R51A1_HUMAN
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 03-AUG-2022, entry version 163.
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}.
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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 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; 160 antibodies from 33 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 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; PTHR15361:SF4; 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
