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Q5VTB9

- RN220_HUMAN

UniProt

Q5VTB9 - RN220_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF220

Gene
RNF220, C1orf164
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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-typeAdd
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
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 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
Complete GO annotation...

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.

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili485 – 51329 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri514 – 55340RING-typeAdd
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 239239Missing in isoform 2. VSP_055437Add
BLAST
Alternative sequencei331 – 3311Q → QVCPLCNRPLAGSEQEMSRH VEHCLSK in isoform 2. VSP_055438

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841A → V in AAH98300. 1 Publication
Sequence conflicti277 – 2771K → E in BAG51705. 1 Publication

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.
ENST00000361799; ENSP00000354872; ENSG00000187147.
ENST00000372247; ENSP00000361321; ENSG00000187147.
ENST00000443020; ENSP00000414640; ENSG00000187147.
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 .
ENST00000361799 ; ENSP00000354872 ; ENSG00000187147 .
ENST00000372247 ; ENSP00000361321 ; ENSG00000187147 .
ENST00000443020 ; ENSP00000414640 ; ENSG00000187147 .
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: September 3, 2014
This is version 99 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

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