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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

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 5544RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF152Curated (EC:6.3.2.-1 Publication)
Alternative name(s):
RING finger protein 152Imported
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)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei167 – 18721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of organelle membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134984811.

Polymorphism and mutation databases

BioMutaiRNF152.
DMDMi41017760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203E3 ubiquitin-protein ligase RNF152PRO_0000056111Add
BLAST

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.
PhosphoSiteiQ8N8N0.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ8N8N0.
CleanExiHS_RNF152.
ExpressionAtlasiQ8N8N0. baseline and differential.
GenevisibleiQ8N8N0. HS.

Organism-specific databases

HPAiHPA015733.

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. 4 interactions.
IntActiQ8N8N0. 4 interactions.
STRINGi9606.ENSP00000316628.

Structurei

3D structure databases

ProteinModelPortaliQ8N8N0.
SMRiQ8N8N0. Positions 9-76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 16560Necessary for interaction with RRAGA1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the RNF152 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 5544RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITF4. Eukaryota.
ENOG4111BNB. LUCA.
GeneTreeiENSGT00730000111317.
HOGENOMiHOG000120123.
HOVERGENiHBG054053.
InParanoidiQ8N8N0.
KOiK15705.
OMAiPWCRGIT.
OrthoDBiEOG7CRTQT.
PhylomeDBiQ8N8N0.
TreeFamiTF331690.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121C → S in BAG53711 (PubMed:14702039).Curated

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_005266650.2.
XP_005266708.1. XM_005266651.2.
XP_005266709.1. XM_005266652.2.
XP_011524179.1. XM_011525877.1.
XP_011524180.1. XM_011525878.1.
XP_011524181.1. XM_011525879.1.
XP_011524182.1. XM_011525880.1.
UniGeneiHs.165062.
Hs.667457.

Genome annotation databases

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

Cross-referencesi

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_005266650.2.
XP_005266708.1. XM_005266651.2.
XP_005266709.1. XM_005266652.2.
XP_011524179.1. XM_011525877.1.
XP_011524180.1. XM_011525878.1.
XP_011524181.1. XM_011525879.1.
XP_011524182.1. XM_011525880.1.
UniGeneiHs.165062.
Hs.667457.

3D structure databases

ProteinModelPortaliQ8N8N0.
SMRiQ8N8N0. Positions 9-76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128647. 4 interactions.
IntActiQ8N8N0. 4 interactions.
STRINGi9606.ENSP00000316628.

PTM databases

iPTMnetiQ8N8N0.
PhosphoSiteiQ8N8N0.

Polymorphism and mutation databases

BioMutaiRNF152.
DMDMi41017760.

Proteomic databases

PaxDbiQ8N8N0.
PRIDEiQ8N8N0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi220441.
GeneCardsiRNF152.
HGNCiHGNC:26811. RNF152.
HPAiHPA015733.
MIMi616512. gene.
neXtProtiNX_Q8N8N0.
PharmGKBiPA134984811.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITF4. Eukaryota.
ENOG4111BNB. LUCA.
GeneTreeiENSGT00730000111317.
HOGENOMiHOG000120123.
HOVERGENiHBG054053.
InParanoidiQ8N8N0.
KOiK15705.
OMAiPWCRGIT.
OrthoDBiEOG7CRTQT.
PhylomeDBiQ8N8N0.
TreeFamiTF331690.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GenomeRNAii220441.
PROiQ8N8N0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N8N0.
CleanExiHS_RNF152.
ExpressionAtlasiQ8N8N0. baseline and differential.
GenevisibleiQ8N8N0. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF14634. zf-RING_5. 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].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
  4. "RNF152, a novel lysosome localized E3 ligase with pro-apoptotic activities."
    Zhang S., Wu W., Wu Y., Zheng J., Suo T., Tang H., Tang J.
    Protein Cell 1:656-663(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, TISSUE SPECIFICITY.
  5. "The ubiquitination of RagA GTPase by RNF152 negatively regulates mTORC1 activation."
    Deng L., Jiang C., Chen L., Jin J., Wei J., Zhao L., Chen M., Pan W., Xu Y., Chu H., Wang X., Ge X., Li D., Liao L., Liu M., Li L., Wang P.
    Mol. Cell 58:804-818(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, INTERACTION WITH RRAGA, REGION.

Entry informationi

Entry nameiRN152_HUMAN
AccessioniPrimary (citable) accession number: Q8N8N0
Secondary accession number(s): B3KV99, Q52LA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 99 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 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

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.