P18858 (DNLI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA ligase 1
EC=6.5.1.1

Alternative name(s):
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1

Gene names

Name:

LIG1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	919 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic activity	ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
Cofactor	Magnesium. Ref.16
Subcellular location	Nucleus.
Sequence similarities	Belongs to the ATP-dependent DNA ligase family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA recombination DNA repair DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA ligation involved in DNA repair Inferred from electronic annotation. Source: InterPro S phase of mitotic cell cycle Traceable author statement. Source: Reactome anatomical structure morphogenesis Traceable author statement PubMed 8696349. Source: ProtInc base-excision repair Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair via homologous recombination Traceable author statement. Source: Reactome double-strand break repair via nonhomologous end joining Inferred from electronic annotation. Source: Compara lagging strand elongation Inferred from Biological aspect of Ancestor. Source: RefGenome nucleotide-excision repair, DNA gap filling Traceable author statement. Source: Reactome response to hydrogen peroxide Inferred from electronic annotation. Source: Compara telomere maintenance via recombination Traceable author statement. Source: Reactome telomere maintenance via semi-conservative replication Traceable author statement. Source: Reactome transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome
Cellular_component	chromosome Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrion Inferred from Biological aspect of Ancestor. Source: RefGenome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Traceable author statement PubMed 8696349. Source: ProtInc DNA ligase (ATP) activity Inferred from Biological aspect of Ancestor. Source: RefGenome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 919

919

DNA ligase 1

PRO_0000059570

Regions

Region

449 – 458

10

Interaction with target DNA

Region

642 – 644

3

Interaction with target DNA

Sites

Active site

568

1

N6-AMP-lysine intermediate By similarity

Metal binding

621

1

Magnesium 1 Probable

Metal binding

720

1

Magnesium 2 Probable

Binding site

566

1

ATP

Binding site

573

1

ATP

Binding site

589

1

ATP

Binding site

725

1

ATP

Binding site

738

1

ATP By similarity

Binding site

744

1

ATP

Site

305

1

Interaction with target DNA

Site

590

1

Interaction with target DNA

Site

770

1

Interaction with target DNA

Site

795

1

Interaction with target DNA

Amino acid modifications

Modified residue

47

1

Phosphoserine Ref.13

Modified residue

49

1

Phosphoserine Ref.12 Ref.13

Modified residue

51

1

Phosphoserine Ref.8 Ref.10 Ref.12 Ref.13 Ref.15

Modified residue

66

1

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.15

Modified residue

76

1

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.15

Modified residue

141

1

Phosphoserine Ref.7 Ref.10 Ref.12 Ref.13 Ref.15

Modified residue

195

1

Phosphothreonine Ref.8 Ref.10 Ref.12 Ref.13 Ref.15

Modified residue

201

1

Phosphoserine Ref.10 Ref.12 Ref.13

Modified residue

233

1

Phosphothreonine Ref.8 Ref.10

Modified residue

911

1

Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15

Modified residue

913

1

Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15

Cross-link

422

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Natural variations

Natural variant

24

1

A → V. Ref.2
Corresponds to variant rs3730855 [ dbSNP | Ensembl ].

VAR_018802

Natural variant

52

1

P → L.
Corresponds to variant rs4987181 [ dbSNP | Ensembl ].

VAR_020194

Natural variant

62

1

R → W. Ref.2
Corresponds to variant rs3730863 [ dbSNP | Ensembl ].

VAR_018803

Natural variant

72

1

D → G.
Corresponds to variant rs4987070 [ dbSNP | Ensembl ].

VAR_020195

Natural variant

152

1

K → E in a colorectal cancer sample; somatic mutation. Ref.18

VAR_036511

Natural variant

249

1

G → E. Ref.2
Corresponds to variant rs3730911 [ dbSNP | Ensembl ].

VAR_016766

Natural variant

267

1

N → S. Ref.2
Corresponds to variant rs3730933 [ dbSNP | Ensembl ].

VAR_016767

Natural variant

349

1

V → M. Ref.2
Corresponds to variant rs3730947 [ dbSNP | Ensembl ].

VAR_018804

Natural variant

369

1

V → I. Ref.2
Corresponds to variant rs3730966 [ dbSNP | Ensembl ].

VAR_018805

Natural variant

409

1

R → H.
Corresponds to variant rs4987068 [ dbSNP | Ensembl ].

VAR_016768

Natural variant

480

1

M → V. Ref.2
Corresponds to variant rs3730980 [ dbSNP | Ensembl ].

VAR_016769

Natural variant

566

1

E → K Found in a patient with a syndrome of immunodeficiency and increased cellular sensitivity to DNA-damaging agents due to LIG1 deficiency; compound heterozygote carrying W-771. Ref.17

VAR_002262

Natural variant

612

1

S → L in a colorectal cancer sample; somatic mutation. Ref.18

VAR_036512

Natural variant

614

1

T → I. Ref.2
Corresponds to variant rs3731003 [ dbSNP | Ensembl ].

VAR_016770

Natural variant

677

1

R → L. Ref.2
Corresponds to variant rs3731008 [ dbSNP | Ensembl ].

VAR_018806

Natural variant

771

1

R → W Found in a patient with a syndrome of immunodeficiency and increased cellular sensitivity to DNA-damaging agents due to LIG1 deficiency; compound heterozygote carrying K-566. Ref.17

VAR_002263

Secondary structure

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919

Helix Strand Turn

Details...

Helix

263 – 265

3

Helix

275 – 278

4

Helix

289 – 300

12

Helix

305 – 322

18

Helix

324 – 326

3

Helix

327 – 335

9

Helix

341 – 343

3

Helix

351 – 362

12

Helix

366 – 376

11

Helix

379 – 382

4

Helix

401 – 413

13

Helix

419 – 433

15

Helix

438 – 446

9

Helix

456 – 469

14

Turn

483 – 486

4

Helix

489 – 509

21

Helix

513 – 527

15

Helix

529 – 531

3

Beta strand

544 – 550

7

Helix

551 – 557

7

Turn

558 – 560

3

Beta strand

563 – 578

16

Beta strand

584 – 587

4

Turn

595 – 597

3

Helix

599 – 603

5

Helix

606 – 608

3

Beta strand

616 – 625

10

Turn

627 – 629

3

Helix

635 – 638

4

Helix

648 – 650

3

Beta strand

653 – 665

13

Helix

675 – 685

11

Turn

690 – 692

3

Beta strand

693 – 695

3

Helix

704 – 716

13

Beta strand

718 – 730

13

Turn

735 – 737

3

Beta strand

739 – 746

8

Helix

747 – 751

5

Beta strand

755 – 767

13

Beta strand

774 – 784

11

Turn

785 – 788

4

Beta strand

789 – 796

8

Helix

802 – 814

13

Beta strand

816 – 819

4

Beta strand

827 – 829

3

Beta strand

833 – 836

4

Beta strand

841 – 854

14

Turn

857 – 861

5

Beta strand

867 – 872

6

Beta strand

874 – 878

5

Helix

884 – 886

3

Helix

890 – 900

11

Sequences

	Sequence		Length	Mass (Da)
	P18858 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: B2854DAE38A8D4AD	FASTA	919	101,736
	10 20 30 40 50 60 MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD SPVKRPGRKA 70 80 90 100 110 120 ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE NNASLSDTSP MDSSPSGIPK 130 140 150 160 170 180 RRTARKQLPK RTIQEVLEEQ SEDEDREAKR KKEEEEEETP KESLTEAEVA TEKEGEDGDQ 190 200 210 220 230 240 PTTPPKPLKT SKAETPTESV SEPEVATKQE LQEEEEQTKP PRRAPKTLSS FFTPRKPAVK 250 260 270 280 290 300 KEVKEEEPGA PGKEGAAEGP LDPSGYNPAK NNYHPVEDAC WKPGQKVPYL AVARTFEKIE 310 320 330 340 350 360 EVSARLRMVE TLSNLLRSVV ALSPPDLLPV LYLSLNHLGP PQQGLELGVG DGVLLKAVAQ 370 380 390 400 410 420 ATGRQLESVR AEAAEKGDVG LVAENSRSTQ RLMLPPPPLT ASGVFSKFRD IARLTGSAST 430 440 450 460 470 480 AKKIDIIKGL FVACRHSEAR FIARSLSGRL RLGLAEQSVL AALSQAVSLT PPGQEFPPAM 490 500 510 520 530 540 VDAGKGKTAE ARKTWLEEQG MILKQTFCEV PDLDRIIPVL LEHGLERLPE HCKLSPGIPL 550 560 570 580 590 600 KPMLAHPTRG ISEVLKRFEE AAFTCEYKYD GQRAQIHALE GGEVKIFSRN QEDNTGKYPD 610 620 630 640 650 660 IISRIPKIKL PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE IQVQVCLYAF 670 680 690 700 710 720 DLIYLNGESL VREPLSRRRQ LLRENFVETE GEFVFATSLD TKDIEQIAEF LEQSVKDSCE 730 740 750 760 770 780 GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL DGVGDTLDLV VIGAYLGRGK RAGRYGGFLL 790 800 810 820 830 840 ASYDEDSEEL QAICKLGTGF SDEELEEHHQ SLKALVLPSP RPYVRIDGAV IPDHWLDPSA 850 860 870 880 890 900 VWEVKCADLS LSPIYPAARG LVDSDKGISL RFPRFIRVRE DKQPEQATTS AQVACLYRKQ 910 SQIQNQQGED SGSDPEDTY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human DNA ligase I cDNA: cloning and functional expression in Saccharomyces cerevisiae." Barnes D.E., Johnston L.H., Kodama K., Tomkinson A.E., Lasko D.D., Lindahl T. Proc. Natl. Acad. Sci. U.S.A. 87:6679-6683(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: T lymphoblast.
[2]	NIEHS SNPs program Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-24; TRP-62; GLU-249; SER-267; MET-349; ILE-369; VAL-480; ILE-614 AND LEU-677.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[4]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[6]	"A wild-type DNA ligase I gene is expressed in Bloom's syndrome cells." Petrini J.H.J., Huwiler K.G., Weaver D.T. Proc. Natl. Acad. Sci. U.S.A. 88:7615-7619(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 716-753.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-76 AND SER-141, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; THR-195 AND THR-233, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-76, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-141; THR-195; SER-201; THR-233; SER-911 AND SER-913, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells." Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X. Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-66; SER-76; SER-141; THR-195; SER-201; SER-911 AND SER-913, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-51; SER-66; SER-76; SER-141; THR-195; SER-201; SER-911 AND SER-913, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; SER-141; THR-195; SER-911 AND SER-913, MASS SPECTROMETRY.
[16]	"Human DNA ligase I completely encircles and partially unwinds nicked DNA." Pascal J.M., O'Brien P.J., Tomkinson A.E., Ellenberger T. Nature 432:473-478(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-919 IN COMPLEX WITH NICKED DNA AND AMP, COFACTOR, ACTIVE SITE.
[17]	"Mutations in the DNA ligase I gene of an individual with immunodeficiencies and cellular hypersensitivity to DNA-damaging agents." Barnes D.E., Tomkinson A.E., Lehmann A.R., Webster A.D.B., Lindahl T. Cell 69:495-503(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LYS-566 AND TRP-771.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-152 AND LEU-612.
+	Additional computationally mapped references.

Web resources

LIG1base

LIG1 mutation db

NIEHS-SNPs

Wikipedia

DNA ligase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M36067 mRNA. Translation: AAA59518.1.
AF527418 Genomic DNA. Translation: AAM77697.1.
AK314210 mRNA. Translation: BAG36885.1.
CH471177 Genomic DNA. Translation: EAW52316.1.
BC108318 mRNA. Translation: AAI08319.1.

IPI

IPI00219841.

PIR

A41275. A36048.

RefSeq

NP_000225.1. NM_000234.1.

UniGene

Hs.1770.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X9N	X-ray	3.00	A	233-919	[»]

ProteinModelPortal

P18858.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24215N.

IntAct

P18858. 2 interactions.

MINT

MINT-141868.

STRING

9606.ENSP00000263274.

PTM databases

PhosphoSite

P18858.

Polymorphism databases

DMDM

118773.

Proteomic databases

PaxDb

P18858.

PeptideAtlas

P18858.

PRIDE

P18858.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263274; ENSP00000263274; ENSG00000105486.

GeneID

3978.

KEGG

hsa:3978.

UCSC

uc002pia.1. human.

Organism-specific databases

CTD

3978.

GeneCards

GC19M048618.

HGNC

HGNC:6598. LIG1.

HPA

CAB037015.

MIM

126391. gene.

neXtProt

NX_P18858.

PharmGKB

PA30372.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1793.

HOGENOM

HOG000036006.

HOVERGEN

HBG005514.

InParanoid

P18858.

KO

K10747.

OMA

AQVACLY.

OrthoDB

EOG4RBQJ6.

PhylomeDB

P18858.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P18858.

Bgee

P18858.

CleanEx

HS_LIG1.

Genevestigator

P18858.

GermOnline

ENSG00000105486. Homo sapiens.

Family and domain databases

Gene3D

1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.

InterPro

IPR000977. DNA_ligase_ATP-dep.
IPR012309. DNA_ligase_ATP-dep_C.
IPR012310. DNA_ligase_ATP-dep_cent.
IPR016059. DNA_ligase_ATP-dep_CS.
IPR012308. DNA_ligase_ATP-dep_N.
IPR012340. NA-bd_OB-fold.
[Graphical view]

Pfam

PF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.
SSF117018. SSF117018. 1 hit.

TIGRFAMs

TIGR00574. dnl1. 1 hit.

PROSITE

PS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P18858.

ChEMBL

CHEMBL5694.

ChiTaRS

LIG1. human.

DrugBank

DB00290. Bleomycin.

EvolutionaryTrace

P18858.

GenomeRNAi

3978.

NextBio

15592.

SOURCE

Search...

Entry information

Entry name

DNLI1_HUMAN

Accession

Primary (citable) accession number: P18858
Secondary accession number(s): B2RAI8, Q32P23

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.