Q9UBZ9 (REV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein REV1
EC=2.7.7.-

Alternative name(s):
Alpha integrin-binding protein 80
Short name=AIBP80
Rev1-like terminal deoxycytidyl transferase

Gene names

Name:	REV1
Synonyms:	REV1L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1251 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.10
Subunit structure	Monomer. Interacts with the DNA polymerase zeta which is composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct and requires that REV3L is in its closed conformation. Interacts with POLH, POLI and POLK. May bind ITGA3. Interacts with FAAP20/C1orf86. Ref.4 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus Probable.
Tissue specificity	Ubiquitous. Ref.1 Ref.3 Ref.4
Domain	The C-terminal domain is necessary for protein interactions.
Sequence similarities	Belongs to the DNA polymerase type-Y family. Contains 1 BRCT domain. Contains 1 umuC domain.
Sequence caution	The sequence AAK43708.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA synthesis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Traceable author statement Ref.1. Source: ProtInc error-prone translesion synthesis Traceable author statement Ref.4. Source: UniProtKB response to UV Inferred from direct assay Ref.4. Source: UniProtKB
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA-directed DNA polymerase activity Traceable author statement. Source: Reactome damaged DNA binding Traceable author statement Ref.1. Source: ProtInc deoxycytidyl transferase activity Inferred from electronic annotation. Source: Compara magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UBZ9-1)

Also known as: REV1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UBZ9-2)

Also known as: REV1S;

The sequence of this isoform differs from the canonical sequence as follows:
     479-479: Missing.

Isoform 3 (identifier: Q9UBZ9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     406-413: DMSVLNSP → RYLLKLSS
     414-1251: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1251

1251

DNA repair protein REV1

PRO_0000173992

Regions

Domain

44 – 131

88

BRCT

Domain

419 – 653

235

UmuC

Nucleotide binding

423 – 427

5

dCTP binding By similarity

Nucleotide binding

510 – 516

7

dCTP binding By similarity

Region

352 – 362

11

Interaction with target DNA By similarity

Region

653 – 656

4

Interaction with target DNA By similarity

Region

709 – 717

9

Interaction with target DNA By similarity

Region

1150 – 1249

100

Protein interaction domain; mediates interaction with DNA polymerase zeta

Motif

1071 – 1078

8

Nuclear localization signal Potential

Sites

Metal binding

423

1

Magnesium 1 By similarity

Metal binding

423

1

Magnesium 2 By similarity

Metal binding

570

1

Magnesium 1 By similarity

Metal binding

571

1

Magnesium 1 By similarity

Binding site

357

1

dCTP By similarity

Binding site

522

1

dCTP By similarity

Binding site

570

1

dCTP By similarity

Site

770

1

Interaction with target DNA By similarity

Site

783

1

Interaction with target DNA By similarity

Natural variations

Alternative sequence

1 – 21

21

Missing in isoform 3.

VSP_012809

Alternative sequence

406 – 413

8

DMSVLNSP → RYLLKLSS in isoform 3.

VSP_012810

Alternative sequence

414 – 1251

838

Missing in isoform 3.

VSP_012811

Alternative sequence

479

1

Missing in isoform 2.

VSP_012812

Natural variant

138

1

V → M.
Corresponds to variant rs3087403 [ dbSNP | Ensembl ].

VAR_021249

Natural variant

257

1

F → S.
Corresponds to variant rs3087386 [ dbSNP | Ensembl ].

VAR_021250

Natural variant

306

1

N → D.
Corresponds to variant rs28382882 [ dbSNP | Ensembl ].

VAR_029193

Natural variant

373

1

N → S.
Corresponds to variant rs3087399 [ dbSNP | Ensembl ].

VAR_021251

Natural variant

656

1

M → V.
Corresponds to variant rs3087394 [ dbSNP | Ensembl ].

VAR_029194

Natural variant

660

1

L → W.
Corresponds to variant rs3087398 [ dbSNP | Ensembl ].

VAR_029195

Natural variant

700

1

D → N.
Corresponds to variant rs28382941 [ dbSNP | Ensembl ].

VAR_029196

Natural variant

704

1

R → Q.
Corresponds to variant rs28382942 [ dbSNP | Ensembl ].

VAR_029197

Natural variant

902

1

P → H.
Corresponds to variant rs28382961 [ dbSNP | Ensembl ].

VAR_029199

Natural variant

902

1

P → S.
Corresponds to variant rs28382960 [ dbSNP | Ensembl ].

VAR_029198

Natural variant

921

1

S → I.
Corresponds to variant rs3087396 [ dbSNP | Ensembl ].

VAR_029200

Natural variant

1003

1

A → T.
Corresponds to variant rs3087401 [ dbSNP | Ensembl ].

VAR_024436

Natural variant

1060

1

P → T.
Corresponds to variant rs3087388 [ dbSNP | Ensembl ].

VAR_029201

Natural variant

1074

1

N → K.
Corresponds to variant rs3087393 [ dbSNP | Ensembl ].

VAR_029202

Natural variant

1091

1

N → T.
Corresponds to variant rs3087392 [ dbSNP | Ensembl ].

VAR_029203

Natural variant

1102

1

L → P.
Corresponds to variant rs3087400 [ dbSNP | Ensembl ].

VAR_029204

Experimental info

Mutagenesis

570

1

D → A: Abolishes transferase activity; when associated with A-571. Ref.3

Mutagenesis

571

1

E → A: Abolishes transferase activity; when associated with A-570. Ref.3

Secondary structure

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1251

Helix Strand Turn

Details...

Turn

48 – 51

4

Beta strand

53 – 56

4

Helix

64 – 73

10

Beta strand

84 – 86

3

Beta strand

89 – 91

3

Helix

99 – 102

4

Beta strand

104 – 106

3

Helix

112 – 120

9

Helix

127 – 129

3

Helix

345 – 355

11

Helix

357 – 375

19

Helix

384 – 387

4

Beta strand

419 – 424

6

Helix

427 – 432

6

Turn

433 – 435

3

Turn

437 – 441

5

Beta strand

444 – 446

3

Helix

463 – 471

9

Turn

472 – 475

4

Helix

500 – 502

3

Beta strand

509 – 511

3

Helix

513 – 516

4

Turn

517 – 519

3

Helix

526 – 532

7

Beta strand

537 – 539

3

Helix

543 – 558

16

Beta strand

564 – 568

5

Beta strand

571 – 575

5

Helix

577 – 583

7

Helix

587 – 602

16

Beta strand

606 – 613

8

Helix

614 – 624

11

Beta strand

629 – 631

3

Helix

634 – 636

3

Helix

637 – 643

7

Helix

646 – 648

3

Helix

654 – 662

9

Helix

668 – 671

4

Helix

676 – 683

8

Helix

685 – 694

10

Turn

695 – 697

3

Beta strand

712 – 716

5

Helix

725 – 745

21

Beta strand

748 – 760

13

Beta strand

776 – 790

15

Helix

793 – 805

13

Helix

811 – 813

3

Beta strand

814 – 826

13

Beta strand

1160 – 1162

3

Helix

1165 – 1179

15

Helix

1184 – 1199

16

Helix

1203 – 1218

16

Helix

1224 – 1243

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (REV1) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 010E261D537DBA80	FASTA	1,251	138,248
	10 20 30 40 50 60 MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS GVAIYVNGYT 70 80 90 100 110 120 DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA 130 140 150 160 170 180 GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP EDPLPGPSNI AKQLNNRVNH IVKKIETENE 190 200 210 220 230 240 VKVNGMNSWN EEDENNDFSF VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD 250 260 270 280 290 300 CLVPMVNSVA SRLSPAFSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL 310 320 330 340 350 360 SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS NFYSHSRLHH 370 380 390 400 410 420 ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV VTDTGDMSVL NSPRHQSCIM 430 440 450 460 470 480 HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR GTGRAPLRPG ANPQLEWQYY QNKILKGKAA 490 500 510 520 530 540 DIPDSSLWEN PDSAQANGID SVLSRAEIAS CSYEARQLGI KNGMFFGHAK QLCPNLQAVP 550 560 570 580 590 600 YDFHAYKEVA QTLYETLASY THNIEAVSCD EALVDITEIL AETKLTPDEF ANAVRMEIKD 610 620 630 640 650 660 QTKCAASVGI GSNILLARMA TRKAKPDGQY HLKPEEVDDF IRGQLVTNLP GVGHSMESKL 670 680 690 700 710 720 ASLGIKTCGD LQYMTMAKLQ KEFGPKTGQM LYRFCRGLDD RPVRTEKERK SVSAEINYGI 730 740 750 760 770 780 RFTQPKEAEA FLLSLSEEIQ RRLEATGMKG KRLTLKIMVR KPGAPVETAK FGGHGICDNI 790 800 810 820 830 840 ARTVTLDQAT DNAKIIGKAM LNMFHTMKLN ISDMRGVGIH VNQLVPTNLN PSTCPSRPSV 850 860 870 880 890 900 QSSHFPSGSY SVRDVFQVQK AKKSTEEEHK EVFRAAVDLE ISSASRTCTF LPPFPAHLPT 910 920 930 940 950 960 SPDTNKAESS GKWNGLHTPV SVQSRLNLSI EVPSPSQLDQ SVLEALPPDL REQVEQVCAV 970 980 990 1000 1010 1020 QQAESHGDKK KEPVNGCNTG ILPQPVGTVL LQIPEPQESN SDAGINLIAL PAFSQVDPEV 1030 1040 1050 1060 1070 1080 FAALPAELQR ELKAAYDQRQ RQGENSTHQQ SASASVPKNP LLHLKAAVKE KKRNKKKKTI 1090 1100 1110 1120 1130 1140 GSPKRIQSPL NNKLLNSPAK TLPGACGSPQ KLIDGFLKHE GPPAEKPLEE LSASTSGVPG 1150 1160 1170 1180 1190 1200 LSSLQSDPAG CVRPPAPNLA GAVEFNDVKT LLREWITTIS DPMEEDILQV VKYCTDLIEE 1210 1220 1230 1240 1250 KDLEKLDLVI KYMKRLMQQS VESVWNMAFD FILDNVQVVL QQTYGSTLKV T
	Isoform 2 (REV1S) [UniParc]. Checksum: B4B1606DB6E866F2	FASTA	1,250	138,177
	10 20 30 40 50 60 MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS GVAIYVNGYT 70 80 90 100 110 120 DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA 130 140 150 160 170 180 GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP EDPLPGPSNI AKQLNNRVNH IVKKIETENE 190 200 210 220 230 240 VKVNGMNSWN EEDENNDFSF VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD 250 260 270 280 290 300 CLVPMVNSVA SRLSPAFSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL 310 320 330 340 350 360 SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS NFYSHSRLHH 370 380 390 400 410 420 ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV VTDTGDMSVL NSPRHQSCIM 430 440 450 460 470 480 HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR GTGRAPLRPG ANPQLEWQYY QNKILKGKAD 490 500 510 520 530 540 IPDSSLWENP DSAQANGIDS VLSRAEIASC SYEARQLGIK NGMFFGHAKQ LCPNLQAVPY 550 560 570 580 590 600 DFHAYKEVAQ TLYETLASYT HNIEAVSCDE ALVDITEILA ETKLTPDEFA NAVRMEIKDQ 610 620 630 640 650 660 TKCAASVGIG SNILLARMAT RKAKPDGQYH LKPEEVDDFI RGQLVTNLPG VGHSMESKLA 670 680 690 700 710 720 SLGIKTCGDL QYMTMAKLQK EFGPKTGQML YRFCRGLDDR PVRTEKERKS VSAEINYGIR 730 740 750 760 770 780 FTQPKEAEAF LLSLSEEIQR RLEATGMKGK RLTLKIMVRK PGAPVETAKF GGHGICDNIA 790 800 810 820 830 840 RTVTLDQATD NAKIIGKAML NMFHTMKLNI SDMRGVGIHV NQLVPTNLNP STCPSRPSVQ 850 860 870 880 890 900 SSHFPSGSYS VRDVFQVQKA KKSTEEEHKE VFRAAVDLEI SSASRTCTFL PPFPAHLPTS 910 920 930 940 950 960 PDTNKAESSG KWNGLHTPVS VQSRLNLSIE VPSPSQLDQS VLEALPPDLR EQVEQVCAVQ 970 980 990 1000 1010 1020 QAESHGDKKK EPVNGCNTGI LPQPVGTVLL QIPEPQESNS DAGINLIALP AFSQVDPEVF 1030 1040 1050 1060 1070 1080 AALPAELQRE LKAAYDQRQR QGENSTHQQS ASASVPKNPL LHLKAAVKEK KRNKKKKTIG 1090 1100 1110 1120 1130 1140 SPKRIQSPLN NKLLNSPAKT LPGACGSPQK LIDGFLKHEG PPAEKPLEEL SASTSGVPGL 1150 1160 1170 1180 1190 1200 SSLQSDPAGC VRPPAPNLAG AVEFNDVKTL LREWITTISD PMEEDILQVV KYCTDLIEEK 1210 1220 1230 1240 1250 DLEKLDLVIK YMKRLMQQSV ESVWNMAFDF ILDNVQVVLQ QTYGSTLKVT
	Isoform 3 [UniParc]. Checksum: A0EA83A568AD74F9	FASTA	392	43,649
	10 20 30 40 50 60 MAAKVQKLEE QFRSDAAMQK DGTSSTIFSG VAIYVNGYTD PSAEELRKLM MLHGGQYHVY 70 80 90 100 110 120 YSRSKTTHII ATNLPNAKIK ELKGEKVIRP EWIVESIKAG RLLSYIPYQL YTKQSSVQKG 130 140 150 160 170 180 LSFNPVCRPE DPLPGPSNIA KQLNNRVNHI VKKIETENEV KVNGMNSWNE EDENNDFSFV 190 200 210 220 230 240 DLEQTSPGRK QNGIPHPRGS TAIFNGHTPS SNGALKTQDC LVPMVNSVAS RLSPAFSQEE 250 260 270 280 290 300 DKAEKSSTDF RDCTLQQLQQ STRNTDALRN PHRTNSFSLS PLHSNTKING AHHSTVQGPS 310 320 330 340 350 360 STKSTSSVST FSKAAPSVPS KPSDCNFISN FYSHSRLHHI SMWKCELTEF VNTLQRQSNG 370 380 390 IFPGREKLKK MKTGRSALVV TDTGRYLLKL SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human REV1 gene codes for a DNA template-dependent dCMP transferase." Lin W., Xin H., Zhang X., Wu X., Yuan F., Wang Z. Nucleic Acids Res. 27:4468-4475(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Tissue: Bone marrow, Leukocyte and T-cell.
[2]	"The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light." Gibbs P.E.M., Wang X.-D., Li Z., McManus T.P., McGregor W.G., Lawrence C.W., Maher V.M. Proc. Natl. Acad. Sci. U.S.A. 97:4186-4191(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ROLE IN UV-INDUCED MUTAGENESIS. Tissue: Brain.
[3]	"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. 276:15051-15058(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, MUTAGENESIS OF ASP-570 AND GLU-571, TISSUE SPECIFICITY. Tissue: Mammary cancer and Testis.
[4]	"Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7." Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M., Fishel R., Takahashi M. J. Biol. Chem. 276:35644-35651(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH REV3L AND MAD2L2. Tissue: Testis.
[5]	"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 T.-O., 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. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Placenta.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., 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 E.A., 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 S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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. 445:351-355(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 479-1251 (ISOFORM 2), INTERACTION WITH ITGA3. Tissue: Placenta.
[8]	"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. 278:12356-12360(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAD2L2.
[9]	"Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1." Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S., Akashi S., Takeda S., Shimizu T., Sato M. J. Biol. Chem. 285:12299-12307(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNA POLYMERASE ZETA.
[10]	"Regulation of Rev1 by the Fanconi anemia core complex." Kim H., Yang K., Dejsuphong D., D'Andrea A.D. Nat. Struct. Mol. Biol. 19:164-170(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH C1ORF86.
[11]	"Solution structure of the BRCT domain from human DNA repair protein REV1." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 43-133.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF151538 mRNA. Translation: AAF06731.1.
AF206019 mRNA. Translation: AAF18986.1.
AB047646 mRNA. Translation: BAB21441.1.
AF357886 mRNA. Translation: AAK43708.1. Different initiation.
AK002087 mRNA. Translation: BAA92079.1.
AC018690 Genomic DNA. Translation: AAY24314.1.
AJ131720 mRNA. Translation: CAB38231.1.

IPI

IPI00008816.
IPI00552928.
IPI00552936.

RefSeq

NP_001032961.1. NM_001037872.1.
NP_057400.1. NM_016316.2.

UniGene

Hs.443077.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EBW	NMR	-	A	44-133	[»]
2LSK	NMR	-	A	1158-1251	[»]
2LSY	NMR	-	A	1158-1251	[»]
3GQC	X-ray	2.50	A/B/C/D	330-833	[»]
3VU7	X-ray	2.80	H	1140-1251	[»]
4GK0	X-ray	2.70	E/F	1117-1251	[»]
4GK5	X-ray	3.21	E/F	1117-1251	[»]

ProteinModelPortal

Q9UBZ9.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-140323.

STRING

9606.ENSP00000258428.

PTM databases

PhosphoSite

Q9UBZ9.

Polymorphism databases

DMDM

59798439.

Proteomic databases

PaxDb

Q9UBZ9.

PRIDE

Q9UBZ9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000258428; ENSP00000258428; ENSG00000135945.
ENST00000393445; ENSP00000377091; ENSG00000135945.

GeneID

51455.

KEGG

hsa:51455.

UCSC

uc002tac.3. human.
uc002tad.3. human.
uc002tae.1. human.

Organism-specific databases

CTD

51455.

GeneCards

GC02M100016.

HGNC

HGNC:14060. REV1.

HPA

HPA044534.
HPA051036.

MIM

606134. gene.

neXtProt

NX_Q9UBZ9.

PharmGKB

PA162401120.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0389.

HOGENOM

HOG000154094.

HOVERGEN

HBG054140.

InParanoid

Q9UBZ9.

KO

K03515.

OMA

YRFCRGL.

OrthoDB

EOG4GF3DF.

PhylomeDB

Q9UBZ9.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q9UBZ9.

Bgee

Q9UBZ9.

CleanEx

HS_REV1.

Genevestigator

Q9UBZ9.

GermOnline

ENSG00000135945. Homo sapiens.

Family and domain databases

Gene3D

3.30.1490.100. 1 hit.

InterPro

IPR001357. BRCT_dom.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
IPR012112. REV1.
[Graphical view]

Pfam

PF00533. BRCT. 1 hit.
PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]

PIRSF

PIRSF036573. REV1. 1 hit.

SMART

SM00292. BRCT. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF100879. DNA_pol_Y-fam_little_finger. 1 hit.

PROSITE

PS50172. BRCT. 1 hit.
PS50173. UMUC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

REV1. human.

EvolutionaryTrace

Q9UBZ9.

GenomeRNAi

51455.

NextBio

55069.

SOURCE

Search...

Entry information

Entry name

REV1_HUMAN

Accession

Primary (citable) accession number: Q9UBZ9
Secondary accession number(s): O95941 , Q53SI7, Q9C0J4, Q9NUP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.