ID   FAP20_BOVIN             Reviewed;         192 AA.
AC   A5PKK9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 73.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal brain;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI42526.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC142525; AAI42526.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001160036.1; NM_001166564.1.
DR   AlphaFoldDB; A5PKK9; -.
DR   SMR; A5PKK9; -.
DR   STRING; 9913.ENSBTAP00000018787; -.
DR   PaxDb; A5PKK9; -.
DR   GeneID; 508039; -.
DR   KEGG; bta:508039; -.
DR   CTD; 199990; -.
DR   eggNOG; ENOG502SE5R; Eukaryota.
DR   HOGENOM; CLU_122192_0_0_1; -.
DR   InParanoid; A5PKK9; -.
DR   OrthoDB; 1366450at2759; -.
DR   TreeFam; TF336358; -.
DR   Proteomes; UP000009136; Unplaced.
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: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   Chromosome; DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..192
FT                   /note="Fanconi anemia core complex-associated protein 20"
FT                   /id="PRO_0000316881"
FT   ZN_FING         156..192
FT                   /note="UBZ2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT   BINDING         182
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   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NZ36"
SQ   SEQUENCE   192 AA;  20654 MW;  C9C8AAA0DA8255C5 CRC64;
     MEATRRSRLS LSRRRPPLGV RPRSNTAGSL PDGGECAKLW TELLRTASAD LNVDGELPPL
     PAFPDQEPRR SPERPPPETF TVGTETFFWT PFPAPSPGRG GNSGGSDLVL SAVRGRTGSP
     QQYAAPELRG TPSAEEQPSE EQPSQRQSSV DGAMTLQSCP MCQVDFAPGL AQLDIDGHLA
     QCLADSTDDI EW