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P18858

- DNLI1_HUMAN

UniProt

P18858 - DNLI1_HUMAN

Protein

DNA ligase 1

Gene

LIG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    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 ligation involved in DNA repair Source: InterPro
    5. DNA metabolic process Source: ProtInc
    6. DNA repair Source: Reactome
    7. DNA strand elongation involved in DNA replication Source: Reactome
    8. double-strand break repair Source: Reactome
    9. double-strand break repair via homologous recombination Source: Reactome
    10. double-strand break repair via nonhomologous end joining Source: Ensembl
    11. lagging strand elongation Source: RefGenome
    12. mitotic cell cycle Source: Reactome
    13. nucleotide-excision repair Source: Reactome
    14. nucleotide-excision repair, DNA gap filling Source: Reactome
    15. response to hydrogen peroxide Source: Ensembl
    16. telomere maintenance Source: Reactome
    17. telomere maintenance via recombination Source: Reactome
    18. telomere maintenance via semi-conservative replication Source: Reactome
    19. transcription-coupled nucleotide-excision repair Source: Reactome

    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

    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

    ArrayExpressiP18858.
    BgeeiP18858.
    CleanExiHS_LIG1.
    GenevestigatoriP18858.

    Organism-specific databases

    HPAiCAB037015.
    HPA041431.
    HPA048071.

    Interactioni

    Protein-protein interaction databases

    BioGridi110166. 6 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.
    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

    MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD    50
    SPVKRPGRKA ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE 100
    NNASLSDTSP MDSSPSGIPK RRTARKQLPK RTIQEVLEEQ SEDEDREAKR 150
    KKEEEEEETP KESLTEAEVA TEKEGEDGDQ PTTPPKPLKT SKAETPTESV 200
    SEPEVATKQE LQEEEEQTKP PRRAPKTLSS FFTPRKPAVK KEVKEEEPGA 250
    PGKEGAAEGP LDPSGYNPAK NNYHPVEDAC WKPGQKVPYL AVARTFEKIE 300
    EVSARLRMVE TLSNLLRSVV ALSPPDLLPV LYLSLNHLGP PQQGLELGVG 350
    DGVLLKAVAQ ATGRQLESVR AEAAEKGDVG LVAENSRSTQ RLMLPPPPLT 400
    ASGVFSKFRD IARLTGSAST AKKIDIIKGL FVACRHSEAR FIARSLSGRL 450
    RLGLAEQSVL AALSQAVSLT PPGQEFPPAM VDAGKGKTAE ARKTWLEEQG 500
    MILKQTFCEV PDLDRIIPVL LEHGLERLPE HCKLSPGIPL KPMLAHPTRG 550
    ISEVLKRFEE AAFTCEYKYD GQRAQIHALE GGEVKIFSRN QEDNTGKYPD 600
    IISRIPKIKL PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE 650
    IQVQVCLYAF DLIYLNGESL VREPLSRRRQ LLRENFVETE GEFVFATSLD 700
    TKDIEQIAEF LEQSVKDSCE GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL 750
    DGVGDTLDLV VIGAYLGRGK RAGRYGGFLL ASYDEDSEEL QAICKLGTGF 800
    SDEELEEHHQ SLKALVLPSP RPYVRIDGAV IPDHWLDPSA VWEVKCADLS 850
    LSPIYPAARG LVDSDKGISL RFPRFIRVRE DKQPEQATTS AQVACLYRKQ 900
    SQIQNQQGED SGSDPEDTY 919
    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.
    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.
    ENST00000601091; ENSP00000471836; ENSG00000105486.
    GeneIDi3978.
    KEGGihsa:3978.
    UCSCiuc002pia.1. human.

    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.
    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. 6 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 .
    ENST00000601091 ; ENSP00000471836 ; ENSG00000105486 .
    GeneIDi 3978.
    KEGGi hsa:3978.
    UCSCi uc002pia.1. human.

    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.
    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

    ArrayExpressi P18858.
    Bgeei P18858.
    CleanExi HS_LIG1.
    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

    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 1, 2014
    This is version 161 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