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REV1

Protein FULL name:

DNA repair protein REV1 isoform 1 [Homo sapiens].


REV1 (Homo sapiens) is product of expression of REV1 gene.


REV1 is involved in:

TLS in Homo sapiens
     


Keywords:



FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.

SUBUNIT: Monomer. Binds MAD2L2, POLH, POLI, POLK and REV3L. May bind ITGA3.

SUBCELLULAR LOCATION: Nucleus (Probable).

TISSUE SPECIFICITY: Ubiquitous.

DOMAIN: The C-terminal domain is necessary for protein interactions.

SIMILARITY: Belongs to the DNA polymerase type-Y family.

SIMILARITY: Contains 1 BRCT domain.

SIMILARITY: Contains 1 umuC domain.

SEQUENCE CAUTION: Sequence=AAK43708.1; Type=Erroneous initiation;


NCBI GenPept GI number(s): 7706681
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9UBZ9 Q9UBZ9
PFAM: - Q9UBZ9 (Link - using uniprot id)
InterPro: - Q9UBZ9 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MRRGGWRKRAENDGWETWGGYMAAKVQKLEEQFRSDAAMQKDGTSSTIFS
GVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKI
KELKGEKVIRPEWIVESIKAGRLLSYIPYQLYTKQSSVQKGLSFNPVCRP
EDPLPGPSNIAKQLNNRVNHIVKKIETENEVKVNGMNSWNEEDENNDFSF
VDLEQTSPGRKQNGIPHPRGSTAIFNGHTPSSNGALKTQDCLVPMVNSVA
SRLSPAFSQEEDKAEKSSTDFRDCTLQQLQQSTRNTDALRNPHRTNSFSL
SPLHSNTKINGAHHSTVQGPSSTKSTSSVSTFSKAAPSVPSKPSDCNFIS
NFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKLKKMKTGRSALV
VTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNR
GTGRAPLRPGANPQLEWQYYQNKILKGKAADIPDSSLWENPDSAQANGID
SVLSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVA
QTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKD
QTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLP
GVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDD
RPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKG
KRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAM
LNMFHTMKLNISDMRGVGIHVNQLVPTNLNPSTCPSRPSVQSSHFPSGSY
SVRDVFQVQKAKKSTEEEHKEVFRAAVDLEISSASRTCTFLPPFPAHLPT
SPDTNKAESSGKWNGLHTPVSVQSRLNLSIEVPSPSQLDQSVLEALPPDL
REQVEQVCAVQQAESHGDKKKEPVNGCNTGILPQPVGTVLLQIPEPQESN
SDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQRQGENSTHQQ
SASASVPKNPLLHLKAAVKEKKRNKKKKTIGSPKRIQSPLNNKLLNSPAK
TLPGACGSPQKLIDGFLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAG
CVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEE
KDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKV
T

REV1 (Homo sapiens) is able to recognize following damages:
REV1 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains. Wixler V, Laplantine E, Geerts D, Sonnenberg A, Petersohn D, Eckes B, Paulsson M, Aumailley M FEBS Lett Jan. 26, 1999
The human REV1 gene codes for a DNA template-dependent dCMP transferase. Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z Nucleic Acids Res Nov. 15, 1999
The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. Gibbs PE, Wang XD, Li Z, McManus TP, McGregor WG, Lawrence CW, Maher VM Proc Natl Acad Sci U S A April 11, 2000
Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. Masuda Y, Takahashi M, Tsunekuni N, Minami T, Sumii M, Miyagawa K, Kamiya K J Biol Chem May 4, 2001
Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. Murakumo Y, Ogura Y, Ishii H, Numata S, Ichihara M, Croce CM, Fishel R, Takahashi M J Biol Chem Sept. 21, 2001
Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. Masuda Y, Ohmae M, Masuda K, Kamiya K J Biol Chem April 4, 2003
Complete sequencing and characterization of 21,243 full-length human cDNAs. 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 TO, 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 Nat Genet Feb. 1, 2004
Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK Nature April 7, 2005
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. 15, 2010.

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