PWP3A_RAT
ID PWP3A_RAT Reviewed; 698 AA.
AC B1H224;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=PWWP domain-containing DNA repair factor 3A {ECO:0000305};
DE Short=PWWP3A {ECO:0000305};
DE AltName: Full=Mutated melanoma-associated antigen 1;
DE Short=MUM-1;
DE AltName: Full=PWWP domain-containing protein MUM1;
GN Name=Pwwp3a {ECO:0000312|RGD:1308340};
GN Synonyms=Mum1 {ECO:0000312|RGD:1308340};
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 MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-168 AND SER-170, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the DNA damage response pathway by contributing
CC to the maintenance of chromatin architecture. Recruited to the vicinity
CC of DNA breaks by TP53BP1 and plays an accessory role to facilitate
CC damage-induced chromatin changes and promoting chromatin relaxation.
CC Required for efficient DNA repair and cell survival following DNA
CC damage (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TP53BP1 (via BRCT domain); the interaction is
CC not dependent on its phosphorylation status. Binds nucleosomes.
CC Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3) (in
CC vitro) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Recruited to DNA
CC damage sites via its interaction with the BRCT domain of TP53BP1.
CC {ECO:0000250}.
CC -!- DOMAIN: The PWWP domain mediates the interaction with nucleosomes.
CC -!- SIMILARITY: Belongs to the PWWP3A family. {ECO:0000305}.
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DR EMBL; BC160828; AAI60828.1; -; mRNA.
DR RefSeq; XP_006241035.1; XM_006240973.3.
DR RefSeq; XP_006241036.1; XM_006240974.3.
DR RefSeq; XP_006241037.1; XM_006240975.3.
DR AlphaFoldDB; B1H224; -.
DR SMR; B1H224; -.
DR STRING; 10116.ENSRNOP00000057438; -.
DR iPTMnet; B1H224; -.
DR PhosphoSitePlus; B1H224; -.
DR PaxDb; B1H224; -.
DR PRIDE; B1H224; -.
DR GeneID; 362838; -.
DR UCSC; RGD:1308340; rat.
DR CTD; 84939; -.
DR RGD; 1308340; Pwwp3a.
DR VEuPathDB; HostDB:ENSRNOG00000024549; -.
DR eggNOG; ENOG502QPRU; Eukaryota.
DR HOGENOM; CLU_388271_0_0_1; -.
DR InParanoid; B1H224; -.
DR OMA; AGMLVWC; -.
DR OrthoDB; 339225at2759; -.
DR PhylomeDB; B1H224; -.
DR TreeFam; TF328774; -.
DR PRO; PR:B1H224; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000024549; Expressed in testis and 19 other tissues.
DR Genevisible; B1H224; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR CDD; cd06080; MUM1_like; 1.
DR InterPro; IPR033368; MUM1.
DR InterPro; IPR035504; MUM1-like_PWWP.
DR InterPro; IPR040263; PWP3A/B.
DR PANTHER; PTHR31333; PTHR31333; 1.
DR PANTHER; PTHR31333:SF4; PTHR31333:SF4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..698
FT /note="PWWP domain-containing DNA repair factor 3A"
FT /id="PRO_0000375870"
FT DOMAIN 399..460
FT /note="PWWP"
FT REGION 102..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DID5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DID5"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DID5"
SQ SEQUENCE 698 AA; 77974 MW; 5F5E838911B971D5 CRC64;
MTDAKYVLCR WEKRLWPAKV LARTETSAKN KRKKEFFLDV QILSLKEKIQ VKSSAVEALQ
KSHIENIAAF LASQNEVPAT PLEELTYRRS LRVALDVLNE RTSLSPESHP VENGSTPSQK
GKPDADMASQ VSSAPSPSFL SEDDQAVAAQ CASKRRWECS PKSLSPLSAS EEDLRCKVDP
KTGLSESGAL GTEVPAPTGD ESQNGSGSQL DHGQESTTKK RQRNSGEKPA RRGKAESGLS
KGDSVAESGG QASSCVALAS PRLPSQTWEG DPCAGVEGCD PVESSGNIRP LLDSERSKGR
LTKRPRLDGG RNPLPRHLGT RTVGAVPSRR SCSGEVTTLR RAGDSDRPEE ADPMSSEEST
GFKSVHSLLE EEEEEEEEEE EEEEPPRILL YHEPRSFEVG MLVWLKYQKY PFWPAVVKSV
RRRDKKASVL FIEGNMNPKG RGITVSLRRL KHFDCKEKHA LLDRAKEDFA QAIGWCVSLI
TDYRVRLGCG SFAGSFLEYY AADISYPVRK SIQQDVLGTR FPQLGKGDPE EPMGDSRLGQ
WRPCRKVLPD RSRAARDKAN QKLVEYIVKA KGAESHLRAI LHSRKPSRWL KTFLSSNQYV
TCMETYLEDE AQLDEVVEYL QGVCRDMDGE MPARGSGDRI RFILDVLLPE AIICAISAVE
AVDYKTAEQK YLRGPTLSYR EKEIFDNELL EERNRRRR
