|
|
|
|
|
|
Description:
DNA repair protein REV1 (EC 2.7.7.-) (Rev1-like terminal deoxycytidyltransferase) (Alpha integrin-binding protein 80) (AIBP80).
Molecular weight: 1382
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) error-prone postreplication DNA repair( GO:0042276 )
Important dates:
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-MAR-2006, entry version 32.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein REV1_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AF151538 | AAF06731.1 | - |
| EMBL | AF206019 | AAF18986.1 | - |
| EMBL | AB047646 | BAB21441.1 | - |
| EMBL | AF357886 | AAK43708.1 | ALT_INIT |
| EMBL | AK002087 | BAA92079.1 | - |
| EMBL | AJ131720 | CAB38231.1 | - |
| HSSP | P96022 | 1IM4 | |
| Ensembl | ENSG00000135945 | Homo sapiens.1 | |
| HGNC | HGNC:14060 | REV1L.1 | |
| MIM | 606134 | gene. | |
| GO | GO:0003684 | F:damaged DNA binding | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006260 | P:DNA replication | TAS. |
| GO | GO:0042276 | P:error-prone postreplication DNA repair | TAS. |
| GO | GO:0006280 | P:mutagenesis | TAS. |
| GO | GO:0009411 | P:response to UV | IDA. |
| InterPro | IPR001357 | BRCT. | |
| InterPro | IPR012112 | REV1. | |
| InterPro | IPR001126 | UMUC_like. | |
| Pfam | PF00533 | BRCT | 1. |
| Pfam | PF00817 | IMS | 1. |
| PIRSF | PIRSF036573 | REV1 | 1. |
| SMART | SM00292 | BRCT | 1. |
| PROSITE | PS50172 | BRCT | 1. |
| PROSITE | PS50173 | UMUC | 1. |
Keywords:
Alternative splicing; DNA damage; DNA repair; DNA synthesis; DNA-binding; Magnesium; Metal-binding; Nuclear protein; Nucleotidyltransferase; Polymorphism; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bone marrow, Leukocyte, and T-cell;
RX MEDLINE=20007892; PubMed=10536157; DOI=10.1093/nar/27.22.4468;
RA Lin W., Xin H., Zhang X., Wu X., Yuan F., Wang Z.;
RT "The human REV1 gene codes for a DNA template-dependent dCMP
RT transferase.";
RL Nucleic Acids Res. 27:4468-4475(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ROLE IN UV-INDUCED
RP MUTAGENESIS.
RC TISSUE=Brain;
RX MEDLINE=20226079; PubMed=10760286; DOI=10.1073/pnas.97.8.4186;
RA Gibbs P.E.M., Wang X.-D., Li Z., McManus T.P., McGregor W.G.,
RA Lawrence C.W., Maher V.M.;
RT "The function of the human homolog of Saccharomyces cerevisiae REV1 is
RT required for mutagenesis induced by UV light.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4186-4191(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, MUTAGENESIS
RP OF ASP-570 AND GLU-571, AND TISSUE SPECIFICITY.
RC TISSUE=Mammary cancer, and Testis;
RX MEDLINE=21226747; PubMed=11278384; DOI=10.1074/jbc.M008082200;
RA Masuda Y., Takahashi M., Tsunekuni N., Minami T., Sumii M.,
RA Miyagawa K., Kamiya K.;
RT "Deoxycytidyl transferase activity of the human REV1 protein is
RT closely associated with the conserved polymerase domain.";
RL J. Biol. Chem. 276:15051-15058(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP AND INTERACTIONS WITH REV3L AND MAD2L2.
RC TISSUE=Testis;
RX MEDLINE=21443799; PubMed=11485998; DOI=10.1074/jbc.M102051200;
RA Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M.,
RA Fishel R., Takahashi M.;
RT "Interactions in the error-prone postreplication repair proteins
RT hREV1, hREV3, and hREV7.";
RL J. Biol. Chem. 276:35644-35651(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 479-1251 (ISOFORM 2), AND INTERACTION
RP WITH ITGA3.
RC TISSUE=Placenta;
RX MEDLINE=99192311; PubMed=10094488; DOI=10.1016/S0014-5793(99)00151-9;
RA Wixler V., Laplantine E., Geerts D., Sonnenberg A., Petersohn D.,
RA Eckes B., Paulsson M., Aumailley M.;
RT "Identification of novel interaction partners for the conserved
RT membrane proximal region of alpha-integrin cytoplasmic domains.";
RL FEBS Lett. 445:351-355(1999).
RN [7]
RP INTERACTION WITH MAD2L2.
RX PubMed=12529368; DOI=10.1074/jbc.M211765200;
RA Masuda Y., Ohmae M., Masuda K., Kamiya K.;
RT "Structure and enzymatic properties of a stable complex of the human
RT REV1 and REV7 proteins.";
RL J. Biol. Chem. 278:12356-12360(2003).
Feature:
CHAIN 1 1251 DNA repair protein REV1.
/FTId=PRO_0000173992.
DOMAIN 44 131 BRCT.
DOMAIN 419 653 UmuC.
REGION 1150 1249 Protein interaction domain (By
similarity).
MOTIF 1071 1078 Nuclear localization signal (Potential).
METAL 423 423 Magnesium (By similarity).
METAL 570 570 Magnesium (By similarity).
VARSPLIC 1 21 Missing (in isoform 3).
/FTId=VSP_012809.
VARSPLIC 406 413 DMSVLNSP -> RYLLKLSS (in isoform 3).
/FTId=VSP_012810.
VARSPLIC 414 1251 Missing (in isoform 3).
/FTId=VSP_012811.
VARSPLIC 479 479 Missing (in isoform 2).
/FTId=VSP_012812.
VARIANT 138 138 V -> M (in dbSNP:3087403).
/FTId=VAR_021249.
VARIANT 257 257 F -> S (in dbSNP:3087386).
/FTId=VAR_021250.
VARIANT 373 373 N -> S (in dbSNP:3087399).
/FTId=VAR_021251.
VARIANT 1003 1003 A -> T (in dbSNP:3087401).
/FTId=VAR_024436.
MUTAGEN 570 570 D->A: Abolishes transferase activity;
when associated with A-571.
MUTAGEN 571 571 E->A: Abolishes transferase activity;
when associated with A-570.
Comments:
-!- FUNCTION: Required for normal induction of mutations by physical
and chemical agents. Has a deoxycytidyl transferase activity which
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.
-!- SUBUNIT: Monomer. Binds POLH, POLI and POLK (By similarity). Binds
MAD2L2 and REV3L. May bind ITGA3.
-!- SUBCELLULAR LOCATION: Nucleus (Probable).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=REV1;
IsoId=Q9UBZ9-1; Sequence=Displayed;
Name=2; Synonyms=REV1S;
IsoId=Q9UBZ9-2; Sequence=VSP_012812;
Name=3;
IsoId=Q9UBZ9-3; Sequence=VSP_012809, VSP_012810, VSP_012811;
Note=No experimental confirmation available;
-!- 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.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
Sequence length: 1251
MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS GVAIYVNGYT
DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA
GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP EDPLPGPSNI AKQLNNRVNH IVKKIETENE
VKVNGMNSWN EEDENNDFSF VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD
CLVPMVNSVA SRLSPAFSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL
SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS NFYSHSRLHH
ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV VTDTGDMSVL NSPRHQSCIM
HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR GTGRAPLRPG ANPQLEWQYY QNKILKGKAA
DIPDSSLWEN PDSAQANGID SVLSRAEIAS CSYEARQLGI KNGMFFGHAK QLCPNLQAVP
YDFHAYKEVA QTLYETLASY THNIEAVSCD EALVDITEIL AETKLTPDEF ANAVRMEIKD
QTKCAASVGI GSNILLARMA TRKAKPDGQY HLKPEEVDDF IRGQLVTNLP GVGHSMESKL
ASLGIKTCGD LQYMTMAKLQ KEFGPKTGQM LYRFCRGLDD RPVRTEKERK SVSAEINYGI
RFTQPKEAEA FLLSLSEEIQ RRLEATGMKG KRLTLKIMVR KPGAPVETAK FGGHGICDNI
ARTVTLDQAT DNAKIIGKAM LNMFHTMKLN ISDMRGVGIH VNQLVPTNLN PSTCPSRPSV
QSSHFPSGSY SVRDVFQVQK AKKSTEEEHK EVFRAAVDLE ISSASRTCTF LPPFPAHLPT
SPDTNKAESS GKWNGLHTPV SVQSRLNLSI EVPSPSQLDQ SVLEALPPDL REQVEQVCAV
QQAESHGDKK KEPVNGCNTG ILPQPVGTVL LQIPEPQESN SDAGINLIAL PAFSQVDPEV
FAALPAELQR ELKAAYDQRQ RQGENSTHQQ SASASVPKNP LLHLKAAVKE KKRNKKKKTI
GSPKRIQSPL NNKLLNSPAK TLPGACGSPQ KLIDGFLKHE GPPAEKPLEE LSASTSGVPG
LSSLQSDPAG CVRPPAPNLA GAVEFNDVKT LLREWITTIS DPMEEDILQV VKYCTDLIEE
KDLEKLDLVI KYMKRLMQQS VESVWNMAFD FILDNVQVVL QQTYGSTLKV T