REPAIRtoire - a database of DNA repair pathways

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Bujnicki Lab Homepage

REV3L

Protein FULL name:

DNA polymerase zeta catalytic subunit [Homo sapiens].


REV3L (Homo sapiens) is product of expression of REV3L gene.


REV3L is involved in:

TLS in Homo sapiens
     


Keywords:



CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

SUBUNIT: Interacts with REV7.

SUBCELLULAR LOCATION: Nucleus (Potential).

TISSUE SPECIFICITY: Ubiquitously expressed.

DOMAIN: Its C-terminal part could serve as the catalytic domain during nucleotide polymerization, while its N-terminal part could provide sites for protein-protein interactions with other factors during translesion DNA synthesis.

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

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


NCBI GenPept GI number(s): 153792012
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O60673 O60673
PFAM: - O60673 (Link - using uniprot id)
InterPro: - O60673 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKT
CLHLHGIFPYLYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQH
VFKVSLVSGMPFYGYHEKERHFMKIYLYNPTMVKRICELLQSGAIMNKFY
QPHEAHIPYLLQLFIDYNLYGMNLINLAAVKFRKARRKSNTLHATGSCKN
HLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDAVAADILNRLD
IEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKK
FQKRLQEILKQNDFSVTLSGSVDYSDGSQEFSAELTLHSEVLSPEMLQCT
PANMVEVHKDKESSKGHTRHKVEEALINEEAILNLMENSQTFQPLTQRLS
ESPVFMDSSPDEALVHLLAGLESDGYRGERNRMPSPCRSFGNNKYPQNSD
DEENEPQIEKEEMELSLVMSQRWDSNIEEHCAKKRSLCRNTHRSSTEDDD
SSSGEEMEWSDNSLLLASLSIPQLDGTADENSDNPLNNENSRTHSSVIAT
SKLSVKPSIFHKDAATLEPSSSAKITFQCKHTSALSSHVLNKEDLIEDLS
QTNKNTEKGLDNSVTSFTNESTYSMKYPGSLSSTVHSENSHKENSKKEIL
PVSSCESSIFDYEEDIPSVTRQVPSRKYTNIRKIEKDSPFIHMHRHPNEN
TLGKNSFNFSDLNHSKNKVSSEGNEKGNSTALSSLFPSSFTENCELLSCS
GENRTMVHSLNSTADESGLNKLKIRYEEFQEHKTEKPSLSQQAAHYMFFP
SVVLSNCLTRPQKLSPVTYKLQPGNKPSRLKLNKRKLAGHQETSTKSSET
GSTKDNFIQNNPCNSNPEKDNALASDLTKTTRGAFENKTPTDGFIDCHFG
DGTLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPME
IGESLDGTLKSRKRRKMSKKLPPVIIKYIIINRFRGRKNMLVKLGKIDSK
EKQVILTEEKMELYKKLAPLKDFWPKVPDSPATKYPIYPLTPKKSHRRKS
KHKSAKKKTGKQQRTNNENIKRTLSFRKKRSHAILSPPSPSYNAETEDCD
LNYSDVMSKLGFLSERSTSPINSSPPRCWSPTDPRAEEIMAAAEKEAMLF
KGPNVYKKTVNSRIGKTSRARAQIKKSKAKLANPSIVTKKRNKRNQTNKL
VDDGKKKPRAKQKTNEKGTSRKHTTLKDEKIKSQSGAEVKFVLKHQNVSE
FASSSGGSQLLFKQKDMPLMGSAVDHPLSASLPTGINAQQKLSGCFSSFL
ESKKSVDLQTFPSSRDDLHPSVVCNSIGPGVSKINVQRPHNQSAMFTLKE
STLIQKNIFDLSNHLSQVAQNTQISSGMSSKIEDNANNIQRNYLSSIGKL
SEYRNSLESKLDQAYTPNFLHCKDSQQQIVCIAEQSKHSETCSPGNTASE
ESQMPNNCFVTSLRSPIKQIAWEQKQRGFILDMSNFKPERVKPRSLSEAI
SQTKALSQCKNRNVSTPSAFGEGQSGLAVLKELLQKRQQKAQNANTTQDP
LSNKHQPNKNISGSLEHNKANKRTRSVTSPRKPRTPRSTKQKEKIPKLLK
VDSLNLQNSSQLDNSVSDDSPIFFSDPGFESCYSLEDSLSPEHNYNFDIN
TIGQTGFCSFYSGSQFVPADQNLPQKFLSDAVQDLFPGQAIEKNEFLSHD
NQKCDEDKHHTTDSASWIRSGTLSPEIFEKSTIDSNENRRHNQWKNSFHP
LTTRSNSIMDSFCVQQAEDCLSEKSRLNRSSVSKEVFLSLPQPNNSDWIQ
GHTRKEMGQSLDSANTSFTAILSSPDGELVDVACEDLELYVSRNNDMLTP
TPDSSPRSTSSPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHDLS
ETIYQEPFCSNPSDVPEKPREIGGRLLMVETRLANDLAEFEGDFSLEGLR
LWKTAFSAMTQNPRPGSPLRSGQGVVNKGSSNSPKMVEDKKIVIMPCKCA
PSRQLVQVWLQAKEEYERSKKLPKTKPTGVVKSAENFSSSVNPDDKPVVP
PKMDVSPCILPTTAHTKEDVDNSQIALQAPTTGCSQTASESQMLPPVASA
SDPEKDEDDDDNYYISYSSPDSPVIPPWQQPISPDSKALNGDDRPSSPVE
ELPSLAFENFLKPIKDGIQKSPCSEPQEPLVISPINTRARTGKCESLCFH
STPIIQRKLLERLPEAPGLSPLSTEPKTQKLSNKKGSNTDTLRRVLLTQA
KNQFAAVNTPQKETSQIDGPSLNNTYGFKVSIQNLQEAKALHEIQNLTLI
SVELHARTRRDLEPDPEFDPICALFYCISSDTPLPDTEKTELTGVIVIDK
DKTVFSQDIRYQTPLLIRSGITGLEVTYAADEKALFHEIANIIKRYDPDI
LLGYEIQMHSWGYLLQRAAALSIDLCRMISRVPDDKIENRFAAERDEYGS
YTMSEINIVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRV
LSDWFDNKTDLYRWKMVDHYVSRVRGNLQMLEQLDLIGKTSEMARLFGIQ
FLHVLTRGSQYRVESMMLRIAKPMNYIPVTPSVQQRSQMRAPQCVPLIME
PESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENLGKYDEFKFGC
TSLRVPPDLLYQVRHDITVSPNGVAFVKPSVRKGVLPRMLEEILKTRFMV
KQSMKAYKQDRALSRMLDARQLGLKLIANVTFGYTSANFSGRMPCIEVGD
SIVHKARETLERAIKLVNDTKKWGARVVYGDTDSMFVLLKGATKEQSFKI
GQEIAEAVTATNPKPVKLKFEKVYLPCVLQTKKRYVGYMYETLDQKDPVF
DAKGIETVRRDSCPAVSKILERSLKLLFETRDISLIKQYVQRQCMKLLEG
KASIQDFIFAKEYRGSFSYKPGACVPALELTRKMLTYDRRSEPQVGERVP
YVIIYGTPGVPLIQLVRRPVEVLQDPTLRLNATYYITKQILPPLARIFSL
IGIDVFSWYHELPRIHKATSSSRSEPEGRKGTISQYFTTLHCPVCDDLTQ
HGICSKCRSQPQHVAVILNQEIRELERQQEQLVKICKNCTGCFDRHIPCV
SLNCPVLFKLSRVNRELSKAPYLRQLLDQF

REV3L (Homo sapiens) is able to recognize following damages:
References:

Title Authors Journal
Alternative splicing, genomic structure, and fine chromosome localization of REV3L. Morelli C, Mungall AJ, Negrini M, Barbanti-Brodano G, Croce CM Cytogenet Cell Genet Jan. 1, 1998
A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta. Gibbs PE, McGregor WG, Maher VM, Nisson P, Lawrence CW Proc Natl Acad Sci U S A June 9, 1998
A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for damage-induced mutagenesis in humans. Lin W, Wu X, Wang Z Mutat Res March 10, 1999
A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, Fishel R J Biol Chem Jan. 11, 2000
The DNA sequence and analysis of human chromosome 6. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S Nature Oct. 23, 2003
Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R Nat Methods Aug. 1, 2005
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009


Last modification of this entry: Oct. 14, 2010.

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