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Protein

E3 ubiquitin-protein ligase RNF139

Gene

Rnf139

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor (By similarity).By similarity

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)DescriptionActionsGraphical viewLength
Zinc fingeri547 – 586RING-type; atypicalPROSITE-ProRule annotationAdd BLAST40

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase, Receptor

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 RNF139 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 139
Translocation in renal carcinoma on chromosome 8 protein
Gene namesi
Name:Rnf139Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1923091. Rnf139.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei51 – 71HelicalSequence analysisAdd BLAST21
Transmembranei85 – 105HelicalSequence analysisAdd BLAST21
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Transmembranei154 – 174HelicalSequence analysisAdd BLAST21
Transmembranei178 – 198HelicalSequence analysisAdd BLAST21
Transmembranei293 – 313HelicalSequence analysisAdd BLAST21
Transmembranei323 – 343HelicalSequence analysisAdd BLAST21
Transmembranei356 – 376HelicalSequence analysisAdd BLAST21
Transmembranei390 – 410HelicalSequence analysisAdd BLAST21
Transmembranei420 – 440HelicalSequence analysisAdd BLAST21
Transmembranei470 – 490HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000560992 – 668E3 ubiquitin-protein ligase RNF139Add BLAST667

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei636PhosphoserineBy similarity1
Modified residuei637PhosphothreonineBy similarity1
Modified residuei667PhosphothreonineCombined sources1

Post-translational modificationi

Autoubiquitinated. Ubiquitination is induced by sterol and leads to ist degradation via the ubiquitin-proteasome pathway (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ7TMV1.
PeptideAtlasiQ7TMV1.
PRIDEiQ7TMV1.

PTM databases

iPTMnetiQ7TMV1.
PhosphoSitePlusiQ7TMV1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000037075.
CleanExiMM_RNF139.

Interactioni

Subunit structurei

Interacts with VHL. Interacts with MHC class I and HM13. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts with SREBF2 (via C-terminal domain). Interacts with SCAP; the interaction inhibits the interaction of SCAP with SEC24B and hampering the ER to Golgi transport of the SCAP/SREBP complex. Interacts with SEC24B. Interacts with INSIG1 and INSIG2. Interacts with EIF3F and EIF3H; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Interacts with XBP1 isoform 1; the interaction induces ubiquitination and degradation of XBP1 isoform 1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046467.

Structurei

3D structure databases

ProteinModelPortaliQ7TMV1.
SMRiQ7TMV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain may be essential for ubiquitin ligase activity.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri547 – 586RING-type; atypicalPROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
HOGENOMiHOG000267029.
HOVERGENiHBG053146.
InParanoidiQ7TMV1.
KOiK15703.
PhylomeDBiQ7TMV1.
TreeFamiTF318635.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR025754. TRC8_N_dom.
IPR001841. Znf_RING.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13705. TRC8_N. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00744. RINGv. 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.

Q7TMV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVGPPQQQ VRMAQQQVWA ALEVALRVPC LYIIDAIFNS YYDSSQSRFC
60 70 80 90 100
IGLQIFLRLL GIVVSSIVLI LSQRSLFKFY MYSSAFLLAA TSVLVNYYAA
110 120 130 140 150
LHIDFYGAYN TSAFGIELLP RKGPSLWMAL IVLQLTFGIG YVTLLQIQSI
160 170 180 190 200
YSQLMILNIL VPIIGLITEL PLHIRETVVL MSSLILIFNT VLVLAVKLKW
210 220 230 240 250
FYYSTRYVYL LVRHMYRIYG LQLLMEDTWK RIRFPDILRV FWLTRITTQA
260 270 280 290 300
TVLMYILRMA NETESFFISW DDFWDVICNL IISGCDSTLT VLGMSAVISS
310 320 330 340 350
IAHYLGLGIL AFIGSTEEDD RRLGFVAPVL FFILALQTGL SGLRPEERLI
360 370 380 390 400
RLSRNMCLLL TAVLHFIHGM TDPVLMSLSA SHVSSFHRHF PVLFVSACLF
410 420 430 440 450
ILPVLLSYVL WHHYALNTWL FAVTAFCVEL CLKVIVSLTV YTLFMIDGYY
460 470 480 490 500
NVLWEKLDDY VYFVRSTGNI IEFIFGVVMF GNGAYTMMFE SGSKIRACMM
510 520 530 540 550
CLHAYFNIYL QVKNGWKTFM NRRTAVKKIN SLPEIKGSHL QEIDDVCAIC
560 570 580 590 600
YHEFTTSARI TPCNHYFHAL CLRKWLYIQD TCPMCHQKVY IEDEIKDNSN
610 620 630 640 650
ASNNNGFIAP NENPNPEEAL REDAAGSDRE LNEDDSTDCD DDAQRERNGG
660
IQHTGAAAAA AEFNDDTD
Length:668
Mass (Da):76,185
Last modified:October 1, 2003 - v1
Checksum:i6DA76DFC64C6374D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti248T → A in BAC28327 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033506 mRNA. Translation: BAC28327.1.
BC052901 mRNA. Translation: AAH52901.1.
CCDSiCCDS27494.1.
RefSeqiNP_780435.1. NM_175226.4.
UniGeneiMm.4537.
Mm.460627.

Genome annotation databases

GeneIDi75841.
KEGGimmu:75841.
UCSCiuc007vtq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033506 mRNA. Translation: BAC28327.1.
BC052901 mRNA. Translation: AAH52901.1.
CCDSiCCDS27494.1.
RefSeqiNP_780435.1. NM_175226.4.
UniGeneiMm.4537.
Mm.460627.

3D structure databases

ProteinModelPortaliQ7TMV1.
SMRiQ7TMV1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046467.

PTM databases

iPTMnetiQ7TMV1.
PhosphoSitePlusiQ7TMV1.

Proteomic databases

PaxDbiQ7TMV1.
PeptideAtlasiQ7TMV1.
PRIDEiQ7TMV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi75841.
KEGGimmu:75841.
UCSCiuc007vtq.2. mouse.

Organism-specific databases

CTDi11236.
MGIiMGI:1923091. Rnf139.

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
HOGENOMiHOG000267029.
HOVERGENiHBG053146.
InParanoidiQ7TMV1.
KOiK15703.
PhylomeDBiQ7TMV1.
TreeFamiTF318635.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ7TMV1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000037075.
CleanExiMM_RNF139.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR025754. TRC8_N_dom.
IPR001841. Znf_RING.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13705. TRC8_N. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRN139_MOUSE
AccessioniPrimary (citable) accession number: Q7TMV1
Secondary accession number(s): Q8BZU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.