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DNA repair protein RAD51 homolog 2 (R51H2) (RAD51 homolog B) (Rad51B) (RAD51-like protein 1)

 RA51B_HUMAN             Reviewed;         384 AA.
O15315; O60914; O75210; Q3Y4F8; Q6FHX8; Q86SY3; Q86SY4; Q86TR0;
Q86U92; Q86U93; Q86U94; Q8N6H4; Q9UPL5;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 2.
25-OCT-2017, entry version 156.
RecName: Full=DNA repair protein RAD51 homolog 2;
Short=R51H2;
AltName: Full=RAD51 homolog B;
Short=Rad51B;
AltName: Full=RAD51-like protein 1;
Name=RAD51B; Synonyms=RAD51L1, REC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9207106; DOI=10.1073/pnas.94.14.7417;
Rice M.C., Smith S.T., Bullrich F., Havre P., Kmiec E.B.;
"Isolation of human and mouse genes based on homology to REC2, a
recombinational repair gene from the fungus Ustilago maydis.";
Proc. Natl. Acad. Sci. U.S.A. 94:7417-7422(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9441753; DOI=10.1006/geno.1997.5062;
Albala J.S., Thelen M.P., Prange C.K., Fan W., Christensen M.,
Thompson L.H., Lennon G.G.;
"Identification of a novel human RAD51 homolog, RAD51B.";
Genomics 46:476-479(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=9512535; DOI=10.1093/nar/26.7.1653;
Cartwright R., Dunn A.M., Simpson P.J., Tambini C.E., Thacker J.;
"Isolation of novel human and mouse genes of the recA/RAD51
recombination-repair gene family.";
Nucleic Acids Res. 26:1653-1659(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
TISSUE=Neuroblastoma;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-9; CYS-82;
TRP-172; CYS-180; ARG-243 AND ALA-250.
NIEHS SNPs program;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 253-310, AND CHROMOSOMAL TRANSLOCATION
WITH HMGA2.
PubMed=12649198;
Quade B.J., Weremowicz S., Neskey D.M., Vanni R., Ladd C., Dal Cin P.,
Morton C.C.;
"Fusion transcripts involving HMGA2 are not a common molecular
mechanism in uterine leiomyomata with rearrangements in 12q15.";
Cancer Res. 63:1351-1358(2003).
[11]
FUNCTION, AND IDENTIFICATION IN THE BCDX2 COMPLEX WITH RAD51C; RAD51D
AND XRCC2.
PubMed=11751635; DOI=10.1101/gad.947001;
Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R.,
McIlwraith M.J., Benson F.E., West S.C.;
"Identification and purification of two distinct complexes containing
the five RAD51 paralogs.";
Genes Dev. 15:3296-3307(2001).
[12]
FUNCTION, AND INTERACTION WITH RAD51C.
PubMed=11751636; DOI=10.1101/gad.935501;
Sigurdsson S., Van Komen S., Bussen W., Schild D., Albala J.S.,
Sung P.;
"Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-
catalyzed DNA strand exchange.";
Genes Dev. 15:3308-3318(2001).
[13]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND
XRCC2.
PubMed=11842113; DOI=10.1093/nar/30.4.1009;
Liu N., Schild D., Thelen M.P., Thompson L.H.;
"Involvement of Rad51C in two distinct protein complexes of Rad51
paralogs in human cells.";
Nucleic Acids Res. 30:1009-1015(2002).
[14]
INTERACTION WITH RAD51C, AND SUBUNIT.
PubMed=11744692; DOI=10.1074/jbc.M108306200;
Miller K.A., Yoshikawa D.M., McConnell I.R., Clark R., Schild D.,
Albala J.S.;
"RAD51C interacts with RAD51B and is central to a larger protein
complex in vivo exclusive of RAD51.";
J. Biol. Chem. 277:8406-8411(2002).
[15]
IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
PubMed=11842112; DOI=10.1093/nar/30.4.1001;
Wiese C., Collins D.W., Albala J.S., Thompson L.H., Kronenberg A.,
Schild D.;
"Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human
cells.";
Nucleic Acids Res. 30:1001-1008(2002).
[16]
INTERACTION WITH RAD51 AND RAD51C.
PubMed=12427746; DOI=10.1074/jbc.M211038200;
Lio Y.-C., Mazin A.V., Kowalczykowski S.C., Chen D.J.;
"Complex formation by the human Rad51B and Rad51C DNA repair proteins
and their activities in vitro.";
J. Biol. Chem. 278:2469-2478(2003).
[17]
CHROMOSOMAL TRANSLOCATION WITH HMGA2.
PubMed=9892177;
Schoenmakers E.F.P.M., Huysmans C., Van de Ven W.J.M.;
"Allelic knockout of novel splice variants of human recombination
repair gene RAD51B in t(12;14) uterine leiomyomas.";
Cancer Res. 59:19-23(1999).
[18]
CHROMOSOMAL TRANSLOCATION WITH HMGA1.
PubMed=11978964;
Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A.,
Drieschner N., Bullerdiek J.;
"Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a
pulmonary chondroid hamartoma.";
Cytogenet. Cell Genet. 95:17-19(2001).
[19]
FUNCTION.
PubMed=12441335; DOI=10.1074/jbc.M210899200;
Yokoyama H., Kurumizaka H., Ikawa S., Yokoyama S., Shibata T.;
"Holliday junction binding activity of the human Rad51B protein.";
J. Biol. Chem. 278:2767-2772(2003).
[20]
INTERACTION WITH RAD51C.
PubMed=14704354; DOI=10.1093/nar/gkg925;
Miller K.A., Sawicka D., Barsky D., Albala J.S.;
"Domain mapping of the Rad51 paralog protein complexes.";
Nucleic Acids Res. 32:169-178(2004).
[21]
PHOSPHORYLATION BY BCR-ABL, AND MUTAGENESIS OF PRO-326.
PubMed=19657362; DOI=10.1038/leu.2009.164;
Slupianek A., Jozwiakowski S.K., Gurdek E., Skorski T.;
"BCR/ABL kinase interacts with and phosphorylates the RAD51 paralog,
RAD51B.";
Leukemia 23:2308-2310(2009).
[22]
INTERACTION WITH SWSAP1.
PubMed=21965664; DOI=10.1074/jbc.M111.271080;
Liu T., Wan L., Wu Y., Chen J., Huang J.;
"hSWS1.SWSAP1 is an evolutionarily conserved complex required for
efficient homologous recombination repair.";
J. Biol. Chem. 286:41758-41766(2011).
[23]
FUNCTION IN MITOTIC CELL PROGRESSION.
PubMed=23108668; DOI=10.1242/jcs.114595;
Rodrigue A., Coulombe Y., Jacquet K., Gagne J.P., Roques C.,
Gobeil S., Poirier G., Masson J.Y.;
"The RAD51 paralogs ensure cellular protection against mitotic defects
and aneuploidy.";
J. Cell Sci. 126:348-359(2013).
[24]
FUNCTION OF THE BCDX2 COMPLEX.
PubMed=23149936; DOI=10.1128/MCB.00465-12;
Chun J., Buechelmaier E.S., Powell S.N.;
"Rad51 paralog complexes BCDX2 and CX3 act at different stages in the
BRCA1-BRCA2-dependent homologous recombination pathway.";
Mol. Cell. Biol. 33:387-395(2013).
[25]
ELECTRON MICROSCOPY OF THE BCDX2 COMPLEX, AND DNA-BINDING OF THE BCDX2
COMPLEX.
PubMed=20207730; DOI=10.1074/jbc.M109.074286;
Compton S.A., Ozgur S., Griffith J.D.;
"Ring-shaped Rad51 paralog protein complexes bind Holliday junctions
and replication forks as visualized by electron microscopy.";
J. Biol. Chem. 285:13349-13356(2010).
-!- FUNCTION: Involved in the homologous recombination repair (HRR)
pathway of double-stranded DNA breaks arising during DNA
replication or induced by DNA-damaging agents. May promote the
assembly of presynaptic RAD51 nucleoprotein filaments. Binds
single-stranded DNA and double-stranded DNA and has DNA-dependent
ATPase activity. Part of the RAD21 paralog protein complex BCDX2
which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA
damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of
RAD51 recruitment. BCDX2 binds predominantly to the intersection
of the four duplex arms of the Holliday junction and to junction
of replication forks. The BCDX2 complex was originally reported to
bind single-stranded DNA, single-stranded gaps in duplex DNA and
specifically to nicks in duplex DNA. The BCDX2 subcomplex
RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase
activity suggesting an involvement in early stages of the HR
pathway. {ECO:0000269|PubMed:11751635,
ECO:0000269|PubMed:11751636, ECO:0000269|PubMed:11842113,
ECO:0000269|PubMed:12441335, ECO:0000269|PubMed:23108668,
ECO:0000269|PubMed:23149936}.
-!- SUBUNIT: Part of the BCDX2 complex consisting of RAD51B, RAD51C,
RAD51D and XRCC2; the complex has a ring-like structure arranged
into a flat disc around a central channel. The BCDX2 subcomplex
RAD51B:RAD51C interacts with RAD51. Interacts with SWSAP1;
involved in homologous recombination repair.
{ECO:0000269|PubMed:11744692, ECO:0000269|PubMed:11751635,
ECO:0000269|PubMed:11751636, ECO:0000269|PubMed:11842112,
ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12427746,
ECO:0000269|PubMed:14704354, ECO:0000269|PubMed:21965664}.
-!- INTERACTION:
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-2824089, EBI-10175124;
O43502:RAD51C; NbExp=10; IntAct=EBI-2824089, EBI-2267048;
O75771:RAD51D; NbExp=5; IntAct=EBI-2824089, EBI-1055693;
Q6NVH7:SWSAP1; NbExp=2; IntAct=EBI-2824089, EBI-5281637;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=O15315-3; Sequence=Displayed;
Name=2; Synonyms=RAD51L1a;
IsoId=O15315-1; Sequence=VSP_008819;
Name=3; Synonyms=RAD51L1b;
IsoId=O15315-2; Sequence=VSP_008818;
Name=4;
IsoId=O15315-4; Sequence=VSP_008820;
Note=No experimental confirmation available.;
Name=5;
IsoId=O15315-5; Sequence=VSP_008817, VSP_008818;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in a wide range of tissues.
-!- PTM: Phosphorylated on tyrosine residues by BCR-ALB.
{ECO:0000269|PubMed:19657362}.
-!- DISEASE: Note=A chromosomal aberration involving RAD51B is found
in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-
24) with HMGA1. {ECO:0000269|PubMed:11978964}.
-!- DISEASE: Note=A chromosomal aberration involving RAD51B is found
in uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with
HMGA2. {ECO:0000269|PubMed:12649198, ECO:0000269|PubMed:9892177}.
-!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD62357.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD66573.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rad51l1/";
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EMBL; U92074; AAB63358.1; -; mRNA.
EMBL; U84138; AAC39723.1; -; mRNA.
EMBL; Y15571; CAA75680.1; -; mRNA.
EMBL; BX161515; CAD61950.1; -; mRNA.
EMBL; BX248061; CAD62357.1; ALT_INIT; mRNA.
EMBL; BX248766; CAD66573.1; ALT_INIT; mRNA.
EMBL; DQ160197; AAZ85144.1; -; Genomic_DNA.
EMBL; AC004518; AAC32426.1; -; Genomic_DNA.
EMBL; AC004518; AAC32425.1; -; Genomic_DNA.
EMBL; CR536560; CAG38797.1; -; mRNA.
EMBL; CH471061; EAW80957.1; -; Genomic_DNA.
EMBL; BC030219; AAH30219.1; -; mRNA.
EMBL; AY138857; AAN60542.1; -; mRNA.
EMBL; AY138858; AAN60543.1; -; mRNA.
EMBL; AY138859; AAN60544.1; -; mRNA.
CCDS; CCDS9789.1; -. [O15315-3]
CCDS; CCDS9790.1; -. [O15315-2]
RefSeq; NP_001308746.1; NM_001321817.1. [O15315-5]
RefSeq; NP_002868.1; NM_002877.5. [O15315-1]
RefSeq; NP_598193.2; NM_133509.3. [O15315-3]
RefSeq; NP_598194.1; NM_133510.3. [O15315-2]
UniGene; Hs.172587; -.
ProteinModelPortal; O15315; -.
BioGrid; 111827; 10.
CORUM; O15315; -.
DIP; DIP-41246N; -.
IntAct; O15315; 11.
MINT; MINT-224850; -.
STRING; 9606.ENSP00000419471; -.
iPTMnet; O15315; -.
PhosphoSitePlus; O15315; -.
BioMuta; RAD51B; -.
PaxDb; O15315; -.
PeptideAtlas; O15315; -.
PRIDE; O15315; -.
TopDownProteomics; O15315-2; -. [O15315-2]
DNASU; 5890; -.
Ensembl; ENST00000471583; ENSP00000418859; ENSG00000182185. [O15315-2]
Ensembl; ENST00000487270; ENSP00000419471; ENSG00000182185. [O15315-3]
Ensembl; ENST00000488612; ENSP00000420061; ENSG00000182185. [O15315-4]
GeneID; 5890; -.
KEGG; hsa:5890; -.
UCSC; uc001xkd.4; human. [O15315-3]
CTD; 5890; -.
DisGeNET; 5890; -.
EuPathDB; HostDB:ENSG00000182185.18; -.
GeneCards; RAD51B; -.
H-InvDB; HIX0022466; -.
HGNC; HGNC:9822; RAD51B.
HPA; CAB016191; -.
HPA; HPA051869; -.
MIM; 150699; phenotype.
MIM; 602948; gene.
neXtProt; NX_O15315; -.
OpenTargets; ENSG00000182185; -.
PharmGKB; PA34178; -.
eggNOG; KOG1433; Eukaryota.
eggNOG; COG0468; LUCA.
GeneTree; ENSGT00860000133731; -.
HOVERGEN; HBG061476; -.
InParanoid; O15315; -.
KO; K10869; -.
OMA; RKEFDTQ; -.
PhylomeDB; O15315; -.
TreeFam; TF101219; -.
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.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; O15315; -.
ChiTaRS; RAD51B; human.
GeneWiki; RAD51L1; -.
GenomeRNAi; 5890; -.
PRO; PR:O15315; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000182185; -.
ExpressionAtlas; O15315; baseline and differential.
Genevisible; O15315; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0000150; F:recombinase activity; IBA:GO_Central.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
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:UniProtKB.
GO; GO:0000707; P:meiotic DNA recombinase assembly; IBA:GO_Central.
GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0042148; P:strand invasion; IBA:GO_Central.
CDD; cd01123; Rad51_DMC1_radA; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
InterPro; IPR016467; DNA_recomb/repair_RecA-like.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR033925; Rad51_DMC1_RadA.
InterPro; IPR030548; RAD51B.
InterPro; IPR020588; RecA_ATP-bd.
PANTHER; PTHR22942:SF15; PTHR22942:SF15; 1.
Pfam; PF08423; Rad51; 1.
PIRSF; PIRSF005856; Rad51; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50162; RECA_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chromosomal rearrangement;
Complete proteome; DNA damage; DNA recombination; DNA repair;
DNA-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 384 DNA repair protein RAD51 homolog 2.
/FTId=PRO_0000122939.
NP_BIND 108 115 ATP. {ECO:0000255}.
REGION 1 75 Interaction with RAD51C.
SITE 252 253 Breakpoint for translocation to form
HMGA2-RAD51B.
VAR_SEQ 1 119 Missing (in isoform 5).
{ECO:0000303|Ref.4}.
/FTId=VSP_008817.
VAR_SEQ 346 384 ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF
-> AYGNS (in isoform 2).
{ECO:0000303|PubMed:9207106,
ECO:0000303|PubMed:9441753,
ECO:0000303|Ref.6}.
/FTId=VSP_008819.
VAR_SEQ 346 384 ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF
-> GQEKP (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:9512535,
ECO:0000303|Ref.4}.
/FTId=VSP_008818.
VAR_SEQ 347 384 TTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF ->
FWHICISGFSIQNRLKENES (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_008820.
VARIANT 9 9 V -> M (in dbSNP:rs34583846).
{ECO:0000269|Ref.5}.
/FTId=VAR_025243.
VARIANT 82 82 F -> C (in dbSNP:rs35282642).
{ECO:0000269|Ref.5}.
/FTId=VAR_025244.
VARIANT 172 172 L -> W (in dbSNP:rs34094401).
{ECO:0000269|Ref.5}.
/FTId=VAR_025245.
VARIANT 180 180 Y -> C (in dbSNP:rs28910275).
{ECO:0000269|Ref.5}.
/FTId=VAR_025246.
VARIANT 207 207 V -> L (in dbSNP:rs28908168).
/FTId=VAR_035437.
VARIANT 243 243 K -> R (in dbSNP:rs34594234).
{ECO:0000269|Ref.5}.
/FTId=VAR_025247.
VARIANT 250 250 S -> A (in dbSNP:rs33929366).
{ECO:0000269|Ref.5}.
/FTId=VAR_025248.
VARIANT 365 365 P -> R (in dbSNP:rs28908468).
/FTId=VAR_051730.
MUTAGEN 326 326 P->L: Abolishes interaction with BCR-ABL
SH3 domain.
{ECO:0000269|PubMed:19657362}.
CONFLICT 281 281 S -> P (in Ref. 9; AAN60542/AAN60543/
AAN60544). {ECO:0000305}.
SEQUENCE 384 AA; 42196 MW; DB0B9AE82F44A52B CRC64;
MGSKKLKRVG LSQELCDRLS RHQILTCQDF LCLSPLELMK VTGLSYRGVH ELLCMVSRAC
APKMQTAYGI KAQRSADFSP AFLSTTLSAL DEALHGGVAC GSLTEITGPP GCGKTQFCIM
MSILATLPTN MGGLEGAVVY IDTESAFSAE RLVEIAESRF PRYFNTEEKL LLTSSKVHLY
RELTCDEVLQ RIESLEEEII SKGIKLVILD SVASVVRKEF DAQLQGNLKE RNKFLAREAS
SLKYLAEEFS IPVILTNQIT THLSGALASQ ADLVSPADDL SLSEGTSGSS CVIAALGNTW
SHSVNTRLIL QYLDSERRQI LIAKSPLAPF TSFVYTIKEE GLVLQETTFC SVTQAELNWA
PEILPPQPPE QLGLQMCHHT QLIF


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