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P18858

- DNLI1_HUMAN

UniProt

P18858 - DNLI1_HUMAN

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Protein

DNA ligase 1

Gene

LIG1

Organism
Homo sapiens (Human)
Status
Reviewed - 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) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).PROSITE-ProRule annotation

Cofactori

Magnesium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei305 – 3051Interaction with target DNA
Binding sitei566 – 5661ATP
Active sitei568 – 5681N6-AMP-lysine intermediatePROSITE-ProRule annotation
Binding sitei573 – 5731ATP
Binding sitei589 – 5891ATP
Sitei590 – 5901Interaction with target DNA
Metal bindingi621 – 6211Magnesium 1Curated
Metal bindingi720 – 7201Magnesium 2Curated
Binding sitei725 – 7251ATP
Binding sitei738 – 7381ATPBy similarity
Binding sitei744 – 7441ATP
Sitei770 – 7701Interaction with target DNA
Sitei795 – 7951Interaction with target DNA

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: ProtInc
  3. DNA ligase (ATP) activity Source: RefGenome
  4. DNA ligase activity Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. base-excision repair Source: Reactome
  3. cell division Source: UniProtKB-KW
  4. DNA biosynthetic process Source: InterPro
  5. DNA ligation involved in DNA repair Source: InterPro
  6. DNA metabolic process Source: ProtInc
  7. DNA repair Source: Reactome
  8. DNA strand elongation involved in DNA replication Source: Reactome
  9. double-strand break repair Source: Reactome
  10. double-strand break repair via homologous recombination Source: Reactome
  11. double-strand break repair via nonhomologous end joining Source: Ensembl
  12. lagging strand elongation Source: RefGenome
  13. mitotic cell cycle Source: Reactome
  14. nucleotide-excision repair Source: Reactome
  15. nucleotide-excision repair, DNA gap filling Source: Reactome
  16. response to hydrogen peroxide Source: Ensembl
  17. telomere maintenance Source: Reactome
  18. telomere maintenance via recombination Source: Reactome
  19. telomere maintenance via semi-conservative replication Source: Reactome
  20. 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

ReactomeiREACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1998. Gap-filling DNA repair synthesis and ligation in GG-NER.
REACT_2192. Removal of DNA patch containing abasic residue.
REACT_74. Gap-filling DNA repair synthesis and ligation in TC-NER.
REACT_8027. Processive synthesis on the C-strand of the telomere.
REACT_977. Resolution of D-loop structures through Holliday junction intermediates.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase 1 (EC:6.5.1.1)
Alternative name(s):
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1
Gene namesi
Name:LIG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:6598. LIG1.

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: RefGenome
  2. Golgi apparatus Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. mitochondrion Source: RefGenome
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 919919DNA ligase 1PRO_0000059570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471Phosphoserine1 Publication
Modified residuei49 – 491Phosphoserine2 Publications
Modified residuei51 – 511Phosphoserine5 Publications
Modified residuei66 – 661Phosphoserine6 Publications
Modified residuei76 – 761Phosphoserine6 Publications
Modified residuei141 – 1411Phosphoserine5 Publications
Modified residuei195 – 1951Phosphothreonine5 Publications
Modified residuei201 – 2011Phosphoserine3 Publications
Modified residuei226 – 2261N6-acetyllysineBy similarity
Modified residuei233 – 2331Phosphothreonine2 Publications
Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei911 – 9111Phosphoserine4 Publications
Modified residuei913 – 9131Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP18858.
PaxDbiP18858.
PeptideAtlasiP18858.
PRIDEiP18858.

PTM databases

PhosphoSiteiP18858.

Expressioni

Gene expression databases

BgeeiP18858.
CleanExiHS_LIG1.
ExpressionAtlasiP18858. baseline and differential.
GenevestigatoriP18858.

Organism-specific databases

HPAiCAB037015.
HPA041431.
HPA048071.

Interactioni

Protein-protein interaction databases

BioGridi110166. 7 interactions.
DIPiDIP-24215N.
IntActiP18858. 3 interactions.
MINTiMINT-141868.
STRINGi9606.ENSP00000263274.

Structurei

Secondary structure

1
919
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi263 – 2653
Helixi275 – 2784
Helixi289 – 30012
Helixi305 – 32218
Helixi324 – 3263
Helixi327 – 3359
Helixi341 – 3433
Helixi351 – 36212
Helixi366 – 37611
Helixi379 – 3824
Helixi401 – 41313
Helixi419 – 43315
Helixi438 – 4469
Helixi456 – 46914
Turni483 – 4864
Helixi489 – 50921
Helixi513 – 52715
Helixi529 – 5313
Beta strandi544 – 5507
Helixi551 – 5577
Turni558 – 5603
Beta strandi563 – 57816
Beta strandi584 – 5874
Turni595 – 5973
Helixi599 – 6035
Helixi606 – 6083
Beta strandi616 – 62510
Turni627 – 6293
Helixi635 – 6384
Helixi648 – 6503
Beta strandi653 – 66513
Helixi675 – 68511
Turni690 – 6923
Beta strandi693 – 6953
Helixi704 – 71613
Beta strandi718 – 73013
Turni735 – 7373
Beta strandi739 – 7468
Helixi747 – 7515
Beta strandi755 – 76713
Beta strandi774 – 78411
Turni785 – 7884
Beta strandi789 – 7968
Helixi802 – 81413
Beta strandi816 – 8194
Beta strandi827 – 8293
Beta strandi833 – 8364
Beta strandi841 – 85414
Turni857 – 8615
Beta strandi867 – 8726
Beta strandi874 – 8785
Helixi884 – 8863
Helixi890 – 90011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9NX-ray3.00A233-919[»]
ProteinModelPortaliP18858.
SMRiP18858. Positions 262-901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18858.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni449 – 45810Interaction with target DNA
Regioni642 – 6443Interaction with target DNA

Sequence similaritiesi

Belongs to the ATP-dependent DNA ligase family.Curated

Phylogenomic databases

eggNOGiCOG1793.
GeneTreeiENSGT00750000117745.
HOGENOMiHOG000036006.
HOVERGENiHBG005514.
InParanoidiP18858.
KOiK10747.
OMAiLDPSGYN.
OrthoDBiEOG7RFTGN.
PhylomeDBiP18858.
TreeFamiTF300342.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
2.40.50.140. 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241A → V.1 Publication
Corresponds to variant rs3730855 [ dbSNP | Ensembl ].
VAR_018802
Natural varianti52 – 521P → L.
Corresponds to variant rs4987181 [ dbSNP | Ensembl ].
VAR_020194
Natural varianti62 – 621R → W.1 Publication
Corresponds to variant rs3730863 [ dbSNP | Ensembl ].
VAR_018803
Natural varianti72 – 721D → G.
Corresponds to variant rs4987070 [ dbSNP | Ensembl ].
VAR_020195
Natural varianti152 – 1521K → E in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036511
Natural varianti249 – 2491G → E.1 Publication
Corresponds to variant rs3730911 [ dbSNP | Ensembl ].
VAR_016766
Natural varianti267 – 2671N → S.1 Publication
Corresponds to variant rs3730933 [ dbSNP | Ensembl ].
VAR_016767
Natural varianti349 – 3491V → M.1 Publication
Corresponds to variant rs3730947 [ dbSNP | Ensembl ].
VAR_018804
Natural varianti369 – 3691V → I.1 Publication
Corresponds to variant rs3730966 [ dbSNP | Ensembl ].
VAR_018805
Natural varianti409 – 4091R → H.
Corresponds to variant rs4987068 [ dbSNP | Ensembl ].
VAR_016768
Natural varianti480 – 4801M → V.1 Publication
Corresponds to variant rs3730980 [ dbSNP | Ensembl ].
VAR_016769
Natural varianti566 – 5661E → 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 Publication
VAR_002262
Natural varianti612 – 6121S → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036512
Natural varianti614 – 6141T → I.1 Publication
Corresponds to variant rs3731003 [ dbSNP | Ensembl ].
VAR_016770
Natural varianti677 – 6771R → L.1 Publication
Corresponds to variant rs3731008 [ dbSNP | Ensembl ].
VAR_018806
Natural varianti771 – 7711R → 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 Publication
VAR_002263

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei796 – 8016LGTGFS → VLGNWG in isoform 2. 1 PublicationVSP_056139
Alternative sequencei802 – 919118Missing in isoform 2. 1 PublicationVSP_056140Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M36067 mRNA. Translation: AAA59518.1.
AF527418 Genomic DNA. Translation: AAM77697.1.
AK314210 mRNA. Translation: BAG36885.1.
AC011466 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]
PIRiA36048. A41275.
RefSeqiNP_000225.1. NM_000234.2.
NP_001275992.1. NM_001289063.1.
NP_001275993.1. NM_001289064.1.
XP_006723279.1. XM_006723216.1.
UniGeneiHs.1770.

Genome annotation databases

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

Polymorphism databases

DMDMi118773.

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:
EMBL
GenBank
DDBJ
Links Updated
M36067 mRNA. Translation: AAA59518.1 .
AF527418 Genomic DNA. Translation: AAM77697.1 .
AK314210 mRNA. Translation: BAG36885.1 .
AC011466 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52316.1 .
BC108318 mRNA. Translation: AAI08319.1 .
BC110622 mRNA. Translation: AAI10623.1 .
CCDSi CCDS12711.1. [P18858-1 ]
PIRi A36048. A41275.
RefSeqi NP_000225.1. NM_000234.2.
NP_001275992.1. NM_001289063.1.
NP_001275993.1. NM_001289064.1.
XP_006723279.1. XM_006723216.1.
UniGenei Hs.1770.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X9N X-ray 3.00 A 233-919 [» ]
ProteinModelPortali P18858.
SMRi P18858. Positions 262-901.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110166. 7 interactions.
DIPi DIP-24215N.
IntActi P18858. 3 interactions.
MINTi MINT-141868.
STRINGi 9606.ENSP00000263274.

Chemistry

BindingDBi P18858.
ChEMBLi CHEMBL5694.
DrugBanki DB00290. Bleomycin.

PTM databases

PhosphoSitei P18858.

Polymorphism databases

DMDMi 118773.

Proteomic databases

MaxQBi P18858.
PaxDbi P18858.
PeptideAtlasi P18858.
PRIDEi P18858.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263274 ; ENSP00000263274 ; ENSG00000105486 . [P18858-1 ]
ENST00000601091 ; ENSP00000471836 ; ENSG00000105486 . [P18858-2 ]
ENST00000613670 ; ENSP00000483027 ; ENSG00000105486 . [P18858-2 ]
GeneIDi 3978.
KEGGi hsa:3978.
UCSCi uc002pia.1. human. [P18858-1 ]

Organism-specific databases

CTDi 3978.
GeneCardsi GC19M048618.
HGNCi HGNC:6598. LIG1.
HPAi CAB037015.
HPA041431.
HPA048071.
MIMi 126391. gene.
neXtProti NX_P18858.
PharmGKBi PA30372.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1793.
GeneTreei ENSGT00750000117745.
HOGENOMi HOG000036006.
HOVERGENi HBG005514.
InParanoidi P18858.
KOi K10747.
OMAi LDPSGYN.
OrthoDBi EOG7RFTGN.
PhylomeDBi P18858.
TreeFami TF300342.

Enzyme and pathway databases

Reactomei REACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1998. Gap-filling DNA repair synthesis and ligation in GG-NER.
REACT_2192. Removal of DNA patch containing abasic residue.
REACT_74. Gap-filling DNA repair synthesis and ligation in TC-NER.
REACT_8027. Processive synthesis on the C-strand of the telomere.
REACT_977. Resolution of D-loop structures through Holliday junction intermediates.

Miscellaneous databases

ChiTaRSi LIG1. human.
EvolutionaryTracei P18858.
GeneWikii LIG1.
GenomeRNAii 3978.
NextBioi 15592.
PROi P18858.
SOURCEi Search...

Gene expression databases

Bgeei P18858.
CleanExi HS_LIG1.
ExpressionAtlasi P18858. baseline and differential.
Genevestigatori P18858.

Family and domain databases

Gene3Di 1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProi 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 ]
Pfami PF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00574. dnl1. 1 hit.
PROSITEi PS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    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] (ISOFORM 1).
    Tissue: Thymus.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Eye.
  7. "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 (ISOFORM 1).
  8. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-141; THR-195; SER-201; THR-233; SER-911 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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.
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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.
  20. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-152 AND LEU-612.

Entry informationi

Entry nameiDNLI1_HUMAN
AccessioniPrimary (citable) accession number: P18858
Secondary accession number(s): B2RAI8, Q2TB12, Q32P23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 162 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

External Data

Dasty 3