DPOLB_HUMAN
ID DPOLB_HUMAN Reviewed; 335 AA.
AC P06746; B2RC78; Q3KP48; Q6FI34;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 243.
DE RecName: Full=DNA polymerase beta;
DE EC=2.7.7.7;
DE EC=4.2.99.-;
GN Name=POLB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10648175; DOI=10.1006/prep.1999.1167;
RA Patterson T.A., Little W., Cheng X., Widen S.G., Kumar A., Beard W.A.,
RA Wilson S.H.;
RT "Molecular cloning and high-level expression of human polymerase beta cDNA
RT and comparison of the purified recombinant human and rat enzymes.";
RL Protein Expr. Purif. 18:100-110(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7705833; DOI=10.1007/bf00208961;
RA Dobashi Y., Kubota Y., Shuin T., Torigoe S., Yao M., Hosaka M.;
RT "Polymorphisms in the human DNA polymerase beta gene.";
RL Hum. Genet. 95:389-390(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Skin;
RX PubMed=7914364; DOI=10.1093/nar/22.14.2719;
RA Chyan Y.-J., Ackerman S., Shepherd N.S., McBride O.W., Widen S.G.,
RA Wilson S.H., Wood T.G.;
RT "The human DNA polymerase beta gene structure. Evidence of alternative
RT splicing in gene expression.";
RL Nucleic Acids Res. 22:2719-2725(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-242.
RG NIEHS SNPs program;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX PubMed=3182828; DOI=10.1016/s0021-9258(18)37488-x;
RA Widen S.G., Kedar P., Wilson S.H.;
RT "Human beta-polymerase gene. Structure of the 5'-flanking region and active
RT promoter.";
RL J. Biol. Chem. 263:16992-16998(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-32.
RX PubMed=3284575; DOI=10.1021/bi00403a010;
RA Abbotts J., Sengupta D.N., Zmudzka B., Widen S.G., Notario V., Wilson S.H.;
RT "Expression of human DNA polymerase beta in Escherichia coli and
RT characterization of the recombinant enzyme.";
RL Biochemistry 27:901-909(1988).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
RX PubMed=2423078; DOI=10.1016/0006-291x(86)90916-2;
RA Sengupta D.N., Zmudzka B.Z., Kumar P., Cobianchi F., Skowronski J.,
RA Wilson S.H.;
RT "Sequence of human DNA polymerase beta mRNA obtained through cDNA
RT cloning.";
RL Biochem. Biophys. Res. Commun. 136:341-347(1986).
RN [11]
RP FUNCTION, AND INTERACTION WITH APEX1.
RX PubMed=9207062; DOI=10.1073/pnas.94.14.7166;
RA Bennett R.A., Wilson D.M. III, Wong D., Demple B.;
RT "Interaction of human apurinic endonuclease and DNA polymerase beta in the
RT base excision repair pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7166-7169(1997).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF LYS-35; TYR-39; LYS-68; LYS-72 AND LYS-84.
RX PubMed=9572863; DOI=10.1021/bi9727545;
RA Matsumoto Y., Kim K., Katz D.S., Feng J.-A.;
RT "Catalytic center of DNA polymerase beta for excision of deoxyribose
RT phosphate groups.";
RL Biochemistry 37:6456-6464(1998).
RN [13]
RP FUNCTION.
RX PubMed=11805079; DOI=10.1074/jbc.c100577200;
RA DeMott M.S., Beyret E., Wong D., Bales B.C., Hwang J.-T., Greenberg M.M.,
RA Demple B.;
RT "Covalent trapping of human DNA polymerase beta by the oxidative DNA lesion
RT 2-deoxyribonolactone.";
RL J. Biol. Chem. 277:7637-7640(2002).
RN [14]
RP METHYLATION AT ARG-83 AND ARG-152 BY PRMT6, AND MUTAGENESIS OF ARG-83 AND
RP ARG-152.
RX PubMed=16600869; DOI=10.1016/j.molcel.2006.02.013;
RA El-Andaloussi N., Valovka T., Toueille M., Steinacher R., Focke F.,
RA Gehrig P., Covic M., Hassa P.O., Schaer P., Huebscher U., Hottiger M.O.;
RT "Arginine methylation regulates DNA polymerase beta.";
RL Mol. Cell 22:51-62(2006).
RN [15]
RP SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND LYS-81, AND
RP MUTAGENESIS OF LYS-41; LYS-61 AND LYS-81.
RX PubMed=19713937; DOI=10.1038/emboj.2009.243;
RA Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J.,
RA Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G., Dianov G.L.;
RT "Ubiquitin ligase ARF-BP1/Mule modulates base excision repair.";
RL EMBO J. 28:3207-3215(2009).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND
RP LYS-81, DEUBIQUITINATION BY USP47, AND INTERACTION WITH USP47.
RX PubMed=21362556; DOI=10.1016/j.molcel.2011.02.016;
RA Parsons J.L., Dianova I.I., Khoronenkova S.V., Edelmann M.J., Kessler B.M.,
RA Dianov G.L.;
RT "USP47 is a deubiquitylating enzyme that regulates base excision repair by
RT controlling steady-state levels of DNA Polymerase beta.";
RL Mol. Cell 41:609-615(2011).
RN [17]
RP INTERACTS WITH FAM168A.
RX PubMed=25260657; DOI=10.1007/s11010-014-2217-x;
RA Liu X., Wang C., Gu Y., Zhang Z., Zheng G., He Z.;
RT "TCRP1 contributes to cisplatin resistance by preventing Pol beta
RT degradation in lung cancer cells.";
RL Mol. Cell. Biochem. 398:175-183(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH DNA; ATP AND METAL
RP IONS.
RX PubMed=8841119; DOI=10.1021/bi9529566;
RA Pelletier H., Sawaya M.R., Wolfle W., Wilson S.H., Kraut J.;
RT "A structural basis for metal ion mutagenicity and nucleotide selectivity
RT in human DNA polymerase beta.";
RL Biochemistry 35:12762-12777(1996).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH DNA AND METAL IONS.
RX PubMed=8841120; DOI=10.1021/bi960790i;
RA Pelletier H., Sawaya M.R.;
RT "Characterization of the metal ion binding helix-hairpin-helix motifs in
RT human DNA polymerase beta by X-ray structural analysis.";
RL Biochemistry 35:12778-12787(1996).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH DNA.
RX PubMed=9287163; DOI=10.1021/bi9703812;
RA Sawaya M.R., Prasad R., Wilson S.H., Kraut J., Pelletier H.;
RT "Crystal structures of human DNA polymerase beta complexed with gapped and
RT nicked DNA: evidence for an induced fit mechanism.";
RL Biochemistry 36:11205-11215(1997).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH DNA.
RX PubMed=12517346; DOI=10.1016/s0969-2126(02)00930-9;
RA Krahn J.M., Beard W.A., Miller H., Grollman A.P., Wilson S.H.;
RT "Structure of DNA polymerase beta with the mutagenic DNA lesion 8-
RT oxodeoxyguanine reveals structural insights into its coding potential.";
RL Structure 11:121-127(2003).
CC -!- FUNCTION: Repair polymerase that plays a key role in base-excision
CC repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that
CC removes the 5' sugar phosphate and also acts as a DNA polymerase that
CC adds one nucleotide to the 3' end of the arising single-nucleotide gap.
CC Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion
CC rather than in a processive fashion as for other DNA polymerases.
CC {ECO:0000269|PubMed:11805079, ECO:0000269|PubMed:21362556,
CC ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9572863}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and
CC USP47. Interacts with FAM168A (PubMed:25260657).
CC {ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:21362556,
CC ECO:0000269|PubMed:25260657, ECO:0000269|PubMed:8841119,
CC ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9207062,
CC ECO:0000269|PubMed:9287163}.
CC -!- INTERACTION:
CC P06746; Q9H5J8: TAF1D; NbExp=4; IntAct=EBI-713836, EBI-716128;
CC P06746; P29144: TPP2; NbExp=8; IntAct=EBI-713836, EBI-1044672;
CC P06746; O76024: WFS1; NbExp=3; IntAct=EBI-713836, EBI-720609;
CC P06746; P18887: XRCC1; NbExp=3; IntAct=EBI-713836, EBI-947466;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in normal
CC conditions. Translocates to the nucleus following DNA damage.
CC -!- DOMAIN: Residues 239-252 form a flexible loop which appears to affect
CC the polymerase fidelity. {ECO:0000250}.
CC -!- PTM: Methylation by PRMT6 stimulates the polymerase activity by
CC enhancing DNA binding and processivity. {ECO:0000269|PubMed:16600869}.
CC -!- PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by
CC HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of
CC STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin,
CC leading to degradation by the proteasome. USP47 mediates the
CC deubiquitination of monoubiquitinated protein, preventing
CC polyubiquitination by STUB1/CHIP and its subsequent degradation.
CC {ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/polb/";
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DR EMBL; L11607; AAB59441.1; -; mRNA.
DR EMBL; D29013; BAA06099.1; -; mRNA.
DR EMBL; U10526; AAB60688.1; -; Genomic_DNA.
DR EMBL; U10516; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10517; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10519; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10520; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10521; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10522; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10523; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10524; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; U10525; AAB60688.1; JOINED; Genomic_DNA.
DR EMBL; AK314976; BAG37475.1; -; mRNA.
DR EMBL; CR536503; CAG38741.1; -; mRNA.
DR EMBL; CR541802; CAG46601.1; -; mRNA.
DR EMBL; AF491812; AAL91594.1; -; Genomic_DNA.
DR EMBL; BC100288; AAI00289.1; -; mRNA.
DR EMBL; BC106909; AAI06910.1; -; mRNA.
DR EMBL; J04201; AAA60134.1; -; Genomic_DNA.
DR EMBL; M13140; AAA60133.1; -; mRNA.
DR CCDS; CCDS6129.1; -.
DR PIR; I55273; I55273.
DR PIR; S48061; S48061.
DR RefSeq; NP_002681.1; NM_002690.2.
DR PDB; 1BPX; X-ray; 2.40 A; A=1-335.
DR PDB; 1BPY; X-ray; 2.20 A; A=1-335.
DR PDB; 1BPZ; X-ray; 2.60 A; A=1-335.
DR PDB; 1MQ2; X-ray; 3.10 A; A=1-335.
DR PDB; 1MQ3; X-ray; 2.80 A; A=1-335.
DR PDB; 1TV9; X-ray; 2.00 A; A=1-335.
DR PDB; 1TVA; X-ray; 2.60 A; A=1-335.
DR PDB; 1ZJM; X-ray; 2.10 A; A=1-335.
DR PDB; 1ZJN; X-ray; 2.61 A; A=1-335.
DR PDB; 1ZQA; X-ray; 3.20 A; A=1-335.
DR PDB; 1ZQB; X-ray; 3.20 A; A=1-335.
DR PDB; 1ZQC; X-ray; 3.20 A; A=1-335.
DR PDB; 1ZQD; X-ray; 3.50 A; A=1-335.
DR PDB; 1ZQE; X-ray; 3.70 A; A=1-335.
DR PDB; 1ZQF; X-ray; 2.90 A; A=1-335.
DR PDB; 1ZQG; X-ray; 3.10 A; A=1-335.
DR PDB; 1ZQH; X-ray; 3.10 A; A=1-335.
DR PDB; 1ZQI; X-ray; 2.70 A; A=1-335.
DR PDB; 1ZQJ; X-ray; 3.30 A; A=1-335.
DR PDB; 1ZQK; X-ray; 3.20 A; A=1-335.
DR PDB; 1ZQL; X-ray; 3.30 A; A=1-335.
DR PDB; 1ZQM; X-ray; 3.20 A; A=1-335.
DR PDB; 1ZQN; X-ray; 3.00 A; A=1-335.
DR PDB; 1ZQO; X-ray; 3.20 A; A=1-335.
DR PDB; 1ZQP; X-ray; 2.80 A; A=1-335.
DR PDB; 1ZQQ; X-ray; 3.30 A; A=1-335.
DR PDB; 1ZQR; X-ray; 3.70 A; A=1-335.
DR PDB; 1ZQS; X-ray; 3.30 A; A=1-335.
DR PDB; 1ZQT; X-ray; 3.40 A; A=1-335.
DR PDB; 2FMP; X-ray; 1.65 A; A=1-335.
DR PDB; 2FMQ; X-ray; 2.20 A; A=1-335.
DR PDB; 2FMS; X-ray; 2.00 A; A=1-335.
DR PDB; 2I9G; X-ray; 2.10 A; A=1-335.
DR PDB; 2ISO; X-ray; 2.10 A; A=1-335.
DR PDB; 2ISP; X-ray; 2.20 A; A=1-335.
DR PDB; 2P66; X-ray; 2.50 A; A=1-335.
DR PDB; 2PXI; X-ray; 2.10 A; A=1-335.
DR PDB; 3C2K; X-ray; 2.40 A; A=1-335.
DR PDB; 3C2L; X-ray; 2.60 A; A=1-335.
DR PDB; 3C2M; X-ray; 2.15 A; A=1-335.
DR PDB; 3GDX; X-ray; 2.20 A; A=10-335.
DR PDB; 3ISB; X-ray; 2.00 A; A=1-335.
DR PDB; 3ISC; X-ray; 2.00 A; A=1-335.
DR PDB; 3ISD; X-ray; 2.60 A; A=1-335.
DR PDB; 3JPN; X-ray; 2.15 A; A=1-335.
DR PDB; 3JPO; X-ray; 2.00 A; A=1-335.
DR PDB; 3JPP; X-ray; 2.10 A; A=1-335.
DR PDB; 3JPQ; X-ray; 1.90 A; A=1-335.
DR PDB; 3JPR; X-ray; 2.10 A; A=1-335.
DR PDB; 3JPS; X-ray; 2.00 A; A=1-335.
DR PDB; 3JPT; X-ray; 2.15 A; A=1-335.
DR PDB; 3LK9; X-ray; 2.50 A; A=1-335.
DR PDB; 3MBY; X-ray; 2.00 A; A=1-335.
DR PDB; 3OGU; X-ray; 1.84 A; A=1-335.
DR PDB; 3RH4; X-ray; 1.92 A; A=1-335.
DR PDB; 3RH5; X-ray; 2.10 A; A=1-335.
DR PDB; 3RH6; X-ray; 2.05 A; A=1-335.
DR PDB; 3RJE; X-ray; 2.10 A; A=1-335.
DR PDB; 3RJF; X-ray; 2.30 A; A=1-335.
DR PDB; 3RJG; X-ray; 2.00 A; A=1-335.
DR PDB; 3RJH; X-ray; 2.20 A; A=1-335.
DR PDB; 3RJI; X-ray; 2.30 A; A=1-335.
DR PDB; 3RJJ; X-ray; 2.00 A; A=1-335.
DR PDB; 3RJK; X-ray; 2.10 A; A=1-335.
DR PDB; 3TFR; X-ray; 2.00 A; A=1-335.
DR PDB; 3TFS; X-ray; 2.00 A; A=1-335.
DR PDB; 4DO9; X-ray; 2.05 A; A=1-335.
DR PDB; 4DOA; X-ray; 2.05 A; A=1-335.
DR PDB; 4DOB; X-ray; 2.05 A; A=1-335.
DR PDB; 4DOC; X-ray; 1.95 A; A=1-335.
DR PDB; 4F5N; X-ray; 1.80 A; A=1-335.
DR PDB; 4F5O; X-ray; 2.00 A; A=1-335.
DR PDB; 4F5P; X-ray; 1.85 A; A=1-335.
DR PDB; 4F5Q; X-ray; 2.25 A; A=1-335.
DR PDB; 4F5R; X-ray; 2.20 A; A/B=1-335.
DR PDB; 4GXI; X-ray; 1.95 A; A=1-335.
DR PDB; 4GXJ; X-ray; 2.20 A; A=1-335.
DR PDB; 4GXK; X-ray; 2.00 A; A=1-335.
DR PDB; 4JWM; X-ray; 2.00 A; A=1-335.
DR PDB; 4JWN; X-ray; 2.39 A; A=1-335.
DR PDB; 4KLD; X-ray; 1.92 A; A=1-335.
DR PDB; 4KLE; X-ray; 1.97 A; A=1-335.
DR PDB; 4KLF; X-ray; 1.85 A; A=1-335.
DR PDB; 4KLG; X-ray; 1.70 A; A=1-335.
DR PDB; 4KLH; X-ray; 1.88 A; A=1-335.
DR PDB; 4KLI; X-ray; 1.60 A; A=1-335.
DR PDB; 4KLJ; X-ray; 1.80 A; A=1-335.
DR PDB; 4KLL; X-ray; 1.84 A; A=1-335.
DR PDB; 4KLM; X-ray; 1.75 A; A=1-335.
DR PDB; 4KLO; X-ray; 1.84 A; A=1-335.
DR PDB; 4KLQ; X-ray; 2.00 A; A=1-335.
DR PDB; 4KLS; X-ray; 1.98 A; A=1-335.
DR PDB; 4KLT; X-ray; 1.98 A; A=1-335.
DR PDB; 4KLU; X-ray; 1.97 A; A=1-335.
DR PDB; 4LVS; X-ray; 2.00 A; A=1-335.
DR PDB; 4M2Y; X-ray; 2.27 A; A=11-335.
DR PDB; 4M47; X-ray; 2.37 A; A=12-335.
DR PDB; 4M9G; X-ray; 2.01 A; A=1-335.
DR PDB; 4M9H; X-ray; 2.39 A; A=1-335.
DR PDB; 4M9J; X-ray; 2.04 A; A=1-335.
DR PDB; 4M9L; X-ray; 2.09 A; A=1-335.
DR PDB; 4M9N; X-ray; 2.28 A; A=1-335.
DR PDB; 4MF2; X-ray; 2.40 A; A=11-335.
DR PDB; 4MF8; X-ray; 2.32 A; A=7-335.
DR PDB; 4MFA; X-ray; 2.27 A; A=11-335.
DR PDB; 4MFC; X-ray; 2.13 A; A=11-335.
DR PDB; 4MFF; X-ray; 2.55 A; A=11-335.
DR PDB; 4NLK; X-ray; 2.49 A; A=7-335.
DR PDB; 4NLN; X-ray; 2.26 A; A=7-335.
DR PDB; 4NLZ; X-ray; 2.68 A; A=7-335.
DR PDB; 4NM1; X-ray; 2.42 A; A=7-335.
DR PDB; 4NM2; X-ray; 2.52 A; A=7-335.
DR PDB; 4NXZ; X-ray; 2.56 A; A=10-335.
DR PDB; 4NY8; X-ray; 2.25 A; A=10-335.
DR PDB; 4O5C; X-ray; 2.36 A; A=7-335.
DR PDB; 4O5E; X-ray; 2.53 A; A=7-335.
DR PDB; 4O5K; X-ray; 2.06 A; A=10-335.
DR PDB; 4O9M; X-ray; 2.30 A; A=1-335.
DR PDB; 4P2H; X-ray; 1.99 A; A=10-335.
DR PDB; 4PGQ; X-ray; 2.30 A; A=7-335.
DR PDB; 4PGX; X-ray; 2.08 A; A=10-335.
DR PDB; 4PGY; X-ray; 2.26 A; A=7-335.
DR PDB; 4PH5; X-ray; 2.55 A; A=10-335.
DR PDB; 4PHA; X-ray; 2.52 A; A=7-335.
DR PDB; 4PHD; X-ray; 2.21 A; A=7-335.
DR PDB; 4PHE; X-ray; 2.15 A; A=7-335.
DR PDB; 4PHP; X-ray; 2.60 A; A=10-335.
DR PDB; 4PPX; X-ray; 2.08 A; A=1-335.
DR PDB; 4R63; X-ray; 1.85 A; A=1-335.
DR PDB; 4R64; X-ray; 2.20 A; A=1-335.
DR PDB; 4R65; X-ray; 1.95 A; A=1-335.
DR PDB; 4R66; X-ray; 2.25 A; A=1-335.
DR PDB; 4RPX; X-ray; 1.90 A; A=1-335.
DR PDB; 4RPY; X-ray; 1.90 A; A=1-335.
DR PDB; 4RPZ; X-ray; 2.19 A; A=1-335.
DR PDB; 4RQ0; X-ray; 2.20 A; A=1-335.
DR PDB; 4RQ1; X-ray; 2.70 A; A=1-335.
DR PDB; 4RQ2; X-ray; 2.20 A; A=1-335.
DR PDB; 4RQ3; X-ray; 2.00 A; A=1-335.
DR PDB; 4RQ4; X-ray; 2.10 A; A=1-335.
DR PDB; 4RQ5; X-ray; 2.32 A; A=1-335.
DR PDB; 4RQ6; X-ray; 2.25 A; A=1-335.
DR PDB; 4RQ7; X-ray; 2.00 A; A=1-335.
DR PDB; 4RQ8; X-ray; 2.00 A; A=1-335.
DR PDB; 4RT2; X-ray; 1.92 A; A=1-335.
DR PDB; 4RT3; X-ray; 1.92 A; A=1-335.
DR PDB; 4TUP; X-ray; 1.80 A; A=7-335.
DR PDB; 4TUQ; X-ray; 2.37 A; A=10-335.
DR PDB; 4TUR; X-ray; 2.17 A; A=7-335.
DR PDB; 4TUS; X-ray; 2.42 A; A=10-335.
DR PDB; 4UAW; X-ray; 1.90 A; A=1-335.
DR PDB; 4UAY; X-ray; 1.98 A; A=1-335.
DR PDB; 4UAZ; X-ray; 1.88 A; A=1-335.
DR PDB; 4UB1; X-ray; 2.34 A; A=1-335.
DR PDB; 4UB2; X-ray; 2.51 A; A=1-335.
DR PDB; 4UB3; X-ray; 2.06 A; A=1-335.
DR PDB; 4UB4; X-ray; 1.95 A; A=1-335.
DR PDB; 4UB5; X-ray; 2.15 A; A=1-335.
DR PDB; 4UBB; X-ray; 1.90 A; A=1-335.
DR PDB; 4UBC; X-ray; 2.00 A; A=1-335.
DR PDB; 4YMM; X-ray; 2.20 A; A=1-335.
DR PDB; 4YMN; X-ray; 2.59 A; A=1-335.
DR PDB; 4YMO; X-ray; 2.15 A; A=1-335.
DR PDB; 4YN4; X-ray; 2.24 A; A=1-335.
DR PDB; 4Z6C; X-ray; 2.68 A; A=1-335.
DR PDB; 4Z6D; X-ray; 2.51 A; A=1-335.
DR PDB; 4Z6E; X-ray; 2.75 A; A=1-335.
DR PDB; 4Z6F; X-ray; 2.44 A; A=1-335.
DR PDB; 5BOL; X-ray; 1.98 A; A=1-335.
DR PDB; 5BOM; X-ray; 2.00 A; A=1-335.
DR PDB; 5BPC; X-ray; 2.00 A; A=1-335.
DR PDB; 5DB6; X-ray; 2.83 A; A=1-335.
DR PDB; 5DB7; X-ray; 2.21 A; A=1-335.
DR PDB; 5DB8; X-ray; 2.55 A; A=1-335.
DR PDB; 5DB9; X-ray; 2.45 A; A=1-335.
DR PDB; 5DBA; X-ray; 1.97 A; A=1-335.
DR PDB; 5DBB; X-ray; 2.25 A; A=1-335.
DR PDB; 5DBC; X-ray; 2.40 A; A=1-335.
DR PDB; 5EOZ; X-ray; 2.09 A; A=1-335.
DR PDB; 5HHH; X-ray; 2.36 A; A=9-335.
DR PDB; 5HHI; X-ray; 2.52 A; A=7-335.
DR PDB; 5J0O; X-ray; 2.00 A; A=1-335.
DR PDB; 5J0P; X-ray; 2.20 A; A=1-335.
DR PDB; 5J0Q; X-ray; 2.00 A; A=1-335.
DR PDB; 5J0R; X-ray; 2.00 A; A=1-335.
DR PDB; 5J0S; X-ray; 2.00 A; A=1-335.
DR PDB; 5J0T; X-ray; 2.00 A; A=1-335.
DR PDB; 5J0U; X-ray; 2.10 A; A=1-335.
DR PDB; 5J0W; X-ray; 2.40 A; A=1-335.
DR PDB; 5J0X; X-ray; 2.00 A; A=1-335.
DR PDB; 5J0Y; X-ray; 2.00 A; A=1-335.
DR PDB; 5J29; X-ray; 2.20 A; A=1-335.
DR PDB; 5J2A; X-ray; 2.50 A; A=1-335.
DR PDB; 5J2B; X-ray; 2.50 A; A=1-335.
DR PDB; 5J2C; X-ray; 2.10 A; A=1-335.
DR PDB; 5J2D; X-ray; 2.10 A; A=1-335.
DR PDB; 5J2E; X-ray; 2.10 A; A=1-335.
DR PDB; 5J2F; X-ray; 2.10 A; A=1-335.
DR PDB; 5J2G; X-ray; 2.10 A; A=1-335.
DR PDB; 5J2H; X-ray; 2.30 A; A=1-335.
DR PDB; 5J2I; X-ray; 2.40 A; A=1-335.
DR PDB; 5J2J; X-ray; 2.20 A; A=1-335.
DR PDB; 5J2K; X-ray; 2.10 A; A=1-335.
DR PDB; 5TB8; X-ray; 2.00 A; A=1-335.
DR PDB; 5TB9; X-ray; 2.49 A; A=1-335.
DR PDB; 5TBA; X-ray; 2.49 A; A=1-335.
DR PDB; 5TBB; X-ray; 2.39 A; A=1-335.
DR PDB; 5TBC; X-ray; 1.85 A; A=1-335.
DR PDB; 5TZV; X-ray; 2.00 A; A=1-335.
DR PDB; 5U2R; X-ray; 1.80 A; A=1-335.
DR PDB; 5U2S; X-ray; 2.30 A; A=1-335.
DR PDB; 5U2T; X-ray; 1.79 A; A=1-335.
DR PDB; 5U8G; X-ray; 2.17 A; A=1-335.
DR PDB; 5U8H; X-ray; 2.15 A; A=1-335.
DR PDB; 5U8I; X-ray; 2.45 A; A=1-335.
DR PDB; 5U9H; X-ray; 1.85 A; A=1-335.
DR PDB; 5UGN; X-ray; 2.00 A; A=1-335.
DR PDB; 5UGO; X-ray; 1.90 A; A=1-335.
DR PDB; 5UGP; X-ray; 1.96 A; A=1-335.
DR PDB; 5V1F; X-ray; 2.18 A; A=1-335.
DR PDB; 5V1G; X-ray; 1.80 A; A=1-335.
DR PDB; 5V1H; X-ray; 1.95 A; A=1-335.
DR PDB; 5V1I; X-ray; 2.04 A; A=1-335.
DR PDB; 5V1J; X-ray; 2.62 A; A=1-335.
DR PDB; 5V1N; X-ray; 2.00 A; A=1-335.
DR PDB; 5V1O; X-ray; 1.80 A; A=1-335.
DR PDB; 5V1P; X-ray; 1.99 A; A=1-335.
DR PDB; 5V1R; X-ray; 2.08 A; A=1-335.
DR PDB; 5VEZ; X-ray; 2.04 A; A=1-335.
DR PDB; 5VRW; X-ray; 2.58 A; A=1-335.
DR PDB; 5VRX; X-ray; 2.20 A; A=1-335.
DR PDB; 5VRY; X-ray; 1.90 A; A=1-335.
DR PDB; 5VRZ; X-ray; 2.05 A; A=1-335.
DR PDB; 5VS0; X-ray; 2.10 A; A=1-335.
DR PDB; 5VS1; X-ray; 2.50 A; A=1-335.
DR PDB; 5VS2; X-ray; 2.33 A; A=1-335.
DR PDB; 5VS3; X-ray; 1.70 A; A=1-335.
DR PDB; 5VS4; X-ray; 1.87 A; A=1-335.
DR PDB; 5WNX; X-ray; 2.55 A; A=1-335.
DR PDB; 5WNY; X-ray; 2.10 A; A=1-335.
DR PDB; 5WNZ; X-ray; 2.20 A; A=1-335.
DR PDB; 5WO0; X-ray; 1.60 A; A=1-335.
DR PDB; 6BEL; X-ray; 1.90 A; A=1-335.
DR PDB; 6BEM; X-ray; 1.88 A; A=1-335.
DR PDB; 6BTE; X-ray; 2.20 A; A=1-335.
DR PDB; 6BTF; X-ray; 1.75 A; A=1-335.
DR PDB; 6CLY; X-ray; 2.19 A; A=1-335.
DR PDB; 6CPQ; X-ray; 1.93 A; A=1-335.
DR PDB; 6CR3; X-ray; 1.95 A; A=1-335.
DR PDB; 6CR4; X-ray; 1.80 A; A=1-335.
DR PDB; 6CR5; X-ray; 1.98 A; A=1-335.
DR PDB; 6CR6; X-ray; 2.10 A; A=1-335.
DR PDB; 6CR7; X-ray; 2.29 A; A=1-335.
DR PDB; 6CR8; X-ray; 2.05 A; A=1-335.
DR PDB; 6CR9; X-ray; 1.96 A; A=1-335.
DR PDB; 6CRB; X-ray; 2.15 A; A=1-335.
DR PDB; 6CRC; X-ray; 2.30 A; A=1-335.
DR PDB; 6CRH; X-ray; 2.33 A; A=1-335.
DR PDB; 6CTI; X-ray; 2.00 A; A=1-335.
DR PDB; 6CTJ; X-ray; 2.10 A; A=1-335.
DR PDB; 6CTK; X-ray; 2.15 A; A=1-335.
DR PDB; 6CTL; X-ray; 2.00 A; A=1-335.
DR PDB; 6CTM; X-ray; 2.10 A; A=1-335.
DR PDB; 6CTN; X-ray; 1.92 A; A=1-335.
DR PDB; 6CTO; X-ray; 2.04 A; A=1-335.
DR PDB; 6CTP; X-ray; 2.20 A; A=1-335.
DR PDB; 6CTQ; X-ray; 1.87 A; A=1-335.
DR PDB; 6CTR; X-ray; 1.85 A; A=1-335.
DR PDB; 6CTT; X-ray; 2.00 A; A=1-335.
DR PDB; 6CTU; X-ray; 1.90 A; A=1-335.
DR PDB; 6CTV; X-ray; 2.02 A; A=1-335.
DR PDB; 6CTW; X-ray; 1.98 A; A=1-335.
DR PDB; 6CTX; X-ray; 2.02 A; A=1-335.
DR PDB; 6CU9; X-ray; 2.04 A; A=1-335.
DR PDB; 6CUA; X-ray; 2.17 A; A=1-335.
DR PDB; 6CUB; X-ray; 2.05 A; A=1-335.
DR PDB; 6DIA; X-ray; 1.97 A; A=1-335.
DR PDB; 6DIC; X-ray; 1.99 A; A=1-335.
DR PDB; 6E3R; X-ray; 2.26 A; A=1-335.
DR PDB; 6E3V; X-ray; 1.96 A; A=1-335.
DR PDB; 6E3W; X-ray; 2.02 A; A=1-335.
DR PDB; 6E3X; X-ray; 2.65 A; A=1-335.
DR PDB; 6G2Q; X-ray; 2.15 A; A=1-335.
DR PDB; 6MR7; X-ray; 2.14 A; A=1-335.
DR PDB; 6MR8; X-ray; 1.90 A; A=1-335.
DR PDB; 6N2R; X-ray; 2.10 A; A=1-335.
DR PDB; 6N2S; X-ray; 2.46 A; A=1-335.
DR PDB; 6N2T; X-ray; 2.60 A; A=1-335.
DR PDB; 6NKR; X-ray; 2.45 A; A=1-335.
DR PDB; 6NKS; X-ray; 2.35 A; A=1-335.
DR PDB; 6NKT; X-ray; 2.60 A; A=1-335.
DR PDB; 6NKU; X-ray; 1.90 A; A=1-335.
DR PDB; 6NKV; X-ray; 1.85 A; A=1-335.
DR PDB; 6NKW; X-ray; 1.98 A; A=1-335.
DR PDB; 6NKX; X-ray; 1.98 A; A=1-335.
DR PDB; 6NKY; X-ray; 2.09 A; A=1-335.
DR PDB; 6NKZ; X-ray; 2.01 A; A=1-335.
DR PDB; 6NL0; X-ray; 1.97 A; A=1-335.
DR PDB; 6PH5; X-ray; 2.60 A; A=1-335.
DR PDB; 6PH6; X-ray; 2.60 A; A=1-335.
DR PDB; 6PKZ; X-ray; 2.74 A; A=1-335.
DR PDB; 6U2O; X-ray; 2.30 A; A=1-335.
DR PDB; 6U6B; X-ray; 3.11 A; A=1-335.
DR PDB; 6UOK; X-ray; 2.55 A; A/F=1-335.
DR PDB; 6UOL; X-ray; 1.94 A; A=1-335.
DR PDB; 6UOM; X-ray; 2.05 A; A=1-335.
DR PDB; 6W2M; X-ray; 2.00 A; A=1-335.
DR PDB; 7ICE; X-ray; 2.80 A; A=1-335.
DR PDB; 7ICF; X-ray; 3.10 A; A=1-335.
DR PDB; 7ICG; X-ray; 3.00 A; A=1-335.
DR PDB; 7ICH; X-ray; 2.90 A; A=1-335.
DR PDB; 7ICI; X-ray; 2.80 A; A=1-335.
DR PDB; 7ICJ; X-ray; 3.50 A; A=1-335.
DR PDB; 7ICK; X-ray; 2.90 A; A=1-335.
DR PDB; 7ICL; X-ray; 3.10 A; A=1-335.
DR PDB; 7ICM; X-ray; 3.00 A; A=1-335.
DR PDB; 7ICN; X-ray; 2.80 A; A=1-335.
DR PDB; 7ICO; X-ray; 3.30 A; A=1-335.
DR PDB; 7ICP; X-ray; 3.00 A; A=1-335.
DR PDB; 7ICQ; X-ray; 2.90 A; A=1-335.
DR PDB; 7ICR; X-ray; 3.00 A; A=1-335.
DR PDB; 7ICS; X-ray; 2.80 A; A=1-335.
DR PDB; 7ICT; X-ray; 2.80 A; A=1-335.
DR PDB; 7ICU; X-ray; 3.30 A; A=1-335.
DR PDB; 7ICV; X-ray; 2.80 A; A=1-335.
DR PDB; 7K96; X-ray; 2.10 A; A=1-335.
DR PDB; 7K97; X-ray; 2.40 A; A=10-335.
DR PDB; 7RBE; X-ray; 1.89 A; A=1-335.
DR PDB; 7RBF; X-ray; 1.84 A; A=1-335.
DR PDB; 7RBG; X-ray; 1.90 A; A=1-335.
DR PDB; 7RBH; X-ray; 1.75 A; A=1-335.
DR PDB; 7RBI; X-ray; 1.93 A; A=1-335.
DR PDB; 7RBJ; X-ray; 1.91 A; A=1-335.
DR PDB; 7RBK; X-ray; 2.20 A; A=1-335.
DR PDB; 7RBL; X-ray; 1.98 A; A=1-335.
DR PDB; 7RBM; X-ray; 2.21 A; A=1-335.
DR PDB; 7RBN; X-ray; 2.90 A; A=1-335.
DR PDB; 7RBO; X-ray; 2.96 A; A=1-335.
DR PDB; 8ICA; X-ray; 3.00 A; A=1-335.
DR PDB; 8ICB; X-ray; 3.10 A; A=1-335.
DR PDB; 8ICC; X-ray; 2.80 A; A=1-335.
DR PDB; 8ICE; X-ray; 3.20 A; A=1-335.
DR PDB; 8ICF; X-ray; 2.90 A; A=1-335.
DR PDB; 8ICG; X-ray; 3.30 A; A=1-335.
DR PDB; 8ICH; X-ray; 3.30 A; A=1-335.
DR PDB; 8ICI; X-ray; 2.80 A; A=1-335.
DR PDB; 8ICJ; X-ray; 3.20 A; A=1-335.
DR PDB; 8ICK; X-ray; 2.70 A; A=1-335.
DR PDB; 8ICL; X-ray; 3.10 A; A=1-335.
DR PDB; 8ICM; X-ray; 2.90 A; A=1-335.
DR PDB; 8ICN; X-ray; 2.80 A; A=1-335.
DR PDB; 8ICO; X-ray; 2.70 A; A=1-335.
DR PDB; 8ICP; X-ray; 2.90 A; A=1-335.
DR PDB; 8ICQ; X-ray; 3.00 A; A=1-335.
DR PDB; 8ICR; X-ray; 2.90 A; A=1-335.
DR PDB; 8ICS; X-ray; 2.90 A; A=1-335.
DR PDB; 8ICT; X-ray; 3.10 A; A=1-335.
DR PDB; 8ICU; X-ray; 3.00 A; A=1-335.
DR PDB; 8ICV; X-ray; 3.20 A; A=1-335.
DR PDB; 8ICW; X-ray; 3.30 A; A=1-335.
DR PDB; 8ICX; X-ray; 3.00 A; A=1-335.
DR PDB; 8ICY; X-ray; 3.10 A; A=1-335.
DR PDB; 8ICZ; X-ray; 3.10 A; A=1-335.
DR PDB; 9ICA; X-ray; 3.00 A; A=1-335.
DR PDB; 9ICB; X-ray; 3.20 A; A=1-335.
DR PDB; 9ICC; X-ray; 3.10 A; A=1-335.
DR PDB; 9ICE; X-ray; 3.30 A; A=1-335.
DR PDB; 9ICF; X-ray; 3.00 A; A=1-335.
DR PDB; 9ICG; X-ray; 3.00 A; A=1-335.
DR PDB; 9ICH; X-ray; 2.90 A; A=1-335.
DR PDB; 9ICI; X-ray; 3.10 A; A=1-335.
DR PDB; 9ICJ; X-ray; 3.10 A; A=1-335.
DR PDB; 9ICK; X-ray; 2.70 A; A=1-335.
DR PDB; 9ICL; X-ray; 2.80 A; A=1-335.
DR PDB; 9ICM; X-ray; 2.90 A; A=1-335.
DR PDB; 9ICN; X-ray; 3.00 A; A=1-335.
DR PDB; 9ICO; X-ray; 2.90 A; A=1-335.
DR PDB; 9ICP; X-ray; 3.10 A; A=1-335.
DR PDB; 9ICQ; X-ray; 2.90 A; A=1-335.
DR PDB; 9ICR; X-ray; 3.00 A; A=1-335.
DR PDB; 9ICS; X-ray; 2.90 A; A=1-335.
DR PDB; 9ICT; X-ray; 3.00 A; A=1-335.
DR PDB; 9ICU; X-ray; 2.90 A; A=1-335.
DR PDB; 9ICV; X-ray; 2.70 A; A=1-335.
DR PDB; 9ICW; X-ray; 2.60 A; A=1-335.
DR PDB; 9ICX; X-ray; 2.60 A; A=1-335.
DR PDB; 9ICY; X-ray; 3.00 A; A=1-335.
DR PDBsum; 1BPX; -.
DR PDBsum; 1BPY; -.
DR PDBsum; 1BPZ; -.
DR PDBsum; 1MQ2; -.
DR PDBsum; 1MQ3; -.
DR PDBsum; 1TV9; -.
DR PDBsum; 1TVA; -.
DR PDBsum; 1ZJM; -.
DR PDBsum; 1ZJN; -.
DR PDBsum; 1ZQA; -.
DR PDBsum; 1ZQB; -.
DR PDBsum; 1ZQC; -.
DR PDBsum; 1ZQD; -.
DR PDBsum; 1ZQE; -.
DR PDBsum; 1ZQF; -.
DR PDBsum; 1ZQG; -.
DR PDBsum; 1ZQH; -.
DR PDBsum; 1ZQI; -.
DR PDBsum; 1ZQJ; -.
DR PDBsum; 1ZQK; -.
DR PDBsum; 1ZQL; -.
DR PDBsum; 1ZQM; -.
DR PDBsum; 1ZQN; -.
DR PDBsum; 1ZQO; -.
DR PDBsum; 1ZQP; -.
DR PDBsum; 1ZQQ; -.
DR PDBsum; 1ZQR; -.
DR PDBsum; 1ZQS; -.
DR PDBsum; 1ZQT; -.
DR PDBsum; 2FMP; -.
DR PDBsum; 2FMQ; -.
DR PDBsum; 2FMS; -.
DR PDBsum; 2I9G; -.
DR PDBsum; 2ISO; -.
DR PDBsum; 2ISP; -.
DR PDBsum; 2P66; -.
DR PDBsum; 2PXI; -.
DR PDBsum; 3C2K; -.
DR PDBsum; 3C2L; -.
DR PDBsum; 3C2M; -.
DR PDBsum; 3GDX; -.
DR PDBsum; 3ISB; -.
DR PDBsum; 3ISC; -.
DR PDBsum; 3ISD; -.
DR PDBsum; 3JPN; -.
DR PDBsum; 3JPO; -.
DR PDBsum; 3JPP; -.
DR PDBsum; 3JPQ; -.
DR PDBsum; 3JPR; -.
DR PDBsum; 3JPS; -.
DR PDBsum; 3JPT; -.
DR PDBsum; 3LK9; -.
DR PDBsum; 3MBY; -.
DR PDBsum; 3OGU; -.
DR PDBsum; 3RH4; -.
DR PDBsum; 3RH5; -.
DR PDBsum; 3RH6; -.
DR PDBsum; 3RJE; -.
DR PDBsum; 3RJF; -.
DR PDBsum; 3RJG; -.
DR PDBsum; 3RJH; -.
DR PDBsum; 3RJI; -.
DR PDBsum; 3RJJ; -.
DR PDBsum; 3RJK; -.
DR PDBsum; 3TFR; -.
DR PDBsum; 3TFS; -.
DR PDBsum; 4DO9; -.
DR PDBsum; 4DOA; -.
DR PDBsum; 4DOB; -.
DR PDBsum; 4DOC; -.
DR PDBsum; 4F5N; -.
DR PDBsum; 4F5O; -.
DR PDBsum; 4F5P; -.
DR PDBsum; 4F5Q; -.
DR PDBsum; 4F5R; -.
DR PDBsum; 4GXI; -.
DR PDBsum; 4GXJ; -.
DR PDBsum; 4GXK; -.
DR PDBsum; 4JWM; -.
DR PDBsum; 4JWN; -.
DR PDBsum; 4KLD; -.
DR PDBsum; 4KLE; -.
DR PDBsum; 4KLF; -.
DR PDBsum; 4KLG; -.
DR PDBsum; 4KLH; -.
DR PDBsum; 4KLI; -.
DR PDBsum; 4KLJ; -.
DR PDBsum; 4KLL; -.
DR PDBsum; 4KLM; -.
DR PDBsum; 4KLO; -.
DR PDBsum; 4KLQ; -.
DR PDBsum; 4KLS; -.
DR PDBsum; 4KLT; -.
DR PDBsum; 4KLU; -.
DR PDBsum; 4LVS; -.
DR PDBsum; 4M2Y; -.
DR PDBsum; 4M47; -.
DR PDBsum; 4M9G; -.
DR PDBsum; 4M9H; -.
DR PDBsum; 4M9J; -.
DR PDBsum; 4M9L; -.
DR PDBsum; 4M9N; -.
DR PDBsum; 4MF2; -.
DR PDBsum; 4MF8; -.
DR PDBsum; 4MFA; -.
DR PDBsum; 4MFC; -.
DR PDBsum; 4MFF; -.
DR PDBsum; 4NLK; -.
DR PDBsum; 4NLN; -.
DR PDBsum; 4NLZ; -.
DR PDBsum; 4NM1; -.
DR PDBsum; 4NM2; -.
DR PDBsum; 4NXZ; -.
DR PDBsum; 4NY8; -.
DR PDBsum; 4O5C; -.
DR PDBsum; 4O5E; -.
DR PDBsum; 4O5K; -.
DR PDBsum; 4O9M; -.
DR PDBsum; 4P2H; -.
DR PDBsum; 4PGQ; -.
DR PDBsum; 4PGX; -.
DR PDBsum; 4PGY; -.
DR PDBsum; 4PH5; -.
DR PDBsum; 4PHA; -.
DR PDBsum; 4PHD; -.
DR PDBsum; 4PHE; -.
DR PDBsum; 4PHP; -.
DR PDBsum; 4PPX; -.
DR PDBsum; 4R63; -.
DR PDBsum; 4R64; -.
DR PDBsum; 4R65; -.
DR PDBsum; 4R66; -.
DR PDBsum; 4RPX; -.
DR PDBsum; 4RPY; -.
DR PDBsum; 4RPZ; -.
DR PDBsum; 4RQ0; -.
DR PDBsum; 4RQ1; -.
DR PDBsum; 4RQ2; -.
DR PDBsum; 4RQ3; -.
DR PDBsum; 4RQ4; -.
DR PDBsum; 4RQ5; -.
DR PDBsum; 4RQ6; -.
DR PDBsum; 4RQ7; -.
DR PDBsum; 4RQ8; -.
DR PDBsum; 4RT2; -.
DR PDBsum; 4RT3; -.
DR PDBsum; 4TUP; -.
DR PDBsum; 4TUQ; -.
DR PDBsum; 4TUR; -.
DR PDBsum; 4TUS; -.
DR PDBsum; 4UAW; -.
DR PDBsum; 4UAY; -.
DR PDBsum; 4UAZ; -.
DR PDBsum; 4UB1; -.
DR PDBsum; 4UB2; -.
DR PDBsum; 4UB3; -.
DR PDBsum; 4UB4; -.
DR PDBsum; 4UB5; -.
DR PDBsum; 4UBB; -.
DR PDBsum; 4UBC; -.
DR PDBsum; 4YMM; -.
DR PDBsum; 4YMN; -.
DR PDBsum; 4YMO; -.
DR PDBsum; 4YN4; -.
DR PDBsum; 4Z6C; -.
DR PDBsum; 4Z6D; -.
DR PDBsum; 4Z6E; -.
DR PDBsum; 4Z6F; -.
DR PDBsum; 5BOL; -.
DR PDBsum; 5BOM; -.
DR PDBsum; 5BPC; -.
DR PDBsum; 5DB6; -.
DR PDBsum; 5DB7; -.
DR PDBsum; 5DB8; -.
DR PDBsum; 5DB9; -.
DR PDBsum; 5DBA; -.
DR PDBsum; 5DBB; -.
DR PDBsum; 5DBC; -.
DR PDBsum; 5EOZ; -.
DR PDBsum; 5HHH; -.
DR PDBsum; 5HHI; -.
DR PDBsum; 5J0O; -.
DR PDBsum; 5J0P; -.
DR PDBsum; 5J0Q; -.
DR PDBsum; 5J0R; -.
DR PDBsum; 5J0S; -.
DR PDBsum; 5J0T; -.
DR PDBsum; 5J0U; -.
DR PDBsum; 5J0W; -.
DR PDBsum; 5J0X; -.
DR PDBsum; 5J0Y; -.
DR PDBsum; 5J29; -.
DR PDBsum; 5J2A; -.
DR PDBsum; 5J2B; -.
DR PDBsum; 5J2C; -.
DR PDBsum; 5J2D; -.
DR PDBsum; 5J2E; -.
DR PDBsum; 5J2F; -.
DR PDBsum; 5J2G; -.
DR PDBsum; 5J2H; -.
DR PDBsum; 5J2I; -.
DR PDBsum; 5J2J; -.
DR PDBsum; 5J2K; -.
DR PDBsum; 5TB8; -.
DR PDBsum; 5TB9; -.
DR PDBsum; 5TBA; -.
DR PDBsum; 5TBB; -.
DR PDBsum; 5TBC; -.
DR PDBsum; 5TZV; -.
DR PDBsum; 5U2R; -.
DR PDBsum; 5U2S; -.
DR PDBsum; 5U2T; -.
DR PDBsum; 5U8G; -.
DR PDBsum; 5U8H; -.
DR PDBsum; 5U8I; -.
DR PDBsum; 5U9H; -.
DR PDBsum; 5UGN; -.
DR PDBsum; 5UGO; -.
DR PDBsum; 5UGP; -.
DR PDBsum; 5V1F; -.
DR PDBsum; 5V1G; -.
DR PDBsum; 5V1H; -.
DR PDBsum; 5V1I; -.
DR PDBsum; 5V1J; -.
DR PDBsum; 5V1N; -.
DR PDBsum; 5V1O; -.
DR PDBsum; 5V1P; -.
DR PDBsum; 5V1R; -.
DR PDBsum; 5VEZ; -.
DR PDBsum; 5VRW; -.
DR PDBsum; 5VRX; -.
DR PDBsum; 5VRY; -.
DR PDBsum; 5VRZ; -.
DR PDBsum; 5VS0; -.
DR PDBsum; 5VS1; -.
DR PDBsum; 5VS2; -.
DR PDBsum; 5VS3; -.
DR PDBsum; 5VS4; -.
DR PDBsum; 5WNX; -.
DR PDBsum; 5WNY; -.
DR PDBsum; 5WNZ; -.
DR PDBsum; 5WO0; -.
DR PDBsum; 6BEL; -.
DR PDBsum; 6BEM; -.
DR PDBsum; 6BTE; -.
DR PDBsum; 6BTF; -.
DR PDBsum; 6CLY; -.
DR PDBsum; 6CPQ; -.
DR PDBsum; 6CR3; -.
DR PDBsum; 6CR4; -.
DR PDBsum; 6CR5; -.
DR PDBsum; 6CR6; -.
DR PDBsum; 6CR7; -.
DR PDBsum; 6CR8; -.
DR PDBsum; 6CR9; -.
DR PDBsum; 6CRB; -.
DR PDBsum; 6CRC; -.
DR PDBsum; 6CRH; -.
DR PDBsum; 6CTI; -.
DR PDBsum; 6CTJ; -.
DR PDBsum; 6CTK; -.
DR PDBsum; 6CTL; -.
DR PDBsum; 6CTM; -.
DR PDBsum; 6CTN; -.
DR PDBsum; 6CTO; -.
DR PDBsum; 6CTP; -.
DR PDBsum; 6CTQ; -.
DR PDBsum; 6CTR; -.
DR PDBsum; 6CTT; -.
DR PDBsum; 6CTU; -.
DR PDBsum; 6CTV; -.
DR PDBsum; 6CTW; -.
DR PDBsum; 6CTX; -.
DR PDBsum; 6CU9; -.
DR PDBsum; 6CUA; -.
DR PDBsum; 6CUB; -.
DR PDBsum; 6DIA; -.
DR PDBsum; 6DIC; -.
DR PDBsum; 6E3R; -.
DR PDBsum; 6E3V; -.
DR PDBsum; 6E3W; -.
DR PDBsum; 6E3X; -.
DR PDBsum; 6G2Q; -.
DR PDBsum; 6MR7; -.
DR PDBsum; 6MR8; -.
DR PDBsum; 6N2R; -.
DR PDBsum; 6N2S; -.
DR PDBsum; 6N2T; -.
DR PDBsum; 6NKR; -.
DR PDBsum; 6NKS; -.
DR PDBsum; 6NKT; -.
DR PDBsum; 6NKU; -.
DR PDBsum; 6NKV; -.
DR PDBsum; 6NKW; -.
DR PDBsum; 6NKX; -.
DR PDBsum; 6NKY; -.
DR PDBsum; 6NKZ; -.
DR PDBsum; 6NL0; -.
DR PDBsum; 6PH5; -.
DR PDBsum; 6PH6; -.
DR PDBsum; 6PKZ; -.
DR PDBsum; 6U2O; -.
DR PDBsum; 6U6B; -.
DR PDBsum; 6UOK; -.
DR PDBsum; 6UOL; -.
DR PDBsum; 6UOM; -.
DR PDBsum; 6W2M; -.
DR PDBsum; 7ICE; -.
DR PDBsum; 7ICF; -.
DR PDBsum; 7ICG; -.
DR PDBsum; 7ICH; -.
DR PDBsum; 7ICI; -.
DR PDBsum; 7ICJ; -.
DR PDBsum; 7ICK; -.
DR PDBsum; 7ICL; -.
DR PDBsum; 7ICM; -.
DR PDBsum; 7ICN; -.
DR PDBsum; 7ICO; -.
DR PDBsum; 7ICP; -.
DR PDBsum; 7ICQ; -.
DR PDBsum; 7ICR; -.
DR PDBsum; 7ICS; -.
DR PDBsum; 7ICT; -.
DR PDBsum; 7ICU; -.
DR PDBsum; 7ICV; -.
DR PDBsum; 7K96; -.
DR PDBsum; 7K97; -.
DR PDBsum; 7RBE; -.
DR PDBsum; 7RBF; -.
DR PDBsum; 7RBG; -.
DR PDBsum; 7RBH; -.
DR PDBsum; 7RBI; -.
DR PDBsum; 7RBJ; -.
DR PDBsum; 7RBK; -.
DR PDBsum; 7RBL; -.
DR PDBsum; 7RBM; -.
DR PDBsum; 7RBN; -.
DR PDBsum; 7RBO; -.
DR PDBsum; 8ICA; -.
DR PDBsum; 8ICB; -.
DR PDBsum; 8ICC; -.
DR PDBsum; 8ICE; -.
DR PDBsum; 8ICF; -.
DR PDBsum; 8ICG; -.
DR PDBsum; 8ICH; -.
DR PDBsum; 8ICI; -.
DR PDBsum; 8ICJ; -.
DR PDBsum; 8ICK; -.
DR PDBsum; 8ICL; -.
DR PDBsum; 8ICM; -.
DR PDBsum; 8ICN; -.
DR PDBsum; 8ICO; -.
DR PDBsum; 8ICP; -.
DR PDBsum; 8ICQ; -.
DR PDBsum; 8ICR; -.
DR PDBsum; 8ICS; -.
DR PDBsum; 8ICT; -.
DR PDBsum; 8ICU; -.
DR PDBsum; 8ICV; -.
DR PDBsum; 8ICW; -.
DR PDBsum; 8ICX; -.
DR PDBsum; 8ICY; -.
DR PDBsum; 8ICZ; -.
DR PDBsum; 9ICA; -.
DR PDBsum; 9ICB; -.
DR PDBsum; 9ICC; -.
DR PDBsum; 9ICE; -.
DR PDBsum; 9ICF; -.
DR PDBsum; 9ICG; -.
DR PDBsum; 9ICH; -.
DR PDBsum; 9ICI; -.
DR PDBsum; 9ICJ; -.
DR PDBsum; 9ICK; -.
DR PDBsum; 9ICL; -.
DR PDBsum; 9ICM; -.
DR PDBsum; 9ICN; -.
DR PDBsum; 9ICO; -.
DR PDBsum; 9ICP; -.
DR PDBsum; 9ICQ; -.
DR PDBsum; 9ICR; -.
DR PDBsum; 9ICS; -.
DR PDBsum; 9ICT; -.
DR PDBsum; 9ICU; -.
DR PDBsum; 9ICV; -.
DR PDBsum; 9ICW; -.
DR PDBsum; 9ICX; -.
DR PDBsum; 9ICY; -.
DR AlphaFoldDB; P06746; -.
DR BMRB; P06746; -.
DR SMR; P06746; -.
DR BioGRID; 111419; 54.
DR CORUM; P06746; -.
DR IntAct; P06746; 34.
DR MINT; P06746; -.
DR STRING; 9606.ENSP00000265421; -.
DR BindingDB; P06746; -.
DR ChEMBL; CHEMBL2392; -.
DR DrugBank; DB07479; (1S)-1,2,3,4-TETRAHYDRO-BENZO[C]PHENANTHRENE-2,3,4-TRIOL.
DR DrugBank; DB00987; Cytarabine.
DR DrugBank; DB03222; dATP.
DR DrugBank; DB14490; Ferrous ascorbate.
DR DrugBank; DB14491; Ferrous fumarate.
DR DrugBank; DB14488; Ferrous gluconate.
DR DrugBank; DB14501; Ferrous glycine sulfate.
DR DrugBank; DB14489; Ferrous succinate.
DR DrugBank; DB01592; Iron.
DR DrugCentral; P06746; -.
DR iPTMnet; P06746; -.
DR PhosphoSitePlus; P06746; -.
DR BioMuta; POLB; -.
DR DMDM; 544186; -.
DR EPD; P06746; -.
DR jPOST; P06746; -.
DR MassIVE; P06746; -.
DR MaxQB; P06746; -.
DR PaxDb; P06746; -.
DR PeptideAtlas; P06746; -.
DR PRIDE; P06746; -.
DR ProteomicsDB; 51926; -.
DR Antibodypedia; 3175; 407 antibodies from 35 providers.
DR CPTC; P06746; 1 antibody.
DR DNASU; 5423; -.
DR Ensembl; ENST00000265421.9; ENSP00000265421.4; ENSG00000070501.12.
DR GeneID; 5423; -.
DR KEGG; hsa:5423; -.
DR MANE-Select; ENST00000265421.9; ENSP00000265421.4; NM_002690.3; NP_002681.1.
DR UCSC; uc003xoz.3; human.
DR CTD; 5423; -.
DR DisGeNET; 5423; -.
DR GeneCards; POLB; -.
DR HGNC; HGNC:9174; POLB.
DR HPA; ENSG00000070501; Low tissue specificity.
DR MIM; 174760; gene.
DR neXtProt; NX_P06746; -.
DR OpenTargets; ENSG00000070501; -.
DR PharmGKB; PA276; -.
DR VEuPathDB; HostDB:ENSG00000070501; -.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000156918; -.
DR HOGENOM; CLU_008698_1_0_1; -.
DR InParanoid; P06746; -.
DR OMA; ITDMLME; -.
DR OrthoDB; 1328151at2759; -.
DR PhylomeDB; P06746; -.
DR TreeFam; TF103002; -.
DR BRENDA; 2.7.7.7; 2681.
DR BRENDA; 4.2.99.B1; 2681.
DR PathwayCommons; P06746; -.
DR Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
DR Reactome; R-HSA-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
DR SignaLink; P06746; -.
DR SIGNOR; P06746; -.
DR BioGRID-ORCS; 5423; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; POLB; human.
DR EvolutionaryTrace; P06746; -.
DR GeneWiki; DNA_polymerase_beta; -.
DR GenomeRNAi; 5423; -.
DR Pharos; P06746; Tchem.
DR PRO; PR:P06746; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P06746; protein.
DR Bgee; ENSG00000070501; Expressed in oocyte and 195 other tissues.
DR ExpressionAtlas; P06746; baseline and differential.
DR Genevisible; P06746; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005876; C:spindle microtubule; IDA:MGI.
DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; TAS:Reactome.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
DR GO; GO:0006287; P:base-excision repair, gap-filling; TAS:Reactome.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0006261; P:DNA-templated DNA replication; TAS:ProtInc.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0007435; P:salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; DNA damage; DNA repair;
KW DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase;
KW Isopeptide bond; Lyase; Magnesium; Metal-binding; Methylation;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Sodium; Transferase;
KW Ubl conjugation.
FT CHAIN 1..335
FT /note="DNA polymerase beta"
FT /id="PRO_0000218778"
FT REGION 183..192
FT /note="DNA-binding"
FT ACT_SITE 72
FT /note="Schiff-base intermediate with DNA"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 103
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 106
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K409"
FT MOD_RES 83
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000269|PubMed:16600869"
FT MOD_RES 152
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000269|PubMed:16600869"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19713937,
FT ECO:0000269|PubMed:21362556"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19713937,
FT ECO:0000269|PubMed:21362556"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19713937,
FT ECO:0000269|PubMed:21362556"
FT VARIANT 242
FT /note="P -> R (in dbSNP:rs3136797)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018881"
FT MUTAGEN 35
FT /note="K->Q,R: Reduces DNA lyase activity slightly."
FT /evidence="ECO:0000269|PubMed:9572863"
FT MUTAGEN 39
FT /note="Y->Q: Abolishes DNA polymerase and DNA lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:9572863"
FT MUTAGEN 41
FT /note="K->R: Abolishes ubiquitination; when associated with
FT R-61 and R-81."
FT /evidence="ECO:0000269|PubMed:19713937"
FT MUTAGEN 61
FT /note="K->R: Abolishes ubiquitination; when associated with
FT R-41 and R-81."
FT /evidence="ECO:0000269|PubMed:19713937"
FT MUTAGEN 68
FT /note="K->Q,R: Reduces DNA lyase activity slightly."
FT /evidence="ECO:0000269|PubMed:9572863"
FT MUTAGEN 72
FT /note="K->Q,R: Abolishes DNA lyase activity. No effect on
FT DNA polymerase activity."
FT /evidence="ECO:0000269|PubMed:9572863"
FT MUTAGEN 81
FT /note="K->R: Abolishes ubiquitination; when associated with
FT R-41 and R-61."
FT /evidence="ECO:0000269|PubMed:19713937"
FT MUTAGEN 83
FT /note="R->K: Slight effect. Abolishes methylation by PRMT6
FT and impairs the polymerase activity; when associated with
FT K-152."
FT /evidence="ECO:0000269|PubMed:16600869"
FT MUTAGEN 84
FT /note="K->R: No effect."
FT /evidence="ECO:0000269|PubMed:9572863"
FT MUTAGEN 152
FT /note="R->K: Slight effect. Abolishes methylation by PRMT6
FT and impairs the polymerase activity; when associated with
FT K-83."
FT /evidence="ECO:0000269|PubMed:16600869"
FT CONFLICT 18
FT /note="M -> K (in Ref. 3; AAB60688)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="L -> R (in Ref. 10; AAA60133)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="I -> Y (in Ref. 10; AAA60133)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> K (in Ref. 10; AAA60133)"
FT /evidence="ECO:0000305"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:5U2T"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1BPY"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:4KLI"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:1ZQD"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3OGU"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4KLL"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4R63"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:4KLI"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:4KLI"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:4KLI"
SQ SEQUENCE 335 AA; 38178 MW; FF9A6D0E6F9A9487 CRC64;
MSKRKAPQET LNGGITDMLT ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK
KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVSGIGPSA ARKFVDEGIK
TLEDLRKNED KLNHHQRIGL KYFGDFEKRI PREEMLQMQD IVLNEVKKVD SEYIATVCGS
FRRGAESSGD MDVLLTHPSF TSESTKQPKL LHQVVEQLQK VHFITDTLSK GETKFMGVCQ
LPSKNDEKEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE
