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Protein

E3 ubiquitin-protein ligase RNF25

Gene

RNF25

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 mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). Stimulates transcription mediated by NF-kappa-B.By similarity1 Publication

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 fingeri135 – 202RING-typePROSITE-ProRule annotationAdd BLAST68

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163481-MONOMER.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF25 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 25
Gene namesi
Name:RNF25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:14662. RNF25.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159C → S: Reduced activation of NF-kappa-B. 1 Publication1
Mutagenesisi161C → S: Strongly reduced activation of NF-kappa-B. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000163481.
PharmGKBiPA34429.

Polymorphism and mutation databases

BioMutaiRNF25.
DMDMi21362899.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000560661 – 459E3 ubiquitin-protein ligase RNF25Add BLAST459

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei450PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96BH1.
MaxQBiQ96BH1.
PaxDbiQ96BH1.
PeptideAtlasiQ96BH1.
PRIDEiQ96BH1.

PTM databases

iPTMnetiQ96BH1.
PhosphoSitePlusiQ96BH1.

Expressioni

Gene expression databases

BgeeiENSG00000163481.
CleanExiHS_RNF25.
ExpressionAtlasiQ96BH1. baseline and differential.
GenevisibleiQ96BH1. HS.

Organism-specific databases

HPAiHPA036420.
HPA036421.

Interactioni

Subunit structurei

Interacts with UBE2D2, and may also interact with UBE2E1 and UBE2E3. Interacts with NKD2 (By similarity). Interacts with RELA.By similarity1 Publication

GO - Molecular functioni

  • NF-kappaB binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122133. 23 interactors.
DIPiDIP-29063N.
IntActiQ96BH1. 12 interactors.
STRINGi9606.ENSP00000295704.

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 26Combined sources12
Turni28 – 30Combined sources3
Beta strandi31 – 34Combined sources4
Turni38 – 40Combined sources3
Beta strandi43 – 49Combined sources7
Beta strandi55 – 58Combined sources4
Beta strandi63 – 70Combined sources8
Beta strandi80 – 89Combined sources10
Helixi91 – 107Combined sources17
Turni108 – 110Combined sources3
Helixi114 – 125Combined sources12
Beta strandi132 – 134Combined sources3
Turni136 – 138Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi156 – 158Combined sources3
Helixi159 – 176Combined sources18
Turni199 – 201Combined sources3
Helixi209 – 214Combined sources6
Helixi229 – 247Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DAYNMR-A11-125[»]
2DMFNMR-A11-134[»]
5D1KX-ray1.78B126-258[»]
5D1LX-ray1.62B126-258[»]
5D1MX-ray1.58B126-258[»]
ProteinModelPortaliQ96BH1.
SMRiQ96BH1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96BH1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 128RWDPROSITE-ProRule annotationAdd BLAST111

Domaini

The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri135 – 202RING-typePROSITE-ProRule annotationAdd BLAST68

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4445. Eukaryota.
ENOG4111H5K. LUCA.
GeneTreeiENSGT00390000001557.
HOGENOMiHOG000012992.
HOVERGENiHBG055249.
InParanoidiQ96BH1.
KOiK10640.
OMAiVPQISIR.
OrthoDBiEOG091G0IBN.
PhylomeDBiQ96BH1.
TreeFamiTF324097.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR006575. RWD-domain.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00591. RWD. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50908. RWD. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96BH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASASAAAG EEDWVLPSEV EVLESIYLDE LQVIKGNGRT SPWEIYITLH
60 70 80 90 100
PATAEDQDSQ YVCFTLVLQV PAEYPHEVPQ ISIRNPRGLS DEQIHTILQV
110 120 130 140 150
LGHVAKAGLG TAMLYELIEK GKEILTDNNI PHGQCVICLY GFQEKEAFTK
160 170 180 190 200
TPCYHYFHCH CLARYIQHME QELKAQGQEQ EQERQHATTK QKAVGVQCPV
210 220 230 240 250
CREPLVYDLA SLKAAPEPQQ PMELYQPSAE SLRQQEERKR LYQRQQERGG
260 270 280 290 300
IIDLEAERNR YFISLQQPPA PAEPESAVDV SKGSQPPSTL AAELSTSPAV
310 320 330 340 350
QSTLPPPLPV ATQHICEKIP GTRSNQQRLG ETQKAMLDPP KPSRGPWRQP
360 370 380 390 400
ERRHPKGGEC HAPKGTRDTQ ELPPPEGPLK EPMDLKPEPH SQGVEGPPQE
410 420 430 440 450
KGPGSWQGPP PRRTRDCVRW ERSKGRTPGS SYPRLPRGQG AYRPGTRRES

LGLESKDGS
Length:459
Mass (Da):51,219
Last modified:December 1, 2001 - v1
Checksum:iCE7C66EF2E988917
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti186H → R in BAD96245 (Ref. 2) Curated1
Sequence conflicti346P → S in BAD96245 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023968 mRNA. Translation: BAB14743.1.
AK289501 mRNA. Translation: BAF82190.1.
AK222525 mRNA. Translation: BAD96245.1.
AC009974 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70645.1.
BC015612 mRNA. Translation: AAH15612.1.
CCDSiCCDS2420.1.
RefSeqiNP_071898.2. NM_022453.2.
UniGeneiHs.471403.

Genome annotation databases

EnsembliENST00000295704; ENSP00000295704; ENSG00000163481.
GeneIDi64320.
KEGGihsa:64320.
UCSCiuc002vit.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023968 mRNA. Translation: BAB14743.1.
AK289501 mRNA. Translation: BAF82190.1.
AK222525 mRNA. Translation: BAD96245.1.
AC009974 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70645.1.
BC015612 mRNA. Translation: AAH15612.1.
CCDSiCCDS2420.1.
RefSeqiNP_071898.2. NM_022453.2.
UniGeneiHs.471403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DAYNMR-A11-125[»]
2DMFNMR-A11-134[»]
5D1KX-ray1.78B126-258[»]
5D1LX-ray1.62B126-258[»]
5D1MX-ray1.58B126-258[»]
ProteinModelPortaliQ96BH1.
SMRiQ96BH1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122133. 23 interactors.
DIPiDIP-29063N.
IntActiQ96BH1. 12 interactors.
STRINGi9606.ENSP00000295704.

PTM databases

iPTMnetiQ96BH1.
PhosphoSitePlusiQ96BH1.

Polymorphism and mutation databases

BioMutaiRNF25.
DMDMi21362899.

Proteomic databases

EPDiQ96BH1.
MaxQBiQ96BH1.
PaxDbiQ96BH1.
PeptideAtlasiQ96BH1.
PRIDEiQ96BH1.

Protocols and materials databases

DNASUi64320.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295704; ENSP00000295704; ENSG00000163481.
GeneIDi64320.
KEGGihsa:64320.
UCSCiuc002vit.4. human.

Organism-specific databases

CTDi64320.
GeneCardsiRNF25.
HGNCiHGNC:14662. RNF25.
HPAiHPA036420.
HPA036421.
MIMi616014. gene.
neXtProtiNX_Q96BH1.
OpenTargetsiENSG00000163481.
PharmGKBiPA34429.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4445. Eukaryota.
ENOG4111H5K. LUCA.
GeneTreeiENSGT00390000001557.
HOGENOMiHOG000012992.
HOVERGENiHBG055249.
InParanoidiQ96BH1.
KOiK10640.
OMAiVPQISIR.
OrthoDBiEOG091G0IBN.
PhylomeDBiQ96BH1.
TreeFamiTF324097.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000163481-MONOMER.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ96BH1.
GeneWikiiRNF25.
GenomeRNAii64320.
PROiQ96BH1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163481.
CleanExiHS_RNF25.
ExpressionAtlasiQ96BH1. baseline and differential.
GenevisibleiQ96BH1. HS.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR006575. RWD-domain.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00591. RWD. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50908. RWD. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNF25_HUMAN
AccessioniPrimary (citable) accession number: Q96BH1
Secondary accession number(s): A8K0D6, Q53HQ5, Q9H874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 138 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 2
    Human chromosome 2: 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.