ID R51A1_HUMAN Reviewed; 352 AA. AC Q96B01; A8K7D3; O43403; Q7Z779; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 12-AUG-2020, entry version 155. DE RecName: Full=RAD51-associated protein 1; DE AltName: Full=RAD51-interacting protein; GN Name=RAD51AP1 {ECO:0000312|EMBL:AAH16330.1, ECO:0000312|HGNC:HGNC:16956}; GN Synonyms=PIR51; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC39554.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH RP RAD51, AND TISSUE SPECIFICITY. RC TISSUE=Cervix carcinoma; RX PubMed=9396801; DOI=10.1093/nar/25.24.4946; RA Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M.; RT "A novel nucleic acid-binding protein that interacts with human rad51 RT recombinase."; RL Nucleic Acids Res. 25:4946-4953(1997). RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC04902.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH16330.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Bone marrow {ECO:0000312|EMBL:AAH16330.1}, and RC Urinary bladder {ECO:0000312|EMBL:AAH06992.1}; 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 [5] RP INTERACTION WITH RAD51, AND MUTAGENESIS OF ARG-333; LEU-336 AND RP 345-LEU-HIS-346. RX PubMed=16990250; DOI=10.1093/nar/gkl665; RA Kovalenko O.V., Wiese C., Schild D.; RT "RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a RT conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51."; RL Nucleic Acids Res. 34:5081-5092(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; SER-280 AND RP SER-327, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP FUNCTION, AND INTERACTION WITH PALB2. RX PubMed=20871616; DOI=10.1038/nsmb.1916; RA Dray E., Etchin J., Wiese C., Saro D., Williams G.J., Hammel M., Yu X., RA Galkin V.E., Liu D., Tsai M.S., Sy S.M., Schild D., Egelman E., Chen J., RA Sung P.; RT "Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2."; RL Nat. Struct. Mol. Biol. 17:1255-1259(2010). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; SER-120 AND RP SER-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66; SER-120; SER-124 AND RP SER-327, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP INTERACTION WITH RAD51. RX PubMed=23754376; DOI=10.1073/pnas.1220662110; RA Yuan J., Chen J.; RT "FIGNL1-containing protein complex is required for efficient homologous RT recombination repair."; RL Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013). CC -!- FUNCTION: May participate in a common DNA damage response pathway CC associated with the activation of homologous recombination and double- CC strand break repair. Functionally cooperates with PALB2 in promoting of CC D-loop formation by RAD51. Binds to single and double stranded DNA, and CC is capable of aggregating DNA. Also binds RNA. CC {ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:9396801}. CC -!- SUBUNIT: Isoform 2 interacts with RAD51. Interacts with PALB2. CC Interacts (via C-terminal region) with RAD51; the interaction is CC direct. {ECO:0000269|PubMed:16990250, ECO:0000269|PubMed:20871616, CC ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:9396801}. CC -!- INTERACTION: CC Q96B01; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-1178724, EBI-747107; CC Q96B01; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-1178724, EBI-11522811; CC Q96B01-2; Q14565: DMC1; NbExp=3; IntAct=EBI-1178743, EBI-930865; CC Q96B01-2; Q86YC2: PALB2; NbExp=2; IntAct=EBI-1178743, EBI-1222653; CC Q96B01-2; Q06609: RAD51; NbExp=6; IntAct=EBI-1178743, EBI-297202; CC Q96B01-2; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-1178743, EBI-747107; CC Q96B01-3; Q06609: RAD51; NbExp=6; IntAct=EBI-1178748, EBI-297202; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with CC RAD51 to multiple nuclear foci. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist. CC {ECO:0000269|PubMed:9396801}; CC Name=1 {ECO:0000305}; CC IsoId=Q96B01-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:9396801}; CC IsoId=Q96B01-2; Sequence=VSP_051739; CC Name=3 {ECO:0000269|PubMed:9396801}; CC IsoId=Q96B01-3; Sequence=VSP_051740; CC -!- TISSUE SPECIFICITY: Highly expressed in testis and thymus. Lower levels CC in colon and small intestine. Little or no expression in spleen, CC prostate, ovary and peripheral blood leukocytes. CC {ECO:0000269|PubMed:9396801}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF006259; AAC39554.1; -; mRNA. DR EMBL; AK096930; BAC04902.1; -; mRNA. DR EMBL; AK291948; BAF84637.1; -; mRNA. DR EMBL; CH471116; EAW88844.1; -; Genomic_DNA. DR EMBL; BC006992; AAH06992.1; -; mRNA. DR EMBL; BC016330; AAH16330.1; -; mRNA. DR CCDS; CCDS44805.1; -. [Q96B01-1] DR CCDS; CCDS8529.1; -. [Q96B01-2] DR RefSeq; NP_001124334.1; NM_001130862.1. [Q96B01-1] DR RefSeq; NP_006470.1; NM_006479.4. [Q96B01-2] DR BioGRID; 115879; 19. DR DIP; DIP-35257N; -. DR IntAct; Q96B01; 17. DR STRING; 9606.ENSP00000228843; -. DR iPTMnet; Q96B01; -. DR PhosphoSitePlus; Q96B01; -. DR BioMuta; RAD51AP1; -. DR DMDM; 68565925; -. DR EPD; Q96B01; -. DR jPOST; Q96B01; -. DR MassIVE; Q96B01; -. DR MaxQB; Q96B01; -. DR PaxDb; Q96B01; -. DR PeptideAtlas; Q96B01; -. DR PRIDE; Q96B01; -. DR ProteomicsDB; 76027; -. [Q96B01-1] DR ProteomicsDB; 76028; -. [Q96B01-2] DR ProteomicsDB; 76029; -. [Q96B01-3] DR TopDownProteomics; Q96B01-1; -. [Q96B01-1] DR Antibodypedia; 22279; 153 antibodies. DR DNASU; 10635; -. DR Ensembl; ENST00000228843; ENSP00000228843; ENSG00000111247. [Q96B01-1] DR Ensembl; ENST00000352618; ENSP00000309479; ENSG00000111247. [Q96B01-2] DR GeneID; 10635; -. DR KEGG; hsa:10635; -. DR UCSC; uc001qmu.4; human. [Q96B01-1] DR CTD; 10635; -. DR DisGeNET; 10635; -. DR EuPathDB; HostDB:ENSG00000111247.14; -. DR GeneCards; RAD51AP1; -. DR HGNC; HGNC:16956; RAD51AP1. DR HPA; ENSG00000111247; Tissue enhanced (lymphoid). DR MIM; 603070; gene. DR neXtProt; NX_Q96B01; -. DR OpenTargets; ENSG00000111247; -. DR PharmGKB; PA134871784; -. DR eggNOG; ENOG502RXRS; Eukaryota. DR GeneTree; ENSGT00940000153414; -. DR HOGENOM; CLU_067355_1_0_1; -. DR InParanoid; Q96B01; -. DR KO; K20778; -. DR OMA; KVQLPVD; -. DR OrthoDB; 1109145at2759; -. DR PhylomeDB; Q96B01; -. DR TreeFam; TF335955; -. DR PathwayCommons; Q96B01; -. DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA). DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates. DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange. DR BioGRID-ORCS; 10635; 10 hits in 878 CRISPR screens. DR ChiTaRS; RAD51AP1; human. DR GenomeRNAi; 10635; -. DR Pharos; Q96B01; Tbio. DR PRO; PR:Q96B01; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q96B01; protein. DR Bgee; ENSG00000111247; Expressed in secondary oocyte and 185 other tissues. DR ExpressionAtlas; Q96B01; baseline and differential. DR Genevisible; Q96B01; HS. DR GO; GO:0000790; C:nuclear chromatin; IDA:ParkinsonsUK-UCL. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL. DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:ParkinsonsUK-UCL. DR GO; GO:0036297; P:interstrand cross-link repair; IMP:ParkinsonsUK-UCL. DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IDA: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 Alternative splicing; DNA damage; DNA recombination; DNA repair; KW DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; KW RNA-binding. FT CHAIN 1..352 FT /note="RAD51-associated protein 1" FT /id="PRO_0000097140" FT REGION 313..352 FT /note="Interaction with RAD51" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231" FT MOD_RES 66 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163" FT MOD_RES 124 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231" FT MOD_RES 327 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163" FT VAR_SEQ 71..87 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9396801" FT /id="VSP_051739" FT VAR_SEQ 258..307 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9396801" FT /id="VSP_051740" FT VARIANT 68 FT /note="K -> Q (in dbSNP:rs34810644)" FT /id="VAR_056976" FT MUTAGEN 333 FT /note="R->A: Strongly decreases interaction with RAD51; FT when associated with Q-336; A-345 and A-346." FT /evidence="ECO:0000269|PubMed:16990250" FT MUTAGEN 336 FT /note="L->Q: Strongly decreases interaction with RAD51; FT when associated with A-333; A-345 and A-346." FT /evidence="ECO:0000269|PubMed:16990250" FT MUTAGEN 345..346 FT /note="LH->AA: Strongly decreases interaction with RAD51; FT when associated with A-333; and Q-336." FT /evidence="ECO:0000269|PubMed:16990250" SQ SEQUENCE 352 AA; 38457 MW; E582EE4BC459DD92 CRC64; MVRPVRHKKP VNYSQFDHSD SDDDFVSATV PLNKKSRTAP KELKQDKPKP NLNNLRKEEI PVQEKTPKKR LPEGTFSIPA SAVPCTKMAL DDKLYQRDLE VALALSVKEL PTVTTNVQNS QDKSIEKHGS SKIETMNKSP HISNCSVASD YLDLDKITVE DDVGGVQGKR KAASKAAAQQ RKILLEGSDG DSANDTEPDF APGEDSEDDS DFCESEDNDE DFSMRKSKVK EIKKKEVKVK SPVEKKEKKS KSKCNALVTS VDSAPAAVKS ESQSLPKKVS LSSDTTRKPL EIRSPSAESK KPKWVPPAAS GGSRSSSSPL VVVSVKSPNQ SLRLGLSRLA RVKPLHPNAT ST //