FAP20_MOUSE
ID FAP20_MOUSE Reviewed; 186 AA.
AC Q3UN58; A2ADD8; Q0VG17;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Liver;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UN58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UN58-2; Sequence=VSP_030817;
CC Name=3;
CC IsoId=Q3UN58-3; Sequence=VSP_030818;
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; AK144436; BAE25889.1; -; mRNA.
DR EMBL; AL670413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117034; AAI17035.1; -; mRNA.
DR EMBL; CA457860; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS57317.1; -. [Q3UN58-1]
DR CCDS; CCDS84835.1; -. [Q3UN58-3]
DR RefSeq; NP_001177374.1; NM_001190445.1. [Q3UN58-1]
DR RefSeq; NP_001334191.1; NM_001347262.1. [Q3UN58-3]
DR AlphaFoldDB; Q3UN58; -.
DR SMR; Q3UN58; -.
DR BioGRID; 212241; 1.
DR STRING; 10090.ENSMUSP00000095354; -.
DR iPTMnet; Q3UN58; -.
DR PhosphoSitePlus; Q3UN58; -.
DR jPOST; Q3UN58; -.
DR PaxDb; Q3UN58; -.
DR PRIDE; Q3UN58; -.
DR ProteomicsDB; 271868; -. [Q3UN58-1]
DR ProteomicsDB; 271869; -. [Q3UN58-2]
DR ProteomicsDB; 271870; -. [Q3UN58-3]
DR Antibodypedia; 52488; 60 antibodies from 14 providers.
DR Ensembl; ENSMUST00000097747; ENSMUSP00000095354; ENSMUSG00000073684. [Q3UN58-2]
DR Ensembl; ENSMUST00000105627; ENSMUSP00000101252; ENSMUSG00000073684. [Q3UN58-3]
DR Ensembl; ENSMUST00000178473; ENSMUSP00000137116; ENSMUSG00000073684. [Q3UN58-1]
DR GeneID; 67513; -.
DR KEGG; mmu:67513; -.
DR UCSC; uc008wda.2; mouse. [Q3UN58-1]
DR CTD; 199990; -.
DR MGI; MGI:1914763; Faap20.
DR VEuPathDB; HostDB:ENSMUSG00000073684; -.
DR eggNOG; ENOG502SE5R; Eukaryota.
DR GeneTree; ENSGT00390000010531; -.
DR HOGENOM; CLU_122192_0_0_1; -.
DR InParanoid; Q3UN58; -.
DR OMA; CARPWAE; -.
DR OrthoDB; 1366450at2759; -.
DR TreeFam; TF336358; -.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 67513; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Faap20; mouse.
DR PRO; PR:Q3UN58; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3UN58; protein.
DR Bgee; ENSMUSG00000073684; Expressed in ileal epithelium and 253 other tissues.
DR ExpressionAtlas; Q3UN58; baseline and differential.
DR Genevisible; Q3UN58; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Chromosome; DNA damage; DNA repair; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..186
FT /note="Fanconi anemia core complex-associated protein 20"
FT /id="PRO_0000316883"
FT ZN_FING 150..186
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 50..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 176
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"
FT VAR_SEQ 1..21
FT /note="MEEERRLRGRLSRRRPPAGGG -> MPRLTLPVLPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030817"
FT VAR_SEQ 22..34
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030818"
FT CONFLICT 184
FT /note="V -> M (in Ref. 3; CA457860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 20038 MW; AD88AF5A0BFD4FA3 CRC64;
MEEERRLRGR LSRRRPPAGG GPPNCRPWFL SEGSKSEPWA ALLRSTVSGT ADWTPNRQPL
PPLPAFPSQE SLPDPESTVP PEAFTVGSKT FSWTPLPPAL RGSGSSRHLF CEPEGSLGSP
TPSLKGCPAL NSGRTPSAQE CVPVQSPLAL LSCPLCQKAF DPKLTQLDVD SHLAQCLAEC
TEDVVW
