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Protein

DNA polymerase zeta catalytic subunit

Gene

REV3L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi3042 – 30421ZincBy similarity
Metal bindingi3045 – 30451ZincBy similarity
Metal bindingi3054 – 30541ZincBy similarity
Metal bindingi3057 – 30571ZincBy similarity
Metal bindingi3086 – 30861Iron-sulfur (4Fe-4S)By similarity
Metal bindingi3089 – 30891Iron-sulfur (4Fe-4S)By similarity
Metal bindingi3099 – 30991Iron-sulfur (4Fe-4S)By similarity
Metal bindingi3104 – 31041Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri3042 – 305716CysA-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA-dependent DNA replication Source: ProtInc
  • DNA repair Source: Reactome
  • error-prone translesion synthesis Source: GO_Central
  • translesion synthesis Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase zeta catalytic subunit (EC:2.7.7.7)
Alternative name(s):
Protein reversionless 3-like
Short name:
REV3-like
Short name:
hREV3
Gene namesi
Name:REV3L
Synonyms:POLZ, REV3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:9968. REV3L.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: Ensembl
  • nucleoplasm Source: Reactome
  • zeta DNA polymerase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34337.

Polymorphism and mutation databases

BioMutaiREV3L.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31303130DNA polymerase zeta catalytic subunitPRO_0000046468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1030 – 10301PhosphoserineCombined sources
Modified residuei1041 – 10411PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60673.
PaxDbiO60673.
PRIDEiO60673.

PTM databases

iPTMnetiO60673.
PhosphoSiteiO60673.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiO60673.
CleanExiHS_REV3L.
ExpressionAtlasiO60673. baseline and differential.
GenevisibleiO60673. HS.

Organism-specific databases

HPAiHPA064853.

Interactioni

Subunit structurei

Interacts with MAD2L2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAD2L2Q9UI955EBI-2871302,EBI-77889

Protein-protein interaction databases

BioGridi111912. 28 interactions.
IntActiO60673. 8 interactions.
MINTiMINT-2796978.
STRINGi9606.ENSP00000351697.

Structurei

Secondary structure

1
3130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1877 – 18826Combined sources
Helixi1887 – 18937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ABDX-ray1.90X/Y1847-1898[»]
3ABEX-ray2.60Z1847-1898[»]
3VU7X-ray2.80Z1847-1898[»]
4EXTX-ray1.90B1873-1895[»]
4GK0X-ray2.70C/D1847-1898[»]
4GK5X-ray3.21C/D1847-1898[»]
ProteinModelPortaliO60673.
SMRiO60673. Positions 1868-1897.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60673.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1847 – 189852Mediates interaction with MAD2L2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3086 – 310419CysB motifAdd
BLAST

Domaini

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.
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated
Contains 1 CysA-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri3042 – 305716CysA-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0968. Eukaryota.
COG0417. LUCA.
GeneTreeiENSGT00550000074640.
HOGENOMiHOG000112263.
HOVERGENiHBG000426.
InParanoidiO60673.
KOiK02350.
OMAiFCSNPSD.
OrthoDBiEOG7F5113.
PhylomeDBiO60673.
TreeFamiTF101072.

Family and domain databases

Gene3Di3.30.420.10. 2 hits.
3.90.1600.10. 2 hits.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR032757. DUF4683.
IPR030559. PolZ_Rev3.
IPR012337. RNaseH-like_dom.
IPR025687. Znf-C4pol.
[Graphical view]
PANTHERiPTHR10322:SF5. PTHR10322:SF5. 4 hits.
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 2 hits.
PF15735. DUF4683. 1 hit.
PF14260. zf-C4pol. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 4 hits.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60673-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MFSVRIVTAD YYMASPLQGL DTCQSPLTQA PVKKVPVVRV FGATPAGQKT
60 70 80 90 100
CLHLHGIFPY LYVPYDGYGQ QPESYLSQMA FSIDRALNVA LGNPSSTAQH
110 120 130 140 150
VFKVSLVSGM PFYGYHEKER HFMKIYLYNP TMVKRICELL QSGAIMNKFY
160 170 180 190 200
QPHEAHIPYL LQLFIDYNLY GMNLINLAAV KFRKARRKSN TLHATGSCKN
210 220 230 240 250
HLSGNSLADT LFRWEQDEIP SSLILEGVEP QSTCELEVDA VAADILNRLD
260 270 280 290 300
IEAQIGGNPG LQAIWEDEKQ RRRNRNETSQ MSQPESQDHR FVPATESEKK
310 320 330 340 350
FQKRLQEILK QNDFSVTLSG SVDYSDGSQE FSAELTLHSE VLSPEMLQCT
360 370 380 390 400
PANMVEVHKD KESSKGHTRH KVEEALINEE AILNLMENSQ TFQPLTQRLS
410 420 430 440 450
ESPVFMDSSP DEALVHLLAG LESDGYRGER NRMPSPCRSF GNNKYPQNSD
460 470 480 490 500
DEENEPQIEK EEMELSLVMS QRWDSNIEEH CAKKRSLCRN THRSSTEDDD
510 520 530 540 550
SSSGEEMEWS DNSLLLASLS IPQLDGTADE NSDNPLNNEN SRTHSSVIAT
560 570 580 590 600
SKLSVKPSIF HKDAATLEPS SSAKITFQCK HTSALSSHVL NKEDLIEDLS
610 620 630 640 650
QTNKNTEKGL DNSVTSFTNE STYSMKYPGS LSSTVHSENS HKENSKKEIL
660 670 680 690 700
PVSSCESSIF DYEEDIPSVT RQVPSRKYTN IRKIEKDSPF IHMHRHPNEN
710 720 730 740 750
TLGKNSFNFS DLNHSKNKVS SEGNEKGNST ALSSLFPSSF TENCELLSCS
760 770 780 790 800
GENRTMVHSL NSTADESGLN KLKIRYEEFQ EHKTEKPSLS QQAAHYMFFP
810 820 830 840 850
SVVLSNCLTR PQKLSPVTYK LQPGNKPSRL KLNKRKLAGH QETSTKSSET
860 870 880 890 900
GSTKDNFIQN NPCNSNPEKD NALASDLTKT TRGAFENKTP TDGFIDCHFG
910 920 930 940 950
DGTLETEQSF GLYGNKYTLR AKRKVNYETE DSESSFVTHN SKISLPHPME
960 970 980 990 1000
IGESLDGTLK SRKRRKMSKK LPPVIIKYII INRFRGRKNM LVKLGKIDSK
1010 1020 1030 1040 1050
EKQVILTEEK MELYKKLAPL KDFWPKVPDS PATKYPIYPL TPKKSHRRKS
1060 1070 1080 1090 1100
KHKSAKKKTG KQQRTNNENI KRTLSFRKKR SHAILSPPSP SYNAETEDCD
1110 1120 1130 1140 1150
LNYSDVMSKL GFLSERSTSP INSSPPRCWS PTDPRAEEIM AAAEKEAMLF
1160 1170 1180 1190 1200
KGPNVYKKTV NSRIGKTSRA RAQIKKSKAK LANPSIVTKK RNKRNQTNKL
1210 1220 1230 1240 1250
VDDGKKKPRA KQKTNEKGTS RKHTTLKDEK IKSQSGAEVK FVLKHQNVSE
1260 1270 1280 1290 1300
FASSSGGSQL LFKQKDMPLM GSAVDHPLSA SLPTGINAQQ KLSGCFSSFL
1310 1320 1330 1340 1350
ESKKSVDLQT FPSSRDDLHP SVVCNSIGPG VSKINVQRPH NQSAMFTLKE
1360 1370 1380 1390 1400
STLIQKNIFD LSNHLSQVAQ NTQISSGMSS KIEDNANNIQ RNYLSSIGKL
1410 1420 1430 1440 1450
SEYRNSLESK LDQAYTPNFL HCKDSQQQIV CIAEQSKHSE TCSPGNTASE
1460 1470 1480 1490 1500
ESQMPNNCFV TSLRSPIKQI AWEQKQRGFI LDMSNFKPER VKPRSLSEAI
1510 1520 1530 1540 1550
SQTKALSQCK NRNVSTPSAF GEGQSGLAVL KELLQKRQQK AQNANTTQDP
1560 1570 1580 1590 1600
LSNKHQPNKN ISGSLEHNKA NKRTRSVTSP RKPRTPRSTK QKEKIPKLLK
1610 1620 1630 1640 1650
VDSLNLQNSS QLDNSVSDDS PIFFSDPGFE SCYSLEDSLS PEHNYNFDIN
1660 1670 1680 1690 1700
TIGQTGFCSF YSGSQFVPAD QNLPQKFLSD AVQDLFPGQA IEKNEFLSHD
1710 1720 1730 1740 1750
NQKCDEDKHH TTDSASWIRS GTLSPEIFEK STIDSNENRR HNQWKNSFHP
1760 1770 1780 1790 1800
LTTRSNSIMD SFCVQQAEDC LSEKSRLNRS SVSKEVFLSL PQPNNSDWIQ
1810 1820 1830 1840 1850
GHTRKEMGQS LDSANTSFTA ILSSPDGELV DVACEDLELY VSRNNDMLTP
1860 1870 1880 1890 1900
TPDSSPRSTS SPSQSKNGSF TPRTANILKP LMSPPSREEI MATLLDHDLS
1910 1920 1930 1940 1950
ETIYQEPFCS NPSDVPEKPR EIGGRLLMVE TRLANDLAEF EGDFSLEGLR
1960 1970 1980 1990 2000
LWKTAFSAMT QNPRPGSPLR SGQGVVNKGS SNSPKMVEDK KIVIMPCKCA
2010 2020 2030 2040 2050
PSRQLVQVWL QAKEEYERSK KLPKTKPTGV VKSAENFSSS VNPDDKPVVP
2060 2070 2080 2090 2100
PKMDVSPCIL PTTAHTKEDV DNSQIALQAP TTGCSQTASE SQMLPPVASA
2110 2120 2130 2140 2150
SDPEKDEDDD DNYYISYSSP DSPVIPPWQQ PISPDSKALN GDDRPSSPVE
2160 2170 2180 2190 2200
ELPSLAFENF LKPIKDGIQK SPCSEPQEPL VISPINTRAR TGKCESLCFH
2210 2220 2230 2240 2250
STPIIQRKLL ERLPEAPGLS PLSTEPKTQK LSNKKGSNTD TLRRVLLTQA
2260 2270 2280 2290 2300
KNQFAAVNTP QKETSQIDGP SLNNTYGFKV SIQNLQEAKA LHEIQNLTLI
2310 2320 2330 2340 2350
SVELHARTRR DLEPDPEFDP ICALFYCISS DTPLPDTEKT ELTGVIVIDK
2360 2370 2380 2390 2400
DKTVFSQDIR YQTPLLIRSG ITGLEVTYAA DEKALFHEIA NIIKRYDPDI
2410 2420 2430 2440 2450
LLGYEIQMHS WGYLLQRAAA LSIDLCRMIS RVPDDKIENR FAAERDEYGS
2460 2470 2480 2490 2500
YTMSEINIVG RITLNLWRIM RNEVALTNYT FENVSFHVLH QRFPLFTFRV
2510 2520 2530 2540 2550
LSDWFDNKTD LYRWKMVDHY VSRVRGNLQM LEQLDLIGKT SEMARLFGIQ
2560 2570 2580 2590 2600
FLHVLTRGSQ YRVESMMLRI AKPMNYIPVT PSVQQRSQMR APQCVPLIME
2610 2620 2630 2640 2650
PESRFYSNSV LVLDFQSLYP SIVIAYNYCF STCLGHVENL GKYDEFKFGC
2660 2670 2680 2690 2700
TSLRVPPDLL YQVRHDITVS PNGVAFVKPS VRKGVLPRML EEILKTRFMV
2710 2720 2730 2740 2750
KQSMKAYKQD RALSRMLDAR QLGLKLIANV TFGYTSANFS GRMPCIEVGD
2760 2770 2780 2790 2800
SIVHKARETL ERAIKLVNDT KKWGARVVYG DTDSMFVLLK GATKEQSFKI
2810 2820 2830 2840 2850
GQEIAEAVTA TNPKPVKLKF EKVYLPCVLQ TKKRYVGYMY ETLDQKDPVF
2860 2870 2880 2890 2900
DAKGIETVRR DSCPAVSKIL ERSLKLLFET RDISLIKQYV QRQCMKLLEG
2910 2920 2930 2940 2950
KASIQDFIFA KEYRGSFSYK PGACVPALEL TRKMLTYDRR SEPQVGERVP
2960 2970 2980 2990 3000
YVIIYGTPGV PLIQLVRRPV EVLQDPTLRL NATYYITKQI LPPLARIFSL
3010 3020 3030 3040 3050
IGIDVFSWYH ELPRIHKATS SSRSEPEGRK GTISQYFTTL HCPVCDDLTQ
3060 3070 3080 3090 3100
HGICSKCRSQ PQHVAVILNQ EIRELERQQE QLVKICKNCT GCFDRHIPCV
3110 3120 3130
SLNCPVLFKL SRVNRELSKA PYLRQLLDQF
Length:3,130
Mass (Da):352,776
Last modified:April 3, 2007 - v2
Checksum:i4FBAA214639DF3C6
GO
Isoform 2 (identifier: O60673-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Show »
Length:3,052
Mass (Da):344,154
Checksum:iB6983F80F81AB4AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2371E → Q in AAC28460 (PubMed:9925914).Curated
Sequence conflicti237 – 2371E → Q in AAB88486 (PubMed:10660610).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti231 – 2311Q → H.2 Publications
Corresponds to variant rs1053911 [ dbSNP | Ensembl ].
VAR_008516
Natural varianti389 – 3891S → T.
VAR_008517
Natural varianti397 – 3971Q → P.1 Publication
Corresponds to variant rs3218579 [ dbSNP | Ensembl ].
VAR_022226
Natural varianti633 – 6331S → G.
Corresponds to variant rs3218598 [ dbSNP | Ensembl ].
VAR_048883
Natural varianti693 – 6931M → T.1 Publication
Corresponds to variant rs3218593 [ dbSNP | Ensembl ].
VAR_022227
Natural varianti962 – 9621R → Q.1 Publication
Corresponds to variant rs17539588 [ dbSNP | Ensembl ].
VAR_022228
Natural varianti1156 – 11561Y → C.3 Publications
Corresponds to variant rs458017 [ dbSNP | Ensembl ].
VAR_022229
Natural varianti1220 – 12201S → L.
Corresponds to variant rs3218600 [ dbSNP | Ensembl ].
VAR_048884
Natural varianti1224 – 12241T → I.6 Publications
Corresponds to variant rs462779 [ dbSNP | Ensembl ].
VAR_022230
Natural varianti1284 – 12841T → P.
Corresponds to variant rs3218578 [ dbSNP | Ensembl ].
VAR_048885
Natural varianti1302 – 13021S → T.1 Publication
Corresponds to variant rs3218597 [ dbSNP | Ensembl ].
VAR_022231
Natural varianti1309 – 13091Q → H.1 Publication
Corresponds to variant rs3218595 [ dbSNP | Ensembl ].
VAR_022232
Natural varianti1339 – 13391P → T.1 Publication
Corresponds to variant rs17539616 [ dbSNP | Ensembl ].
VAR_022233
Natural varianti1469 – 14691Q → P.1 Publication
Corresponds to variant rs3218572 [ dbSNP | Ensembl ].
VAR_022234
Natural varianti1540 – 15401K → E.2 Publications
Corresponds to variant rs1053913 [ dbSNP | Ensembl ].
VAR_008518
Natural varianti1576 – 15761S → L.1 Publication
Corresponds to variant rs3218582 [ dbSNP | Ensembl ].
VAR_022235
Natural varianti1713 – 17131D → N.1 Publication
Corresponds to variant rs3218585 [ dbSNP | Ensembl ].
VAR_022236
Natural varianti1724 – 17241S → T.1 Publication
Corresponds to variant rs17539644 [ dbSNP | Ensembl ].
VAR_022237
Natural varianti1791 – 17911P → S.1 Publication
Corresponds to variant rs17539651 [ dbSNP | Ensembl ].
VAR_022238
Natural varianti1812 – 18121D → H.1 Publication
Corresponds to variant rs3218599 [ dbSNP | Ensembl ].
VAR_022239
Natural varianti1923 – 19231G → R.1 Publication
Corresponds to variant rs3218604 [ dbSNP | Ensembl ].
VAR_022240
Natural varianti1970 – 19701R → H.1 Publication
Corresponds to variant rs3218606 [ dbSNP | Ensembl ].
VAR_022241
Natural varianti2015 – 20151E → V.1 Publication
Corresponds to variant rs17539692 [ dbSNP | Ensembl ].
VAR_022242
Natural varianti2075 – 20751I → M.1 Publication
Corresponds to variant rs17510963 [ dbSNP | Ensembl ].
VAR_022243
Natural varianti2607 – 26071S → T.
VAR_008519
Natural varianti2762 – 27621R → Q.1 Publication
Corresponds to variant rs3218592 [ dbSNP | Ensembl ].
VAR_022244
Natural varianti3064 – 30641V → I.1 Publication
Corresponds to variant rs3204953 [ dbSNP | Ensembl ].
VAR_016147

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7878Missing in isoform 2. 1 PublicationVSP_024121Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF058701 mRNA. Translation: AAC24357.1.
AF071798 mRNA. Translation: AAC24009.1.
AF157476 mRNA. Translation: AAD40184.1.
AF179428 mRNA. Translation: AAG09402.1.
AF179429 mRNA. Translation: AAG09403.1.
AF078695 mRNA. Translation: AAC28460.1.
AY684169 Genomic DNA. Translation: AAT74627.1.
AL080317, AL136310, AL512325 Genomic DNA. Translation: CAI19192.1.
AL136310, AL080317, AL512325 Genomic DNA. Translation: CAI20509.1.
AL512325, AL080317, AL136310 Genomic DNA. Translation: CAI20998.1.
AF035537 mRNA. Translation: AAB88486.1.
CCDSiCCDS5091.2. [O60673-1]
CCDS69177.1. [O60673-2]
RefSeqiNP_001273360.1. NM_001286431.1. [O60673-2]
NP_001273361.1. NM_001286432.1. [O60673-2]
NP_002903.3. NM_002912.4. [O60673-1]
XP_006715606.1. XM_006715543.2. [O60673-1]
XP_006715607.1. XM_006715544.2. [O60673-2]
UniGeneiHs.232021.

Genome annotation databases

EnsembliENST00000358835; ENSP00000351697; ENSG00000009413. [O60673-1]
ENST00000368802; ENSP00000357792; ENSG00000009413. [O60673-1]
ENST00000368805; ENSP00000357795; ENSG00000009413. [O60673-1]
ENST00000435970; ENSP00000402003; ENSG00000009413. [O60673-2]
GeneIDi5980.
KEGGihsa:5980.
UCSCiuc003puy.6. human. [O60673-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF058701 mRNA. Translation: AAC24357.1.
AF071798 mRNA. Translation: AAC24009.1.
AF157476 mRNA. Translation: AAD40184.1.
AF179428 mRNA. Translation: AAG09402.1.
AF179429 mRNA. Translation: AAG09403.1.
AF078695 mRNA. Translation: AAC28460.1.
AY684169 Genomic DNA. Translation: AAT74627.1.
AL080317, AL136310, AL512325 Genomic DNA. Translation: CAI19192.1.
AL136310, AL080317, AL512325 Genomic DNA. Translation: CAI20509.1.
AL512325, AL080317, AL136310 Genomic DNA. Translation: CAI20998.1.
AF035537 mRNA. Translation: AAB88486.1.
CCDSiCCDS5091.2. [O60673-1]
CCDS69177.1. [O60673-2]
RefSeqiNP_001273360.1. NM_001286431.1. [O60673-2]
NP_001273361.1. NM_001286432.1. [O60673-2]
NP_002903.3. NM_002912.4. [O60673-1]
XP_006715606.1. XM_006715543.2. [O60673-1]
XP_006715607.1. XM_006715544.2. [O60673-2]
UniGeneiHs.232021.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ABDX-ray1.90X/Y1847-1898[»]
3ABEX-ray2.60Z1847-1898[»]
3VU7X-ray2.80Z1847-1898[»]
4EXTX-ray1.90B1873-1895[»]
4GK0X-ray2.70C/D1847-1898[»]
4GK5X-ray3.21C/D1847-1898[»]
ProteinModelPortaliO60673.
SMRiO60673. Positions 1868-1897.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111912. 28 interactions.
IntActiO60673. 8 interactions.
MINTiMINT-2796978.
STRINGi9606.ENSP00000351697.

PTM databases

iPTMnetiO60673.
PhosphoSiteiO60673.

Polymorphism and mutation databases

BioMutaiREV3L.

Proteomic databases

MaxQBiO60673.
PaxDbiO60673.
PRIDEiO60673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358835; ENSP00000351697; ENSG00000009413. [O60673-1]
ENST00000368802; ENSP00000357792; ENSG00000009413. [O60673-1]
ENST00000368805; ENSP00000357795; ENSG00000009413. [O60673-1]
ENST00000435970; ENSP00000402003; ENSG00000009413. [O60673-2]
GeneIDi5980.
KEGGihsa:5980.
UCSCiuc003puy.6. human. [O60673-1]

Organism-specific databases

CTDi5980.
GeneCardsiREV3L.
H-InvDBHIX0017582.
HGNCiHGNC:9968. REV3L.
HPAiHPA064853.
MIMi602776. gene.
neXtProtiNX_O60673.
PharmGKBiPA34337.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0968. Eukaryota.
COG0417. LUCA.
GeneTreeiENSGT00550000074640.
HOGENOMiHOG000112263.
HOVERGENiHBG000426.
InParanoidiO60673.
KOiK02350.
OMAiFCSNPSD.
OrthoDBiEOG7F5113.
PhylomeDBiO60673.
TreeFamiTF101072.

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.

Miscellaneous databases

ChiTaRSiREV3L. human.
EvolutionaryTraceiO60673.
GeneWikiiREV3L.
GenomeRNAii5980.
NextBioi23277.
PROiO60673.
SOURCEiSearch...

Gene expression databases

BgeeiO60673.
CleanExiHS_REV3L.
ExpressionAtlasiO60673. baseline and differential.
GenevisibleiO60673. HS.

Family and domain databases

Gene3Di3.30.420.10. 2 hits.
3.90.1600.10. 2 hits.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR032757. DUF4683.
IPR030559. PolZ_Rev3.
IPR012337. RNaseH-like_dom.
IPR025687. Znf-C4pol.
[Graphical view]
PANTHERiPTHR10322:SF5. PTHR10322:SF5. 4 hits.
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 2 hits.
PF15735. DUF4683. 1 hit.
PF14260. zf-C4pol. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 4 hits.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta."
    Gibbs P.E.M., McGregor W.G., Maher V.M., Nisson P., Lawrence C.W.
    Proc. Natl. Acad. Sci. U.S.A. 95:6876-6880(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-1224.
    Tissue: Fetal brain.
  2. "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. 433:89-98(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-1224.
    Tissue: Bone marrow and Leukocyte.
  3. "Cloning and characterization of hREV3, the human homolog of S. cerevisiae REV3."
    Murakumo Y., Rasio D., Roth T., Negrini M., Croce C.M., Fishel R.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-1224.
  4. "Alternative splicing, genomic structure, and fine chromosome localization of REV3L."
    Morelli C., Mungall A.J., Negrini M., Barbanti-Brodano G., Croce C.M.
    Cytogenet. Cell Genet. 83:18-20(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS HIS-231; CYS-1156; ILE-1224 AND GLU-1540.
    Tissue: Testis.
  5. NIEHS SNPs program
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-397; THR-693; GLN-962; CYS-1156; ILE-1224; THR-1302; HIS-1309; THR-1339; PRO-1469; LEU-1576; ASN-1713; THR-1724; SER-1791; HIS-1812; ARG-1923; HIS-1970; VAL-2015; MET-2075; GLN-2762 AND ILE-3064.
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 C.M., Fishel R.
    J. Biol. Chem. 275:4391-4397(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-3130 (ISOFORM 1), VARIANTS HIS-231; CYS-1156; ILE-1224 AND GLU-1540, INTERACTION WITH MAD2L2.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030 AND THR-1041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1847-1898 IN COMPLEX WITH MAD2L2.

Entry informationi

Entry nameiDPOLZ_HUMAN
AccessioniPrimary (citable) accession number: O60673
Secondary accession number(s): O43214, Q5TC33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 3, 2007
Last modified: May 11, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.