FAP20_RAT
ID FAP20_RAT Reviewed; 184 AA.
AC D4AAA5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Fanconi anemia core complex-associated protein 20 {ECO:0000250|UniProtKB:Q6NZ36};
DE AltName: Full=FANCA-associated protein of 20 kDa {ECO:0000250|UniProtKB:Q6NZ36};
DE AltName: Full=Fanconi anemia-associated protein of 20 kDa {ECO:0000250|UniProtKB:Q6NZ36};
GN Name=Faap20 {ECO:0000250|UniProtKB:Q6NZ36};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Fanconi anemia (FA) complex required to
CC recruit the FA complex to DNA interstrand cross-links (ICLs) and
CC promote ICLs repair. Following DNA damage recognizes and binds 'Lys-
CC 63'-linked ubiquitin generated by RNF8 at ICLs and recruits other
CC components of the FA complex. Promotes translesion synthesis via
CC interaction with REV1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Fanconi anemia (FA) complex. Interacts with
CC FANCA; interaction is direct. Interacts with REV1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6NZ36}.
CC Chromosome {ECO:0000250|UniProtKB:Q6NZ36}. Note=Following DNA damage,
CC recruited to DNA interstrand cross-links (ICLs) sites by binding to
CC ubiquitin generated by RNF8. {ECO:0000250|UniProtKB:Q6NZ36}.
CC -!- DOMAIN: The UBZ2-type zinc finger binds both 'Lys-48'- and 'Lys-63'-
CC linked polyubiquitin with preference for 'Lys-63'-linked polyubiquitin.
CC {ECO:0000255|PROSITE-ProRule:PRU01254}.
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DR EMBL; CH473968; EDL81292.1; -; Genomic_DNA.
DR RefSeq; NP_001102168.1; NM_001108698.1.
DR AlphaFoldDB; D4AAA5; -.
DR SMR; D4AAA5; -.
DR STRING; 10116.ENSRNOP00000052229; -.
DR PaxDb; D4AAA5; -.
DR Ensembl; ENSRNOT00000055361; ENSRNOP00000052229; ENSRNOG00000036876.
DR GeneID; 362678; -.
DR KEGG; rno:362678; -.
DR CTD; 199990; -.
DR RGD; 1308923; Faap20.
DR eggNOG; ENOG502SE5R; Eukaryota.
DR GeneTree; ENSGT00390000010531; -.
DR HOGENOM; CLU_122192_0_0_1; -.
DR InParanoid; D4AAA5; -.
DR OMA; CARPWAE; -.
DR OrthoDB; 1366450at2759; -.
DR PhylomeDB; D4AAA5; -.
DR TreeFam; TF336358; -.
DR Reactome; R-RNO-6783310; Fanconi Anemia Pathway.
DR PRO; PR:D4AAA5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000036876; Expressed in pancreas and 19 other tissues.
DR Genevisible; D4AAA5; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0140036; F:ubiquitin-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:RGD.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR InterPro; IPR031491; FANCA_interact.
DR InterPro; IPR031490; UBZ2_FAAP20.
DR Pfam; PF15751; FANCA_interact; 1.
DR Pfam; PF15750; UBZ_FAAP20; 1.
DR PROSITE; PS51906; ZF_UBZ2; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..184
FT /note="Fanconi anemia core complex-associated protein 20"
FT /id="PRO_0000419699"
FT ZN_FING 148..184
FT /note="UBZ2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZ36"
SQ SEQUENCE 184 AA; 20005 MW; 6D1541DAD9114AFB CRC64;
MEEERRLRGR LSRRRPPAGG GPPNCRPWFL SEESKSEPWA ALLRSTVGGN TDWTPNSQPL
PPLPAFPSQE SLPDPESTVP PEVFTVGSKT FSWTPFPPAL RGSGSSCRLL RCPEGSPGSP
APSLKGCPAL DSRQTPSTQE CVQSQLVLLN CPLCQKAFDP KLTQLDVDSH LAQCLAESTE
DVVW
