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Protein

E3 ubiquitin-protein ligase RNF128

Gene

RNF128

Organism
Homo sapiens (Human)
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.2 Publications

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

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of cytokine biosynthetic process Source: Ensembl
  • positive regulation of protein catabolic process in the vacuole Source: BHF-UCL
  • protein localization to lysosome Source: BHF-UCL
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • regulation of protein stability Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000133135-MONOMER.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-5689896. Ovarian tumor domain proteases.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF128 (EC:6.3.2.-)
Alternative name(s):
Gene related to anergy in lymphocytes protein
Short name:
GRAIL
RING finger protein 128
Gene namesi
Name:RNF128
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:21153. RNF128.

Subcellular locationi

Topology

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi79589.
OpenTargetsiENSG00000133135.
PharmGKBiPA134868457.

Polymorphism and mutation databases

BioMutaiRNF128.
DMDMi74751443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 38Sequence analysisAdd BLAST38
ChainiPRO_000026141239 – 428E3 ubiquitin-protein ligase RNF128Add BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi48N-linked (GlcNAc...)Sequence analysis1
Glycosylationi59N-linked (GlcNAc...)Sequence analysis1
Glycosylationi101N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8TEB7.
PaxDbiQ8TEB7.
PeptideAtlasiQ8TEB7.
PRIDEiQ8TEB7.

PTM databases

PhosphoSitePlusiQ8TEB7.

Expressioni

Inductioni

Induced under anergic conditions. Up-regulated during T-cell anergy induction following signaling through the T-cell antigen receptor.1 Publication

Gene expression databases

BgeeiENSG00000133135.
CleanExiHS_RNF128.
ExpressionAtlasiQ8TEB7. baseline and differential.
GenevisibleiQ8TEB7. HS.

Organism-specific databases

HPAiHPA019675.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-2341619,EBI-743771
CEP76Q8TAP65EBI-2341619,EBI-742887

Protein-protein interaction databases

BioGridi122731. 15 interactors.
IntActiQ8TEB7. 6 interactors.
STRINGi9606.ENSP00000255499.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 52Combined sources11
Beta strandi61 – 71Combined sources11
Beta strandi80 – 85Combined sources6
Beta strandi116 – 122Combined sources7
Helixi128 – 137Combined sources10
Beta strandi141 – 146Combined sources6
Beta strandi165 – 171Combined sources7
Helixi173 – 184Combined sources12
Beta strandi189 – 199Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ICUX-ray2.10A38-204[»]
ProteinModelPortaliQ8TEB7.
SMRiQ8TEB7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TEB7.

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.

Sequence similaritiesi

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

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.
InParanoidiQ8TEB7.
KOiK10629.
OMAiTVPGDWG.
OrthoDBiEOG091G08OR.
PhylomeDBiQ8TEB7.
TreeFamiTF317486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TEB7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGPPPGAGVS CRGGCGFSRL LAWCFLLALS PQAPGSRGAE AVWTAYLNVS
60 70 80 90 100
WRVPHTGVNR TVWELSEEGV YGQDSPLEPV AGVLVPPDGP GALNACNPHT
110 120 130 140 150
NFTVPTVWGS TVQVSWLALI QRGGGCTFAD KIHLAYERGA SGAVIFNFPG
160 170 180 190 200
TRNEVIPMSH PGAVDIVAIM IGNLKGTKIL QSIQRGIQVT MVIEVGKKHG
210 220 230 240 250
PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ SRKQRQLKAD
260 270 280 290 300
AKKAIGRLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH
310 320 330 340 350
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEISNSA
360 370 380 390 400
SSHEEDNRSE TASSGYASVQ GTDEPPLEEH VQSTNESLQL VNHEANSVAV
410 420
DVIPHVDNPT FEEDETPNQE TAVREIKS
Length:428
Mass (Da):46,521
Last modified:June 1, 2002 - v1
Checksum:i32F9CDB32BF208FA
GO
Isoform 2 (identifier: Q8TEB7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: MGPPPGAGVS...RNEVIPMSHP → MNQENRSSFF...GNQTIQMANF

Note: No experimental confirmation available.
Show »
Length:402
Mass (Da):44,617
Checksum:iCCE3A965DB2F4F2E
GO

Sequence cautioni

The sequence BAB15682 differs from that shown. Reason: Frameshift at position 291.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4P → L in AAK77554 (PubMed:12705856).Curated1
Sequence conflicti214S → P in AAK77554 (PubMed:12705856).Curated1
Sequence conflicti223V → G in AAK77554 (PubMed:12705856).Curated1
Sequence conflicti255I → L in BAB15682 (PubMed:14702039).Curated1
Sequence conflicti257R → G in AAH56677 (PubMed:15489334).Curated1
Sequence conflicti261R → L in BAB15682 (PubMed:14702039).Curated1
Sequence conflicti336V → A in BAB15682 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0216851 – 161MGPPP…PMSHP → MNQENRSSFFWLLVIFTFLL KITASFSMSAYVTVTYYNET SNYTAIETCECGVYGLASPV ANAMGVVGIPKNNNYQACDH NTEFSNTKKPWIALIERGNC TFSEKIQTAGRRNADAVVIY NAPETGNQTIQMANF in isoform 2. 1 PublicationAdd BLAST161

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF394689 mRNA. Translation: AAK77554.1.
AK027169 mRNA. Translation: BAB15682.1. Frameshift.
AK074264 mRNA. Translation: BAB85033.1.
AK126553 mRNA. Translation: BAC86589.1.
AL391315 Genomic DNA. Translation: CAI39545.1.
AL391315, AL606833 Genomic DNA. Translation: CAI39546.1.
AL606833, AL391315 Genomic DNA. Translation: CAI41228.1.
BC030951 mRNA. Translation: AAH30951.1.
BC056677 mRNA. Translation: AAH56677.1.
BC063404 mRNA. Translation: AAH63404.1.
CCDSiCCDS14520.1. [Q8TEB7-2]
CCDS14521.1. [Q8TEB7-1]
RefSeqiNP_078815.3. NM_024539.3. [Q8TEB7-2]
NP_919445.1. NM_194463.1. [Q8TEB7-1]
UniGeneiHs.496542.

Genome annotation databases

EnsembliENST00000255499; ENSP00000255499; ENSG00000133135. [Q8TEB7-1]
ENST00000324342; ENSP00000316127; ENSG00000133135. [Q8TEB7-2]
GeneIDi79589.
KEGGihsa:79589.
UCSCiuc004emk.4. human. [Q8TEB7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF394689 mRNA. Translation: AAK77554.1.
AK027169 mRNA. Translation: BAB15682.1. Frameshift.
AK074264 mRNA. Translation: BAB85033.1.
AK126553 mRNA. Translation: BAC86589.1.
AL391315 Genomic DNA. Translation: CAI39545.1.
AL391315, AL606833 Genomic DNA. Translation: CAI39546.1.
AL606833, AL391315 Genomic DNA. Translation: CAI41228.1.
BC030951 mRNA. Translation: AAH30951.1.
BC056677 mRNA. Translation: AAH56677.1.
BC063404 mRNA. Translation: AAH63404.1.
CCDSiCCDS14520.1. [Q8TEB7-2]
CCDS14521.1. [Q8TEB7-1]
RefSeqiNP_078815.3. NM_024539.3. [Q8TEB7-2]
NP_919445.1. NM_194463.1. [Q8TEB7-1]
UniGeneiHs.496542.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ICUX-ray2.10A38-204[»]
ProteinModelPortaliQ8TEB7.
SMRiQ8TEB7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122731. 15 interactors.
IntActiQ8TEB7. 6 interactors.
STRINGi9606.ENSP00000255499.

PTM databases

PhosphoSitePlusiQ8TEB7.

Polymorphism and mutation databases

BioMutaiRNF128.
DMDMi74751443.

Proteomic databases

MaxQBiQ8TEB7.
PaxDbiQ8TEB7.
PeptideAtlasiQ8TEB7.
PRIDEiQ8TEB7.

Protocols and materials databases

DNASUi79589.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255499; ENSP00000255499; ENSG00000133135. [Q8TEB7-1]
ENST00000324342; ENSP00000316127; ENSG00000133135. [Q8TEB7-2]
GeneIDi79589.
KEGGihsa:79589.
UCSCiuc004emk.4. human. [Q8TEB7-1]

Organism-specific databases

CTDi79589.
DisGeNETi79589.
GeneCardsiRNF128.
HGNCiHGNC:21153. RNF128.
HPAiHPA019675.
MIMi300439. gene.
neXtProtiNX_Q8TEB7.
OpenTargetsiENSG00000133135.
PharmGKBiPA134868457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4628. Eukaryota.
ENOG410Z5DF. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
HOVERGENiHBG057659.
InParanoidiQ8TEB7.
KOiK10629.
OMAiTVPGDWG.
OrthoDBiEOG091G08OR.
PhylomeDBiQ8TEB7.
TreeFamiTF317486.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000133135-MONOMER.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-5689896. Ovarian tumor domain proteases.

Miscellaneous databases

ChiTaRSiRNF128. human.
EvolutionaryTraceiQ8TEB7.
GeneWikiiRNF128.
GenomeRNAii79589.
PROiQ8TEB7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000133135.
CleanExiHS_RNF128.
ExpressionAtlasiQ8TEB7. baseline and differential.
GenevisibleiQ8TEB7. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRN128_HUMAN
AccessioniPrimary (citable) accession number: Q8TEB7
Secondary accession number(s): A0PJI4
, Q6PH80, Q6ZTJ8, Q96RF3, Q9H5E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2002
Last modified: November 30, 2016
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.