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RAD51-associated protein 1 (RAD51-interacting protein)

 R51A1_HUMAN             Reviewed;         352 AA.
Q96B01; A8K7D3; O43403; Q7Z779;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 134.
RecName: Full=RAD51-associated protein 1;
AltName: Full=RAD51-interacting protein;
Name=RAD51AP1 {ECO:0000312|EMBL:AAH16330.1,
ECO:0000312|HGNC:HGNC:16956}; Synonyms=PIR51;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC39554.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION
WITH RAD51, AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9396801; DOI=10.1093/nar/25.24.4946;
Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M.;
"A novel nucleic acid-binding protein that interacts with human rad51
recombinase.";
Nucleic Acids Res. 25:4946-4953(1997).
[2] {ECO:0000305, ECO:0000312|EMBL:BAC04902.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305, ECO:0000312|EMBL:AAH16330.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Bone marrow {ECO:0000312|EMBL:AAH16330.1}, and
Urinary bladder {ECO:0000312|EMBL:AAH06992.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH RAD51, AND MUTAGENESIS OF ARG-333; LEU-336 AND
345-LEU-HIS-346.
PubMed=16990250; DOI=10.1093/nar/gkl665;
Kovalenko O.V., Wiese C., Schild D.;
"RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a
conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51.";
Nucleic Acids Res. 34:5081-5092(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; SER-280 AND
SER-327, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
FUNCTION, AND INTERACTION WITH PALB2.
PubMed=20871616; DOI=10.1038/nsmb.1916;
Dray E., Etchin J., Wiese C., Saro D., Williams G.J., Hammel M.,
Yu X., Galkin V.E., Liu D., Tsai M.S., Sy S.M., Schild D., Egelman E.,
Chen J., Sung P.;
"Enhancement of RAD51 recombinase activity by the tumor suppressor
PALB2.";
Nat. Struct. Mol. Biol. 17:1255-1259(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; SER-120 AND
SER-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66; SER-120; SER-124 AND
SER-327, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
INTERACTION WITH RAD51.
PubMed=23754376; DOI=10.1073/pnas.1220662110;
Yuan J., Chen J.;
"FIGNL1-containing protein complex is required for efficient
homologous recombination repair.";
Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013).
-!- FUNCTION: May participate in a common DNA damage response pathway
associated with the activation of homologous recombination and
double-strand break repair. Functionally cooperates with PALB2 in
promoting of D-loop formation by RAD51. Binds to single and double
stranded DNA, and is capable of aggregating DNA. Also binds RNA.
{ECO:0000269|PubMed:20871616, ECO:0000269|PubMed:9396801}.
-!- SUBUNIT: Isoform 2 interacts with RAD51. Interacts with PALB2.
Interacts (via C-terminal region) with RAD51; the interaction is
direct. {ECO:0000269|PubMed:16990250, ECO:0000269|PubMed:20871616,
ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:9396801}.
-!- INTERACTION:
Q14565:DMC1; NbExp=3; IntAct=EBI-1178743, EBI-930865;
Q86YC2:PALB2; NbExp=2; IntAct=EBI-1178743, EBI-1222653;
Q06609:RAD51; NbExp=6; IntAct=EBI-1178743, EBI-297202;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-1178743, EBI-747107;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
RAD51 to multiple nuclear foci. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.
{ECO:0000269|PubMed:9396801};
Name=1 {ECO:0000305};
IsoId=Q96B01-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:9396801};
IsoId=Q96B01-2; Sequence=VSP_051739;
Name=3 {ECO:0000269|PubMed:9396801};
IsoId=Q96B01-3; Sequence=VSP_051740;
-!- TISSUE SPECIFICITY: Highly expressed in testis and thymus. Lower
levels in colon and small intestine. Little or no expression in
spleen, prostate, ovary and peripheral blood leukocytes.
{ECO:0000269|PubMed:9396801}.
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EMBL; AF006259; AAC39554.1; -; mRNA.
EMBL; AK096930; BAC04902.1; -; mRNA.
EMBL; AK291948; BAF84637.1; -; mRNA.
EMBL; CH471116; EAW88844.1; -; Genomic_DNA.
EMBL; BC006992; AAH06992.1; -; mRNA.
EMBL; BC016330; AAH16330.1; -; mRNA.
CCDS; CCDS44805.1; -. [Q96B01-1]
CCDS; CCDS8529.1; -. [Q96B01-2]
RefSeq; NP_001124334.1; NM_001130862.1. [Q96B01-1]
RefSeq; NP_006470.1; NM_006479.4. [Q96B01-2]
UniGene; Hs.730696; -.
ProteinModelPortal; Q96B01; -.
BioGrid; 115879; 15.
DIP; DIP-35257N; -.
IntAct; Q96B01; 10.
STRING; 9606.ENSP00000228843; -.
iPTMnet; Q96B01; -.
PhosphoSitePlus; Q96B01; -.
BioMuta; RAD51AP1; -.
DMDM; 68565925; -.
EPD; Q96B01; -.
MaxQB; Q96B01; -.
PaxDb; Q96B01; -.
PeptideAtlas; Q96B01; -.
PRIDE; Q96B01; -.
TopDownProteomics; Q96B01-1; -. [Q96B01-1]
DNASU; 10635; -.
Ensembl; ENST00000228843; ENSP00000228843; ENSG00000111247. [Q96B01-1]
Ensembl; ENST00000352618; ENSP00000309479; ENSG00000111247. [Q96B01-2]
GeneID; 10635; -.
KEGG; hsa:10635; -.
UCSC; uc001qmu.4; human. [Q96B01-1]
CTD; 10635; -.
DisGeNET; 10635; -.
EuPathDB; HostDB:ENSG00000111247.14; -.
GeneCards; RAD51AP1; -.
HGNC; HGNC:16956; RAD51AP1.
HPA; HPA051499; -.
MIM; 603070; gene.
neXtProt; NX_Q96B01; -.
OpenTargets; ENSG00000111247; -.
PharmGKB; PA134871784; -.
eggNOG; ENOG410IICA; Eukaryota.
eggNOG; ENOG4111WAW; LUCA.
GeneTree; ENSGT00730000111239; -.
HOGENOM; HOG000116153; -.
HOVERGEN; HBG079699; -.
InParanoid; Q96B01; -.
KO; K20778; -.
OMA; EDFSMRK; -.
OrthoDB; EOG091G0OEX; -.
PhylomeDB; Q96B01; -.
TreeFam; TF335955; -.
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
ChiTaRS; RAD51AP1; human.
GenomeRNAi; 10635; -.
PRO; PR:Q96B01; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111247; -.
CleanEx; HS_RAD51AP1; -.
ExpressionAtlas; Q96B01; baseline and differential.
Genevisible; Q96B01; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0043234; C:protein complex; IMP:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:ParkinsonsUK-UCL.
GO; GO:0036297; P:interstrand cross-link repair; IMP:ParkinsonsUK-UCL.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
InterPro; IPR026632; RAD51-assoc_prot_1.
InterPro; IPR031419; RAD51_interact.
PANTHER; PTHR15361:SF4; PTHR15361:SF4; 1.
Pfam; PF15696; RAD51_interact; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; DNA damage;
DNA recombination; DNA repair; DNA-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; RNA-binding.
CHAIN 1 352 RAD51-associated protein 1.
/FTId=PRO_0000097140.
REGION 313 352 Interaction with RAD51.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 66 66 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 71 87 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9396801}.
/FTId=VSP_051739.
VAR_SEQ 258 307 Missing (in isoform 3).
{ECO:0000303|PubMed:9396801}.
/FTId=VSP_051740.
VARIANT 68 68 K -> Q (in dbSNP:rs34810644).
/FTId=VAR_056976.
MUTAGEN 333 333 R->A: Strongly decreases interaction with
RAD51; when associated with Q-336; A-345
and A-346. {ECO:0000269|PubMed:16990250}.
MUTAGEN 336 336 L->Q: Strongly decreases interaction with
RAD51; when associated with A-333; A-345
and A-346. {ECO:0000269|PubMed:16990250}.
MUTAGEN 345 346 LH->AA: Strongly decreases interaction
with RAD51; when associated with A-333;
and Q-336. {ECO:0000269|PubMed:16990250}.
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


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