Entry euk:RN217_HUMAN

ID   RN217_HUMAN             Reviewed;         542 AA.
AC   Q8TC41; H7C5V4; Q5TCA4; Q9BX48;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 4.
DT   10-MAY-2017, entry version 118.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase RNF217;
DE            EC=2.3.2.- {ECO:0000250|UniProtKB:O60260};
DE   AltName: Full=IBR domain-containing protein 1;
DE   AltName: Full=RING finger protein 217;
GN   Name=RNF217; Synonyms=C6orf172, IBRDC1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       E2 ubiquitin-conjugating enzymes in the form of a thioester and
CC       then directly transfers the ubiquitin to targeted substrates.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC       enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC       conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC       protein]-L-lysine. {ECO:0000250|UniProtKB:O60260}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8TC41-1; Sequence=Displayed;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on partial mRNA and EST data.;
CC       Name=2;
CC         IsoId=Q8TC41-2; Sequence=VSP_054705, VSP_054706;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC       interact with the E2 conjugating enzyme UBE2L3 and function like
CC       HECT-type E3 enzymes: they bind E2s via the first RING domain, but
CC       require an obligate trans-thiolation step during the ubiquitin
CC       transfer, requiring a conserved cysteine residue in the second
CC       RING domain. {ECO:0000250|UniProtKB:O60260}.
CC   -!- SIMILARITY: Belongs to the RBR family. RNF217 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL136128; CAC36346.1; -; Genomic_DNA.
DR   EMBL; AL136128; CAI22999.1; -; Genomic_DNA.
DR   EMBL; AL355296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026087; AAH26087.1; -; mRNA.
DR   CCDS; CCDS5129.1; -. [Q8TC41-2]
DR   CCDS; CCDS69191.1; -. [Q8TC41-1]
DR   RefSeq; NP_001273327.1; NM_001286398.2. [Q8TC41-1]
DR   RefSeq; NP_689766.1; NM_152553.4. [Q8TC41-2]
DR   UniGene; Hs.12876; -.
DR   UniGene; Hs.368639; -.
DR   UniGene; Hs.656715; -.
DR   UniGene; Hs.661833; -.
DR   ProteinModelPortal; Q8TC41; -.
DR   BioGrid; 127540; 6.
DR   STRING; 9606.ENSP00000352734; -.
DR   iPTMnet; Q8TC41; -.
DR   PhosphoSitePlus; Q8TC41; -.
DR   DMDM; 313104196; -.
DR   EPD; Q8TC41; -.
DR   MaxQB; Q8TC41; -.
DR   PaxDb; Q8TC41; -.
DR   PeptideAtlas; Q8TC41; -.
DR   PRIDE; Q8TC41; -.
DR   Ensembl; ENST00000359704; ENSP00000352734; ENSG00000146373. [Q8TC41-2]
DR   Ensembl; ENST00000521654; ENSP00000428698; ENSG00000146373. [Q8TC41-1]
DR   GeneID; 154214; -.
DR   KEGG; hsa:154214; -.
DR   UCSC; uc003pzr.5; human. [Q8TC41-1]
DR   CTD; 154214; -.
DR   DisGeNET; 154214; -.
DR   GeneCards; RNF217; -.
DR   HGNC; HGNC:21487; RNF217.
DR   HPA; HPA029598; -.
DR   neXtProt; NX_Q8TC41; -.
DR   OpenTargets; ENSG00000146373; -.
DR   PharmGKB; PA162401868; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   eggNOG; ENOG410XP9Y; LUCA.
DR   GeneTree; ENSGT00730000111285; -.
DR   HOVERGEN; HBG096781; -.
DR   InParanoid; Q8TC41; -.
DR   KO; K11977; -.
DR   OrthoDB; EOG091G0R5I; -.
DR   TreeFam; TF330860; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   ChiTaRS; RNF217; human.
DR   GenomeRNAi; 154214; -.
DR   PRO; PR:Q8TC41; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000146373; -.
DR   CleanEx; HS_RNF217; -.
DR   ExpressionAtlas; Q8TC41; baseline and differential.
DR   Genevisible; Q8TC41; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   PANTHER; PTHR11685; PTHR11685; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Membrane; Metal-binding;
KW   Polymorphism; Reference proteome; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    542       Probable E3 ubiquitin-protein ligase
FT                                RNF217.
FT                                /FTId=PRO_0000084128.
FT   TRANSMEM    503    523       Helical. {ECO:0000255}.
FT   ZN_FING     263    308       RING-type; degenerate.
FT   ZN_FING     338    396       IBR-type 1.
FT   ZN_FING     416    457       IBR-type 2.
FT   ACT_SITE    436    436       {ECO:0000250|UniProtKB:Q9Y4X5}.
FT   VAR_SEQ       1    294       MGEEQSTVSGGGGPQESQTLASGTAGHPEPPRPQGDSARAP
FT                                PLRAASAEPSGGGCGSDWGCADTSAPEPARSLGPPGWSKSR
FT                                APAQPAGLALTGPLNPQTLPLQLELEEEEEEAGDRKEGGDE
FT                                QQEAPPGEELEPRTRVGAADGLVLDVLGQRRPSLAKRQVFC
FT                                SVYCVESDLPEAPASEQLSPPASPPGAPPVLNPPSTRSSFP
FT                                SPRLSLPTDSLSPDGGSIELEFYLAPEPFSMPSLLGAPPYS
FT                                GLGGVGDPYVPLMVLMCRVCLEDKPIKPLPCCKKAVCEECL
FT                                KVYLSAQ -> MK (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054705.
FT   VAR_SEQ     519    542       GLFVFPIYCLCKKQRKRSRTGMHW -> VEEIKTYWNLISG
FT                                RTRNQTQHLAPQPVLLSDMLYCLKQVFICISYLLPL (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054706.
FT   VARIANT     381    381       V -> I (in dbSNP:rs475076).
FT                                /FTId=VAR_024160.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       411    456       ipfam:IBR [T]
FT   MYHIT       328    396       ismart:IBR [T]
FT   MYHIT       340    396       ipfam:IBR [T]
FT   MYHIT       403    474       ismart:IBR [T]
SQ   SEQUENCE   542 AA;  59372 MW;  99A463D91873CC6E CRC64;
     MGEEQSTVSG GGGPQESQTL ASGTAGHPEP PRPQGDSARA PPLRAASAEP SGGGCGSDWG
     CADTSAPEPA RSLGPPGWSK SRAPAQPAGL ALTGPLNPQT LPLQLELEEE EEEAGDRKEG
     GDEQQEAPPG EELEPRTRVG AADGLVLDVL GQRRPSLAKR QVFCSVYCVE SDLPEAPASE
     QLSPPASPPG APPVLNPPST RSSFPSPRLS LPTDSLSPDG GSIELEFYLA PEPFSMPSLL
     GAPPYSGLGG VGDPYVPLMV LMCRVCLEDK PIKPLPCCKK AVCEECLKVY LSAQVQLGQV
     EIKCPITECF EFLEETTVVY NLTHEDSIKY KYFLELGRID SSTKPCPQCK HFTTFKKKGH
     IPTPSRSESK YKIQCPTCQF VWCFKCHSPW HEGVNCKEYK KGDKLLRHWA SEIEHGQRNA
     QKCPKCKIHI QRTEGCDHMT CSQCNTNFCY RCGERYRQLR FFGDHTSNLS IFGCKYRYLP
     ERPHLRRLVR GSVCAGKLFI APLIMVLGLA LGAIAVVIGL FVFPIYCLCK KQRKRSRTGM
     HW
//