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DNA cross-link repair 1A protein (SNM1 homolog A) (hSNM1) (hSNM1A)

 DCR1A_HUMAN             Reviewed;        1040 AA.
Q6PJP8; D3DRC1; Q14701; Q6P5Y3; Q6PKL4;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
28-FEB-2018, entry version 128.
RecName: Full=DNA cross-link repair 1A protein;
AltName: Full=SNM1 homolog A;
Short=hSNM1;
Short=hSNM1A;
Name=DCLRE1A; Synonyms=KIAA0086, SNM1, SNM1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-58; ASP-59;
ASP-71; LEU-287; HIS-317 AND PHE-859.
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-317.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-317 AND
TRP-582.
TISSUE=Cervix, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
SUBCELLULAR LOCATION.
PubMed=10848582; DOI=10.1128/MCB.20.13.4553-4561.2000;
Dronkert M.L.G., de Wit J., Boeve M., Vasconcelos M.L., van Steeg H.,
Tan T.L.R., Hoeijmakers J.H.J., Kanaar R.;
"Disruption of mouse SNM1 causes increased sensitivity to the DNA
interstrand cross-linking agent mitomycin C.";
Mol. Cell. Biol. 20:4553-4561(2000).
[7]
INDUCTION.
PubMed=12509242;
Zhang X., Richie C., Legerski R.J.;
"Translation of hSNM1 is mediated by an internal ribosome entry site
that upregulates expression during mitosis.";
DNA Repair 1:379-390(2002).
[8]
INTERACTION WITH TP53BP1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=12446782; DOI=10.1128/MCB.22.24.8635-8647.2002;
Richie C.T., Peterson C., Lu T., Hittelman W.N., Carpenter P.B.,
Legerski R.J.;
"hSnm1 colocalizes and physically associates with 53BP1 before and
after DNA damage.";
Mol. Cell. Biol. 22:8635-8647(2002).
[9]
FUNCTION, AND INTERACTION WITH CDC27.
PubMed=15542852; DOI=10.1128/MCB.24.23.10448-10455.2004;
Akhter S., Richie C.T., Deng J.M., Brey E., Zhang X., Patrick C. Jr.,
Behringer R.R., Legerski R.J.;
"Deficiency in SNM1 abolishes an early mitotic checkpoint induced by
spindle stress.";
Mol. Cell. Biol. 24:10448-10455(2004).
[10]
SUBCELLULAR LOCATION, INTERACTION WITH PIAS1, AND MUTAGENESIS OF
ASP-838 AND HIS-994.
PubMed=15572677; DOI=10.1128/MCB.24.24.10733-10741.2004;
Ishiai M., Kimura M., Namikoshi K., Yamazoe M., Yamamoto K.,
Arakawa H., Agematsu K., Matsushita N., Takeda S., Buerstedde J.-M.,
Takata M.;
"DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear
focus formation.";
Mol. Cell. Biol. 24:10733-10741(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202; LYS-236; LYS-269;
LYS-353; LYS-361; LYS-429; LYS-488; LYS-508; LYS-517; LYS-533;
LYS-536; LYS-668; LYS-670 AND LYS-674, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: May be required for DNA interstrand cross-link repair.
Also required for checkpoint mediated cell cycle arrest in early
prophase in response to mitotic spindle poisons.
{ECO:0000269|PubMed:15542852}.
-!- SUBUNIT: Binds constitutively to TP53BP1. Binds CDC27, which is
itself a component of the anaphase promoting complex (APC). Binds
PIAS1.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10848582,
ECO:0000269|PubMed:12446782, ECO:0000269|PubMed:15572677}. Note=In
some cells it may be found in typically 1 or 2 discrete nuclear
aggregates of unknown function which also contain TP53BP1. Also
found in multiple discrete nuclear foci which increase in number
following treatment with ionizing radiation or interstrand cross-
linking agents. These foci overlap with those formed by the MRN
complex (composed of MRE11, RAD50 and NBN) and BRCA1.
-!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
pancreas, placenta and skeletal muscle.
{ECO:0000269|PubMed:12446782}.
-!- INDUCTION: During mitosis. The mRNA encoding this protein contains
an internal ribosome entry site (IRES) in its 5'-UTR. This 5'-UTR
generally suppresses translation while specifically promoting
expression during mitosis, when cap-dependent translation may be
impaired. {ECO:0000269|PubMed:12509242}.
-!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase
(DRMBL) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA07646.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/dclre1a/";
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EMBL; D42045; BAA07646.2; ALT_INIT; mRNA.
EMBL; AY607842; AAT09762.1; -; Genomic_DNA.
EMBL; AL592546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49489.1; -; Genomic_DNA.
EMBL; CH471066; EAW49490.1; -; Genomic_DNA.
EMBL; BC013124; AAH13124.1; -; mRNA.
EMBL; BC062582; AAH62582.1; -; mRNA.
CCDS; CCDS7584.1; -.
RefSeq; NP_001258745.1; NM_001271816.1.
RefSeq; NP_055696.3; NM_014881.4.
RefSeq; XP_006718153.1; XM_006718090.1.
RefSeq; XP_011538731.1; XM_011540429.1.
UniGene; Hs.1560; -.
UniGene; Hs.703616; -.
PDB; 4B87; X-ray; 2.16 A; A=676-1040.
PDB; 5AHR; X-ray; 2.19 A; A=700-1040.
PDB; 5NZW; X-ray; 2.70 A; A=698-1040.
PDB; 5NZX; X-ray; 1.47 A; A=698-1040.
PDB; 5NZY; X-ray; 1.55 A; A=698-1040.
PDBsum; 4B87; -.
PDBsum; 5AHR; -.
PDBsum; 5NZW; -.
PDBsum; 5NZX; -.
PDBsum; 5NZY; -.
ProteinModelPortal; Q6PJP8; -.
SMR; Q6PJP8; -.
BioGrid; 115263; 6.
IntAct; Q6PJP8; 1.
STRING; 9606.ENSP00000355185; -.
iPTMnet; Q6PJP8; -.
PhosphoSitePlus; Q6PJP8; -.
DMDM; 311033461; -.
EPD; Q6PJP8; -.
MaxQB; Q6PJP8; -.
PaxDb; Q6PJP8; -.
PeptideAtlas; Q6PJP8; -.
PRIDE; Q6PJP8; -.
Ensembl; ENST00000361384; ENSP00000355185; ENSG00000198924.
Ensembl; ENST00000369305; ENSP00000358311; ENSG00000198924.
GeneID; 9937; -.
KEGG; hsa:9937; -.
UCSC; uc001law.4; human.
CTD; 9937; -.
DisGeNET; 9937; -.
EuPathDB; HostDB:ENSG00000198924.7; -.
GeneCards; DCLRE1A; -.
HGNC; HGNC:17660; DCLRE1A.
HPA; HPA036907; -.
MIM; 609682; gene.
neXtProt; NX_Q6PJP8; -.
OpenTargets; ENSG00000198924; -.
PharmGKB; PA27174; -.
eggNOG; KOG1361; Eukaryota.
eggNOG; COG1236; LUCA.
GeneTree; ENSGT00530000063183; -.
HOGENOM; HOG000168450; -.
HOVERGEN; HBG081418; -.
InParanoid; Q6PJP8; -.
KO; K15340; -.
OMA; PDGLLCT; -.
OrthoDB; EOG091G0DBZ; -.
PhylomeDB; Q6PJP8; -.
TreeFam; TF314510; -.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
ChiTaRS; DCLRE1A; human.
GeneWiki; DCLRE1A; -.
GenomeRNAi; 9937; -.
PRO; PR:Q6PJP8; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000198924; -.
CleanEx; HS_DCLRE1A; -.
Genevisible; Q6PJP8; HS.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IDA:CACAO.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
Gene3D; 3.60.15.10; -; 2.
InterPro; IPR011084; DRMBL.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
Pfam; PF07522; DRMBL; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Complete proteome;
DNA damage; DNA repair; Isopeptide bond; Mitosis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 1040 DNA cross-link repair 1A protein.
/FTId=PRO_0000209116.
REGION 1 190 Nuclear localization region.
REGION 396 614 Nuclear focus formation.
MOD_RES 590 590 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JIC3}.
CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 236 236 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 361 361 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 429 429 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 488 488 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 508 508 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 517 517 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 533 533 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 536 536 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 668 668 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 674 674 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 58 58 K -> E (in dbSNP:rs17235066).
{ECO:0000269|Ref.2}.
/FTId=VAR_023286.
VARIANT 59 59 E -> D (in dbSNP:rs17228665).
{ECO:0000269|Ref.2}.
/FTId=VAR_023287.
VARIANT 71 71 G -> D (in dbSNP:rs17228672).
{ECO:0000269|Ref.2}.
/FTId=VAR_023288.
VARIANT 287 287 P -> L (in dbSNP:rs17235094).
{ECO:0000269|Ref.2}.
/FTId=VAR_023289.
VARIANT 317 317 D -> H (in dbSNP:rs3750898).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_023290.
VARIANT 582 582 G -> W (in dbSNP:rs17855759).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030574.
VARIANT 859 859 I -> F (in dbSNP:rs11196530).
{ECO:0000269|Ref.2}.
/FTId=VAR_023291.
MUTAGEN 838 838 D->N: Impaired nuclear focus formation,
reduced interaction with PIAS and
increased sensitivity to cisplatin.
{ECO:0000269|PubMed:15572677}.
MUTAGEN 994 994 H->A: Impaired nuclear focus formation,
reduced interaction with PIAS and
increased sensitivity to cisplatin.
{ECO:0000269|PubMed:15572677}.
HELIX 703 705 {ECO:0000244|PDB:5NZX}.
TURN 708 711 {ECO:0000244|PDB:5NZX}.
STRAND 712 715 {ECO:0000244|PDB:5NZX}.
STRAND 718 721 {ECO:0000244|PDB:5NZX}.
STRAND 727 729 {ECO:0000244|PDB:5NZX}.
HELIX 735 738 {ECO:0000244|PDB:5NZX}.
STRAND 749 751 {ECO:0000244|PDB:5NZX}.
HELIX 753 762 {ECO:0000244|PDB:5NZX}.
HELIX 767 769 {ECO:0000244|PDB:5NZX}.
STRAND 770 772 {ECO:0000244|PDB:5NZX}.
STRAND 779 781 {ECO:0000244|PDB:5NZX}.
STRAND 784 790 {ECO:0000244|PDB:5NZX}.
STRAND 792 794 {ECO:0000244|PDB:5NZX}.
STRAND 798 803 {ECO:0000244|PDB:5NZX}.
STRAND 809 812 {ECO:0000244|PDB:5NZX}.
HELIX 820 824 {ECO:0000244|PDB:5NZX}.
HELIX 826 829 {ECO:0000244|PDB:5NZX}.
STRAND 834 837 {ECO:0000244|PDB:5NZX}.
HELIX 851 868 {ECO:0000244|PDB:5NZX}.
STRAND 872 881 {ECO:0000244|PDB:5NZX}.
HELIX 884 894 {ECO:0000244|PDB:5NZX}.
HELIX 902 908 {ECO:0000244|PDB:5NZX}.
HELIX 916 918 {ECO:0000244|PDB:5NZX}.
STRAND 920 922 {ECO:0000244|PDB:5NZX}.
HELIX 924 926 {ECO:0000244|PDB:5NZX}.
STRAND 928 933 {ECO:0000244|PDB:5NZX}.
HELIX 934 936 {ECO:0000244|PDB:5NZX}.
HELIX 939 945 {ECO:0000244|PDB:5NZX}.
HELIX 949 951 {ECO:0000244|PDB:5NZX}.
STRAND 955 961 {ECO:0000244|PDB:5NZX}.
STRAND 967 970 {ECO:0000244|PDB:5NZY}.
STRAND 979 981 {ECO:0000244|PDB:5NZX}.
STRAND 984 989 {ECO:0000244|PDB:5NZX}.
HELIX 997 1007 {ECO:0000244|PDB:5NZX}.
STRAND 1010 1014 {ECO:0000244|PDB:5NZX}.
HELIX 1021 1038 {ECO:0000244|PDB:5NZX}.
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


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EIAAB10652 Chicken,chSNM1C,DCLRE1C,DNA cross-link repair 1C protein,Gallus gallus,Protein artemis,SNM1 homolog C,SNM1C,SNM1-like protein
EIAAB10653 ARTEMIS,ASCID,DCLRE1C,DNA cross-link repair 1C protein,Homo sapiens,hSNM1C,Human,Protein artemis,Protein A-SCID,SCIDA,SNM1 homolog C,SNM1C,SNM1-like protein
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EIAAB10647 5' exonuclease Apollo,DCLRE1B,DNA cross-link repair 1B protein,Homo sapiens,hSNM1B,Human,SNM1 homolog B,SNM1B,SNMIB
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CSB-EL006551CH Chicken DNA cross-link repair 1A protein(DCLRE1A) ELISA kit SpeciesChicken 96T
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