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Q96BH1

- RNF25_HUMAN

UniProt

Q96BH1 - RNF25_HUMAN

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Protein
E3 ubiquitin-protein ligase RNF25
Gene
RNF25
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri135 – 20268RING-type
Add
BLAST

GO - Molecular functioni

  1. NF-kappaB binding Source: UniProtKB
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  2. protein ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. 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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:14662. RNF25.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591C → S: Reduced activation of NF-kappa-B. 1 Publication
Mutagenesisi161 – 1611C → S: Strongly reduced activation of NF-kappa-B. 1 Publication

Organism-specific databases

PharmGKBiPA34429.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459E3 ubiquitin-protein ligase RNF25
PRO_0000056066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei450 – 4501Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96BH1.
PaxDbiQ96BH1.
PRIDEiQ96BH1.

PTM databases

PhosphoSiteiQ96BH1.

Expressioni

Gene expression databases

ArrayExpressiQ96BH1.
BgeeiQ96BH1.
CleanExiHS_RNF25.
GenevestigatoriQ96BH1.

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.1 Publication

Protein-protein interaction databases

BioGridi122133. 14 interactions.
DIPiDIP-29063N.
IntActiQ96BH1. 10 interactions.
STRINGi9606.ENSP00000295704.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2612
Turni28 – 303
Beta strandi31 – 344
Turni38 – 403
Beta strandi43 – 497
Beta strandi55 – 584
Beta strandi63 – 708
Beta strandi80 – 8910
Helixi91 – 10717
Turni108 – 1103
Helixi114 – 12512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAYNMR-A11-125[»]
2DMFNMR-A11-134[»]
ProteinModelPortaliQ96BH1.
SMRiQ96BH1. Positions 5-134.

Miscellaneous databases

EvolutionaryTraceiQ96BH1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 128111RWD
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 RWD domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG243985.
HOGENOMiHOG000012992.
HOVERGENiHBG055249.
InParanoidiQ96BH1.
KOiK10640.
OMAiVPQISIR.
OrthoDBiEOG7HXCRM.
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.
PF13639. zf-RING_2. 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

MAASASAAAG EEDWVLPSEV EVLESIYLDE LQVIKGNGRT SPWEIYITLH    50
PATAEDQDSQ YVCFTLVLQV PAEYPHEVPQ ISIRNPRGLS DEQIHTILQV 100
LGHVAKAGLG TAMLYELIEK GKEILTDNNI PHGQCVICLY GFQEKEAFTK 150
TPCYHYFHCH CLARYIQHME QELKAQGQEQ EQERQHATTK QKAVGVQCPV 200
CREPLVYDLA SLKAAPEPQQ PMELYQPSAE SLRQQEERKR LYQRQQERGG 250
IIDLEAERNR YFISLQQPPA PAEPESAVDV SKGSQPPSTL AAELSTSPAV 300
QSTLPPPLPV ATQHICEKIP GTRSNQQRLG ETQKAMLDPP KPSRGPWRQP 350
ERRHPKGGEC HAPKGTRDTQ ELPPPEGPLK EPMDLKPEPH SQGVEGPPQE 400
KGPGSWQGPP PRRTRDCVRW ERSKGRTPGS SYPRLPRGQG AYRPGTRRES 450
LGLESKDGS 459
Length:459
Mass (Da):51,219
Last modified:December 1, 2001 - v1
Checksum:iCE7C66EF2E988917
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861H → R in BAD96245. 1 Publication
Sequence conflicti346 – 3461P → S in BAD96245. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi21362899.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2420.1.
RefSeqi NP_071898.2. NM_022453.2.
UniGenei Hs.471403.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DAY NMR - A 11-125 [» ]
2DMF NMR - A 11-134 [» ]
ProteinModelPortali Q96BH1.
SMRi Q96BH1. Positions 5-134.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122133. 14 interactions.
DIPi DIP-29063N.
IntActi Q96BH1. 10 interactions.
STRINGi 9606.ENSP00000295704.

PTM databases

PhosphoSitei Q96BH1.

Polymorphism databases

DMDMi 21362899.

Proteomic databases

MaxQBi Q96BH1.
PaxDbi Q96BH1.
PRIDEi Q96BH1.

Protocols and materials databases

DNASUi 64320.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295704 ; ENSP00000295704 ; ENSG00000163481 .
GeneIDi 64320.
KEGGi hsa:64320.
UCSCi uc002vit.3. human.

Organism-specific databases

CTDi 64320.
GeneCardsi GC02M219528.
HGNCi HGNC:14662. RNF25.
HPAi HPA036420.
HPA036421.
neXtProti NX_Q96BH1.
PharmGKBi PA34429.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243985.
HOGENOMi HOG000012992.
HOVERGENi HBG055249.
InParanoidi Q96BH1.
KOi K10640.
OMAi VPQISIR.
OrthoDBi EOG7HXCRM.
PhylomeDBi Q96BH1.
TreeFami TF324097.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTracei Q96BH1.
GeneWikii RNF25.
GenomeRNAii 64320.
NextBioi 66233.
PROi Q96BH1.

Gene expression databases

ArrayExpressi Q96BH1.
Bgeei Q96BH1.
CleanExi HS_RNF25.
Genevestigatori Q96BH1.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR006575. RWD-domain.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF05773. RWD. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
SM00591. RWD. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS50908. RWD. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Placenta.
  6. "RING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunit."
    Asamitsu K., Tetsuka T., Kanazawa S., Okamoto T.
    J. Biol. Chem. 278:26879-26887(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RELA, MUTAGENESIS OF CYS-159 AND CYS-161.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An extended conformation of the RWD domain of human RING finger protein 25."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 10-134.

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: September 3, 2014
This is version 118 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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