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Q5VTB9

- RN220_HUMAN

UniProt

Q5VTB9 - RN220_HUMAN

Protein

E3 ubiquitin-protein ligase RNF220

Gene

RNF220

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B.By similarity

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri514 – 55340RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein autoubiquitination 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 RNF220 (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 220
    Gene namesi
    Name:RNF220
    Synonyms:C1orf164
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25552. RNF220.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162401886.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 566566E3 ubiquitin-protein ligase RNF220PRO_0000277657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei390 – 3901Phosphoserine1 Publication

    Post-translational modificationi

    Auto-ubiquitinated; leads to proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ5VTB9.
    PaxDbiQ5VTB9.
    PRIDEiQ5VTB9.

    PTM databases

    PhosphoSiteiQ5VTB9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5VTB9.
    BgeeiQ5VTB9.
    CleanExiHS_RNF220.
    GenevestigatoriQ5VTB9.

    Organism-specific databases

    HPAiHPA027578.
    HPA054358.

    Interactioni

    Subunit structurei

    Interacts with SIN3B.By similarity

    Protein-protein interaction databases

    BioGridi120481. 4 interactions.
    IntActiQ5VTB9. 6 interactions.
    MINTiMINT-4826954.
    STRINGi9606.ENSP00000347548.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5VTB9.
    SMRiQ5VTB9. Positions 512-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni514 – 5229Required for targeting to the cytoplasmBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili485 – 51329Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri514 – 55340RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG43032.
    HOGENOMiHOG000293278.
    HOVERGENiHBG055526.
    OMAiPYLPNPL.
    OrthoDBiEOG7RFTJ2.
    PhylomeDBiQ5VTB9.
    TreeFamiTF324716.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5VTB9-1) [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

    MDLHRAAFKM ENSSYLPNPL ASPALMVLAS TAEASRDASI PCQQPRPFGV    50
    PVSVDKDVHI PFTNGSYTFA SMYHRQGGVP GTFANRDFPP SLLHLHPQFA 100
    PPNLDCTPIS MLNHSGVGAF RPFASTEDRE SYQSAFTPAK RLKNCHDTES 150
    PHLRFSDADG KEYDFGTQLP SSSPGSLKVD DTGKKIFAVS GLISDREASS 200
    SPEDRNDRCK KKAAALFDSQ APICPICQVL LRPSELQEHM EQELEQLAQL 250
    PSSKNSLLKD AMAPGTPKSL LLSASIKREG ESPTASPHSS ATDDLHHSDR 300
    YQTFLRVRAN RQTRLNARIG KMKRRKQDEG QREGSCMAED DAVDIEHENN 350
    NRFEEYEWCG QKRIRATTLL EGGFRGSGFI MCSGKENPDS DADLDVDGDD 400
    TLEYGKPQYT EADVIPCTGE EPGEAKEREA LRGAVLNGGP PSTRITPEFS 450
    KWASDEMPST SNGESSKQEA MQKTCKNSDI EKITEDSAVT TFEALKARVR 500
    ELERQLSRGD RYKCLICMDS YSMPLTSIQC WHVHCEECWL RTLGAKKLCP 550
    QCNTITAPGD LRRIYL 566
    Length:566
    Mass (Da):62,765
    Last modified:December 7, 2004 - v1
    Checksum:iAAE3C723032B062B
    GO
    Isoform 2 (identifier: Q5VTB9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-239: Missing.
         331-331: Q → QVCPLCNRPLAGSEQEMSRHVEHCLSK

    Note: No experimental confirmation available.

    Show »
    Length:353
    Mass (Da):39,570
    Checksum:i9014236EFCF08F29
    GO

    Sequence cautioni

    The sequence BAA91704.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841A → V in AAH98300. (PubMed:15489334)Curated
    Sequence conflicti277 – 2771K → E in BAG51705. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 239239Missing in isoform 2. 1 PublicationVSP_055437Add
    BLAST
    Alternative sequencei331 – 3311Q → QVCPLCNRPLAGSEQEMSRH VEHCLSK in isoform 2. 1 PublicationVSP_055438

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001459 mRNA. Translation: BAA91704.1. Different initiation.
    AK056424 mRNA. Translation: BAG51705.1.
    AK297228 mRNA. Translation: BAG59711.1.
    AL596225, AL122004, AL359373 Genomic DNA. Translation: CAH72320.1.
    AL359373, AL122004, AL596225 Genomic DNA. Translation: CAI16124.1.
    AL122004, AL359373, AL596225 Genomic DNA. Translation: CAI22343.1.
    BC034221 mRNA. Translation: AAH34221.1.
    BC098266 mRNA. Translation: AAH98266.1.
    BC098300 mRNA. Translation: AAH98300.1.
    CCDSiCCDS510.1.
    RefSeqiNP_060620.2. NM_018150.2.
    XP_005271051.1. XM_005270994.1.
    UniGeneiHs.456557.

    Genome annotation databases

    EnsembliENST00000355387; ENSP00000347548; ENSG00000187147. [Q5VTB9-1]
    ENST00000361799; ENSP00000354872; ENSG00000187147. [Q5VTB9-1]
    ENST00000372247; ENSP00000361321; ENSG00000187147. [Q5VTB9-1]
    ENST00000443020; ENSP00000414640; ENSG00000187147. [Q5VTB9-3]
    GeneIDi55182.
    KEGGihsa:55182.
    UCSCiuc001clv.1. human.

    Polymorphism databases

    DMDMi74756788.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001459 mRNA. Translation: BAA91704.1 . Different initiation.
    AK056424 mRNA. Translation: BAG51705.1 .
    AK297228 mRNA. Translation: BAG59711.1 .
    AL596225 , AL122004 , AL359373 Genomic DNA. Translation: CAH72320.1 .
    AL359373 , AL122004 , AL596225 Genomic DNA. Translation: CAI16124.1 .
    AL122004 , AL359373 , AL596225 Genomic DNA. Translation: CAI22343.1 .
    BC034221 mRNA. Translation: AAH34221.1 .
    BC098266 mRNA. Translation: AAH98266.1 .
    BC098300 mRNA. Translation: AAH98300.1 .
    CCDSi CCDS510.1.
    RefSeqi NP_060620.2. NM_018150.2.
    XP_005271051.1. XM_005270994.1.
    UniGenei Hs.456557.

    3D structure databases

    ProteinModelPortali Q5VTB9.
    SMRi Q5VTB9. Positions 512-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120481. 4 interactions.
    IntActi Q5VTB9. 6 interactions.
    MINTi MINT-4826954.
    STRINGi 9606.ENSP00000347548.

    PTM databases

    PhosphoSitei Q5VTB9.

    Polymorphism databases

    DMDMi 74756788.

    Proteomic databases

    MaxQBi Q5VTB9.
    PaxDbi Q5VTB9.
    PRIDEi Q5VTB9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355387 ; ENSP00000347548 ; ENSG00000187147 . [Q5VTB9-1 ]
    ENST00000361799 ; ENSP00000354872 ; ENSG00000187147 . [Q5VTB9-1 ]
    ENST00000372247 ; ENSP00000361321 ; ENSG00000187147 . [Q5VTB9-1 ]
    ENST00000443020 ; ENSP00000414640 ; ENSG00000187147 . [Q5VTB9-3 ]
    GeneIDi 55182.
    KEGGi hsa:55182.
    UCSCi uc001clv.1. human.

    Organism-specific databases

    CTDi 55182.
    GeneCardsi GC01P044870.
    H-InvDB HIX0000517.
    HGNCi HGNC:25552. RNF220.
    HPAi HPA027578.
    HPA054358.
    neXtProti NX_Q5VTB9.
    PharmGKBi PA162401886.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43032.
    HOGENOMi HOG000293278.
    HOVERGENi HBG055526.
    OMAi PYLPNPL.
    OrthoDBi EOG7RFTJ2.
    PhylomeDBi Q5VTB9.
    TreeFami TF324716.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi RNF220. human.
    GeneWikii RNF220.
    GenomeRNAii 55182.
    NextBioi 59011.
    PROi Q5VTB9.

    Gene expression databases

    ArrayExpressi Q5VTB9.
    Bgeei Q5VTB9.
    CleanExi HS_RNF220.
    Genevestigatori Q5VTB9.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi 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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Brain.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRN220_HUMAN
    AccessioniPrimary (citable) accession number: Q5VTB9
    Secondary accession number(s): B3KPJ3
    , B4DLZ9, E9PCS1, Q4KMX2, Q9NVP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 100 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3