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DCLRE1A

Protein FULL name:

DNA-crosslink repair gene SNM1 [Homo sapiens].


DCLRE1A (Homo sapiens) is product of expression of DCLRE1A gene.


DCLRE1A is involved in:

DDS in Homo sapiens
     


Keywords:



FUNCTION: May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons.

SUBUNIT: Binds constitutively to TP53BP1. Binds CDC27, which is itself a component of the anaphase promoting complex (APC). Binds PIAS1.

SUBCELLULAR LOCATION: Nucleus. Note=In some cells it may be found in typically 1 or 2 discrete nuclear aggregates of unknown function which also contain TP53BP1. Also found in multiple discrete nuclear foci which increase in number following treatment with ionizing radiation or interstrand cross-linking agents. These foci overlap with those formed by the MRN complex (composed of MRE11A, RAD50 and NBN) and BRCA1.

TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, pancreas, placenta and skeletal muscle.

INDUCTION: During mitosis. The mRNA encoding this protein contains an internal ribosome entry site (IRES) in its 5'-UTR. This 5'-UTR generally suppresses translation while specifically promoting expression during mitosis, when cap-dependent translation may be impaired.

SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.

SEQUENCE CAUTION: Sequence=BAA07646.2; Type=Erroneous initiation;

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


NCBI GenPept GI number(s): 42734319
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q6PJP8 Q6PJP8
PFAM: - Q6PJP8 (Link - using uniprot id)
InterPro: - Q6PJP8 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MLEDISEEDIWEYKSKRKPKRVDPNNGSKNILKSVEKATDGKYQSKRSRN
RKRAAEAKEVKDHEVPLGNAGCQTSVASSQNSSCGDGIQQTQDKETTPGK
LCRTQKSQHVSPKIRPVYDGYCPNCQMPFSSLIGQTPRWHVFECLDSPPR
SETECPDGLLCTSTIPFHYKRYTHFLLAQSRAGDHPFSSPSPASGGSFSE
TKSGVLCSLEERWSSYQNQTDNSVSNDPLLMTQYFKKSPSLTEASEKIST
HIQTSQQALQFTDFVENDKLVGVALRLANNSEHINLPLPENDFSDCEISY
SPLQSDEDTHDIDEKPHDSQEQLFFTESSKDGSLEEDDDSCGFFKKRHGP
LLKDQDESCPKVNSFLTRDKYDEGLYRFNSLNDLSQPISQNNESTLPYDL
ACTGGDFVLFPPALAGKLAASVHQATKAKPDEPEFHSAQSNKQKQVIEES
SVYNQVSLPLVKSLMLKPFESQVEGYLSSQPTQNTIRKLSSENLNAKNNT
NSACFCRKALEGVPVGKATILNTENLSSTPAPKYLKILPSGLKYNARHPS
TKVMKQMDIGVYFGLPPKRKEEKLLGESALEWINLNPVPSPNQKRSSQCK
RKAEKSLSDLEFDASTLHESQLSVELSSERSQRQKKRCRKSNSLQEGACQ
KRSDHLINTESEAVNLSKVKVFTKSAHGGLQRGNKKIPESSNVGGSRKKT
CPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVY
CSEITGNLLKNKLHVQEQYIHPLPLDTECIVNGVKVVLLDANHCPGAVMI
LFYLPNGTVILHTGDFRADPSMERSLLADQKVHMLYLDTTYCSPEYTFPS
QQEVIRFAINTAFEAVTLNPHALVVCGTYSIGKEKVFLAIADVLGSKVGM
SQEKYKTLQCLNIPEINSLITTDMCSSLVHLLPMMQINFKGLQSHLKKCG
GKYNQILAFRPTGWTHSNKFTRIADVIPQTKGNISIYGIPYSEHSSYLEM
KRFVQWLKPQKIIPTVNVGTWKSRSTMEKYFREWKLEAGY

DCLRE1A (Homo sapiens) is able to recognize following damages:
DCLRE1A (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al. DNA Res Jan. 1, 1995
Disruption of mouse SNM1 causes increased sensitivity to the DNA interstrand cross-linking agent mitomycin C. Dronkert ML, de Wit J, Boeve M, Vasconcelos ML, van Steeg H, Tan TL, Hoeijmakers JH, Kanaar R Mol Cell Biol July 1, 2000
Translation of hSNM1 is mediated by an internal ribosome entry site that upregulates expression during mitosis. Zhang X, Richie C, Legerski RJ DNA Repair (Amst) May 1, 2002
hSnm1 colocalizes and physically associates with 53BP1 before and after DNA damage. Richie CT, Peterson C, Lu T, Hittelman WN, Carpenter PB, Legerski RJ Mol Cell Biol Dec. 1, 2002
The DNA sequence and comparative analysis of human chromosome 10. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J Nature May 27, 2004
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
Deficiency in SNM1 abolishes an early mitotic checkpoint induced by spindle stress. Akhter S, Richie CT, Deng JM, Brey E, Zhang X, Patrick C Jr, Behringer RR, Legerski RJ Mol Cell Biol Dec. 1, 2004
DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation. Ishiai M, Kimura M, Namikoshi K, Yamazoe M, Yamamoto K, Arakawa H, Agematsu K, Matsushita N, Takeda S, Buerstedde JM, Takata M Mol Cell Biol Dec. 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. 12, 2010.

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