SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P49916

- DNLI3_HUMAN

UniProt

P49916 - DNLI3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA ligase 3

Gene
LIG3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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).

Cofactori

Magnesium By similarity.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri93 – 18593PARP-typeAdd
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
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, 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
Complete GO annotation...

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.

Miscellaneous databases

EvolutionaryTraceiP49916.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini933 – 100977BRCTAdd
BLAST

Sequence similaritiesi

Contains 1 BRCT domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri93 – 18593PARP-typeAdd
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. VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 159 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

Similar proteinsi