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P49916

- DNLI3_HUMAN

UniProt

P49916 - DNLI3_HUMAN

Protein

DNA ligase 3

Gene

LIG3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    Interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.

    Catalytic activityi

    ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).PROSITE-ProRule annotation

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei506 – 5061ATPBy similarity
    Active sitei508 – 5081N6-AMP-lysine intermediatePROSITE-ProRule annotation
    Binding sitei513 – 5131ATPBy similarity
    Binding sitei528 – 5281ATPBy similarity
    Metal bindingi560 – 5601Magnesium 1By similarity
    Metal bindingi655 – 6551Magnesium 2By similarity
    Binding sitei660 – 6601ATPBy similarity
    Binding sitei671 – 6711ATPBy similarity
    Binding sitei675 – 6751ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri93 – 18593PARP-typePROSITE-ProRule annotationAdd
    BLAST

    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. protein binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: Reactome
    2. base-excision repair, DNA ligation Source: Ensembl
    3. DNA repair Source: Reactome
    4. double-strand break repair via nonhomologous end joining Source: Ensembl
    5. lagging strand elongation Source: RefGenome
    6. mitochondrial DNA repair Source: Ensembl
    7. negative regulation of DNA recombination Source: Ensembl
    8. nucleotide-excision repair Source: RefGenome
    9. reciprocal meiotic recombination Source: ProtInc
    10. spermatogenesis Source: ProtInc

    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, Zinc

    Enzyme and pathway databases

    BRENDAi6.5.1.1. 2681.
    ReactomeiREACT_933. Resolution of AP sites via the single-nucleotide replacement pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA ligase 3 (EC:6.5.1.1)
    Alternative name(s):
    DNA ligase III
    Polydeoxyribonucleotide synthase [ATP] 3
    Gene namesi
    Name:LIG3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6600. LIG3.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: RefGenome
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. synaptonemal complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30374.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10091009DNA ligase 3PRO_0000059574Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei210 – 2101Phosphoserine3 Publications
    Modified residuei227 – 2271Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49916.
    PaxDbiP49916.
    PRIDEiP49916.

    PTM databases

    PhosphoSiteiP49916.

    Expressioni

    Tissue specificityi

    Testis, thymus, prostate and heart.

    Gene expression databases

    ArrayExpressiP49916.
    BgeeiP49916.
    CleanExiHS_LIG3.
    GenevestigatoriP49916.

    Organism-specific databases

    HPAiHPA006723.

    Interactioni

    Protein-protein interaction databases

    BioGridi110168. 22 interactions.
    IntActiP49916. 7 interactions.
    MINTiMINT-4531178.
    STRINGi9606.ENSP00000367787.

    Structurei

    Secondary structure

    1
    1009
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 976
    Beta strandi117 – 1248
    Helixi140 – 14910
    Beta strandi152 – 1543
    Beta strandi161 – 1655
    Turni166 – 1683
    Helixi171 – 18515
    Beta strandi188 – 1903
    Helixi259 – 2613
    Helixi263 – 27412
    Helixi279 – 29113
    Helixi303 – 3108
    Turni312 – 3143
    Helixi323 – 33412
    Helixi338 – 3447
    Helixi345 – 3473
    Helixi350 – 35910
    Beta strandi362 – 3643
    Helixi374 – 38512
    Helixi390 – 40112
    Helixi407 – 41610
    Beta strandi421 – 4233
    Helixi426 – 4316
    Helixi437 – 4437
    Helixi447 – 45913
    Beta strandi485 – 4884
    Helixi492 – 4987
    Beta strandi503 – 5075
    Beta strandi511 – 5199
    Beta strandi522 – 5265
    Helixi535 – 5373
    Turni538 – 5403
    Helixi541 – 5433
    Helixi545 – 5484
    Beta strandi553 – 56412
    Turni566 – 5683
    Helixi574 – 5774
    Helixi579 – 5846
    Beta strandi590 – 60011
    Helixi610 – 62011
    Turni625 – 6273
    Beta strandi628 – 6303
    Beta strandi633 – 6364
    Helixi639 – 65113
    Beta strandi657 – 6637
    Beta strandi671 – 6766
    Turni678 – 6803
    Beta strandi688 – 69811
    Beta strandi710 – 7167
    Turni718 – 7203
    Beta strandi721 – 7299
    Helixi735 – 7406
    Turni741 – 7433
    Beta strandi780 – 7878
    Beta strandi789 – 7913
    Beta strandi795 – 7973
    Beta strandi800 – 8045
    Beta strandi816 – 8194
    Helixi822 – 8309
    Helixi924 – 9274
    Turni930 – 9323
    Beta strandi936 – 9383
    Beta strandi942 – 9443
    Helixi952 – 96110
    Helixi969 – 9746
    Beta strandi976 – 9805
    Beta strandi982 – 9843
    Beta strandi988 – 9914
    Helixi993 – 100210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IMONMR-A924-1009[»]
    1IN1NMR-A924-1009[»]
    1UW0NMR-A88-204[»]
    3L2PX-ray3.00A257-833[»]
    3PC7X-ray1.65A/B924-1009[»]
    3PC8X-ray2.31C/D924-1008[»]
    3QVGX-ray2.26A/C924-1008[»]
    ProteinModelPortaliP49916.
    SMRiP49916. Positions 88-204, 257-833, 928-1008.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49916.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini933 – 100977BRCTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ATP-dependent DNA ligase family.Curated
    Contains 1 BRCT domain.PROSITE-ProRule annotation
    Contains 1 PARP-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri93 – 18593PARP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1793.
    HOGENOMiHOG000007653.
    HOVERGENiHBG005515.
    InParanoidiP49916.
    KOiK10776.
    OMAiLFSEMKH.
    OrthoDBiEOG7BKCT2.
    PhylomeDBiP49916.
    TreeFamiTF316220.

    Family and domain databases

    Gene3Di1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1740.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    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.
    IPR001510. Znf_PARP.
    [Graphical view]
    PfamiPF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF04675. DNA_ligase_A_N. 1 hit.
    PF00645. zf-PARP. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 1 hit.
    [Graphical view]
    SUPFAMiSSF117018. SSF117018. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF52113. SSF52113. 1 hit.
    TIGRFAMsiTIGR00574. dnl1. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS00697. DNA_LIGASE_A1. 1 hit.
    PS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    PS00347. PARP_ZN_FINGER_1. 1 hit.
    PS50064. PARP_ZN_FINGER_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: P49916-1) [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

    MSLAFKIFFP QTLRALSRKE LCLFRKHHWR DVRQFSQWSE TDLLHGHPLF     50
    LRRKPVLSFQ GSHLRSRATY LVFLPGLHVG LCSGPCEMAE QRFCVDYAKR 100
    GTAGCKKCKE KIVKGVCRIG KVVPNPFSES GGDMKEWYHI KCMFEKLERA 150
    RATTKKIEDL TELEGWEELE DNEKEQITQH IADLSSKAAG TPKKKAVVQA 200
    KLTTTGQVTS PVKGASFVTS TNPRKFSGFS AKPNNSGEAP SSPTPKRSLS 250
    SSKCDPRHKD CLLREFRKLC AMVADNPSYN TKTQIIQDFL RKGSAGDGFH 300
    GDVYLTVKLL LPGVIKTVYN LNDKQIVKLF SRIFNCNPDD MARDLEQGDV 350
    SETIRVFFEQ SKSFPPAAKS LLTIQEVDEF LLRLSKLTKE DEQQQALQDI 400
    ASRCTANDLK CIIRLIKHDL KMNSGAKHVL DALDPNAYEA FKASRNLQDV 450
    VERVLHNAQE VEKEPGQRRA LSVQASLMTP VQPMLAEACK SVEYAMKKCP 500
    NGMFSEIKYD GERVQVHKNG DHFSYFSRSL KPVLPHKVAH FKDYIPQAFP 550
    GGHSMILDSE VLLIDNKTGK PLPFGTLGVH KKAAFQDANV CLFVFDCIYF 600
    NDVSLMDRPL CERRKFLHDN MVEIPNRIMF SEMKRVTKAL DLADMITRVI 650
    QEGLEGLVLK DVKGTYEPGK RHWLKVKKDY LNEGAMADTA DLVVLGAFYG 700
    QGSKGGMMSI FLMGCYDPGS QKWCTVTKCA GGHDDATLAR LQNELDMVKI 750
    SKDPSKIPSW LKVNKIYYPD FIVPDPKKAA VWEITGAEFS KSEAHTADGI 800
    SIRFPRCTRI RDDKDWKSAT NLPQLKELYQ LSKEKADFTV VAGDEGSSTT 850
    GGSSEENKGP SGSAVSRKAP SKPSASTKKA EGKLSNSNSK DGNMQTAKPS 900
    AMKVGEKLAT KSSPVKVGEK RKAADETLCQ TKVLLDIFTG VRLYLPPSTP 950
    DFSRLRRYFV AFDGDLVQEF DMTSATHVLG SRDKNPAAQQ VSPEWIWACI 1000
    RKRRLVAPC 1009
    Length:1,009
    Mass (Da):112,907
    Last modified:July 7, 2009 - v2
    Checksum:i0E4057E33C3F19A6
    GO
    Isoform Beta (identifier: P49916-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         933-1009: VLLDIFTGVR...IRKRRLVAPC → RRPASEQRGRTVPAGRR

    Show »
    Length:949
    Mass (Da):106,018
    Checksum:i0C10E40E0686DB77
    GO

    Sequence cautioni

    The sequence AAA85022.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAL91592.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA59230.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti224 – 2241R → W.
    Corresponds to variant rs3744356 [ dbSNP | Ensembl ].
    VAR_020196
    Natural varianti717 – 7171D → N in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036513
    Natural varianti867 – 8671R → H.1 Publication
    Corresponds to variant rs3136025 [ dbSNP | Ensembl ].
    VAR_018807
    Natural varianti898 – 8981K → T.
    Corresponds to variant rs4986974 [ dbSNP | Ensembl ].
    VAR_021938
    Natural varianti986 – 9861P → S.
    Corresponds to variant rs4986973 [ dbSNP | Ensembl ].
    VAR_020197

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei933 – 100977VLLDI…LVAPC → RRPASEQRGRTVPAGRR in isoform Beta. 1 PublicationVSP_001302Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84740 mRNA. Translation: CAA59230.1. Different initiation.
    U40671 mRNA. Translation: AAA85022.1. Different initiation.
    AF491645 Genomic DNA. Translation: AAL91592.1. Different initiation.
    AC004223 Genomic DNA. No translation available.
    AC022903 Genomic DNA. No translation available.
    CH471147 Genomic DNA. Translation: EAW80199.1.
    BC068005 mRNA. Translation: AAH68005.1.
    CCDSiCCDS11284.2. [P49916-1]
    CCDS11285.2. [P49916-2]
    PIRiI37292.
    RefSeqiNP_002302.2. NM_002311.4. [P49916-2]
    NP_039269.2. NM_013975.3. [P49916-1]
    XP_005258028.1. XM_005257971.2. [P49916-1]
    UniGeneiHs.100299.

    Genome annotation databases

    EnsembliENST00000262327; ENSP00000262327; ENSG00000005156. [P49916-2]
    ENST00000378526; ENSP00000367787; ENSG00000005156. [P49916-1]
    GeneIDi3980.
    KEGGihsa:3980.
    UCSCiuc002hik.2. human. [P49916-1]

    Polymorphism databases

    DMDMi251757259.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    DNA ligase entry

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84740 mRNA. Translation: CAA59230.1 . Different initiation.
    U40671 mRNA. Translation: AAA85022.1 . Different initiation.
    AF491645 Genomic DNA. Translation: AAL91592.1 . Different initiation.
    AC004223 Genomic DNA. No translation available.
    AC022903 Genomic DNA. No translation available.
    CH471147 Genomic DNA. Translation: EAW80199.1 .
    BC068005 mRNA. Translation: AAH68005.1 .
    CCDSi CCDS11284.2. [P49916-1 ]
    CCDS11285.2. [P49916-2 ]
    PIRi I37292.
    RefSeqi NP_002302.2. NM_002311.4. [P49916-2 ]
    NP_039269.2. NM_013975.3. [P49916-1 ]
    XP_005258028.1. XM_005257971.2. [P49916-1 ]
    UniGenei Hs.100299.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IMO NMR - A 924-1009 [» ]
    1IN1 NMR - A 924-1009 [» ]
    1UW0 NMR - A 88-204 [» ]
    3L2P X-ray 3.00 A 257-833 [» ]
    3PC7 X-ray 1.65 A/B 924-1009 [» ]
    3PC8 X-ray 2.31 C/D 924-1008 [» ]
    3QVG X-ray 2.26 A/C 924-1008 [» ]
    ProteinModelPortali P49916.
    SMRi P49916. Positions 88-204, 257-833, 928-1008.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110168. 22 interactions.
    IntActi P49916. 7 interactions.
    MINTi MINT-4531178.
    STRINGi 9606.ENSP00000367787.

    Chemistry

    DrugBanki DB00290. Bleomycin.

    PTM databases

    PhosphoSitei P49916.

    Polymorphism databases

    DMDMi 251757259.

    Proteomic databases

    MaxQBi P49916.
    PaxDbi P49916.
    PRIDEi P49916.

    Protocols and materials databases

    DNASUi 3980.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262327 ; ENSP00000262327 ; ENSG00000005156 . [P49916-2 ]
    ENST00000378526 ; ENSP00000367787 ; ENSG00000005156 . [P49916-1 ]
    GeneIDi 3980.
    KEGGi hsa:3980.
    UCSCi uc002hik.2. human. [P49916-1 ]

    Organism-specific databases

    CTDi 3980.
    GeneCardsi GC17P033307.
    HGNCi HGNC:6600. LIG3.
    HPAi HPA006723.
    MIMi 600940. gene.
    neXtProti NX_P49916.
    PharmGKBi PA30374.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1793.
    HOGENOMi HOG000007653.
    HOVERGENi HBG005515.
    InParanoidi P49916.
    KOi K10776.
    OMAi LFSEMKH.
    OrthoDBi EOG7BKCT2.
    PhylomeDBi P49916.
    TreeFami TF316220.

    Enzyme and pathway databases

    BRENDAi 6.5.1.1. 2681.
    Reactomei REACT_933. Resolution of AP sites via the single-nucleotide replacement pathway.

    Miscellaneous databases

    ChiTaRSi LIG3. human.
    EvolutionaryTracei P49916.
    GeneWikii LIG3.
    GenomeRNAii 3980.
    NextBioi 15598.
    PROi P49916.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49916.
    Bgeei P49916.
    CleanExi HS_LIG3.
    Genevestigatori P49916.

    Family and domain databases

    Gene3Di 1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1740.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    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.
    IPR001510. Znf_PARP.
    [Graphical view ]
    Pfami PF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF04675. DNA_ligase_A_N. 1 hit.
    PF00645. zf-PARP. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF117018. SSF117018. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF52113. SSF52113. 1 hit.
    TIGRFAMsi TIGR00574. dnl1. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS00697. DNA_LIGASE_A1. 1 hit.
    PS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    PS00347. PARP_ZN_FINGER_1. 1 hit.
    PS50064. PARP_ZN_FINGER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination."
      Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C., Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E., Haseltine W.A., Lindahl T.
      Mol. Cell. Biol. 15:3206-3216(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
      Tissue: Prostate.
    2. "Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination."
      Chen J., Tomkinson A.E., Ramos W., Mackey Z.B., Danehower S., Walter C.A., Schultz R.A., Besterman J.M., Husain I.
      Mol. Cell. Biol. 15:5412-5422(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
      Tissue: Testis.
    3. NIEHS SNPs program
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-867.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [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] (ISOFORM ALPHA).
      Tissue: Pancreas.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Expression, purification, and biophysical characterization of the BRCT domain of human DNA ligase IIIalpha."
      Thornton K.H., Krishnan V.V., West M.G., Popham J., Ramirez M., Thelen M.P., Cosman M.
      Protein Expr. Purif. 21:401-411(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 924-1009.
    16. "Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha."
      Kulczyk A.W., Yang J.C., Neuhaus D.
      J. Mol. Biol. 341:723-738(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-204.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-717.

    Entry informationi

    Entry nameiDNLI3_HUMAN
    AccessioniPrimary (citable) accession number: P49916
    Secondary accession number(s): Q16714, Q6NVK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 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 17
      Human chromosome 17: 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