DCR1A_HUMAN
ID DCR1A_HUMAN Reviewed; 1040 AA.
AC Q6PJP8; D3DRC1; Q14701; Q6P5Y3; Q6PKL4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DNA cross-link repair 1A protein;
DE AltName: Full=Beta-lactamase DCLRE1A;
DE EC=3.5.2.6 {ECO:0000269|PubMed:31434986};
DE AltName: Full=SNM1 homolog A;
DE Short=hSNM1;
DE Short=hSNM1A;
GN Name=DCLRE1A; Synonyms=KIAA0086, SNM1, SNM1A;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-58; ASP-59; ASP-71;
RP LEU-287; HIS-317 AND PHE-859.
RG NIEHS SNPs program;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-317.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-317 AND TRP-582.
RC TISSUE=Cervix, and Lung;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10848582; DOI=10.1128/mcb.20.13.4553-4561.2000;
RA Dronkert M.L.G., de Wit J., Boeve M., Vasconcelos M.L., van Steeg H.,
RA Tan T.L.R., Hoeijmakers J.H.J., Kanaar R.;
RT "Disruption of mouse SNM1 causes increased sensitivity to the DNA
RT interstrand cross-linking agent mitomycin C.";
RL Mol. Cell. Biol. 20:4553-4561(2000).
RN [7]
RP INDUCTION.
RX PubMed=12509242; DOI=10.1016/s1568-7864(02)00015-0;
RA Zhang X., Richie C., Legerski R.J.;
RT "Translation of hSNM1 is mediated by an internal ribosome entry site that
RT upregulates expression during mitosis.";
RL DNA Repair 1:379-390(2002).
RN [8]
RP INTERACTION WITH TP53BP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12446782; DOI=10.1128/mcb.22.24.8635-8647.2002;
RA Richie C.T., Peterson C., Lu T., Hittelman W.N., Carpenter P.B.,
RA Legerski R.J.;
RT "hSnm1 colocalizes and physically associates with 53BP1 before and after
RT DNA damage.";
RL Mol. Cell. Biol. 22:8635-8647(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH CDC27.
RX PubMed=15542852; DOI=10.1128/mcb.24.23.10448-10455.2004;
RA Akhter S., Richie C.T., Deng J.M., Brey E., Zhang X., Patrick C. Jr.,
RA Behringer R.R., Legerski R.J.;
RT "Deficiency in SNM1 abolishes an early mitotic checkpoint induced by
RT spindle stress.";
RL Mol. Cell. Biol. 24:10448-10455(2004).
RN [10]
RP SUBCELLULAR LOCATION, INTERACTION WITH PIAS1, AND MUTAGENESIS OF ASP-838
RP AND HIS-994.
RX PubMed=15572677; DOI=10.1128/mcb.24.24.10733-10741.2004;
RA Ishiai M., Kimura M., Namikoshi K., Yamazoe M., Yamamoto K., Arakawa H.,
RA Agematsu K., Matsushita N., Takeda S., Buerstedde J.-M., Takata M.;
RT "DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus
RT formation.";
RL Mol. Cell. Biol. 24:10733-10741(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202; LYS-236; LYS-269; LYS-353;
RP LYS-361; LYS-429; LYS-488; LYS-508; LYS-517; LYS-533; LYS-536; LYS-668;
RP LYS-670 AND LYS-674, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=31434986; DOI=10.1038/s41598-019-48723-y;
RA Diene S.M., Pinault L., Keshri V., Armstrong N., Khelaifia S.,
RA Chabriere E., Caetano-Anolles G., Colson P., La Scola B., Rolain J.M.,
RA Pontarotti P., Raoult D.;
RT "Human metallo-beta-lactamase enzymes degrade penicillin.";
RL Sci. Rep. 9:12173-12173(2019).
CC -!- FUNCTION: May be required for DNA interstrand cross-link repair. Also
CC required for checkpoint mediated cell cycle arrest in early prophase in
CC response to mitotic spindle poisons. Possesses beta-lactamase activity,
CC catalyzing the hydrolysis of penicillin G and nitrocefin
CC (PubMed:31434986). Exhibits no activity towards other beta-lactam
CC antibiotic classes including cephalosporins (cefotaxime) and
CC carbapenems (imipenem) (PubMed:31434986).
CC {ECO:0000269|PubMed:15542852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000269|PubMed:31434986};
CC -!- ACTIVITY REGULATION: Beta-lactamase activity is inhibited by sulbactam.
CC {ECO:0000269|PubMed:31434986}.
CC -!- SUBUNIT: Binds constitutively to TP53BP1. Binds CDC27, which is itself
CC a component of the anaphase promoting complex (APC). Binds PIAS1.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10848582,
CC ECO:0000269|PubMed:12446782, ECO:0000269|PubMed:15572677}. Note=In some
CC cells it may be found in typically 1 or 2 discrete nuclear aggregates
CC of unknown function which also contain TP53BP1. Also found in multiple
CC discrete nuclear foci which increase in number following treatment with
CC ionizing radiation or interstrand cross-linking agents. These foci
CC overlap with those formed by the MRN complex (composed of MRE11, RAD50
CC and NBN) and BRCA1.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, pancreas,
CC placenta and skeletal muscle. {ECO:0000269|PubMed:12446782}.
CC -!- INDUCTION: During mitosis. The mRNA encoding this protein contains an
CC internal ribosome entry site (IRES) in its 5'-UTR. This 5'-UTR
CC generally suppresses translation while specifically promoting
CC expression during mitosis, when cap-dependent translation may be
CC impaired. {ECO:0000269|PubMed:12509242}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07646.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/dclre1a/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D42045; BAA07646.2; ALT_INIT; mRNA.
DR EMBL; AY607842; AAT09762.1; -; Genomic_DNA.
DR EMBL; AL592546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49489.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49490.1; -; Genomic_DNA.
DR EMBL; BC013124; AAH13124.1; -; mRNA.
DR EMBL; BC062582; AAH62582.1; -; mRNA.
DR CCDS; CCDS7584.1; -.
DR RefSeq; NP_001258745.1; NM_001271816.1.
DR RefSeq; NP_055696.3; NM_014881.4.
DR RefSeq; XP_006718153.1; XM_006718090.1.
DR RefSeq; XP_011538731.1; XM_011540429.1.
DR PDB; 4B87; X-ray; 2.16 A; A=676-1040.
DR PDB; 5AHR; X-ray; 2.19 A; A=700-1040.
DR PDB; 5NZW; X-ray; 2.70 A; A=698-1040.
DR PDB; 5NZX; X-ray; 1.47 A; A=698-1040.
DR PDB; 5NZY; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q1J; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q1K; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q1L; X-ray; 1.76 A; A=698-1040.
DR PDB; 5Q1M; X-ray; 1.56 A; A=698-1040.
DR PDB; 5Q1N; X-ray; 1.38 A; A=698-1040.
DR PDB; 5Q1O; X-ray; 1.25 A; A=698-1040.
DR PDB; 5Q1P; X-ray; 1.56 A; A=698-1040.
DR PDB; 5Q1Q; X-ray; 1.44 A; A=698-1040.
DR PDB; 5Q1R; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q1S; X-ray; 1.62 A; A=698-1040.
DR PDB; 5Q1T; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q1U; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q1V; X-ray; 1.57 A; A=698-1040.
DR PDB; 5Q1W; X-ray; 1.68 A; A=698-1040.
DR PDB; 5Q1X; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q1Y; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q1Z; X-ray; 1.41 A; A=698-1040.
DR PDB; 5Q20; X-ray; 1.76 A; A=698-1040.
DR PDB; 5Q22; X-ray; 1.18 A; A=698-1040.
DR PDB; 5Q23; X-ray; 1.32 A; A=698-1040.
DR PDB; 5Q24; X-ray; 1.35 A; A=698-1040.
DR PDB; 5Q25; X-ray; 1.43 A; A=698-1040.
DR PDB; 5Q26; X-ray; 1.66 A; A=698-1040.
DR PDB; 5Q27; X-ray; 1.83 A; A=698-1040.
DR PDB; 5Q28; X-ray; 1.52 A; A=698-1040.
DR PDB; 5Q29; X-ray; 1.46 A; A=698-1040.
DR PDB; 5Q2A; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q2B; X-ray; 1.33 A; A=698-1040.
DR PDB; 5Q2C; X-ray; 1.53 A; A=698-1040.
DR PDB; 5Q2D; X-ray; 1.40 A; A=698-1040.
DR PDB; 5Q2E; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q2F; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q2G; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q2H; X-ray; 1.72 A; A=698-1040.
DR PDB; 5Q2I; X-ray; 2.33 A; A=698-1040.
DR PDB; 5Q2J; X-ray; 1.30 A; A=698-1040.
DR PDB; 5Q2K; X-ray; 1.65 A; A=698-1040.
DR PDB; 5Q2L; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q2M; X-ray; 1.28 A; A=698-1040.
DR PDB; 5Q2N; X-ray; 1.38 A; A=698-1040.
DR PDB; 5Q2O; X-ray; 1.75 A; A=698-1040.
DR PDB; 5Q2P; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q2Q; X-ray; 1.44 A; A=698-1040.
DR PDB; 5Q2R; X-ray; 1.37 A; A=698-1040.
DR PDB; 5Q2S; X-ray; 1.52 A; A=698-1040.
DR PDB; 5Q2T; X-ray; 1.52 A; A=698-1040.
DR PDB; 5Q2U; X-ray; 1.37 A; A=698-1040.
DR PDB; 5Q2V; X-ray; 1.58 A; A=698-1040.
DR PDB; 5Q2W; X-ray; 1.53 A; A=698-1040.
DR PDB; 5Q2X; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q2Y; X-ray; 1.61 A; A=698-1040.
DR PDB; 5Q2Z; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q30; X-ray; 1.80 A; A=698-1040.
DR PDB; 5Q31; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q32; X-ray; 1.87 A; A=698-1040.
DR PDB; 5Q33; X-ray; 1.37 A; A=698-1040.
DR PDB; 5Q34; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q35; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q36; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q37; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q38; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q39; X-ray; 1.70 A; A=698-1040.
DR PDB; 5Q3A; X-ray; 1.48 A; A=698-1040.
DR PDB; 5Q3B; X-ray; 2.52 A; A=698-1040.
DR PDB; 5Q3C; X-ray; 1.41 A; A=698-1040.
DR PDB; 5Q3D; X-ray; 1.71 A; A=698-1040.
DR PDB; 5Q3E; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q3F; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q3G; X-ray; 1.29 A; A=698-1040.
DR PDB; 5Q3H; X-ray; 1.56 A; A=698-1040.
DR PDB; 5Q3I; X-ray; 1.53 A; A=698-1040.
DR PDB; 5Q3J; X-ray; 1.44 A; A=698-1040.
DR PDB; 5Q3K; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q3L; X-ray; 1.61 A; A=698-1040.
DR PDB; 5Q3M; X-ray; 1.34 A; A=698-1040.
DR PDB; 5Q3N; X-ray; 1.62 A; A=698-1040.
DR PDB; 5Q3O; X-ray; 1.60 A; A=698-1040.
DR PDB; 5Q3P; X-ray; 1.44 A; A=698-1040.
DR PDB; 5Q3Q; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q3R; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q3S; X-ray; 1.72 A; A=698-1040.
DR PDB; 5Q3T; X-ray; 1.52 A; A=698-1040.
DR PDB; 5Q3U; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q3V; X-ray; 1.52 A; A=698-1040.
DR PDB; 5Q3W; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q3X; X-ray; 1.38 A; A=698-1040.
DR PDB; 5Q3Y; X-ray; 1.45 A; A=698-1040.
DR PDB; 5Q3Z; X-ray; 1.84 A; A=698-1040.
DR PDB; 5Q40; X-ray; 2.04 A; A=698-1040.
DR PDB; 5Q41; X-ray; 1.95 A; A=698-1040.
DR PDB; 5Q42; X-ray; 1.68 A; A=698-1040.
DR PDB; 5Q43; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q44; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q45; X-ray; 1.64 A; A=698-1040.
DR PDB; 5Q46; X-ray; 2.01 A; A=698-1040.
DR PDB; 5Q47; X-ray; 1.38 A; A=698-1040.
DR PDB; 5Q48; X-ray; 1.44 A; A=698-1040.
DR PDB; 5Q49; X-ray; 1.38 A; A=698-1040.
DR PDB; 5Q4A; X-ray; 1.83 A; A=698-1040.
DR PDB; 5Q4B; X-ray; 1.60 A; A=698-1040.
DR PDB; 5Q4C; X-ray; 2.73 A; A=698-1040.
DR PDB; 5Q4D; X-ray; 1.80 A; A=698-1040.
DR PDB; 5Q4E; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q4F; X-ray; 1.97 A; A=698-1040.
DR PDB; 5Q4G; X-ray; 1.75 A; A=698-1040.
DR PDB; 5Q4H; X-ray; 1.53 A; A=698-1040.
DR PDB; 5Q4I; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q4J; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q4K; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q4L; X-ray; 1.60 A; A=698-1040.
DR PDB; 5Q4M; X-ray; 1.60 A; A=698-1040.
DR PDB; 5Q4N; X-ray; 1.71 A; A=698-1040.
DR PDB; 5Q4O; X-ray; 1.83 A; A=698-1040.
DR PDB; 5Q4P; X-ray; 1.40 A; A=698-1040.
DR PDB; 5Q4Q; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q4R; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q4S; X-ray; 1.72 A; A=698-1040.
DR PDB; 5Q4T; X-ray; 1.77 A; A=698-1040.
DR PDB; 5Q4U; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q4V; X-ray; 1.59 A; A=698-1040.
DR PDB; 5Q4W; X-ray; 1.80 A; A=698-1040.
DR PDB; 5Q4X; X-ray; 1.66 A; A=698-1040.
DR PDB; 5Q4Y; X-ray; 1.69 A; A=698-1040.
DR PDB; 5Q4Z; X-ray; 1.60 A; A=698-1040.
DR PDB; 5Q50; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q51; X-ray; 1.34 A; A=698-1040.
DR PDB; 5Q52; X-ray; 1.70 A; A=698-1040.
DR PDB; 5Q53; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q54; X-ray; 1.30 A; A=698-1040.
DR PDB; 5Q55; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q56; X-ray; 1.87 A; A=698-1040.
DR PDB; 5Q57; X-ray; 1.65 A; A=698-1040.
DR PDB; 5Q58; X-ray; 1.75 A; A=698-1040.
DR PDB; 5Q59; X-ray; 1.86 A; A=698-1040.
DR PDB; 5Q5A; X-ray; 2.26 A; A=698-1040.
DR PDB; 5Q5B; X-ray; 1.58 A; A=698-1040.
DR PDB; 5Q5C; X-ray; 1.38 A; A=698-1040.
DR PDB; 5Q5D; X-ray; 1.71 A; A=698-1040.
DR PDB; 5Q5E; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q5F; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q5G; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q5H; X-ray; 1.36 A; A=698-1040.
DR PDB; 5Q5I; X-ray; 1.65 A; A=698-1040.
DR PDB; 5Q5J; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q5K; X-ray; 2.81 A; A=698-1040.
DR PDB; 5Q5L; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q5M; X-ray; 1.57 A; A=698-1040.
DR PDB; 5Q5N; X-ray; 2.42 A; A=698-1040.
DR PDB; 5Q5O; X-ray; 2.07 A; A=698-1040.
DR PDB; 5Q5P; X-ray; 1.58 A; A=698-1040.
DR PDB; 5Q5Q; X-ray; 1.45 A; A=698-1040.
DR PDB; 5Q5R; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q5S; X-ray; 1.70 A; A=698-1040.
DR PDB; 5Q5T; X-ray; 1.80 A; A=698-1040.
DR PDB; 5Q5U; X-ray; 1.88 A; A=698-1040.
DR PDB; 5Q5V; X-ray; 1.86 A; A=698-1040.
DR PDB; 5Q5W; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q5X; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q5Y; X-ray; 1.82 A; A=698-1040.
DR PDB; 5Q5Z; X-ray; 1.48 A; A=698-1040.
DR PDB; 5Q60; X-ray; 1.40 A; A=698-1040.
DR PDB; 5Q61; X-ray; 1.71 A; A=698-1040.
DR PDB; 5Q62; X-ray; 1.52 A; A=698-1040.
DR PDB; 5Q63; X-ray; 1.82 A; A=698-1040.
DR PDB; 5Q64; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q65; X-ray; 1.78 A; A=698-1040.
DR PDB; 5Q66; X-ray; 1.51 A; A=698-1040.
DR PDB; 5Q67; X-ray; 1.65 A; A=698-1040.
DR PDB; 5Q68; X-ray; 1.86 A; A=698-1040.
DR PDB; 5Q69; X-ray; 1.84 A; A=698-1040.
DR PDB; 5Q6A; X-ray; 1.71 A; A=698-1040.
DR PDB; 5Q6B; X-ray; 2.62 A; A=698-1040.
DR PDB; 5Q6C; X-ray; 1.53 A; A=698-1040.
DR PDB; 5Q6D; X-ray; 1.48 A; A=698-1040.
DR PDB; 5Q6E; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q6F; X-ray; 1.55 A; A=698-1040.
DR PDB; 5Q6G; X-ray; 1.48 A; A=698-1040.
DR PDB; 5Q6H; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q6I; X-ray; 1.68 A; A=698-1040.
DR PDB; 5Q6J; X-ray; 1.70 A; A=698-1040.
DR PDB; 5Q6K; X-ray; 1.67 A; A=698-1040.
DR PDB; 5Q6L; X-ray; 1.82 A; A=698-1040.
DR PDB; 5Q6M; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q6N; X-ray; 1.52 A; A=698-1040.
DR PDB; 5Q6O; X-ray; 1.40 A; A=698-1040.
DR PDB; 5Q6P; X-ray; 1.54 A; A=698-1040.
DR PDB; 5Q6Q; X-ray; 1.36 A; A=698-1040.
DR PDB; 5Q6R; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q6S; X-ray; 1.56 A; A=698-1040.
DR PDB; 5Q6T; X-ray; 1.59 A; A=698-1040.
DR PDB; 5Q6U; X-ray; 1.33 A; A=698-1040.
DR PDB; 5Q6V; X-ray; 1.29 A; A=698-1040.
DR PDB; 5Q6W; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q6X; X-ray; 1.43 A; A=698-1040.
DR PDB; 5Q6Y; X-ray; 1.67 A; A=698-1040.
DR PDB; 5Q6Z; X-ray; 1.62 A; A=698-1040.
DR PDB; 5Q70; X-ray; 1.31 A; A=698-1040.
DR PDB; 5Q71; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q72; X-ray; 1.31 A; A=698-1040.
DR PDB; 5Q73; X-ray; 1.36 A; A=698-1040.
DR PDB; 5Q74; X-ray; 1.21 A; A=698-1040.
DR PDB; 5Q75; X-ray; 1.36 A; A=698-1040.
DR PDB; 5Q76; X-ray; 1.28 A; A=698-1040.
DR PDB; 5Q77; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q78; X-ray; 1.25 A; A=698-1040.
DR PDB; 5Q79; X-ray; 1.83 A; A=698-1040.
DR PDB; 5Q7A; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q7B; X-ray; 1.25 A; A=698-1040.
DR PDB; 5Q7C; X-ray; 1.20 A; A=698-1040.
DR PDB; 5Q7D; X-ray; 1.32 A; A=698-1040.
DR PDB; 5Q7E; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q7F; X-ray; 1.64 A; A=698-1040.
DR PDB; 5Q7G; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q7H; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q7I; X-ray; 1.26 A; A=698-1040.
DR PDB; 5Q7J; X-ray; 1.54 A; A=698-1040.
DR PDB; 5Q7K; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q7L; X-ray; 1.61 A; A=698-1040.
DR PDB; 5Q7M; X-ray; 1.26 A; A=698-1040.
DR PDB; 5Q7N; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q7O; X-ray; 1.32 A; A=698-1040.
DR PDB; 5Q7P; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q7Q; X-ray; 1.76 A; A=698-1040.
DR PDB; 5Q7R; X-ray; 1.62 A; A=698-1040.
DR PDB; 5Q7S; X-ray; 1.31 A; A=698-1040.
DR PDB; 5Q7T; X-ray; 1.67 A; A=698-1040.
DR PDB; 5Q7U; X-ray; 2.11 A; A=698-1040.
DR PDB; 5Q7V; X-ray; 1.62 A; A=698-1040.
DR PDB; 5Q7W; X-ray; 1.27 A; A=698-1040.
DR PDB; 5Q7X; X-ray; 1.69 A; A=698-1040.
DR PDB; 5Q7Y; X-ray; 1.39 A; A=698-1040.
DR PDB; 5Q7Z; X-ray; 1.65 A; A=698-1040.
DR PDB; 5Q80; X-ray; 1.43 A; A=698-1040.
DR PDB; 5Q81; X-ray; 1.51 A; A=698-1040.
DR PDB; 5Q82; X-ray; 1.20 A; A=698-1040.
DR PDB; 5Q83; X-ray; 1.28 A; A=698-1040.
DR PDB; 5Q84; X-ray; 1.88 A; A=698-1040.
DR PDB; 5Q85; X-ray; 1.80 A; A=698-1040.
DR PDB; 5Q86; X-ray; 1.31 A; A=698-1040.
DR PDB; 5Q87; X-ray; 1.34 A; A=698-1040.
DR PDB; 5Q88; X-ray; 1.78 A; A=698-1040.
DR PDB; 5Q89; X-ray; 1.91 A; A=698-1040.
DR PDB; 5Q8A; X-ray; 1.43 A; A=698-1040.
DR PDB; 5Q8B; X-ray; 1.63 A; A=698-1040.
DR PDB; 5Q8C; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q8D; X-ray; 1.23 A; A=698-1040.
DR PDB; 5Q8E; X-ray; 1.63 A; A=698-1040.
DR PDB; 5Q8F; X-ray; 1.36 A; A=698-1040.
DR PDB; 5Q8G; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q8H; X-ray; 1.90 A; A=698-1040.
DR PDB; 5Q8I; X-ray; 1.35 A; A=698-1040.
DR PDB; 5Q8J; X-ray; 1.79 A; A=698-1040.
DR PDB; 5Q8K; X-ray; 1.79 A; A=698-1040.
DR PDB; 5Q8L; X-ray; 1.42 A; A=698-1040.
DR PDB; 5Q8M; X-ray; 1.71 A; A=698-1040.
DR PDB; 5Q8N; X-ray; 1.41 A; A=698-1040.
DR PDB; 5Q8O; X-ray; 1.67 A; A=698-1040.
DR PDB; 5Q8P; X-ray; 1.45 A; A=698-1040.
DR PDB; 5Q8Q; X-ray; 1.89 A; A=698-1040.
DR PDB; 5Q8R; X-ray; 1.90 A; A=698-1040.
DR PDB; 5Q8S; X-ray; 1.61 A; A=698-1040.
DR PDB; 5Q8T; X-ray; 2.00 A; A=698-1040.
DR PDB; 5Q8U; X-ray; 1.54 A; A=698-1040.
DR PDB; 5Q8V; X-ray; 1.32 A; A=698-1040.
DR PDB; 5Q8W; X-ray; 1.57 A; A=698-1040.
DR PDB; 5Q8X; X-ray; 1.23 A; A=698-1040.
DR PDB; 5Q8Y; X-ray; 1.51 A; A=698-1040.
DR PDB; 5Q8Z; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q90; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q91; X-ray; 1.46 A; A=698-1040.
DR PDB; 5Q92; X-ray; 2.11 A; A=698-1040.
DR PDB; 5Q93; X-ray; 1.68 A; A=698-1040.
DR PDB; 5Q94; X-ray; 1.90 A; A=698-1040.
DR PDB; 5Q95; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q96; X-ray; 1.83 A; A=698-1040.
DR PDB; 5Q97; X-ray; 1.97 A; A=698-1040.
DR PDB; 5Q98; X-ray; 1.76 A; A=698-1040.
DR PDB; 5Q99; X-ray; 1.31 A; A=698-1040.
DR PDB; 5Q9A; X-ray; 1.67 A; A=698-1040.
DR PDB; 5Q9B; X-ray; 1.45 A; A=698-1040.
DR PDB; 5Q9C; X-ray; 1.46 A; A=698-1040.
DR PDB; 5Q9D; X-ray; 1.69 A; A=698-1040.
DR PDB; 5Q9E; X-ray; 1.45 A; A=698-1040.
DR PDB; 5Q9F; X-ray; 1.28 A; A=698-1040.
DR PDB; 5Q9G; X-ray; 1.60 A; A=698-1040.
DR PDB; 5Q9H; X-ray; 1.81 A; A=698-1040.
DR PDB; 5Q9I; X-ray; 1.46 A; A=698-1040.
DR PDB; 5Q9J; X-ray; 1.76 A; A=698-1040.
DR PDB; 5Q9K; X-ray; 1.78 A; A=698-1040.
DR PDB; 5Q9L; X-ray; 1.59 A; A=698-1040.
DR PDB; 5Q9M; X-ray; 1.30 A; A=698-1040.
DR PDB; 5Q9N; X-ray; 1.47 A; A=698-1040.
DR PDB; 5Q9O; X-ray; 1.37 A; A=698-1040.
DR PDB; 5Q9P; X-ray; 1.48 A; A=698-1040.
DR PDB; 5Q9Q; X-ray; 1.50 A; A=698-1040.
DR PDB; 5Q9R; X-ray; 1.72 A; A=698-1040.
DR PDB; 5Q9S; X-ray; 1.43 A; A=698-1040.
DR PDB; 5Q9T; X-ray; 1.37 A; A=698-1040.
DR PDB; 5Q9U; X-ray; 1.49 A; A=698-1040.
DR PDB; 5Q9V; X-ray; 1.43 A; A=698-1040.
DR PDB; 5Q9W; X-ray; 1.53 A; A=698-1040.
DR PDB; 5Q9X; X-ray; 1.67 A; A=698-1040.
DR PDB; 5Q9Y; X-ray; 1.64 A; A=698-1040.
DR PDB; 5Q9Z; X-ray; 1.77 A; A=698-1040.
DR PDB; 5QA0; X-ray; 1.47 A; A=698-1040.
DR PDB; 5QA1; X-ray; 1.46 A; A=698-1040.
DR PDB; 5QA2; X-ray; 1.56 A; A=698-1040.
DR PDBsum; 4B87; -.
DR PDBsum; 5AHR; -.
DR PDBsum; 5NZW; -.
DR PDBsum; 5NZX; -.
DR PDBsum; 5NZY; -.
DR PDBsum; 5Q1J; -.
DR PDBsum; 5Q1K; -.
DR PDBsum; 5Q1L; -.
DR PDBsum; 5Q1M; -.
DR PDBsum; 5Q1N; -.
DR PDBsum; 5Q1O; -.
DR PDBsum; 5Q1P; -.
DR PDBsum; 5Q1Q; -.
DR PDBsum; 5Q1R; -.
DR PDBsum; 5Q1S; -.
DR PDBsum; 5Q1T; -.
DR PDBsum; 5Q1U; -.
DR PDBsum; 5Q1V; -.
DR PDBsum; 5Q1W; -.
DR PDBsum; 5Q1X; -.
DR PDBsum; 5Q1Y; -.
DR PDBsum; 5Q1Z; -.
DR PDBsum; 5Q20; -.
DR PDBsum; 5Q22; -.
DR PDBsum; 5Q23; -.
DR PDBsum; 5Q24; -.
DR PDBsum; 5Q25; -.
DR PDBsum; 5Q26; -.
DR PDBsum; 5Q27; -.
DR PDBsum; 5Q28; -.
DR PDBsum; 5Q29; -.
DR PDBsum; 5Q2A; -.
DR PDBsum; 5Q2B; -.
DR PDBsum; 5Q2C; -.
DR PDBsum; 5Q2D; -.
DR PDBsum; 5Q2E; -.
DR PDBsum; 5Q2F; -.
DR PDBsum; 5Q2G; -.
DR PDBsum; 5Q2H; -.
DR PDBsum; 5Q2I; -.
DR PDBsum; 5Q2J; -.
DR PDBsum; 5Q2K; -.
DR PDBsum; 5Q2L; -.
DR PDBsum; 5Q2M; -.
DR PDBsum; 5Q2N; -.
DR PDBsum; 5Q2O; -.
DR PDBsum; 5Q2P; -.
DR PDBsum; 5Q2Q; -.
DR PDBsum; 5Q2R; -.
DR PDBsum; 5Q2S; -.
DR PDBsum; 5Q2T; -.
DR PDBsum; 5Q2U; -.
DR PDBsum; 5Q2V; -.
DR PDBsum; 5Q2W; -.
DR PDBsum; 5Q2X; -.
DR PDBsum; 5Q2Y; -.
DR PDBsum; 5Q2Z; -.
DR PDBsum; 5Q30; -.
DR PDBsum; 5Q31; -.
DR PDBsum; 5Q32; -.
DR PDBsum; 5Q33; -.
DR PDBsum; 5Q34; -.
DR PDBsum; 5Q35; -.
DR PDBsum; 5Q36; -.
DR PDBsum; 5Q37; -.
DR PDBsum; 5Q38; -.
DR PDBsum; 5Q39; -.
DR PDBsum; 5Q3A; -.
DR PDBsum; 5Q3B; -.
DR PDBsum; 5Q3C; -.
DR PDBsum; 5Q3D; -.
DR PDBsum; 5Q3E; -.
DR PDBsum; 5Q3F; -.
DR PDBsum; 5Q3G; -.
DR PDBsum; 5Q3H; -.
DR PDBsum; 5Q3I; -.
DR PDBsum; 5Q3J; -.
DR PDBsum; 5Q3K; -.
DR PDBsum; 5Q3L; -.
DR PDBsum; 5Q3M; -.
DR PDBsum; 5Q3N; -.
DR PDBsum; 5Q3O; -.
DR PDBsum; 5Q3P; -.
DR PDBsum; 5Q3Q; -.
DR PDBsum; 5Q3R; -.
DR PDBsum; 5Q3S; -.
DR PDBsum; 5Q3T; -.
DR PDBsum; 5Q3U; -.
DR PDBsum; 5Q3V; -.
DR PDBsum; 5Q3W; -.
DR PDBsum; 5Q3X; -.
DR PDBsum; 5Q3Y; -.
DR PDBsum; 5Q3Z; -.
DR PDBsum; 5Q40; -.
DR PDBsum; 5Q41; -.
DR PDBsum; 5Q42; -.
DR PDBsum; 5Q43; -.
DR PDBsum; 5Q44; -.
DR PDBsum; 5Q45; -.
DR PDBsum; 5Q46; -.
DR PDBsum; 5Q47; -.
DR PDBsum; 5Q48; -.
DR PDBsum; 5Q49; -.
DR PDBsum; 5Q4A; -.
DR PDBsum; 5Q4B; -.
DR PDBsum; 5Q4C; -.
DR PDBsum; 5Q4D; -.
DR PDBsum; 5Q4E; -.
DR PDBsum; 5Q4F; -.
DR PDBsum; 5Q4G; -.
DR PDBsum; 5Q4H; -.
DR PDBsum; 5Q4I; -.
DR PDBsum; 5Q4J; -.
DR PDBsum; 5Q4K; -.
DR PDBsum; 5Q4L; -.
DR PDBsum; 5Q4M; -.
DR PDBsum; 5Q4N; -.
DR PDBsum; 5Q4O; -.
DR PDBsum; 5Q4P; -.
DR PDBsum; 5Q4Q; -.
DR PDBsum; 5Q4R; -.
DR PDBsum; 5Q4S; -.
DR PDBsum; 5Q4T; -.
DR PDBsum; 5Q4U; -.
DR PDBsum; 5Q4V; -.
DR PDBsum; 5Q4W; -.
DR PDBsum; 5Q4X; -.
DR PDBsum; 5Q4Y; -.
DR PDBsum; 5Q4Z; -.
DR PDBsum; 5Q50; -.
DR PDBsum; 5Q51; -.
DR PDBsum; 5Q52; -.
DR PDBsum; 5Q53; -.
DR PDBsum; 5Q54; -.
DR PDBsum; 5Q55; -.
DR PDBsum; 5Q56; -.
DR PDBsum; 5Q57; -.
DR PDBsum; 5Q58; -.
DR PDBsum; 5Q59; -.
DR PDBsum; 5Q5A; -.
DR PDBsum; 5Q5B; -.
DR PDBsum; 5Q5C; -.
DR PDBsum; 5Q5D; -.
DR PDBsum; 5Q5E; -.
DR PDBsum; 5Q5F; -.
DR PDBsum; 5Q5G; -.
DR PDBsum; 5Q5H; -.
DR PDBsum; 5Q5I; -.
DR PDBsum; 5Q5J; -.
DR PDBsum; 5Q5K; -.
DR PDBsum; 5Q5L; -.
DR PDBsum; 5Q5M; -.
DR PDBsum; 5Q5N; -.
DR PDBsum; 5Q5O; -.
DR PDBsum; 5Q5P; -.
DR PDBsum; 5Q5Q; -.
DR PDBsum; 5Q5R; -.
DR PDBsum; 5Q5S; -.
DR PDBsum; 5Q5T; -.
DR PDBsum; 5Q5U; -.
DR PDBsum; 5Q5V; -.
DR PDBsum; 5Q5W; -.
DR PDBsum; 5Q5X; -.
DR PDBsum; 5Q5Y; -.
DR PDBsum; 5Q5Z; -.
DR PDBsum; 5Q60; -.
DR PDBsum; 5Q61; -.
DR PDBsum; 5Q62; -.
DR PDBsum; 5Q63; -.
DR PDBsum; 5Q64; -.
DR PDBsum; 5Q65; -.
DR PDBsum; 5Q66; -.
DR PDBsum; 5Q67; -.
DR PDBsum; 5Q68; -.
DR PDBsum; 5Q69; -.
DR PDBsum; 5Q6A; -.
DR PDBsum; 5Q6B; -.
DR PDBsum; 5Q6C; -.
DR PDBsum; 5Q6D; -.
DR PDBsum; 5Q6E; -.
DR PDBsum; 5Q6F; -.
DR PDBsum; 5Q6G; -.
DR PDBsum; 5Q6H; -.
DR PDBsum; 5Q6I; -.
DR PDBsum; 5Q6J; -.
DR PDBsum; 5Q6K; -.
DR PDBsum; 5Q6L; -.
DR PDBsum; 5Q6M; -.
DR PDBsum; 5Q6N; -.
DR PDBsum; 5Q6O; -.
DR PDBsum; 5Q6P; -.
DR PDBsum; 5Q6Q; -.
DR PDBsum; 5Q6R; -.
DR PDBsum; 5Q6S; -.
DR PDBsum; 5Q6T; -.
DR PDBsum; 5Q6U; -.
DR PDBsum; 5Q6V; -.
DR PDBsum; 5Q6W; -.
DR PDBsum; 5Q6X; -.
DR PDBsum; 5Q6Y; -.
DR PDBsum; 5Q6Z; -.
DR PDBsum; 5Q70; -.
DR PDBsum; 5Q71; -.
DR PDBsum; 5Q72; -.
DR PDBsum; 5Q73; -.
DR PDBsum; 5Q74; -.
DR PDBsum; 5Q75; -.
DR PDBsum; 5Q76; -.
DR PDBsum; 5Q77; -.
DR PDBsum; 5Q78; -.
DR PDBsum; 5Q79; -.
DR PDBsum; 5Q7A; -.
DR PDBsum; 5Q7B; -.
DR PDBsum; 5Q7C; -.
DR PDBsum; 5Q7D; -.
DR PDBsum; 5Q7E; -.
DR PDBsum; 5Q7F; -.
DR PDBsum; 5Q7G; -.
DR PDBsum; 5Q7H; -.
DR PDBsum; 5Q7I; -.
DR PDBsum; 5Q7J; -.
DR PDBsum; 5Q7K; -.
DR PDBsum; 5Q7L; -.
DR PDBsum; 5Q7M; -.
DR PDBsum; 5Q7N; -.
DR PDBsum; 5Q7O; -.
DR PDBsum; 5Q7P; -.
DR PDBsum; 5Q7Q; -.
DR PDBsum; 5Q7R; -.
DR PDBsum; 5Q7S; -.
DR PDBsum; 5Q7T; -.
DR PDBsum; 5Q7U; -.
DR PDBsum; 5Q7V; -.
DR PDBsum; 5Q7W; -.
DR PDBsum; 5Q7X; -.
DR PDBsum; 5Q7Y; -.
DR PDBsum; 5Q7Z; -.
DR PDBsum; 5Q80; -.
DR PDBsum; 5Q81; -.
DR PDBsum; 5Q82; -.
DR PDBsum; 5Q83; -.
DR PDBsum; 5Q84; -.
DR PDBsum; 5Q85; -.
DR PDBsum; 5Q86; -.
DR PDBsum; 5Q87; -.
DR PDBsum; 5Q88; -.
DR PDBsum; 5Q89; -.
DR PDBsum; 5Q8A; -.
DR PDBsum; 5Q8B; -.
DR PDBsum; 5Q8C; -.
DR PDBsum; 5Q8D; -.
DR PDBsum; 5Q8E; -.
DR PDBsum; 5Q8F; -.
DR PDBsum; 5Q8G; -.
DR PDBsum; 5Q8H; -.
DR PDBsum; 5Q8I; -.
DR PDBsum; 5Q8J; -.
DR PDBsum; 5Q8K; -.
DR PDBsum; 5Q8L; -.
DR PDBsum; 5Q8M; -.
DR PDBsum; 5Q8N; -.
DR PDBsum; 5Q8O; -.
DR PDBsum; 5Q8P; -.
DR PDBsum; 5Q8Q; -.
DR PDBsum; 5Q8R; -.
DR PDBsum; 5Q8S; -.
DR PDBsum; 5Q8T; -.
DR PDBsum; 5Q8U; -.
DR PDBsum; 5Q8V; -.
DR PDBsum; 5Q8W; -.
DR PDBsum; 5Q8X; -.
DR PDBsum; 5Q8Y; -.
DR PDBsum; 5Q8Z; -.
DR PDBsum; 5Q90; -.
DR PDBsum; 5Q91; -.
DR PDBsum; 5Q92; -.
DR PDBsum; 5Q93; -.
DR PDBsum; 5Q94; -.
DR PDBsum; 5Q95; -.
DR PDBsum; 5Q96; -.
DR PDBsum; 5Q97; -.
DR PDBsum; 5Q98; -.
DR PDBsum; 5Q99; -.
DR PDBsum; 5Q9A; -.
DR PDBsum; 5Q9B; -.
DR PDBsum; 5Q9C; -.
DR PDBsum; 5Q9D; -.
DR PDBsum; 5Q9E; -.
DR PDBsum; 5Q9F; -.
DR PDBsum; 5Q9G; -.
DR PDBsum; 5Q9H; -.
DR PDBsum; 5Q9I; -.
DR PDBsum; 5Q9J; -.
DR PDBsum; 5Q9K; -.
DR PDBsum; 5Q9L; -.
DR PDBsum; 5Q9M; -.
DR PDBsum; 5Q9N; -.
DR PDBsum; 5Q9O; -.
DR PDBsum; 5Q9P; -.
DR PDBsum; 5Q9Q; -.
DR PDBsum; 5Q9R; -.
DR PDBsum; 5Q9S; -.
DR PDBsum; 5Q9T; -.
DR PDBsum; 5Q9U; -.
DR PDBsum; 5Q9V; -.
DR PDBsum; 5Q9W; -.
DR PDBsum; 5Q9X; -.
DR PDBsum; 5Q9Y; -.
DR PDBsum; 5Q9Z; -.
DR PDBsum; 5QA0; -.
DR PDBsum; 5QA1; -.
DR PDBsum; 5QA2; -.
DR AlphaFoldDB; Q6PJP8; -.
DR SMR; Q6PJP8; -.
DR BioGRID; 115263; 21.
DR IntAct; Q6PJP8; 5.
DR MINT; Q6PJP8; -.
DR STRING; 9606.ENSP00000355185; -.
DR BindingDB; Q6PJP8; -.
DR ChEMBL; CHEMBL4105903; -.
DR iPTMnet; Q6PJP8; -.
DR PhosphoSitePlus; Q6PJP8; -.
DR BioMuta; DCLRE1A; -.
DR DMDM; 311033461; -.
DR EPD; Q6PJP8; -.
DR jPOST; Q6PJP8; -.
DR MassIVE; Q6PJP8; -.
DR MaxQB; Q6PJP8; -.
DR PaxDb; Q6PJP8; -.
DR PeptideAtlas; Q6PJP8; -.
DR PRIDE; Q6PJP8; -.
DR ProteomicsDB; 67214; -.
DR Antibodypedia; 31894; 115 antibodies from 22 providers.
DR DNASU; 9937; -.
DR Ensembl; ENST00000361384.7; ENSP00000355185.2; ENSG00000198924.8.
DR Ensembl; ENST00000369305.1; ENSP00000358311.1; ENSG00000198924.8.
DR GeneID; 9937; -.
DR KEGG; hsa:9937; -.
DR MANE-Select; ENST00000361384.7; ENSP00000355185.2; NM_014881.5; NP_055696.3.
DR UCSC; uc001law.4; human.
DR CTD; 9937; -.
DR DisGeNET; 9937; -.
DR GeneCards; DCLRE1A; -.
DR HGNC; HGNC:17660; DCLRE1A.
DR HPA; ENSG00000198924; Low tissue specificity.
DR MIM; 609682; gene.
DR neXtProt; NX_Q6PJP8; -.
DR OpenTargets; ENSG00000198924; -.
DR PharmGKB; PA27174; -.
DR VEuPathDB; HostDB:ENSG00000198924; -.
DR eggNOG; KOG1361; Eukaryota.
DR GeneTree; ENSGT00940000158766; -.
DR HOGENOM; CLU_014243_0_0_1; -.
DR InParanoid; Q6PJP8; -.
DR OMA; SMERYPA; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q6PJP8; -.
DR TreeFam; TF314510; -.
DR PathwayCommons; Q6PJP8; -.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; Q6PJP8; -.
DR BioGRID-ORCS; 9937; 20 hits in 1083 CRISPR screens.
DR ChiTaRS; DCLRE1A; human.
DR GeneWiki; DCLRE1A; -.
DR GenomeRNAi; 9937; -.
DR Pharos; Q6PJP8; Tbio.
DR PRO; PR:Q6PJP8; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6PJP8; protein.
DR Bgee; ENSG00000198924; Expressed in secondary oocyte and 136 other tissues.
DR Genevisible; Q6PJP8; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IDA:CACAO.
DR GO; GO:0008800; F:beta-lactamase activity; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; DNA damage; DNA repair; Hydrolase;
KW Isopeptide bond; Metal-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1040
FT /note="DNA cross-link repair 1A protein"
FT /id="PRO_0000209116"
FT ZN_FING 119..149
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 1..190
FT /note="Nuclear localization region"
FT REGION 15..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..614
FT /note="Nuclear focus formation"
FT REGION 582..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIC3"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 508
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 533
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 668
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 674
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 58
FT /note="K -> E (in dbSNP:rs17235066)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023286"
FT VARIANT 59
FT /note="E -> D (in dbSNP:rs17228665)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023287"
FT VARIANT 71
FT /note="G -> D (in dbSNP:rs17228672)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023288"
FT VARIANT 287
FT /note="P -> L (in dbSNP:rs17235094)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023289"
FT VARIANT 317
FT /note="D -> H (in dbSNP:rs3750898)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_023290"
FT VARIANT 582
FT /note="G -> W (in dbSNP:rs17855759)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030574"
FT VARIANT 859
FT /note="I -> F (in dbSNP:rs11196530)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023291"
FT MUTAGEN 838
FT /note="D->N: Impaired nuclear focus formation, reduced
FT interaction with PIAS and increased sensitivity to
FT cisplatin."
FT /evidence="ECO:0000269|PubMed:15572677"
FT MUTAGEN 994
FT /note="H->A: Impaired nuclear focus formation, reduced
FT interaction with PIAS and increased sensitivity to
FT cisplatin."
FT /evidence="ECO:0000269|PubMed:15572677"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:5Q22"
FT TURN 708..711
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 726..729
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 735..738
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 753..761
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 767..769
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 775..777
FT /evidence="ECO:0007829|PDB:5Q7S"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 784..790
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 798..803
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 809..812
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 820..824
FT /evidence="ECO:0007829|PDB:5Q22"
FT TURN 826..829
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 833..837
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 851..868
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 872..881
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 885..893
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 902..909
FT /evidence="ECO:0007829|PDB:5Q22"
FT TURN 910..912
FT /evidence="ECO:0007829|PDB:5Q9Z"
FT HELIX 916..918
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 920..922
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 924..926
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 928..933
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 934..936
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 939..947
FT /evidence="ECO:0007829|PDB:5Q22"
FT TURN 948..951
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 954..963
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 966..969
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 973..975
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 984..990
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 997..1007
FT /evidence="ECO:0007829|PDB:5Q22"
FT STRAND 1010..1014
FT /evidence="ECO:0007829|PDB:5Q22"
FT HELIX 1021..1038
FT /evidence="ECO:0007829|PDB:5Q22"
SQ SEQUENCE 1040 AA; 116400 MW; 708FFA1F75451803 CRC64;
MLEDISEEDI WEYKSKRKPK RVDPNNGSKN ILKSVEKATD GKYQSKRSRN RKRAAEAKEV
KDHEVPLGNA GCQTSVASSQ NSSCGDGIQQ TQDKETTPGK LCRTQKSQHV SPKIRPVYDG
YCPNCQMPFS SLIGQTPRWH VFECLDSPPR SETECPDGLL CTSTIPFHYK RYTHFLLAQS
RAGDHPFSSP SPASGGSFSE TKSGVLCSLE ERWSSYQNQT DNSVSNDPLL MTQYFKKSPS
LTEASEKIST HIQTSQQALQ FTDFVENDKL VGVALRLANN SEHINLPLPE NDFSDCEISY
SPLQSDEDTH DIDEKPDDSQ EQLFFTESSK DGSLEEDDDS CGFFKKRHGP LLKDQDESCP
KVNSFLTRDK YDEGLYRFNS LNDLSQPISQ NNESTLPYDL ACTGGDFVLF PPALAGKLAA
SVHQATKAKP DEPEFHSAQS NKQKQVIEES SVYNQVSLPL VKSLMLKPFE SQVEGYLSSQ
PTQNTIRKLS SENLNAKNNT NSACFCRKAL EGVPVGKATI LNTENLSSTP APKYLKILPS
GLKYNARHPS TKVMKQMDIG VYFGLPPKRK EEKLLGESAL EGINLNPVPS PNQKRSSQCK
RKAEKSLSDL EFDASTLHES QLSVELSSER SQRQKKRCRK SNSLQEGACQ KRSDHLINTE
SEAVNLSKVK VFTKSAHGGL QRGNKKIPES SNVGGSRKKT CPFYKKIPGT GFTVDAFQYG
VVEGCTAYFL THFHSDHYAG LSKHFTFPVY CSEITGNLLK NKLHVQEQYI HPLPLDTECI
VNGVKVVLLD ANHCPGAVMI LFYLPNGTVI LHTGDFRADP SMERSLLADQ KVHMLYLDTT
YCSPEYTFPS QQEVIRFAIN TAFEAVTLNP HALVVCGTYS IGKEKVFLAI ADVLGSKVGM
SQEKYKTLQC LNIPEINSLI TTDMCSSLVH LLPMMQINFK GLQSHLKKCG GKYNQILAFR
PTGWTHSNKF TRIADVIPQT KGNISIYGIP YSEHSSYLEM KRFVQWLKPQ KIIPTVNVGT
WKSRSTMEKY FREWKLEAGY
