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Protein

E3 ubiquitin-protein ligase RNF128

Gene

Rnf128

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

Functioni

E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals (By similarity).By similarity2 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.

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 fingeri277 – 318RING-type; atypicalPROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5689880. Ub-specific processing proteases.
R-MMU-5689896. Ovarian tumor domain proteases.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF128 (EC:2.3.2.27)
Alternative name(s):
Gene related to anergy in lymphocytes protein
Goliath-related E3 ubiquitin-protein ligase 1
RING finger protein 128
RING-type E3 ubiquitin transferase RNF128Curated
Gene namesi
Name:Rnf128
Synonyms:Grail, Greul1
ORF Names:MNCb-3816
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1914139. Rnf128.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei208 – 228HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi277C → G: Loss of ubiquitination activity. 1 Publication1
Mutagenesisi280C → G: Loss of ubiquitination activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 38Sequence analysisAdd BLAST38
ChainiPRO_000026141339 – 428E3 ubiquitin-protein ligase RNF128Add BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi48N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi59N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi101N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Auto-ubiquitinated. Controls the development of T-cell clonal anergy by ubiquitination.By similarity

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9D304.
PaxDbiQ9D304.
PRIDEiQ9D304.

PTM databases

iPTMnetiQ9D304.
PhosphoSitePlusiQ9D304.

Expressioni

Tissue specificityi

Expressed in brain, kidney, heart, liver, ovary, testis and thymus. Expression increased as early as 4 hours by 5- to 7-fold in anergized cultures as compared to resting or activated cells.1 Publication

Developmental stagei

At E6.0, expressed in both the extraembryonic endoderm and extraembryonic ectoderm. After the beginning of gastrulation, expression remains extraembryonic, and is mostly confined to the visceral endoderm. At E8.5, expression appears within the mesodermally derived allantois, and is highly expressed in the epithelial layer of the yolk sac. At E9.5, expressed in the hindgut and adjoining yolk sac. At stage E10, appears to be widely expressed throughout the embryo with higher expression within the branchial arches and within intersomitic endothelial cells.1 Publication

Inductioni

Induced under anergic conditions. Up-regulated during T-cell anergy induction following signaling through the T-cell antigen receptor.By similarity

Gene expression databases

BgeeiENSMUSG00000031438.
CleanExiMM_RNF128.
ExpressionAtlasiQ9D304. baseline and differential.
GenevisibleiQ9D304. MM.

Interactioni

Protein-protein interaction databases

BioGridi211790. 5 interactors.
STRINGi10090.ENSMUSP00000108649.

Structurei

3D structure databases

ProteinModelPortaliQ9D304.
SMRiQ9D304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 183PAAdd BLAST109

Domaini

Binding to E2 ubiquitin-conjugating enzyme requires an intact RING finger domain.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri277 – 318RING-type; atypicalPROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG4628. Eukaryota.
ENOG410Z5DF. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
HOVERGENiHBG057659.
InParanoidiQ9D304.
KOiK10629.
OrthoDBiEOG091G08OR.
PhylomeDBiQ9D304.
TreeFamiTF317486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR003137. PA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
PfamiView protein in Pfam
PF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
SMARTiView protein in SMART
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS50089. ZF_RING_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D304-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPPPGIGVY CRGGCGAARL LAWCFLLALS PHAPGSRGAE AVWTAYLNVS
60 70 80 90 100
WRVPHTGVNR TVWELSEEGV YGQDSPLEPV SGVLVPPDGP GALNACNPHT
110 120 130 140 150
NFTVPTVWGS TVQVSWLALI QRGGGCTFAD KIHLASERGA SGAVIFNFPG
160 170 180 190 200
TRNEVIPMSH PGAGDIVAIM IGNLKGTKIL QSIQRGIQVT MVIEVGKKHG
210 220 230 240 250
PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ SRKQRQLKAD
260 270 280 290 300
AKKAIGKLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH
310 320 330 340 350
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEASNTA
360 370 380 390 400
SPHEEDSRSE TASSGYASVQ GADEPPLEEH AQSANENLQL VNHEANSVAV
410 420
DVVPHVDNPT FEEDETPDQE AAVREIKS
Length:428
Mass (Da):46,276
Last modified:June 1, 2001 - v1
Checksum:i480DCF46C75E238F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti125G → S in BAB23613 (PubMed:16141072).Curated1
Sequence conflicti131K → N in BAB23613 (PubMed:16141072).Curated1
Sequence conflicti132I → V in BAA95033 (Ref. 3) Curated1
Sequence conflicti352P → H in BAE27025 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY112656 mRNA. Translation: AAM51876.1.
AF426411 mRNA. Translation: AAL34514.1.
AB041548 mRNA. Translation: BAA95033.1.
AK004847 mRNA. Translation: BAB23613.1.
AK008312 mRNA. Translation: BAB25595.3.
AK018582 mRNA. Translation: BAB31291.1.
AK146266 mRNA. Translation: BAE27025.1.
AK167031 mRNA. Translation: BAE39203.1.
BC010477 mRNA. Translation: AAH10477.1.
CCDSiCCDS30435.1.
RefSeqiNP_001241690.1. NM_001254761.1.
NP_075759.3. NM_023270.5.
UniGeneiMm.27764.

Genome annotation databases

EnsembliENSMUST00000113026; ENSMUSP00000108649; ENSMUSG00000031438.
GeneIDi66889.
KEGGimmu:66889.
UCSCiuc009uki.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiRN128_MOUSE
AccessioniPrimary (citable) accession number: Q9D304
Secondary accession number(s): Q3UJY0
, Q9CVG1, Q9DBN3, Q9JJF8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: August 30, 2017
This is version 125 of the entry and version 1 of the sequence. See 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