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Protein

E3 ubiquitin-protein ligase RNF25

Gene

Rnf25

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 mediates ubiquitination and subsequent proteasomal degradation of NKD2. Stimulates transcription mediated by NF-kappa-B (By similarity).By similarity2 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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri134 – 19966RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • NF-kappaB binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

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

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF25 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 25
RING finger protein AO7
Gene namesi
Name:Rnf25
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1890215. Rnf25.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi134 – 1341C → S: No E2 binding. Loss of ubiquitination activity. 1 Publication
Mutagenesisi137 – 1371C → S: No E2 binding. Loss of ubiquitination activity. 1 Publication
Mutagenesisi152 – 1521C → S: No E2 binding. Loss of ubiquitination activity. 1 Publication
Mutagenesisi157 – 1571H → C: No E2 binding. Loss of ubiquitination activity. 1 Publication
Mutagenesisi158 – 1581C → S: No E2 binding. Loss of ubiquitination activity. 1 Publication
Mutagenesisi160 – 1601C → S: No E2 binding. Loss of ubiquitination activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456E3 ubiquitin-protein ligase RNF25PRO_0000056067Add
BLAST

Post-translational modificationi

Ubiquitinated.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9QZR0.
MaxQBiQ9QZR0.
PaxDbiQ9QZR0.
PRIDEiQ9QZR0.

PTM databases

iPTMnetiQ9QZR0.
PhosphoSiteiQ9QZR0.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9QZR0.
CleanExiMM_RNF25.
ExpressionAtlasiQ9QZR0. baseline and differential.
GenevisibleiQ9QZR0. MM.

Interactioni

Subunit structurei

Interacts with UBE2D2, and may also interact with UBE2E1 and UBE2E3. Interacts with RELA (By similarity). Interacts with NKD2.By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208313. 5 interactions.
STRINGi10090.ENSMUSP00000027357.

Structurei

3D structure databases

ProteinModelPortaliQ9QZR0.
SMRiQ9QZR0. Positions 5-133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 127110RWDPROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri134 – 19966RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4445. Eukaryota.
ENOG4111H5K. LUCA.
GeneTreeiENSGT00390000001557.
HOGENOMiHOG000012992.
HOVERGENiHBG055249.
InParanoidiQ9QZR0.
KOiK10640.
OMAiVPQISIR.
PhylomeDBiQ9QZR0.
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.

Q9QZR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASASTAAG EEDWVLPSEV EVLESIYLDE LQVMKGNGRS PWEIFITLHP
60 70 80 90 100
ATAEVQDSQF VCFTLVLRIP VQYPHEVPQI SIRNPRGLSD EQIHKISQAL
110 120 130 140 150
GHVAKEGLGT AMLYELIEKG KEILTDNNIP HGQCVICLYG FQEKEAFTKT
160 170 180 190 200
PCYHYFHCHC LARYIQHMEQ ELTTQEQEQE RQHVVTKQKA VGVQCPVCRE
210 220 230 240 250
PLVYDLASLK AAPEPQQPME LYQPSAESLR QQEELKLLYQ RQQEKGGIID
260 270 280 290 300
LEAERNRYFI SLQQPPAALE PESAVDVSRE PQPPNALSAE QSTSLADQST
310 320 330 340 350
LPTSLPMTTQ YTYEKTSGAG PNQQRPGETQ KSVLDPPRHG RGSWRQYDRR
360 370 380 390 400
HPKGGECCTP KGTSEIHELP PPEKPLKETV DLKAEPRNKG LTGHPQEKGP
410 420 430 440 450
GSWQGPSARR TRDCARWERS KNRTPGSCYP HLPRGQGAYR SGTRREPLGL

ESEEGS
Length:456
Mass (Da):51,227
Last modified:June 6, 2002 - v2
Checksum:i75FA1351F8E9C4E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1832QH → HD in AAD48057 (PubMed:10500182).Curated
Sequence conflicti244 – 2441E → K in BAB22071 (PubMed:16141072).Curated
Sequence conflicti445 – 4451R → G in BAB22071 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171060 mRNA. Translation: AAD48057.1.
AK002399 mRNA. Translation: BAB22071.1.
AK171752 mRNA. Translation: BAE42650.1.
BC022715 mRNA. Translation: AAH22715.1.
BC048821 mRNA. Translation: AAH48821.1.
CCDSiCCDS15052.1.
RefSeqiNP_001292159.1. NM_001305230.1.
NP_067288.2. NM_021313.3.
UniGeneiMm.280920.
Mm.448381.

Genome annotation databases

EnsembliENSMUST00000027357; ENSMUSP00000027357; ENSMUSG00000026171.
GeneIDi57751.
KEGGimmu:57751.
UCSCiuc007bms.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171060 mRNA. Translation: AAD48057.1.
AK002399 mRNA. Translation: BAB22071.1.
AK171752 mRNA. Translation: BAE42650.1.
BC022715 mRNA. Translation: AAH22715.1.
BC048821 mRNA. Translation: AAH48821.1.
CCDSiCCDS15052.1.
RefSeqiNP_001292159.1. NM_001305230.1.
NP_067288.2. NM_021313.3.
UniGeneiMm.280920.
Mm.448381.

3D structure databases

ProteinModelPortaliQ9QZR0.
SMRiQ9QZR0. Positions 5-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208313. 5 interactions.
STRINGi10090.ENSMUSP00000027357.

PTM databases

iPTMnetiQ9QZR0.
PhosphoSiteiQ9QZR0.

Proteomic databases

EPDiQ9QZR0.
MaxQBiQ9QZR0.
PaxDbiQ9QZR0.
PRIDEiQ9QZR0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027357; ENSMUSP00000027357; ENSMUSG00000026171.
GeneIDi57751.
KEGGimmu:57751.
UCSCiuc007bms.3. mouse.

Organism-specific databases

CTDi64320.
MGIiMGI:1890215. Rnf25.

Phylogenomic databases

eggNOGiKOG4445. Eukaryota.
ENOG4111H5K. LUCA.
GeneTreeiENSGT00390000001557.
HOGENOMiHOG000012992.
HOVERGENiHBG055249.
InParanoidiQ9QZR0.
KOiK10640.
OMAiVPQISIR.
PhylomeDBiQ9QZR0.
TreeFamiTF324097.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ9QZR0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZR0.
CleanExiMM_RNF25.
ExpressionAtlasiQ9QZR0. baseline and differential.
GenevisibleiQ9QZR0. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination."
    Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-134; CYS-137; CYS-152; HIS-157; CYS-158 AND CYS-160, INTERACTION WITH UBE2D2; UBE2E1 AND UBE2E3, UBIQUITINATION, TISSUE SPECIFICITY.
    Tissue: T-cell lymphoma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Kidney and Spleen.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "EGF receptor-independent action of TGF-alpha protects Naked2 from AO7-mediated ubiquitylation and proteasomal degradation."
    Ding W., Li C., Hu T., Graves-Deal R., Fotia A.B., Weissman A.M., Coffey R.J.
    Proc. Natl. Acad. Sci. U.S.A. 105:13433-13438(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NKD2.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiRNF25_MOUSE
AccessioniPrimary (citable) accession number: Q9QZR0
Secondary accession number(s): Q3TAL8, Q9DCW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 6, 2002
Last modified: June 8, 2016
This is version 126 of the entry and version 2 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.