Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UBZ9 (REV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1251 AA.
Sequence statusComplete.
Protein existenceEvidence 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.11

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.10 Ref.11

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12511251DNA repair protein REV1
PRO_0000173992

Regions

Domain44 – 13188BRCT
Domain419 – 653235UmuC
Nucleotide binding423 – 4275dCTP binding By similarity
Nucleotide binding510 – 5167dCTP binding By similarity
Region352 – 36211Interaction with target DNA By similarity
Region653 – 6564Interaction with target DNA By similarity
Region709 – 7179Interaction with target DNA By similarity
Region1150 – 1249100Protein interaction domain; mediates interaction with DNA polymerase zeta
Motif1071 – 10788Nuclear localization signal Potential

Sites

Metal binding4231Magnesium 1 By similarity
Metal binding4231Magnesium 2 By similarity
Metal binding5701Magnesium 1 By similarity
Metal binding5711Magnesium 1 By similarity
Binding site3571dCTP By similarity
Binding site5221dCTP By similarity
Binding site5701dCTP By similarity
Site7701Interaction with target DNA By similarity
Site7831Interaction with target DNA By similarity

Natural variations

Alternative sequence1 – 2121Missing in isoform 3.
VSP_012809
Alternative sequence406 – 4138DMSVLNSP → RYLLKLSS in isoform 3.
VSP_012810
Alternative sequence414 – 1251838Missing in isoform 3.
VSP_012811
Alternative sequence4791Missing in isoform 2.
VSP_012812
Natural variant1381V → M.
Corresponds to variant rs3087403 [ dbSNP | Ensembl ].
VAR_021249
Natural variant2571F → S.
Corresponds to variant rs3087386 [ dbSNP | Ensembl ].
VAR_021250
Natural variant3061N → D.
Corresponds to variant rs28382882 [ dbSNP | Ensembl ].
VAR_029193
Natural variant3731N → S.
Corresponds to variant rs3087399 [ dbSNP | Ensembl ].
VAR_021251
Natural variant6561M → V.
Corresponds to variant rs3087394 [ dbSNP | Ensembl ].
VAR_029194
Natural variant6601L → W.
Corresponds to variant rs3087398 [ dbSNP | Ensembl ].
VAR_029195
Natural variant7001D → N.
Corresponds to variant rs28382941 [ dbSNP | Ensembl ].
VAR_029196
Natural variant7041R → Q.
Corresponds to variant rs28382942 [ dbSNP | Ensembl ].
VAR_029197
Natural variant9021P → H.
Corresponds to variant rs28382961 [ dbSNP | Ensembl ].
VAR_029199
Natural variant9021P → S.
Corresponds to variant rs28382960 [ dbSNP | Ensembl ].
VAR_029198
Natural variant9211S → I.
Corresponds to variant rs3087396 [ dbSNP | Ensembl ].
VAR_029200
Natural variant10031A → T.
Corresponds to variant rs3087401 [ dbSNP | Ensembl ].
VAR_024436
Natural variant10601P → T.
Corresponds to variant rs3087388 [ dbSNP | Ensembl ].
VAR_029201
Natural variant10741N → K.
Corresponds to variant rs3087393 [ dbSNP | Ensembl ].
VAR_029202
Natural variant10911N → T.
Corresponds to variant rs3087392 [ dbSNP | Ensembl ].
VAR_029203
Natural variant11021L → P.
Corresponds to variant rs3087400 [ dbSNP | Ensembl ].
VAR_029204

Experimental info

Mutagenesis5701D → A: Abolishes transferase activity; when associated with A-571. Ref.3
Mutagenesis5711E → A: Abolishes transferase activity; when associated with A-570. Ref.3

Secondary structure

...................................................................................................... 1251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (REV1) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 010E261D537DBA80

FASTA1,251138,248
        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 

« Hide

Isoform 2 (REV1S) [UniParc].

Checksum: B4B1606DB6E866F2
Show »

FASTA1,250138,177
Isoform 3 [UniParc].

Checksum: A0EA83A568AD74F9
Show »

FASTA39243,649

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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.
[11]"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.
[12]"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.
RefSeqNP_001032961.1. NM_001037872.1.
NP_057400.1. NM_016316.2.
UniGeneHs.443077.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBWNMR-A44-133[»]
2LSINMR-A1156-1251[»]
2LSKNMR-A1158-1251[»]
2LSYNMR-A1158-1251[»]
3GQCX-ray2.50A/B/C/D330-833[»]
3VU7X-ray2.80H1140-1251[»]
4BA9X-ray2.73A/B/C/D/E/F1158-1242[»]
4EXTX-ray1.90A1156-1251[»]
4GK0X-ray2.70E/F1117-1251[»]
4GK5X-ray3.21E/F1117-1251[»]
ProteinModelPortalQ9UBZ9.
SMRQ9UBZ9. Positions 48-133, 344-828, 1156-1251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119551. 15 interactions.
IntActQ9UBZ9. 3 interactions.
MINTMINT-140323.
STRING9606.ENSP00000258428.

PTM databases

PhosphoSiteQ9UBZ9.

Polymorphism databases

DMDM59798439.

Proteomic databases

PaxDbQ9UBZ9.
PRIDEQ9UBZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258428; ENSP00000258428; ENSG00000135945. [Q9UBZ9-1]
ENST00000393445; ENSP00000377091; ENSG00000135945. [Q9UBZ9-2]
GeneID51455.
KEGGhsa:51455.
UCSCuc002tac.3. human. [Q9UBZ9-2]
uc002tad.3. human. [Q9UBZ9-1]
uc002tae.1. human. [Q9UBZ9-3]

Organism-specific databases

CTD51455.
GeneCardsGC02M100016.
HGNCHGNC:14060. REV1.
HPAHPA044534.
HPA051036.
MIM606134. gene.
neXtProtNX_Q9UBZ9.
PharmGKBPA162401120.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0389.
HOGENOMHOG000154094.
HOVERGENHBG054140.
InParanoidQ9UBZ9.
KOK03515.
OMAYRFCRGL.
OrthoDBEOG761BTT.
PhylomeDBQ9UBZ9.
TreeFamTF314488.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
SignaLinkQ9UBZ9.

Gene expression databases

ArrayExpressQ9UBZ9.
BgeeQ9UBZ9.
CleanExHS_REV1.
GenevestigatorQ9UBZ9.

Family and domain databases

Gene3D3.30.1490.100. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. 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]
PfamPF00533. BRCT. 1 hit.
PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
PIRSFPIRSF036573. REV1. 1 hit.
SMARTSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF100879. SSF100879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSREV1. human.
EvolutionaryTraceQ9UBZ9.
GeneWikiREV1.
GenomeRNAi51455.
NextBio55069.
PROQ9UBZ9.
SOURCESearch...

Entry information

Entry nameREV1_HUMAN
AccessionPrimary (citable) accession number: Q9UBZ9
Secondary accession number(s): O95941 expand/collapse secondary AC list , Q53SI7, Q9C0J4, Q9NUP2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM