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RAD51L1

Protein FULL name:

DNA repair protein RAD51 homolog 2 isoform 1 [Homo sapiens].


RAD51L1 (Homo sapiens) is product of expression of RAD51L1 gene.






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. The RAD51B- RAD51C dimer exhibits single-stranded DNA-dependent ATPase activity. The BCDX2 complex binds single-stranded DNA, single- stranded gaps in duplex DNA and specifically to nicks in duplex DNA.

SUBUNIT: Interacts with RAD51C. Part of a BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2. Part of a complex consisting of RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3. Part of a complex with RAD51C and RAD51.

SUBCELLULAR LOCATION: Nucleus (Probable).

TISSUE SPECIFICITY: Expressed in a wide range of tissues.

DISEASE: Note=A chromosomal aberration involving RAD51L1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23- 24) with HMGA1.

DISEASE: A chromosomal aberration involving RAD51L1 is found in uterine leiomyoma (UL) [MIM:150699]. Translocation t(12;14)(q15;q23-24) with HMGA2.

SIMILARITY: Belongs to the recA family. RAD51 subfamily.

SEQUENCE CAUTION: Sequence=CAD62357.1; Type=Erroneous initiation; Sequence=CAD66573.1; Type=Erroneous initiation;

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 10835029
19924117
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O15315 O15315
PFAM: - O15315 (Link - using uniprot id)
InterPro: - O15315 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MGSKKLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVH
ELLCMVSRACAPKMQTAYGIKAQRSADFSPAFLSTTLSALDEALHGGVAC
GSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAE
RLVEIAESRFPRYFNTEEKLLLTSSKVHLYRELTCDEVLQRIESLEEEII
SKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLAREASSLKYLAEEFS
IPVILTNQITTHLSGALASQADLVSPADDLSLSEGTSGSSCVIAALGNTW
SHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGLVLQAYGNS

RAD51L1 (Homo sapiens) is able to recognize following damages:
References:

Title Authors Journal
Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis. Rice MC, Smith ST, Bullrich F, Havre P, Kmiec EB Proc Natl Acad Sci U S A July 8, 1997
Identification of a novel human RAD51 homolog, RAD51B. Albala JS, Thelen MP, Prange C, Fan W, Christensen M, Thompson LH, Lennon GG Genomics Dec. 15, 1997
Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family. Cartwright R, Dunn AM, Simpson PJ, Tambini CE, Thacker J Nucleic Acids Res April 1, 1998
Allelic knockout of novel splice variants of human recombination repair gene RAD51B in t(12;14) uterine leiomyomas. Schoenmakers EF, Huysmans C, Van de Ven WJ Cancer Res Feb. 1, 1999
Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a pulmonary chondroid hamartoma. Blank C, Schoenmakers EF, Rogalla P, Huys EH, van Rijk AA, Drieschner N, Bullerdiek J Cytogenet Cell Genet Jan. 1, 2001
Identification and purification of two distinct complexes containing the five RAD51 paralogs. Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC Genes Dev Dec. 15, 2001
Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange. Sigurdsson S, Van Komen S, Bussen W, Schild D, Albala JS, Sung P Genes Dev Dec. 15, 2001
Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells. Liu N, Schild D, Thelen MP, Thompson LH Nucleic Acids Res Jan. 15, 2002
Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells. Wiese C, Collins DW, Albala JS, Thompson LH, Kronenberg A, Schild D Nucleic Acids Res Jan. 15, 2002
RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51. Miller KA, Yoshikawa DM, McConnell IR, Clark R, Schild D, Albala JS J Biol Chem March 8, 2002
The DNA sequence and analysis of human chromosome 14. Heilig R, Eckenberg R, Petit JL, 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, Bruls 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, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J Nature Jan. 6, 2003
Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro. Lio YC, Mazin AV, Kowalczykowski SC, Chen DJ J Biol Chem Feb. 24, 2003
Fusion transcripts involving HMGA2 are not a common molecular mechanism in uterine leiomyomata with rearrangements in 12q15. Quade BJ, Weremowicz S, Neskey DM, Vanni R, Ladd C, Dal Cin P, Morton CC Cancer Res March 15, 2003
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004


Last modification of this entry: Oct. 11, 2010.

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