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 14-DEC-2022, entry version 165. DE RecName: Full=RAD51-associated protein 1 {ECO:0000305}; DE Short=HsRAD51AP1 {ECO:0000303|PubMed:25288561}; DE AltName: Full=RAD51-interacting protein {ECO:0000303|PubMed:9396801}; GN Name=RAD51AP1 {ECO:0000303|PubMed:16990250, ECO:0000312|HGNC:HGNC:16956}; GN Synonyms=PIR51 {ECO:0000303|PubMed:9396801}; 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: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: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: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 FUNCTION, SUBUNIT, INTERACTION WITH RAD51, DNA-BINDING, AND MUTAGENESIS OF RP 327-SER--THR-352. RX PubMed=17996710; DOI=10.1016/j.molcel.2007.08.025; RA Modesti M., Budzowska M., Baldeyron C., Demmers J.A., Ghirlando R., RA Kanaar R.; RT "RAD51AP1 is a structure-specific DNA binding protein that stimulates joint RT molecule formation during RAD51-mediated homologous recombination."; RL Mol. Cell 28:468-481(2007). RN [7] RP FUNCTION, INTERACTION WITH RAD51, AND MUTAGENESIS OF 328-PRO--THR-352; RP LEU-336 AND HIS-346. RX PubMed=17996711; DOI=10.1016/j.molcel.2007.08.027; RA Wiese C., Dray E., Groesser T., San Filippo J., Shi I., Collins D.W., RA Tsai M.S., Williams G.J., Rydberg B., Sung P., Schild D.; RT "Promotion of homologous recombination and genomic stability by RAD51AP1 RT via RAD51 recombinase enhancement."; RL Mol. Cell 28:482-490(2007). RN [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] RP INTERACTION WITH DMC1 AND RAD51, AND MUTAGENESIS OF TRP-304. RX PubMed=21903585; DOI=10.1074/jbc.m111.290015; RA Dunlop M.H., Dray E., Zhao W., Tsai M.S., Wiese C., Schild D., Sung P.; RT "RAD51-associated protein 1 (RAD51AP1) interacts with the meiotic RT recombinase DMC1 through a conserved motif."; RL J. Biol. Chem. 286:37328-37334(2011). RN [14] RP FUNCTION, INTERACTION WITH DMC1, AND MUTAGENESIS OF LEU-336 AND HIS-346. 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). RN [15] 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 [16] RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF 34-LYS--ARG-37; 34-LYS--LYS-47; RP 248-LYS--LYS-253 AND 300-LYS--TRP-304. RX PubMed=22375013; DOI=10.1074/jbc.c112.352161; RA Dunlop M.H., Dray E., Zhao W., San Filippo J., Tsai M.S., Leung S.G., RA Schild D., Wiese C., Sung P.; RT "Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in RT homologous DNA repair."; RL J. Biol. Chem. 287:12343-12347(2012). RN [17] 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 [18] 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). RN [19] RP FUNCTION. RX PubMed=25288561; DOI=10.1016/j.dnarep.2014.09.007; RA Parplys A.C., Kratz K., Speed M.C., Leung S.G., Schild D., Wiese C.; RT "RAD51AP1-deficiency in vertebrate cells impairs DNA replication."; RL DNA Repair 24:87-97(2014). RN [20] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=26323318; DOI=10.1093/nar/gkv859; RA Parplys A.C., Zhao W., Sharma N., Groesser T., Liang F., Maranon D.G., RA Leung S.G., Grundt K., Dray E., Idate R., Oestvold A.C., Schild D., RA Sung P., Wiese C.; RT "NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination RT and genome stability."; RL Nucleic Acids Res. 43:9817-9834(2015). RN [21] RP FUNCTION, INTERACTION WITH WDR48, AND MUTAGENESIS OF 150-ASP--ASP-153 AND RP LYS-156. RX PubMed=27463890; DOI=10.1080/15384101.2016.1209613; RA Cukras S., Lee E., Palumbo E., Benavidez P., Moldovan G.L., Kee Y.; RT "The USP1-UAF1 complex interacts with RAD51AP1 to promote homologous RT recombination repair."; RL Cell Cycle 15:2636-2646(2016). RN [22] RP FUNCTION, INTERACTION WITH WDR48, AND MUTAGENESIS OF 154-LEU--ILE-157 AND RP 157-ILE--VAL-159. RX PubMed=27239033; DOI=10.1016/j.celrep.2016.05.007; RA Liang F., Longerich S., Miller A.S., Tang C., Buzovetsky O., Xiong Y., RA Maranon D.G., Wiese C., Kupfer G.M., Sung P.; RT "Promotion of RAD51-mediated homologous DNA pairing by the RAD51AP1-UAF1 RT complex."; RL Cell Rep. 15:2118-2126(2016). RN [23] RP FUNCTION, AND DNA-BINDING. RX PubMed=31253762; DOI=10.1038/s41467-019-10408-5; RA Liang F., Miller A.S., Longerich S., Tang C., Maranon D., Williamson E.A., RA Hromas R., Wiese C., Kupfer G.M., Sung P.; RT "DNA requirement in FANCD2 deubiquitination by USP1-UAF1-RAD51AP1 in the RT Fanconi anemia DNA damage response."; RL Nat. Commun. 10:2849-2849(2019). RN [24] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAD52, UBIQUITINATION AT RP LYS-269, SUMOYLATION AT LYS-269, AND MUTAGENESIS OF LYS-44; RP 154-LEU--VAL-159; LYS-240; LYS-269 AND LYS-326. RX PubMed=31400850; DOI=10.1016/j.molcel.2019.06.043; RA Barroso-Gonzalez J., Garcia-Exposito L., Hoang S.M., Lynskey M.L., RA Roncaioli J.L., Ghosh A., Wallace C.T., de Vitis M., Modesti M., RA Bernstein K.A., Sarkar S.N., Watkins S.C., O'Sullivan R.J.; RT "RAD51AP1 is an essential mediator of alternative lengthening of RT telomeres."; RL Mol. Cell 76:11-26(2019). RN [25] RP ERRATUM OF PUBMED:31400850. RX PubMed=31585101; DOI=10.1016/j.molcel.2019.08.009; RA Barroso-Gonzalez J., Garcia-Exposito L., Hoang S.M., Lynskey M.L., RA Roncaioli J.L., Ghosh A., Wallace C.T., Modesti M., Bernstein K.A., RA Sarkar S.N., Watkins S.C., O'Sullivan R.J.; RT "RAD51AP1 is an essential mediator of alternative lengthening of RT telomeres."; RL Mol. Cell 76:217-217(2019). RN [26] RP FUNCTION, AND DNA-BINDING. RX PubMed=32350107; DOI=10.1074/jbc.ra120.013714; RA Liang F., Miller A.S., Tang C., Maranon D., Williamson E.A., Hromas R., RA Wiese C., Zhao W., Sung P., Kupfer G.M.; RT "The DNA-binding activity of USP1-associated factor 1 is required for RT efficient RAD51-mediated homologous DNA pairing and homology-directed DNA RT repair."; RL J. Biol. Chem. 295:8186-8194(2020). CC -!- FUNCTION: Structure-specific DNA-binding protein involved in DNA repair CC by promoting RAD51-mediated homologous recombination (PubMed:17996710, CC PubMed:17996711, PubMed:20871616, PubMed:25288561, PubMed:26323318). CC Acts by stimulating D-Loop formation by RAD51: specifically enhances CC joint molecule formation through its structure-specific DNA interaction CC and its interaction with RAD51 (PubMed:17996710, PubMed:17996711). CC Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and CC secondary DNA structures, such as D-loop structures: has a strong CC preference for branched-DNA structures that are obligatory CC intermediates during joint molecule formation (PubMed:9396801, CC PubMed:17996711, PubMed:22375013, PubMed:17996710). Cooperates with CC WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both CC WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during CC homologous recombination and DNA repair (PubMed:27463890, CC PubMed:27239033, PubMed:32350107). WDR48/UAF1 and RAD51AP1 also have a CC coordinated role in DNA-binding to promote USP1-mediated CC deubiquitination of FANCD2 (PubMed:31253762). Also involved in meiosis CC by promoting DMC1-mediated homologous meiotic recombination CC (PubMed:21307306). Key mediator of alternative lengthening of telomeres CC (ALT) pathway, a homology-directed repair mechanism of telomere CC elongation that controls proliferation in aggressive cancers, by CC stimulating homologous recombination (PubMed:31400850). May also bind CC RNA; additional evidences are however required to confirm RNA-binding CC in vivo (PubMed:9396801). {ECO:0000269|PubMed:17996710, CC ECO:0000269|PubMed:17996711, ECO:0000269|PubMed:20871616, CC ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:22375013, CC ECO:0000269|PubMed:25288561, ECO:0000269|PubMed:26323318, CC ECO:0000269|PubMed:27239033, ECO:0000269|PubMed:27463890, CC ECO:0000269|PubMed:31253762, ECO:0000269|PubMed:31400850, CC ECO:0000269|PubMed:32350107, ECO:0000269|PubMed:9396801}. CC -!- SUBUNIT: Monomer; elongated monodisperse monomer (PubMed:17996710). CC Interacts (via C-terminal region) with RAD51; the interaction is direct CC (PubMed:16990250, PubMed:23754376, PubMed:9396801, PubMed:17996710, CC PubMed:17996711, PubMed:21903585). Interacts (via SIM motif) with CC WDR48/UAF1; WDR48/UAF1 and RAD51AP1 cooperate together to stimulate CC RAD51-mediated homologous recombination (HR) (PubMed:27463890, CC PubMed:27239033). Interacts (via WVPP motif) with DMC1; the interaction CC is direct (PubMed:21903585, PubMed:21307306). Interacts with PALB2 CC (PubMed:20871616). Interacts with RAD52 (PubMed:31400850). CC {ECO:0000269|PubMed:16990250, ECO:0000269|PubMed:17996710, CC ECO:0000269|PubMed:17996711, ECO:0000269|PubMed:20871616, CC ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:21903585, CC ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:27239033, CC ECO:0000269|PubMed:27463890, ECO:0000269|PubMed:31400850, CC ECO:0000269|PubMed:9396801}. CC -!- SUBUNIT: [Isoform 3]: Does not interact with DMC1; lack of interaction CC is caused by the absence of the WVPP motif in this isoform. CC {ECO:0000269|PubMed:21903585}. 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: Chromosome {ECO:0000269|PubMed:26323318, CC ECO:0000269|PubMed:31400850}. Nucleus {ECO:0000269|PubMed:26323318}. CC Chromosome, telomere {ECO:0000269|PubMed:31400850}. Note=Colocalizes CC with RAD51 to multiple nuclear foci (By similarity). Colocalizes with CC DMC1 on meiotic chromatin (By similarity). CC {ECO:0000250|UniProtKB:Q8C551}. 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:0000303|PubMed:9396801}; CC IsoId=Q96B01-2; Sequence=VSP_051739; CC Name=3 {ECO:0000303|PubMed:9396801}; CC IsoId=Q96B01-3; Sequence=VSP_051740; CC -!- TISSUE SPECIFICITY: Highly expressed in testis and thymus CC (PubMed:9396801). Lower levels in colon and small intestine CC (PubMed:9396801). Little or no expression in spleen, prostate, ovary CC and peripheral blood leukocytes (PubMed:9396801). CC {ECO:0000269|PubMed:9396801}. CC -!- PTM: Sumoylation with SUMO2/3 by NSMCE2/MMS21 promotes stabilization, CC possibly by preventing ubiquitination (PubMed:31400850). Sumoylation is CC required for alternative lengthening of telomeres (ALT) pathway CC (PubMed:31400850). {ECO:0000269|PubMed:31400850}. 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 AlphaFoldDB; Q96B01; -. DR BioGRID; 115879; 30. DR DIP; DIP-35257N; -. DR IntAct; Q96B01; 18. DR MINT; Q96B01; -. DR STRING; 9606.ENSP00000228843; -. DR GlyGen; Q96B01; 1 site, 1 O-linked glycan (1 site). 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 ProteomicsDB; 76027; -. [Q96B01-1] DR ProteomicsDB; 76028; -. [Q96B01-2] DR ProteomicsDB; 76029; -. [Q96B01-3] DR TopDownProteomics; Q96B01-1; -. [Q96B01-1] DR Antibodypedia; 22279; 158 antibodies from 32 providers. DR DNASU; 10635; -. DR Ensembl; ENST00000228843.13; ENSP00000228843.9; ENSG00000111247.15. [Q96B01-1] DR Ensembl; ENST00000352618.9; ENSP00000309479.7; ENSG00000111247.15. [Q96B01-2] DR GeneID; 10635; -. DR KEGG; hsa:10635; -. DR MANE-Select; ENST00000352618.9; ENSP00000309479.7; NM_006479.5; NP_006470.1. [Q96B01-2] DR UCSC; uc001qmu.4; human. [Q96B01-1] DR AGR; HGNC:16956; -. DR CTD; 10635; -. DR DisGeNET; 10635; -. DR GeneCards; RAD51AP1; -. DR HGNC; HGNC:16956; RAD51AP1. DR HPA; ENSG00000111247; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 603070; gene. DR neXtProt; NX_Q96B01; -. DR OpenTargets; ENSG00000111247; -. DR PharmGKB; PA134871784; -. DR VEuPathDB; HostDB:ENSG00000111247; -. DR eggNOG; ENOG502RXRS; Eukaryota. DR GeneTree; ENSGT00940000153414; -. DR HOGENOM; CLU_067355_1_0_1; -. DR InParanoid; Q96B01; -. DR OMA; CVKAPPS; -. 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 Reactome; R-HSA-9701192; Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function. DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function. DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function. DR Reactome; R-HSA-9709603; Impaired BRCA2 binding to PALB2. DR SignaLink; Q96B01; -. DR SIGNOR; Q96B01; -. DR BioGRID-ORCS; 10635; 18 hits in 1082 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 137 other tissues. DR ExpressionAtlas; Q96B01; baseline and differential. DR Genevisible; Q96B01; HS. DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. 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:0062037; F:D-loop DNA binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0000217; F:DNA secondary structure binding; IDA: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:0006974; P:cellular response to DNA damage stimulus; 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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IDA:UniProtKB. 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; RAD51-ASSOCIATED PROTEIN 1; 1. DR Pfam; PF15696; RAD51_interact; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chromosome; DNA damage; DNA recombination; KW DNA repair; DNA-binding; Isopeptide bond; Meiosis; Nucleus; Phosphoprotein; KW Reference proteome; RNA-binding; Telomere; Ubl conjugation. FT CHAIN 1..352 FT /note="RAD51-associated protein 1" FT /id="PRO_0000097140" FT REGION 1..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 30..49 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:22375013" FT REGION 115..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 162..323 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 243..304 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:22375013" FT REGION 313..352 FT /note="Interaction with RAD51" FT /evidence="ECO:0000269|PubMed:16990250, FT ECO:0000269|PubMed:17996710, ECO:0000269|PubMed:17996711, FT ECO:0000269|PubMed:21903585" FT MOTIF 154..159 FT /note="SIM motif" FT /evidence="ECO:0000269|PubMed:27239033, FT ECO:0000269|PubMed:27463890" FT MOTIF 304..307 FT /note="WVPP motif" FT /evidence="ECO:0000269|PubMed:21903585" FT COMPBIAS 10..24 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 37..71 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 198..218 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 219..253 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 254..290 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 66 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 124 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 327 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 251 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin; alternate)" FT /evidence="ECO:0000305|PubMed:31400850" FT CROSSLNK 269 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:31400850" 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 34..47 FT /note="KKSRTAPKELKQDK->AASATAPAELAQDA: In K6RA; impaired FT DNA-binding." FT /evidence="ECO:0000269|PubMed:22375013" FT MUTAGEN 34..37 FT /note="KKSR->AASA: In K2RA; impaired DNA-binding." FT /evidence="ECO:0000269|PubMed:22375013" FT MUTAGEN 44 FT /note="K->R: Does not affect sumoylation." FT /evidence="ECO:0000269|PubMed:31400850" FT MUTAGEN 150..153 FT /note="DYLD->AYLA: Abolished interaction with WDR48/UAF1." FT /evidence="ECO:0000269|PubMed:27463890" FT MUTAGEN 154..159 FT /note="LDKITV->ADKATA: Reduced sumoylation. Reduced FT ubiquitination." FT /evidence="ECO:0000269|PubMed:31400850" FT MUTAGEN 154..157 FT /note="LDKI->ADKA: Decreased interaction with WDR48/UAF1." FT /evidence="ECO:0000269|PubMed:27239033" FT MUTAGEN 156 FT /note="K->R: Does not affect interaction with WDR48/UAF1." FT /evidence="ECO:0000269|PubMed:27463890" FT MUTAGEN 157..159 FT /note="ITV->ATA: Decreased interaction with WDR48/UAF1." FT /evidence="ECO:0000269|PubMed:27239033" FT MUTAGEN 240 FT /note="K->R: Does not affect sumoylation." FT /evidence="ECO:0000269|PubMed:31400850" FT MUTAGEN 248..253 FT /note="KKSKSK->AASASA: In K4A; reduced DNA-binding. In FT K7WA; strongly decreased DNA-binding; when associated with FT 300-A--A-304." FT /evidence="ECO:0000269|PubMed:22375013" FT MUTAGEN 269 FT /note="K->R: Strongly reduced sumoylation. Strongly reduced FT ubiquitination." FT /evidence="ECO:0000269|PubMed:31400850" FT MUTAGEN 300..304 FT /note="KKPKW->AAPAA: In K3WA; reduced DNA-binding. In K7WA; FT strongly decreased DNA-binding; when associated with 248- FT A--A-253." FT /evidence="ECO:0000269|PubMed:22375013" FT MUTAGEN 304 FT /note="W->A: Abolished interaction with DMC1 without FT affecting interaction with RAD51." FT /evidence="ECO:0000269|PubMed:21903585" FT MUTAGEN 326 FT /note="K->R: Does not affect sumoylation." FT /evidence="ECO:0000269|PubMed:31400850" FT MUTAGEN 327..352 FT /note="Missing: Abolished interaction with RAD51." FT /evidence="ECO:0000269|PubMed:17996710" FT MUTAGEN 328..352 FT /note="Missing: In mutant delta25; abolished interaction FT with RAD51." FT /evidence="ECO:0000269|PubMed:17996711" 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. Decreased FT interacting with RAD51 and ability to stimulate RAD51- FT mediated homologous recombination. Does not affect FT interaction with DMC1." FT /evidence="ECO:0000269|PubMed:16990250, FT ECO:0000269|PubMed:17996711, ECO:0000269|PubMed:21307306" 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" FT MUTAGEN 346 FT /note="H->A: Decreased interacting with RAD51 and ability FT to stimulate RAD51-mediated homologous recombination. Does FT not affect interaction with DMC1." FT /evidence="ECO:0000269|PubMed:17996711, FT ECO:0000269|PubMed:21307306" 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 //