphoSitePlusiQ8N8N0.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000176641.
CleanExiHS_RNF152.
ExpressionAtlasiQ8N8N0. baseline and differential.
GenevisibleiQ8N8N0. HS.

Interactioni

Subunit structurei

Interacts with RRAGA (inactive GDP-bound form); stimulated by amino acid starvation.1 Publication

GO - Molecular functioni

  • small GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi128647. 5 interactors.
IntActiQ8N8N0. 5 interactors.
STRINGi9606.ENSP00000316628.

Structurei

3D structure databases

ProteinModelPortaliQ8N8N0.
SMRiQ8N8N0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 165Necessary for interaction with RRAGA1 PublicationAdd BLAST60

Sequence similaritiesi

Belongs to the RNF152 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri12 – 55RING-typePROSITE-ProRule annotationAdd BLAST44

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITF4. Eukaryota.
ENOG4111BNB. LUCA.
GeneTreeiENSGT00730000111317.
HOGENOMiHOG000120123.
HOVERGENiHBG054053.
InParanoidiQ8N8N0.
KOiK15705.
OMAiPWCRGIT.
OrthoDBiEOG091G0KUF.
PhylomeDBiQ8N8N0.
TreeFamiTF331690.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR033609. RNF152.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
PANTHERiPTHR25464. PTHR25464. 1 hit.
PfamiView protein in Pfam
PF14634. zf-RING_5. 1 hit.
SMARTiView protein in SMART
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS50089. ZF_RING_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8N8N0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METLSQDSLL ECQICFNYYS PRRRPKLLDC KHTCCSVCLQ QMRTSQKDVR
60 70 80 90 100
CPWCRGVTKL PPGFSVSQLP DDPEVLAVIA IPHTSEHTPV FIKLPSNGCY
110 120 130 140 150
MLPLPISKER ALLPGDMGCR LLPGSQQKSV TVVTIPAEQQ PLQGGAPQEA
160 170 180 190 200
VEEEQDRRGV VKSSTWSGVC TVILVACVLV FLLGIVLHNM SCISKRFTVI

SCG
Length:203
Mass (Da):22,357
Last modified:October 1, 2002 - v1
Checksum:i0DFA570D00744BFA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12C → S in BAG53711 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096495 mRNA. Translation: BAC04805.1.
AK122758 mRNA. Translation: BAG53711.1.
AC105094 Genomic DNA. No translation available.
BC094004 mRNA. Translation: AAH94004.1.
BC111956 mRNA. Translation: AAI11957.1.
CCDSiCCDS11978.1.
RefSeqiNP_775828.1. NM_173557.2.
XP_005266707.1. XM_005266650.3.
XP_005266709.1. XM_005266652.3.
XP_011524180.1. XM_011525878.2.
XP_011524181.1. XM_011525879.2.
XP_016881101.1. XM_017025612.1.
XP_016881102.1. XM_017025613.1.
UniGeneiHs.165062.
Hs.667457.

Genome annotation databases

EnsembliENST00000312828; ENSP00000316628; ENSG00000176641.
GeneIDi220441.
KEGGihsa:220441.
UCSCiuc002lih.2. human.

Similar proteinsi

Entry informationi

Entry nameiRN152_HUMAN
AccessioniPrimary (citable) accession number: Q8N8N0
Secondary accession number(s): B3KV99, Q52LA4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2002
Last modified: August 30, 2017
This is version 108 of the entry and version 1 of the sequence. See 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 18
    Human chromosome 18: 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