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P06766

- DPOLB_RAT

UniProt

P06766 - DPOLB_RAT

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Protein

DNA polymerase beta

Gene

Polb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.

Catalytic activityi

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

Cofactori

Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei72 – 721Schiff-base intermediate with DNABy similarity
Metal bindingi101 – 1011Sodium; via carbonyl oxygen
Metal bindingi103 – 1031Sodium; via carbonyl oxygen
Metal bindingi106 – 1061Sodium; via carbonyl oxygen
Metal bindingi190 – 1901Magnesium 1
Metal bindingi190 – 1901Magnesium 2
Metal bindingi192 – 1921Magnesium 1
Metal bindingi192 – 1921Magnesium 2
Metal bindingi256 – 2561Magnesium 2

GO - Molecular functioni

  1. damaged DNA binding Source: RGD
  2. DNA binding Source: UniProtKB
  3. DNA-directed DNA polymerase activity Source: UniProtKB
  4. lyase activity Source: UniProtKB
  5. metal ion binding Source: UniProtKB

GO - Biological processi

  1. aging Source: RGD
  2. base-excision repair Source: UniProtKB
  3. base-excision repair, gap-filling Source: RGD
  4. cellular response to DNA damage stimulus Source: UniProtKB
  5. DNA biosynthetic process Source: RGD
  6. DNA-dependent DNA replication Source: GOC
  7. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  8. neuron apoptotic process Source: Ensembl
  9. pyrimidine dimer repair Source: RGD
  10. response to ethanol Source: RGD
  11. response to gamma radiation Source: RGD
  12. response to hyperoxia Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Lyase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, DNA synthesis

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Sodium

Enzyme and pathway databases

ReactomeiREACT_225345. Resolution of AP sites via the single-nucleotide replacement pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase beta (EC:2.7.7.7, EC:4.2.99.-)
Gene namesi
Name:Polb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi3363. Polb.

Subcellular locationi

Nucleus. Cytoplasm By similarity
Note: Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage By similarity.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: RGD
  3. spindle microtubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi190 – 1901D → E or S: Loss of activity. 1 Publication
Mutagenesisi191 – 1911M → I: No loss of activity.
Mutagenesisi191 – 1911M → T: 50% loss of activity.
Mutagenesisi192 – 1921D → E or S: Loss of activity. 1 Publication
Mutagenesisi246 – 2461D → V: Misincorporates T nucleotide opposite G/C template. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335DNA polymerase betaPRO_0000218780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki41 – 41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei72 – 721N6-acetyllysineBy similarity
Cross-linki81 – 81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei83 – 831Omega-N-methylarginine; by PRMT6By similarity
Modified residuei152 – 1521Omega-N-methylarginine; by PRMT6By similarity

Post-translational modificationi

Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.By similarity
Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation By similarity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

PaxDbiP06766.
PRIDEiP06766.

PTM databases

PhosphoSiteiP06766.

Expressioni

Gene expression databases

ExpressionAtlasiP06766. baseline and differential.
GenevestigatoriP06766.

Interactioni

Subunit structurei

Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47 By similarity. Monomer.By similarity

Protein-protein interaction databases

DIPiDIP-44707N.
MINTiMINT-1504350.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2816
Beta strandi29 – 313
Helixi33 – 4816
Helixi56 – 616
Beta strandi62 – 643
Helixi67 – 7610
Beta strandi79 – 813
Helixi83 – 908
Helixi92 – 1009
Turni101 – 1044
Helixi108 – 1158
Turni116 – 1183
Helixi122 – 1265
Helixi129 – 1313
Helixi134 – 1418
Turni142 – 1443
Helixi145 – 1473
Helixi152 – 16918
Beta strandi174 – 1774
Helixi179 – 1824
Beta strandi186 – 19611
Turni202 – 2043
Helixi208 – 22013
Beta strandi224 – 2307
Beta strandi232 – 2398
Beta strandi244 – 2474
Beta strandi253 – 2597
Helixi262 – 2643
Helixi265 – 2739
Helixi276 – 28813
Beta strandi291 – 2933
Beta strandi298 – 3014
Beta strandi303 – 3053
Helixi316 – 3227
Helixi330 – 3323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BNONMR-A1-87[»]
1BNPNMR-A1-87[»]
1BPBX-ray2.30A88-335[»]
1BPDX-ray3.60A1-335[»]
1BPEX-ray2.90A1-335[»]
1DK2NMR-A2-87[»]
1DK3NMR-A1-87[»]
1HUOX-ray2.60A/B1-335[»]
1HUZX-ray2.60A/B1-335[»]
1JN3X-ray2.35A85-335[»]
1NOMX-ray3.00A88-335[»]
1RPLX-ray2.30A85-335[»]
1ZQUX-ray2.60A88-335[»]
1ZQVX-ray2.70A88-335[»]
1ZQWX-ray2.30A88-335[»]
1ZQXX-ray2.50A88-335[»]
1ZQYX-ray2.30A88-335[»]
1ZQZX-ray2.70A88-335[»]
2BPCX-ray2.80A88-335[»]
2BPFX-ray2.90A1-335[»]
2BPGX-ray3.60A/B1-335[»]
2VANX-ray2.10A91-335[»]
3K75X-ray2.95D/E91-335[»]
3LQCX-ray2.35B142-335[»]
3UXNX-ray2.50A/B1-335[»]
3UXOX-ray2.10A/B1-335[»]
3UXPX-ray2.72A/B1-335[»]
3V72X-ray2.49A1-335[»]
3V7JX-ray2.25A4-335[»]
3V7KX-ray2.27A4-335[»]
3V7LX-ray2.66A4-335[»]
ProteinModelPortaliP06766.
SMRiP06766. Positions 10-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06766.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 19210DNA binding

Domaini

Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity.

Sequence similaritiesi

Belongs to the DNA polymerase type-X family.Curated

Phylogenomic databases

eggNOGiCOG1796.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000007787.
HOVERGENiHBG002359.
InParanoidiP06766.
KOiK02330.
OMAiRYREPKD.
OrthoDBiEOG7RJPRK.
PhylomeDBiP06766.
TreeFamiTF103002.

Family and domain databases

Gene3Di1.10.8.310. 1 hit.
3.30.210.10. 1 hit.
InterProiIPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR028207. DNA_pol_B_palm_palm.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR002008. DNA_pol_X_beta-like.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027420. PolB_N.
IPR029398. PolB_thumb.
[Graphical view]
PfamiPF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]
PRINTSiPR00869. DNAPOLX.
PR00870. DNAPOLXBETA.
SMARTiSM00278. HhH1. 2 hits.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
PROSITEiPS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06766-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKRKAPQET LNGGITDMLV ELANFEKNVS QAIHKYNAYR KAASVIAKYP
60 70 80 90 100
HKIKSGAEAK KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL
110 120 130 140 150
TRVTGIGPSA ARKLVDEGIK TLEDLRKNED KLNHHQRIGL KYFEDFEKRI
160 170 180 190 200
PREEMLQMQD IVLNEVKKLD PEYIATVCGS FRRGAESSGD MDVLLTHPNF
210 220 230 240 250
TSESSKQPKL LHRVVEQLQK VRFITDTLSK GETKFMGVCQ LPSENDENEY
260 270 280 290 300
PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
310 320 330
LGVTGVAGEP LPVDSEQDIF DYIQWRYREP KDRSE
Length:335
Mass (Da):38,327
Last modified:January 23, 2007 - v4
Checksum:iBBF8498C0D3FBFC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281L → R in AAA41901. (PubMed:3597402)Curated
Sequence conflicti228 – 2281L → R in AAB00389. 1 PublicationCurated
Sequence conflicti228 – 2281L → R in AAA41900. (PubMed:2873575)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02776 mRNA. Translation: AAA41901.1.
U38801 mRNA. Translation: AAB00389.1.
BC098668 mRNA. Translation: AAH98668.1.
M13961 mRNA. Translation: AAA41900.1.
PIRiA27112.
RefSeqiNP_058837.2. NM_017141.2.
UniGeneiRn.9346.

Genome annotation databases

EnsembliENSRNOT00000026039; ENSRNOP00000026039; ENSRNOG00000019150.
GeneIDi29240.
KEGGirno:29240.
UCSCiRGD:3363. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02776 mRNA. Translation: AAA41901.1 .
U38801 mRNA. Translation: AAB00389.1 .
BC098668 mRNA. Translation: AAH98668.1 .
M13961 mRNA. Translation: AAA41900.1 .
PIRi A27112.
RefSeqi NP_058837.2. NM_017141.2.
UniGenei Rn.9346.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BNO NMR - A 1-87 [» ]
1BNP NMR - A 1-87 [» ]
1BPB X-ray 2.30 A 88-335 [» ]
1BPD X-ray 3.60 A 1-335 [» ]
1BPE X-ray 2.90 A 1-335 [» ]
1DK2 NMR - A 2-87 [» ]
1DK3 NMR - A 1-87 [» ]
1HUO X-ray 2.60 A/B 1-335 [» ]
1HUZ X-ray 2.60 A/B 1-335 [» ]
1JN3 X-ray 2.35 A 85-335 [» ]
1NOM X-ray 3.00 A 88-335 [» ]
1RPL X-ray 2.30 A 85-335 [» ]
1ZQU X-ray 2.60 A 88-335 [» ]
1ZQV X-ray 2.70 A 88-335 [» ]
1ZQW X-ray 2.30 A 88-335 [» ]
1ZQX X-ray 2.50 A 88-335 [» ]
1ZQY X-ray 2.30 A 88-335 [» ]
1ZQZ X-ray 2.70 A 88-335 [» ]
2BPC X-ray 2.80 A 88-335 [» ]
2BPF X-ray 2.90 A 1-335 [» ]
2BPG X-ray 3.60 A/B 1-335 [» ]
2VAN X-ray 2.10 A 91-335 [» ]
3K75 X-ray 2.95 D/E 91-335 [» ]
3LQC X-ray 2.35 B 142-335 [» ]
3UXN X-ray 2.50 A/B 1-335 [» ]
3UXO X-ray 2.10 A/B 1-335 [» ]
3UXP X-ray 2.72 A/B 1-335 [» ]
3V72 X-ray 2.49 A 1-335 [» ]
3V7J X-ray 2.25 A 4-335 [» ]
3V7K X-ray 2.27 A 4-335 [» ]
3V7L X-ray 2.66 A 4-335 [» ]
ProteinModelPortali P06766.
SMRi P06766. Positions 10-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-44707N.
MINTi MINT-1504350.

Chemistry

BindingDBi P06766.
ChEMBLi CHEMBL4343.

PTM databases

PhosphoSitei P06766.

Proteomic databases

PaxDbi P06766.
PRIDEi P06766.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000026039 ; ENSRNOP00000026039 ; ENSRNOG00000019150 .
GeneIDi 29240.
KEGGi rno:29240.
UCSCi RGD:3363. rat.

Organism-specific databases

CTDi 5423.
RGDi 3363. Polb.

Phylogenomic databases

eggNOGi COG1796.
GeneTreei ENSGT00530000063002.
HOGENOMi HOG000007787.
HOVERGENi HBG002359.
InParanoidi P06766.
KOi K02330.
OMAi RYREPKD.
OrthoDBi EOG7RJPRK.
PhylomeDBi P06766.
TreeFami TF103002.

Enzyme and pathway databases

Reactomei REACT_225345. Resolution of AP sites via the single-nucleotide replacement pathway.

Miscellaneous databases

EvolutionaryTracei P06766.
NextBioi 608510.
PROi P06766.

Gene expression databases

ExpressionAtlasi P06766. baseline and differential.
Genevestigatori P06766.

Family and domain databases

Gene3Di 1.10.8.310. 1 hit.
3.30.210.10. 1 hit.
InterProi IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR028207. DNA_pol_B_palm_palm.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR002008. DNA_pol_X_beta-like.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027420. PolB_N.
IPR029398. PolB_thumb.
[Graphical view ]
Pfami PF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view ]
PRINTSi PR00869. DNAPOLX.
PR00870. DNAPOLXBETA.
SMARTi SM00278. HhH1. 2 hits.
SM00483. POLXc. 1 hit.
[Graphical view ]
SUPFAMi SSF47802. SSF47802. 1 hit.
PROSITEi PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Homology between mammalian DNA polymerase beta and terminal deoxynucleotidyltransferase."
    Matsukage A., Nishikawa K., Ooi T., Seto Y., Yamaguchi M.
    J. Biol. Chem. 262:8960-8962(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Konopinski R., Nowak R., Siedlecki J.A.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  4. "Structure of rat DNA polymerase beta revealed by partial amino acid sequencing and cDNA cloning."
    Zmudzka B.Z., Sengupta D., Matsukage A., Cobianchi F., Kumar P., Wilson S.H.
    Proc. Natl. Acad. Sci. U.S.A. 83:5106-5110(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
  5. "Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain."
    Kumar P., Widen S.G., Williams K.R., Kedar P., Karpel R.L., Wilson S.H.
    J. Biol. Chem. 265:2124-2131(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION TO 228.
  6. "Site-directed mutagenesis of recombinant rat DNA polymerase beta: involvement of arginine-183 in primer recognition."
    Date T., Yamamoto S., Tanihara K., Nishimoto Y., Liu N., Matsukage A.
    Biochemistry 29:5027-5034(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPORTANCE OF ARG-183 IN PRIMER BINDING.
  7. "Aspartic acid residues at positions 190 and 192 of rat DNA polymerase beta are involved in primer binding."
    Date T., Yamamoto S., Tanihara K., Nishimoto Y., Matsukage A.
    Biochemistry 30:5286-5292(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-190 AND ASP-192, IMPORTANCE OF ASP-190 AND ASP-192 IN PRIMER BINDING.
  8. "Mammalian DNA polymerase beta: characterization of a 16-kDa transdomain fragment containing the nucleic acid-binding activities of the native enzyme."
    Casas-Finet J.R., Kumar A., Karpel R.L., Wilson S.H.
    Biochemistry 31:10272-10280(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING REGION.
  9. "The D246V mutant of DNA polymerase beta misincorporates nucleotides: evidence for a role for the flexible loop in DNA positioning within the active site."
    Dalal S., Kosa J.L., Sweasy J.B.
    J. Biol. Chem. 279:577-584(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-246, IMPORTANCE OF ASP-246 IN FIDELITY.
  10. "2.3-A crystal structure of the catalytic domain of DNA polymerase beta."
    Davies J.F. II, Almassy R.J., Hostomska Z., Ferre R.A., Hostomsky Z.
    Cell 76:1123-1133(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  11. "Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism."
    Sawaya M.R., Pelletier H., Kumar A., Wilson S.H., Kraut J.
    Science 264:1930-1935(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  12. "Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis."
    Pelletier H., Sawaya M.R.
    Biochemistry 35:12778-12787(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  13. "Insight into the catalytic mechanism of DNA polymerase beta: structures of intermediate complexes."
    Arndt J.W., Gong W., Zhong X., Showalter A.K., Liu J., Dunlap C.A., Lin Z., Paxson C., Tsai M.-D., Chan M.K.
    Biochemistry 40:5368-5375(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  14. "Three-dimensional solution structure of the N-terminal domain of DNA polymerase beta and mapping of the ssDNA interaction interface."
    Liu D., Prasad R., Wilson S.H., DeRose E.F., Mullen G.P.
    Biochemistry 35:6188-6200(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-87.
  15. "Backbone dynamics and refined solution structure of the N-terminal domain of DNA polymerase beta. Correlation with DNA binding and dRP lyase activity."
    Maciejewski M.W., Liu D., Prasad R., Wilson S.H., Mullen G.P.
    J. Mol. Biol. 296:229-253(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-87.

Entry informationi

Entry nameiDPOLB_RAT
AccessioniPrimary (citable) accession number: P06766
Secondary accession number(s): Q4G081
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3