PWP3A_MOUSE
ID PWP3A_MOUSE Reviewed; 682 AA.
AC Q6DID5; Q3TCZ4; Q6NST9; Q8C5E3; Q8R1V6; Q9R1R7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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; Synonyms=Mum1 {ECO:0000312|MGI:MGI:1915364};
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis, and Visual cortex;
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 MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Eye, and Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 276-682.
RC STRAIN=CD-1; TISSUE=Testis;
RA Goto M., Eddy E.M.;
RT "Ubiquitously expressing genes.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-345 AND SER-346, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23031.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA82658.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC37397.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 5'-end.; Evidence={ECO:0000305};
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DR EMBL; AK078792; BAC37397.1; ALT_SEQ; mRNA.
DR EMBL; AK158750; BAE34640.1; -; mRNA.
DR EMBL; AK170459; BAE41811.1; -; mRNA.
DR EMBL; BC023031; AAH23031.1; ALT_INIT; mRNA.
DR EMBL; BC069883; AAH69883.1; -; mRNA.
DR EMBL; BC075617; AAH75617.1; -; mRNA.
DR EMBL; AB030505; BAA82658.1; ALT_FRAME; mRNA.
DR CCDS; CCDS24014.1; -.
DR RefSeq; NP_075920.4; NM_023431.5.
DR RefSeq; XP_006514088.1; XM_006514025.2.
DR AlphaFoldDB; Q6DID5; -.
DR SMR; Q6DID5; -.
DR IntAct; Q6DID5; 1.
DR MINT; Q6DID5; -.
DR STRING; 10090.ENSMUSP00000020365; -.
DR iPTMnet; Q6DID5; -.
DR PhosphoSitePlus; Q6DID5; -.
DR SwissPalm; Q6DID5; -.
DR EPD; Q6DID5; -.
DR MaxQB; Q6DID5; -.
DR PaxDb; Q6DID5; -.
DR PeptideAtlas; Q6DID5; -.
DR PRIDE; Q6DID5; -.
DR ProteomicsDB; 287640; -.
DR Antibodypedia; 10456; 243 antibodies from 35 providers.
DR Ensembl; ENSMUST00000020365; ENSMUSP00000020365; ENSMUSG00000020156.
DR GeneID; 68114; -.
DR KEGG; mmu:68114; -.
DR UCSC; uc007gch.1; mouse.
DR CTD; 84939; -.
DR MGI; MGI:1915364; Pwwp3a.
DR VEuPathDB; HostDB:ENSMUSG00000020156; -.
DR eggNOG; ENOG502QPRU; Eukaryota.
DR GeneTree; ENSGT00390000001700; -.
DR HOGENOM; CLU_388271_0_0_1; -.
DR InParanoid; Q6DID5; -.
DR OMA; AGMLVWC; -.
DR OrthoDB; 339225at2759; -.
DR PhylomeDB; Q6DID5; -.
DR TreeFam; TF328774; -.
DR BioGRID-ORCS; 68114; 5 hits in 112 CRISPR screens.
DR ChiTaRS; Mum1; mouse.
DR PRO; PR:Q6DID5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6DID5; protein.
DR Bgee; ENSMUSG00000020156; Expressed in spermatocyte and 266 other tissues.
DR ExpressionAtlas; Q6DID5; baseline and differential.
DR Genevisible; Q6DID5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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..682
FT /note="PWWP domain-containing DNA repair factor 3A"
FT /id="PRO_0000295047"
FT DOMAIN 383..444
FT /note="PWWP"
FT REGION 121..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1H224"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 59
FT /note="L -> M (in Ref. 1; BAC37397)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="L -> Q (in Ref. 3; BAA82658)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..406
FT /note="VVKSVRR -> PTRPVRP (in Ref. 2; AAH69883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 76069 MW; 53C3B9085ECD2733 CRC64;
MTDAKYVLCR WGKRLWPAKV LARTETSAKN KKKKEFFLDV QILSLKEKIQ VKSSAVEALQ
KSHIENIAAF LASQNEVPAT PLEELTYRRS LRVALDVLNE RTSLSPESHP IEDGITLSQK
EKTDADVASQ VSSAPSPSLL GEDGQAVVAQ CASKRRSEYS SKSLLPSSAL EDHLRCQVGP
KTGLSESGAG DKSQDDSGLQ LDHGQESTTK KRQRNLGEKP TRRRRSESGL SKGESVLKSQ
GQASSCVALA SPRPPSQTRD EEPCAGVKGC DWVKSSGNIR PLSASERSRG CPTKRPRLDG
GQNPPTRQLG TRTVGAAPCP RSCSGEVTML CSAGAGDKPE EDPVSSEEST GFKSTHSLLE
EEEEEEEEPP RILLYHEPRS FEVGMLVWLK YQKYPFWPAV VKSVRRRDKK ASVLFIEGNM
NPKGRGITVS LRRLKHFDCK EKHALLDRAK EDFAQAIGWC VSLITDYRVR LGCGSFAGSF
LEYYAADISY PVRKSIQQDV LGTRFPQLGK GDPEEPVGDS QLGQWRPCRK VLPDRSRAAR
DRANQKLVEY IVKAKGAESH LRAILHSRKP SRWLKTFLSS SQCVTCMETY LEDEAQLDEV
VEYLQGVCRD MDGQVPERGS GDRIRFILDV LLPEAIICAI SAVEAVDYKT AEQKYIRGPT
LSYREKEIFD NELLEERNRR RR
