REPAIRtoire - a database of DNA repair pathways

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RAD54B

Protein FULL name:

DNA repair and recombination protein RAD54B [Homo sapiens].


RAD54B (Homo sapiens) is product of expression of RAD54B gene.






FUNCTION: Involved in DNA repair and mitotic recombination. May play an active role in recombination processes in concert with other members of the RAD52 epistasis group.

SUBUNIT: Interacts with RAD51 through the NH2-terminal domain. Immunoprecipitation experiments show that the interaction is constitutive and not induced by ionizing radiation. The interaction may be indirect.

SUBCELLULAR LOCATION: Nucleus (Probable).

TISSUE SPECIFICITY: Abundantly expressed in testis and spleen. Relatively low levels observed in thymus, prostate, ovary and colon.

SIMILARITY: Belongs to the SNF2/RAD54 helicase family.

SIMILARITY: Contains 1 helicase ATP-binding domain.

SIMILARITY: Contains 1 helicase C-terminal domain.


NCBI GenPept GI number(s): 6912622
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9Y620 Q9Y620
PFAM: - Q9Y620 (Link - using uniprot id)
InterPro: - Q9Y620 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MRRSAAPSQLQGNSFKKPKFIPPGRSNPGLNEEITKLNPDIKLFEGVAIN
NTFLPSQNDLRICSLNLPSEESTREINNRDNCSGKYCFEAPTLATLDPPH
TVHSAPKEVAVSKEQEEKSDSLVKYFSVVWCKPSKKKHKKWEGDAVLIVK
GKSFILKNLEGKDIGRGIGYKFKELEKIEEGQTLMICGKEIEVMGVISPD
DFSSGRCFQLGGGSTAISHSSQVARKCFSNPFKSVCKPSSKENRQNDFQN
CKPRHDPYTPNSLVMPRPDKNHQWVFNKNCFPLVDVVIDPYLVYHLRPHQ
KEGIIFLYECVMGMRMNGRCGAILADEMGLGKTLQCISLIWTLQCQGPYG
GKPVIKKTLIVTPGSLVNNWKKEFQKWLGSERIKIFTVDQDHKVEEFIKS
IFYSVLIISYEMLLRSLDQIKNIKFDLLICDEGHRLKNSAIKTTTALISL
SCEKRIILTGTPIQNDLQEFFALIDFVNPGILGSLSSYRKIYEEPIILSR
EPSASEEEKELGERRAAELTCLTGLFILRRTQEIINKYLPPKIENVVFCR
PGALQIELYRKLLNSQVVRFCLQGLLENSPHLICIGALKKLCNHPCLLFN
SIKEKECSSTCDKNEEKSLYKGLLSVFPADYNPLLFTEKESGKLQVLSKL
LAVIHELRPTEKVVLVSNYTQTLNILQEVCKRHGYAYTRLDGQTPISQRQ
QIVDGFNSQHSSFFIFLLSSKAGGVGLNLIGGSHLILYDIDWNPATDIQA
MSRVWRDGQKYPVHIYRLLTTGTIEEKIYQRQISKQGLCGAVVDLTKTSE
HIQFSVEELKNLFTLHESSDCVTHDLLDCECTGEEVHTGDSLEKFIVSRD
CQLGPHHQKSNSLKPLSMSQLKQWKHFSGDHLNLTDPFLERITENVSFIF
QNITTQATGT

RAD54B (Homo sapiens) is able to recognize following damages:
RAD54B (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Mutations of a novel human RAD54 homologue, RAD54B, in primary cancer. Hiramoto T, Nakanishi T, Sumiyoshi T, Fukuda T, Matsuura S, Tauchi H, Komatsu K, Shibasaki Y, Inui H, Watatani M, Yasutomi M, Sumii K, Kajiyama G, Kamada N, Miyagawa K, Kamiya K Oncogene June 3, 1999
A novel human rad54 homologue, Rad54B, associates with Rad51. Tanaka K, Hiramoto T, Fukuda T, Miyagawa K J Biol Chem Aug. 25, 2000
A role for RAD54B in homologous recombination in human cells. Miyagawa K, Tsuruga T, Kinomura A, Usui K, Katsura M, Tashiro S, Mishima H, Tanaka K EMBO J Feb. 15, 2002
Human Rad54B is a double-stranded DNA-dependent ATPase and has biochemical properties different from its structural homolog in yeast, Tid1/Rdh54. Tanaka K, Kagawa W, Kinebuchi T, Kurumizaka H, Miyagawa K Nucleic Acids Res March 15, 2002
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
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009


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

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