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Q96BH1

- RNF25_HUMAN

UniProt

Q96BH1 - RNF25_HUMAN

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
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri135 – 20268RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. NF-kappaB binding Source: UniProtKB
    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

    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

    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 RNF25PRO_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.By similarity1 Publication

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    459
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96BH1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 128111RWDPROSITE-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 fingeri135 – 20268RING-typePROSITE-ProRule annotationAdd
    BLAST

    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 119 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