PAF15_BOVIN
ID PAF15_BOVIN Reviewed; 111 AA.
AC Q5E9B2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=PCNA-associated factor {ECO:0000250|UniProtKB:Q15004};
DE AltName: Full=PCNA-associated factor of 15 kDa;
DE Short=PAF15;
DE Short=p15PAF;
DE AltName: Full=PCNA-clamp-associated factor {ECO:0000250|UniProtKB:Q15004};
GN Name=PCLAF {ECO:0000250|UniProtKB:Q15004}; Synonyms=PAF;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PCNA-binding protein that acts as a regulator of DNA repair
CC during DNA replication. Following DNA damage, the interaction with PCNA
CC is disrupted, facilitating the interaction between monoubiquitinated
CC PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at
CC stalled replisomes, facilitating the bypass of replication-fork-
CC blocking lesions. Also acts as a regulator of centrosome number (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (when monoubiquitinated at Lys-15 and Lys-24) with
CC PCNA. Interacts with isoform 2/p33ING1b of ING1. Interacts with BRCA1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15004}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}.
CC Note=Following DNA damage, localizes to DNA damage sites. Colocalizes
CC with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA. {ECO:0000250}.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C
CC complex. {ECO:0000250}.
CC -!- DOMAIN: The D-box (destruction box) mediates the interaction with APC/C
CC proteins, and acts as a recognition signal for degradation via the
CC ubiquitin-proteasome pathway. {ECO:0000250}.
CC -!- DOMAIN: The initiation motif is required for efficient chain initiation
CC by the APC/C complex E2 ligase UBE2C. It determines the rate of
CC substrate's degradation without affecting its affinity for the APC/C, a
CC mechanism used by the APC/C to control the timing of substrate
CC proteolysis during the cell cycle (By similarity). {ECO:0000250}.
CC -!- PTM: Monoubiquitinated at Lys-15 and Lys-24 during normal S phase,
CC promoting its association with PCNA. Also diubiquitinated at these 2
CC sites. Following DNA damage, monoubiquitin chains at Lys-15 and Lys-24
CC are probably extended, leading to disrupt the interaction with PCNA.
CC Polyubiquitinated by the APC/C complex at the mitotic exit, leading to
CC its degradation by the proteasome (By similarity). {ECO:0000250}.
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DR EMBL; BT021008; AAX09025.1; -; mRNA.
DR EMBL; BC102403; AAI02404.1; -; mRNA.
DR RefSeq; NP_001015678.1; NM_001015678.2.
DR AlphaFoldDB; Q5E9B2; -.
DR STRING; 9913.ENSBTAP00000051194; -.
DR PaxDb; Q5E9B2; -.
DR PRIDE; Q5E9B2; -.
DR Ensembl; ENSBTAT00000054209; ENSBTAP00000051194; ENSBTAG00000039462.
DR GeneID; 540737; -.
DR KEGG; bta:540737; -.
DR CTD; 9768; -.
DR VEuPathDB; HostDB:ENSBTAG00000039462; -.
DR eggNOG; ENOG502S3UM; Eukaryota.
DR GeneTree; ENSGT00510000048252; -.
DR HOGENOM; CLU_142343_0_0_1; -.
DR InParanoid; Q5E9B2; -.
DR OMA; QPDHTDE; -.
DR OrthoDB; 1508906at2759; -.
DR TreeFam; TF333199; -.
DR Reactome; R-BTA-5656169; Termination of translesion DNA synthesis.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000039462; Expressed in pharyngeal tonsil and 96 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR InterPro; IPR040444; PCNA-AF.
DR InterPro; IPR031444; PCNA-AF_dom.
DR PANTHER; PTHR15679; PTHR15679; 1.
DR Pfam; PF15715; PAF; 1.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; DNA damage; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..111
FT /note="PCNA-associated factor"
FT /id="PRO_0000284064"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..34
FT /note="D-box"
FT MOTIF 62..72
FT /note="PIP-box"
FT MOTIF 78..80
FT /note="KEN box"
FT MOTIF 85..97
FT /note="Initiation motif"
FT COMPBIAS 24..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQX4"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15004"
SQ SEQUENCE 111 AA; 11910 MW; EB7C386504164148 CRC64;
MVRTKANSVP GSYRKVVASR APRKVLGSST SAANSTPLSS RKAENKYAGG NPVCVRPTPK
WQKGIGEFFS LSPKDSEKEN RIPEEAGSSG LGKAKRKACP LPPDHTDDEK E
