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P49916

- DNLI3_HUMAN

UniProt

P49916 - DNLI3_HUMAN

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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).PROSITE-ProRule annotation

Cofactori

Mg2+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. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: Reactome
  2. base-excision repair, DNA ligation Source: Ensembl
  3. DNA biosynthetic process Source: InterPro
  4. DNA repair Source: Reactome
  5. double-strand break repair via nonhomologous end joining Source: Ensembl
  6. lagging strand elongation Source: RefGenome
  7. mitochondrial DNA repair Source: Ensembl
  8. negative regulation of DNA recombination Source: Ensembl
  9. nucleotide-excision repair Source: RefGenome
  10. reciprocal meiotic recombination Source: ProtInc
  11. 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

BgeeiP49916.
CleanExiHS_LIG3.
ExpressionAtlasiP49916. baseline and differential.
GenevestigatoriP49916.

Organism-specific databases

HPAiHPA006723.

Interactioni

Protein-protein interaction databases

BioGridi110168. 34 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 – 976Combined sources
Beta strandi117 – 1248Combined sources
Helixi140 – 14910Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi161 – 1655Combined sources
Turni166 – 1683Combined sources
Helixi171 – 18515Combined sources
Beta strandi188 – 1903Combined sources
Helixi259 – 2613Combined sources
Helixi263 – 27412Combined sources
Helixi279 – 29113Combined sources
Helixi303 – 3108Combined sources
Turni312 – 3143Combined sources
Helixi323 – 33412Combined sources
Helixi338 – 3447Combined sources
Helixi345 – 3473Combined sources
Helixi350 – 35910Combined sources
Beta strandi362 – 3643Combined sources
Helixi374 – 38512Combined sources
Helixi390 – 40112Combined sources
Helixi407 – 41610Combined sources
Beta strandi421 – 4233Combined sources
Helixi426 – 4316Combined sources
Helixi437 – 4437Combined sources
Helixi447 – 45913Combined sources
Beta strandi485 – 4884Combined sources
Helixi492 – 4987Combined sources
Beta strandi503 – 5075Combined sources
Beta strandi511 – 5199Combined sources
Beta strandi522 – 5265Combined sources
Helixi535 – 5373Combined sources
Turni538 – 5403Combined sources
Helixi541 – 5433Combined sources
Helixi545 – 5484Combined sources
Beta strandi553 – 56412Combined sources
Turni566 – 5683Combined sources
Helixi574 – 5774Combined sources
Helixi579 – 5846Combined sources
Beta strandi590 – 60011Combined sources
Helixi610 – 62011Combined sources
Turni625 – 6273Combined sources
Beta strandi628 – 6303Combined sources
Beta strandi633 – 6364Combined sources
Helixi639 – 65113Combined sources
Beta strandi657 – 6637Combined sources
Beta strandi671 – 6766Combined sources
Turni678 – 6803Combined sources
Beta strandi688 – 69811Combined sources
Beta strandi710 – 7167Combined sources
Turni718 – 7203Combined sources
Beta strandi721 – 7299Combined sources
Helixi735 – 7406Combined sources
Turni741 – 7433Combined sources
Beta strandi780 – 7878Combined sources
Beta strandi789 – 7913Combined sources
Beta strandi795 – 7973Combined sources
Beta strandi800 – 8045Combined sources
Beta strandi816 – 8194Combined sources
Helixi822 – 8309Combined sources
Helixi924 – 9274Combined sources
Turni930 – 9323Combined sources
Beta strandi936 – 9383Combined sources
Beta strandi942 – 9443Combined sources
Helixi952 – 96110Combined sources
Helixi969 – 9746Combined sources
Beta strandi976 – 9805Combined sources
Beta strandi982 – 9843Combined sources
Beta strandi988 – 9914Combined sources
Helixi993 – 100210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00750000117695.
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

        10         20         30         40         50
MSLAFKIFFP QTLRALSRKE LCLFRKHHWR DVRQFSQWSE TDLLHGHPLF
60 70 80 90 100
LRRKPVLSFQ GSHLRSRATY LVFLPGLHVG LCSGPCEMAE QRFCVDYAKR
110 120 130 140 150
GTAGCKKCKE KIVKGVCRIG KVVPNPFSES GGDMKEWYHI KCMFEKLERA
160 170 180 190 200
RATTKKIEDL TELEGWEELE DNEKEQITQH IADLSSKAAG TPKKKAVVQA
210 220 230 240 250
KLTTTGQVTS PVKGASFVTS TNPRKFSGFS AKPNNSGEAP SSPTPKRSLS
260 270 280 290 300
SSKCDPRHKD CLLREFRKLC AMVADNPSYN TKTQIIQDFL RKGSAGDGFH
310 320 330 340 350
GDVYLTVKLL LPGVIKTVYN LNDKQIVKLF SRIFNCNPDD MARDLEQGDV
360 370 380 390 400
SETIRVFFEQ SKSFPPAAKS LLTIQEVDEF LLRLSKLTKE DEQQQALQDI
410 420 430 440 450
ASRCTANDLK CIIRLIKHDL KMNSGAKHVL DALDPNAYEA FKASRNLQDV
460 470 480 490 500
VERVLHNAQE VEKEPGQRRA LSVQASLMTP VQPMLAEACK SVEYAMKKCP
510 520 530 540 550
NGMFSEIKYD GERVQVHKNG DHFSYFSRSL KPVLPHKVAH FKDYIPQAFP
560 570 580 590 600
GGHSMILDSE VLLIDNKTGK PLPFGTLGVH KKAAFQDANV CLFVFDCIYF
610 620 630 640 650
NDVSLMDRPL CERRKFLHDN MVEIPNRIMF SEMKRVTKAL DLADMITRVI
660 670 680 690 700
QEGLEGLVLK DVKGTYEPGK RHWLKVKKDY LNEGAMADTA DLVVLGAFYG
710 720 730 740 750
QGSKGGMMSI FLMGCYDPGS QKWCTVTKCA GGHDDATLAR LQNELDMVKI
760 770 780 790 800
SKDPSKIPSW LKVNKIYYPD FIVPDPKKAA VWEITGAEFS KSEAHTADGI
810 820 830 840 850
SIRFPRCTRI RDDKDWKSAT NLPQLKELYQ LSKEKADFTV VAGDEGSSTT
860 870 880 890 900
GGSSEENKGP SGSAVSRKAP SKPSASTKKA EGKLSNSNSK DGNMQTAKPS
910 920 930 940 950
AMKVGEKLAT KSSPVKVGEK RKAADETLCQ TKVLLDIFTG VRLYLPPSTP
960 970 980 990 1000
DFSRLRRYFV AFDGDLVQEF DMTSATHVLG SRDKNPAAQQ VSPEWIWACI

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 34 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.
GeneTreei ENSGT00750000117695.
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

Bgeei P49916.
CleanExi HS_LIG3.
ExpressionAtlasi P49916. baseline and differential.
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: November 26, 2014
This is version 162 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