R51A1_MOUSE
ID R51A1_MOUSE Reviewed; 337 AA.
AC Q8C551; O55219; Q8BP36; Q99L94; Q9D0J0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=RAD51-associated protein 1 {ECO:0000305};
DE AltName: Full=RAB22 {ECO:0000303|PubMed:9192668};
GN Name=Rad51ap1 {ECO:0000312|MGI:MGI:1098224};
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] {ECO:0000312|EMBL:AAB91541.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RAD51, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Testis, and Thymus;
RX PubMed=9192668; DOI=10.1073/pnas.94.13.6927;
RA Mizuta R., LaSalle J.M., Cheng H.-L., Shinohara A., Ogawa H.,
RA Copeland N.G., Jenkins N.A., Lalande M., Alt F.W.;
RT "RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the
RT RAD51 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6927-6932(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Forelimb, and Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH03738.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH03738.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and 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).
RN [6]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=21307306; DOI=10.1073/pnas.1016454108;
RA Dray E., Dunlop M.H., Kauppi L., San Filippo J., Wiese C., Tsai M.S.,
RA Begovic S., Schild D., Jasin M., Keeney S., Sung P.;
RT "Molecular basis for enhancement of the meiotic DMC1 recombinase by RAD51
RT associated protein 1 (RAD51AP1).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3560-3565(2011).
CC -!- FUNCTION: Structure-specific DNA-binding protein involved in DNA repair
CC by promoting RAD51-mediated homologous recombination. Acts by
CC stimulating D-Loop formation by RAD51: specifically enhances joint
CC molecule formation through its structure-specific DNA interaction and
CC its interaction with RAD51. Binds single-stranded DNA (ssDNA), double-
CC stranded DNA (dsDNA) and secondary DNA structures, such as D-loop
CC structures: has a strong preference for branched-DNA structures that
CC are obligatory intermediates during joint molecule formation.
CC Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous
CC recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in
CC DNA-binding during homologous recombination and DNA repair. WDR48/UAF1
CC and RAD51AP1 also have a coordinated role in DNA-binding to promote
CC USP1-mediated deubiquitination of FANCD2. Also involved in meiosis by
CC promoting DMC1-mediated homologous meiotic recombination.
CC {ECO:0000250|UniProtKB:Q96B01}.
CC -!- SUBUNIT: Monomer; elongated monodisperse monomer (By similarity).
CC Interacts (via C-terminal region) with RAD51; the interaction is direct
CC (PubMed:9192668). Interacts (via SIM motif) with WDR48/UAF1; WDR48/UAF1
CC and RAD51AP1 cooperate together to stimulate RAD51-mediated homologous
CC recombination (HR) (By similarity). Interacts (via WVPP motif) with
CC DMC1; the interaction is direct (By similarity). Interacts with PALB2.
CC Interacts with RAD52 (By similarity). {ECO:0000250|UniProtKB:Q96B01,
CC ECO:0000269|PubMed:9192668}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:21307306,
CC ECO:0000269|PubMed:9192668}. Nucleus {ECO:0000269|PubMed:21307306,
CC ECO:0000269|PubMed:9192668}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q96B01}. Note=Colocalizes with RAD51 to multiple
CC nuclear foci (PubMed:9192668, PubMed:21307306). Colocalizes with DMC1
CC on meiotic chromatin (PubMed:21307306). {ECO:0000269|PubMed:21307306,
CC ECO:0000269|PubMed:9192668}.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in testis
CC (PubMed:9192668). Also expressed in spleen, thymus and bone marrow
CC (PubMed:9192668). Not detected in heart, kidney or liver
CC (PubMed:9192668). {ECO:0000269|PubMed:9192668}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in 15 to 21 days postpartum (dpp)
CC testes. {ECO:0000269|PubMed:21307306}.
CC -!- PTM: Sumoylation with SUMO2/3 by NSMCE2/MMS21 promotes stabilization,
CC possibly by preventing ubiquitination. {ECO:0000250|UniProtKB:Q96B01}.
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DR EMBL; U93583; AAB91541.1; -; mRNA.
DR EMBL; AK011379; BAB27579.1; -; mRNA.
DR EMBL; AK077829; BAC37025.1; -; mRNA.
DR EMBL; AK079525; BAC37671.1; -; mRNA.
DR EMBL; BC003738; AAH03738.1; -; mRNA.
DR CCDS; CCDS39644.1; -.
DR RefSeq; NP_001334384.1; NM_001347455.1.
DR RefSeq; NP_033039.2; NM_009013.4.
DR AlphaFoldDB; Q8C551; -.
DR BioGRID; 202565; 1.
DR STRING; 10090.ENSMUSP00000107841; -.
DR iPTMnet; Q8C551; -.
DR PhosphoSitePlus; Q8C551; -.
DR EPD; Q8C551; -.
DR jPOST; Q8C551; -.
DR MaxQB; Q8C551; -.
DR PaxDb; Q8C551; -.
DR PeptideAtlas; Q8C551; -.
DR PRIDE; Q8C551; -.
DR ProteomicsDB; 300284; -.
DR DNASU; 19362; -.
DR GeneID; 19362; -.
DR KEGG; mmu:19362; -.
DR UCSC; uc009dvi.1; mouse.
DR CTD; 10635; -.
DR MGI; MGI:1098224; Rad51ap1.
DR eggNOG; ENOG502RXRS; Eukaryota.
DR InParanoid; Q8C551; -.
DR OrthoDB; 1109145at2759; -.
DR PhylomeDB; Q8C551; -.
DR TreeFam; TF335955; -.
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR BioGRID-ORCS; 19362; 5 hits in 108 CRISPR screens.
DR ChiTaRS; Rad51ap1; mouse.
DR PRO; PR:Q8C551; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C551; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0062037; F:D-loop DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000217; F:DNA secondary structure binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IPI:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; ISS:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR InterPro; IPR026632; RAD51-assoc_prot_1.
DR InterPro; IPR031419; RAD51_interact.
DR PANTHER; PTHR15361:SF4; PTHR15361:SF4; 1.
DR Pfam; PF15696; RAD51_interact; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Isopeptide bond; Meiosis; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Telomere; Ubl conjugation.
FT CHAIN 1..337
FT /note="RAD51-associated protein 1"
FT /id="PRO_0000097141"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..50
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT REGION 88..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..286
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT REGION 295..334
FT /note="Interaction with RAD51"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT MOTIF 138..143
FT /note="SIM motif"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT MOTIF 286..289
FT /note="WVPP motif"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO; alternate)"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin; alternate)"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT CONFLICT 5
FT /note="T -> I (in Ref. 2; BAB27579/BAC37025/BAC37671)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="T -> A (in Ref. 1; AAB91541)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="E -> G (in Ref. 1; AAB91541)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="G -> D (in Ref. 1; AAB91541)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="R -> H (in Ref. 2; BAB27579/BAC37025/BAC37671)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="Missing (in Ref. 2; BAC37025)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="K -> R (in Ref. 3; AAH03738)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..337
FT /note="VR -> SAVAEKDLLGPWDLQAGLSYSAST (in Ref. 2;
FT BAC37671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 36227 MW; 7691E9515079783A CRC64;
MVRPTRNRKP INYSQFEDSG NDSDDDFISS STPVNKSKTV PKVLKQDKPK PNLKNLQKEE
VLPTEPPKKR VALDDKVFQR GLEVALALSV KELPTLTNQV KKSKEKSTDK QGKEKTENTG
KPPRVSNCSV ASDDVEDLDK ITEEGDASSV EGERKSPSQA KAPRRRAPSE GSDGSSANDT
ESESATGEGS ESDPDFDESK ESDEDFGVRR SKESKKKTVQ KKPAGEKKER KSKPKCEASV
TSVDPAPAAI KSGSPSLPQA VGLPSEATRK PAIMCSPSAE SKRPKWVPPA ASGSRNSSSN
ALAGTPAKSP SQSLRLGLSR LAPVKRLHPS ATSSQVR
