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Protein

DNA ligase 1

Gene

LIG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.

Catalytic activityi

ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.PROSITE-ProRule annotation

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei566ATPCombined sources1 Publication1
Active sitei568N6-AMP-lysine intermediatePROSITE-ProRule annotation1
Binding sitei573ATPCombined sources1 Publication1
Binding sitei589ATP1
Metal bindingi621Magnesium 1Curated1
Metal bindingi720Magnesium 2Curated1
Binding sitei725ATPCombined sources1 Publication1
Binding sitei738ATPBy similarity1
Binding sitei744ATPCombined sources1 Publication1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: ProtInc
  • DNA ligase (ATP) activity Source: GO_Central
  • DNA ligase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • base-excision repair Source: BHF-UCL
  • cell division Source: UniProtKB-KW
  • DNA biosynthetic process Source: InterPro
  • DNA metabolic process Source: ProtInc
  • DNA repair Source: ProtInc
  • mismatch repair Source: Reactome
  • nucleotide-excision repair, DNA gap filling Source: Reactome
  • Okazaki fragment processing involved in mitotic DNA replication Source: GO_Central
  • telomere maintenance via recombination Source: Reactome
  • transcription-coupled nucleotide-excision repair Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS02747-MONOMER.
BRENDAi6.5.1.1. 2681.
ReactomeiR-HSA-110362. POLB-Dependent Long Patch Base Excision Repair.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-174414. Processive synthesis on the C-strand of the telomere.
R-HSA-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-HSA-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-69183. Processive synthesis on the lagging strand.
SIGNORiP18858.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase 1 (EC:6.5.1.1PROSITE-ProRule annotation)
Alternative name(s):
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1
Gene namesi
Name:LIG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6598. LIG1.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: HPA
  • intracellular membrane-bounded organelle Source: HPA
  • mitochondrion Source: GO_Central
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi3978.
OpenTargetsiENSG00000105486.
PharmGKBiPA30372.

Chemistry databases

ChEMBLiCHEMBL5694.
DrugBankiDB00290. Bleomycin.

Polymorphism and mutation databases

BioMutaiLIG1.
DMDMi118773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000595701 – 919DNA ligase 1Add BLAST919

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei47PhosphoserineCombined sources1
Modified residuei49PhosphoserineCombined sources1
Modified residuei51PhosphoserineCombined sources1
Modified residuei66PhosphoserineCombined sources1
Modified residuei76PhosphoserineCombined sources1
Modified residuei141PhosphoserineCombined sources1
Modified residuei195PhosphothreonineCombined sources1
Modified residuei199PhosphoserineCombined sources1
Modified residuei201PhosphoserineCombined sources1
Modified residuei207PhosphothreonineCombined sources1
Modified residuei226N6-acetyllysineBy similarity1
Modified residuei229PhosphoserineCombined sources1
Modified residuei230PhosphoserineCombined sources1
Modified residuei233PhosphothreonineCombined sources1
Modified residuei798PhosphothreonineCombined sources1
Modified residuei801PhosphoserineCombined sources1
Modified residuei819PhosphoserineCombined sources1
Modified residuei911PhosphoserineCombined sources1
Modified residuei913PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP18858.
MaxQBiP18858.
PaxDbiP18858.
PeptideAtlasiP18858.
PRIDEiP18858.

PTM databases

iPTMnetiP18858.
PhosphoSitePlusiP18858.

Expressioni

Gene expression databases

BgeeiENSG00000105486.
CleanExiHS_LIG1.
ExpressionAtlasiP18858. baseline and differential.
GenevisibleiP18858. HS.

Organism-specific databases

HPAiCAB037015.
HPA041431.
HPA048071.

Interactioni

Subunit structurei

Interacts with PCNA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei305Interaction with target DNA1
Sitei590Interaction with target DNA1
Sitei770Interaction with target DNA1
Sitei795Interaction with target DNA1

Protein-protein interaction databases

BioGridi110166. 16 interactors.
DIPiDIP-24215N.
IntActiP18858. 7 interactors.
MINTiMINT-141868.
STRINGi9606.ENSP00000263274.

Chemistry databases

BindingDBiP18858.

Structurei

Secondary structure

1919
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi263 – 265Combined sources3
Helixi275 – 278Combined sources4
Helixi289 – 300Combined sources12
Helixi305 – 322Combined sources18
Helixi324 – 326Combined sources3
Helixi327 – 335Combined sources9
Helixi341 – 343Combined sources3
Helixi351 – 362Combined sources12
Helixi366 – 376Combined sources11
Helixi379 – 382Combined sources4
Helixi401 – 413Combined sources13
Helixi419 – 433Combined sources15
Helixi438 – 446Combined sources9
Helixi456 – 469Combined sources14
Turni483 – 486Combined sources4
Helixi489 – 509Combined sources21
Helixi513 – 527Combined sources15
Helixi529 – 531Combined sources3
Beta strandi544 – 550Combined sources7
Helixi551 – 557Combined sources7
Turni558 – 560Combined sources3
Beta strandi563 – 578Combined sources16
Beta strandi584 – 587Combined sources4
Turni595 – 597Combined sources3
Helixi599 – 603Combined sources5
Helixi606 – 608Combined sources3
Beta strandi616 – 625Combined sources10
Turni627 – 629Combined sources3
Helixi635 – 638Combined sources4
Helixi648 – 650Combined sources3
Beta strandi653 – 665Combined sources13
Helixi675 – 685Combined sources11
Turni690 – 692Combined sources3
Beta strandi693 – 695Combined sources3
Helixi704 – 716Combined sources13
Beta strandi718 – 730Combined sources13
Turni735 – 737Combined sources3
Beta strandi739 – 746Combined sources8
Helixi747 – 751Combined sources5
Beta strandi755 – 767Combined sources13
Beta strandi774 – 784Combined sources11
Turni785 – 788Combined sources4
Beta strandi789 – 796Combined sources8
Helixi802 – 814Combined sources13
Beta strandi816 – 819Combined sources4
Beta strandi827 – 829Combined sources3
Beta strandi833 – 836Combined sources4
Beta strandi841 – 854Combined sources14
Turni857 – 861Combined sources5
Beta strandi867 – 872Combined sources6
Beta strandi874 – 878Combined sources5
Helixi884 – 886Combined sources3
Helixi890 – 900Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X9NX-ray3.00A233-919[»]
ProteinModelPortaliP18858.
SMRiP18858.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18858.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni449 – 458Interaction with target DNA10
Regioni642 – 644Interaction with target DNA3

Sequence similaritiesi

Belongs to the ATP-dependent DNA ligase family.Curated

Phylogenomic databases

eggNOGiKOG0967. Eukaryota.
COG1793. LUCA.
GeneTreeiENSGT00860000133792.
HOGENOMiHOG000036006.
HOVERGENiHBG005514.
InParanoidiP18858.
KOiK10747.
OMAiPQVVIEV.
OrthoDBiEOG091G06OS.
PhylomeDBiP18858.
TreeFamiTF300342.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
InterProiIPR000977. 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]
PfamiPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00574. dnl1. 1 hit.
PROSITEiPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P18858-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD
60 70 80 90 100
SPVKRPGRKA ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE
110 120 130 140 150
NNASLSDTSP MDSSPSGIPK RRTARKQLPK RTIQEVLEEQ SEDEDREAKR
160 170 180 190 200
KKEEEEEETP KESLTEAEVA TEKEGEDGDQ PTTPPKPLKT SKAETPTESV
210 220 230 240 250
SEPEVATKQE LQEEEEQTKP PRRAPKTLSS FFTPRKPAVK KEVKEEEPGA
260 270 280 290 300
PGKEGAAEGP LDPSGYNPAK NNYHPVEDAC WKPGQKVPYL AVARTFEKIE
310 320 330 340 350
EVSARLRMVE TLSNLLRSVV ALSPPDLLPV LYLSLNHLGP PQQGLELGVG
360 370 380 390 400
DGVLLKAVAQ ATGRQLESVR AEAAEKGDVG LVAENSRSTQ RLMLPPPPLT
410 420 430 440 450
ASGVFSKFRD IARLTGSAST AKKIDIIKGL FVACRHSEAR FIARSLSGRL
460 470 480 490 500
RLGLAEQSVL AALSQAVSLT PPGQEFPPAM VDAGKGKTAE ARKTWLEEQG
510 520 530 540 550
MILKQTFCEV PDLDRIIPVL LEHGLERLPE HCKLSPGIPL KPMLAHPTRG
560 570 580 590 600
ISEVLKRFEE AAFTCEYKYD GQRAQIHALE GGEVKIFSRN QEDNTGKYPD
610 620 630 640 650
IISRIPKIKL PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE
660 670 680 690 700
IQVQVCLYAF DLIYLNGESL VREPLSRRRQ LLRENFVETE GEFVFATSLD
710 720 730 740 750
TKDIEQIAEF LEQSVKDSCE GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL
760 770 780 790 800
DGVGDTLDLV VIGAYLGRGK RAGRYGGFLL ASYDEDSEEL QAICKLGTGF
810 820 830 840 850
SDEELEEHHQ SLKALVLPSP RPYVRIDGAV IPDHWLDPSA VWEVKCADLS
860 870 880 890 900
LSPIYPAARG LVDSDKGISL RFPRFIRVRE DKQPEQATTS AQVACLYRKQ
910
SQIQNQQGED SGSDPEDTY
Length:919
Mass (Da):101,736
Last modified:November 1, 1990 - v1
Checksum:iB2854DAE38A8D4AD
GO
Isoform 2 (identifier: P18858-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     796-801: LGTGFS → VLGNWG
     802-919: Missing.

Note: No experimental confirmation available.
Show »
Length:801
Mass (Da):88,516
Checksum:i1AC26C5FB793684F
GO
Isoform 3 (identifier: P18858-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-36: Missing.
     153-153: Missing.

Note: No experimental confirmation available.
Show »
Length:888
Mass (Da):98,228
Checksum:i6A59D9975C259D9F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01880224A → V.1 PublicationCorresponds to variant rs3730855dbSNPEnsembl.1
Natural variantiVAR_02019452P → L.Corresponds to variant rs4987181dbSNPEnsembl.1
Natural variantiVAR_01880362R → W.1 PublicationCorresponds to variant rs3730863dbSNPEnsembl.1
Natural variantiVAR_02019572D → G.Corresponds to variant rs4987070dbSNPEnsembl.1
Natural variantiVAR_036511152K → E in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs780748107dbSNPEnsembl.1
Natural variantiVAR_016766249G → E.1 PublicationCorresponds to variant rs3730911dbSNPEnsembl.1
Natural variantiVAR_016767267N → S.1 PublicationCorresponds to variant rs3730933dbSNPEnsembl.1
Natural variantiVAR_018804349V → M.1 PublicationCorresponds to variant rs3730947dbSNPEnsembl.1
Natural variantiVAR_018805369V → I.1 PublicationCorresponds to variant rs3730966dbSNPEnsembl.1
Natural variantiVAR_016768409R → H.Corresponds to variant rs4987068dbSNPEnsembl.1
Natural variantiVAR_016769480M → V.1 PublicationCorresponds to variant rs3730980dbSNPEnsembl.1
Natural variantiVAR_002262566E → 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. 1 PublicationCorresponds to variant rs121434560dbSNPEnsembl.1
Natural variantiVAR_036512612S → L in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs780324684dbSNPEnsembl.1
Natural variantiVAR_016770614T → I.1 PublicationCorresponds to variant rs3731003dbSNPEnsembl.1
Natural variantiVAR_018806677R → L.1 PublicationCorresponds to variant rs3731008dbSNPEnsembl.1
Natural variantiVAR_002263771R → 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. 1 PublicationCorresponds to variant rs121434561dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0573207 – 36Missing in isoform 3. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_057321153Missing in isoform 3. 1 Publication1
Alternative sequenceiVSP_056139796 – 801LGTGFS → VLGNWG in isoform 2. 1 Publication6
Alternative sequenceiVSP_056140802 – 919Missing in isoform 2. 1 PublicationAdd BLAST118

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36067 mRNA. Translation: AAA59518.1.
AF527418 Genomic DNA. Translation: AAM77697.1.
AK300370 mRNA. Translation: BAG62106.1.
AK314210 mRNA. Translation: BAG36885.1.
AC011466 Genomic DNA. No translation available.
KC877741 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52316.1.
BC108318 mRNA. Translation: AAI08319.1.
BC110622 mRNA. Translation: AAI10623.1.
CCDSiCCDS12711.1. [P18858-1]
CCDS74409.1. [P18858-3]
PIRiA36048. A41275.
RefSeqiNP_000225.1. NM_000234.2. [P18858-1]
NP_001275992.1. NM_001289063.1. [P18858-3]
NP_001275993.1. NM_001289064.1.
NP_001307899.1. NM_001320970.1.
NP_001307900.1. NM_001320971.1.
UniGeneiHs.1770.

Genome annotation databases

EnsembliENST00000263274; ENSP00000263274; ENSG00000105486. [P18858-1]
ENST00000427526; ENSP00000442841; ENSG00000105486. [P18858-3]
ENST00000601091; ENSP00000471836; ENSG00000105486. [P18858-2]
ENST00000613670; ENSP00000483027; ENSG00000105486. [P18858-2]
GeneIDi3978.
KEGGihsa:3978.
UCSCiuc002pia.2. human. [P18858-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

LIG1base

LIG1 mutation db

NIEHS-SNPs
Wikipedia

DNA ligase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36067 mRNA. Translation: AAA59518.1.
AF527418 Genomic DNA. Translation: AAM77697.1.
AK300370 mRNA. Translation: BAG62106.1.
AK314210 mRNA. Translation: BAG36885.1.
AC011466 Genomic DNA. No translation available.
KC877741 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52316.1.
BC108318 mRNA. Translation: AAI08319.1.
BC110622 mRNA. Translation: AAI10623.1.
CCDSiCCDS12711.1. [P18858-1]
CCDS74409.1. [P18858-3]
PIRiA36048. A41275.
RefSeqiNP_000225.1. NM_000234.2. [P18858-1]
NP_001275992.1. NM_001289063.1. [P18858-3]
NP_001275993.1. NM_001289064.1.
NP_001307899.1. NM_001320970.1.
NP_001307900.1. NM_001320971.1.
UniGeneiHs.1770.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X9NX-ray3.00A233-919[»]
ProteinModelPortaliP18858.
SMRiP18858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110166. 16 interactors.
DIPiDIP-24215N.
IntActiP18858. 7 interactors.
MINTiMINT-141868.
STRINGi9606.ENSP00000263274.

Chemistry databases

BindingDBiP18858.
ChEMBLiCHEMBL5694.
DrugBankiDB00290. Bleomycin.

PTM databases

iPTMnetiP18858.
PhosphoSitePlusiP18858.

Polymorphism and mutation databases

BioMutaiLIG1.
DMDMi118773.

Proteomic databases

EPDiP18858.
MaxQBiP18858.
PaxDbiP18858.
PeptideAtlasiP18858.
PRIDEiP18858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263274; ENSP00000263274; ENSG00000105486. [P18858-1]
ENST00000427526; ENSP00000442841; ENSG00000105486. [P18858-3]
ENST00000601091; ENSP00000471836; ENSG00000105486. [P18858-2]
ENST00000613670; ENSP00000483027; ENSG00000105486. [P18858-2]
GeneIDi3978.
KEGGihsa:3978.
UCSCiuc002pia.2. human. [P18858-1]

Organism-specific databases

CTDi3978.
DisGeNETi3978.
GeneCardsiLIG1.
HGNCiHGNC:6598. LIG1.
HPAiCAB037015.
HPA041431.
HPA048071.
MIMi126391. gene.
neXtProtiNX_P18858.
OpenTargetsiENSG00000105486.
PharmGKBiPA30372.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0967. Eukaryota.
COG1793. LUCA.
GeneTreeiENSGT00860000133792.
HOGENOMiHOG000036006.
HOVERGENiHBG005514.
InParanoidiP18858.
KOiK10747.
OMAiPQVVIEV.
OrthoDBiEOG091G06OS.
PhylomeDBiP18858.
TreeFamiTF300342.

Enzyme and pathway databases

BioCyciZFISH:HS02747-MONOMER.
BRENDAi6.5.1.1. 2681.
ReactomeiR-HSA-110362. POLB-Dependent Long Patch Base Excision Repair.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-174414. Processive synthesis on the C-strand of the telomere.
R-HSA-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-HSA-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-HSA-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-69183. Processive synthesis on the lagging strand.
SIGNORiP18858.

Miscellaneous databases

ChiTaRSiLIG1. human.
EvolutionaryTraceiP18858.
GeneWikiiLIG1.
GenomeRNAii3978.
PROiP18858.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105486.
CleanExiHS_LIG1.
ExpressionAtlasiP18858. baseline and differential.
GenevisibleiP18858. HS.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
InterProiIPR000977. 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]
PfamiPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00574. dnl1. 1 hit.
PROSITEiPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNLI1_HUMAN
AccessioniPrimary (citable) accession number: P18858
Secondary accession number(s): B2RAI8
, B4DTU4, Q2TB12, Q32P23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 30, 2016
This is version 186 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.