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Protein

E3 ubiquitin-protein ligase RNF220

Gene

RNF220

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

Functioni

E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 promoting Wnt signaling (PubMed:25266658).By similarity1 Publication

Pathway: 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 fingeri514 – 55340RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • 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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25552. RNF220.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401886.

Polymorphism and mutation databases

BioMutaiRNF220.
DMDMi74756788.

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

BgeeiQ5VTB9.
CleanExiHS_RNF220.
ExpressionAtlasiQ5VTB9. baseline and differential.
GenevisibleiQ5VTB9. HS.

Organism-specific databases

HPAiHPA027578.

Interactioni

Subunit structurei

Interacts with SIN3B (By similarity). Interacts with CTNNB1 (via Armadillo repeats 2-8) (PubMed:25266658). Interacts with USP7 (via MATH domain) (PubMed:25266658).By similarity1 Publication

Protein-protein interaction databases

BioGridi120481. 8 interactions.
IntActiQ5VTB9. 6 interactions.
MINTiMINT-4826954.
STRINGi9606.ENSP00000347548.

Structurei

3D structure databases

ProteinModelPortaliQ5VTB9.
SMRiQ5VTB9. Positions 511-554.
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.
GeneTreeiENSGT00390000016573.
HOGENOMiHOG000293278.
HOVERGENiHBG055526.
InParanoidiQ5VTB9.
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. AlignAdd to basket

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

        10         20         30         40         50
MDLHRAAFKM ENSSYLPNPL ASPALMVLAS TAEASRDASI PCQQPRPFGV
60 70 80 90 100
PVSVDKDVHI PFTNGSYTFA SMYHRQGGVP GTFANRDFPP SLLHLHPQFA
110 120 130 140 150
PPNLDCTPIS MLNHSGVGAF RPFASTEDRE SYQSAFTPAK RLKNCHDTES
160 170 180 190 200
PHLRFSDADG KEYDFGTQLP SSSPGSLKVD DTGKKIFAVS GLISDREASS
210 220 230 240 250
SPEDRNDRCK KKAAALFDSQ APICPICQVL LRPSELQEHM EQELEQLAQL
260 270 280 290 300
PSSKNSLLKD AMAPGTPKSL LLSASIKREG ESPTASPHSS ATDDLHHSDR
310 320 330 340 350
YQTFLRVRAN RQTRLNARIG KMKRRKQDEG QREGSCMAED DAVDIEHENN
360 370 380 390 400
NRFEEYEWCG QKRIRATTLL EGGFRGSGFI MCSGKENPDS DADLDVDGDD
410 420 430 440 450
TLEYGKPQYT EADVIPCTGE EPGEAKEREA LRGAVLNGGP PSTRITPEFS
460 470 480 490 500
KWASDEMPST SNGESSKQEA MQKTCKNSDI EKITEDSAVT TFEALKARVR
510 520 530 540 550
ELERQLSRGD RYKCLICMDS YSMPLTSIQC WHVHCEECWL RTLGAKKLCP
560
QCNTITAPGD LRRIYL
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.Curated

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:
EMBLi
GenBanki
DDBJi
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. [Q5VTB9-1]
RefSeqiNP_060620.2. NM_018150.2. [Q5VTB9-1]
XP_005271051.1. XM_005270994.1. [Q5VTB9-1]
UniGeneiHs.456557.

Genome annotation databases

EnsembliENST00000355387; ENSP00000347548; ENSG00000187147. [Q5VTB9-1]
ENST00000361799; ENSP00000354872; ENSG00000187147. [Q5VTB9-1]
ENST00000372247; ENSP00000361321; ENSG00000187147. [Q5VTB9-1]
GeneIDi55182.
KEGGihsa:55182.
UCSCiuc001clv.1. human. [Q5VTB9-1]
uc010oky.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q5VTB9-1]
RefSeqiNP_060620.2. NM_018150.2. [Q5VTB9-1]
XP_005271051.1. XM_005270994.1. [Q5VTB9-1]
UniGeneiHs.456557.

3D structure databases

ProteinModelPortaliQ5VTB9.
SMRiQ5VTB9. Positions 511-554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120481. 8 interactions.
IntActiQ5VTB9. 6 interactions.
MINTiMINT-4826954.
STRINGi9606.ENSP00000347548.

PTM databases

PhosphoSiteiQ5VTB9.

Polymorphism and mutation databases

BioMutaiRNF220.
DMDMi74756788.

Proteomic databases

MaxQBiQ5VTB9.
PaxDbiQ5VTB9.
PRIDEiQ5VTB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355387; ENSP00000347548; ENSG00000187147. [Q5VTB9-1]
ENST00000361799; ENSP00000354872; ENSG00000187147. [Q5VTB9-1]
ENST00000372247; ENSP00000361321; ENSG00000187147. [Q5VTB9-1]
GeneIDi55182.
KEGGihsa:55182.
UCSCiuc001clv.1. human. [Q5VTB9-1]
uc010oky.1. human.

Organism-specific databases

CTDi55182.
GeneCardsiGC01P044870.
H-InvDBHIX0000517.
HGNCiHGNC:25552. RNF220.
HPAiHPA027578.
MIMi616136. gene.
neXtProtiNX_Q5VTB9.
PharmGKBiPA162401886.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43032.
GeneTreeiENSGT00390000016573.
HOGENOMiHOG000293278.
HOVERGENiHBG055526.
InParanoidiQ5VTB9.
OMAiPYLPNPL.
OrthoDBiEOG7RFTJ2.
PhylomeDBiQ5VTB9.
TreeFamiTF324716.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiRNF220. human.
GeneWikiiRNF220.
GenomeRNAii55182.
NextBioi35473180.
PROiQ5VTB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VTB9.
CleanExiHS_RNF220.
ExpressionAtlasiQ5VTB9. baseline and differential.
GenevisibleiQ5VTB9. HS.

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]
ProtoNetiSearch...

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] (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].
  7. "The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7-mediated deubiquitination of beta-catenin."
    Ma P., Yang X., Kong Q., Li C., Yang S., Li Y., Mao B.
    Mol. Cell. Biol. 34:4355-4366(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNB1 AND USP7, FUNCTION.

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: June 24, 2015
This is version 108 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.