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Protein

DNA ligase

Gene

LIG1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Biological processi

DNA damage, DNA recombinationUniRule annotation, DNA repairUniRule annotation, DNA replicationUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligaseUniRule annotation (EC:6.5.1.1UniRule annotation)
Gene namesi
Name:LIG1Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6598. LIG1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

EPDiF5GZ28.

Expressioni

Gene expression databases

BgeeiF5GZ28.
ExpressionAtlasiF5GZ28. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliF5GZ28.
SMRiF5GZ28. Positions 194-833.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini580 – 716137DNA_LIGASE_A3InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ATP-dependent DNA ligase family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00840000129855.

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]

Sequencei

Sequence statusi: Complete.

F5GZ28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD
60 70 80 90 100
SPVKRPGRKA ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE
110 120 130 140 150
NNASLSDTSP MDSSPSGIPK RRTEAETPTE SVSEPEVATK QELQEEEEQT
160 170 180 190 200
KPPRRAPKTL SSFFTPRKPA VKKEVKEEEP GAPGKEGAAE GPLDPSGYNP
210 220 230 240 250
AKNNYHPVED ACWKPGQKVP YLAVARTFEK IEEVSARLRM VETLSNLLRS
260 270 280 290 300
VVALSPPDLL PVLYLSLNHL GPPQQGLELG VGDGVLLKAV AQATGRQLES
310 320 330 340 350
VRAEAAEKGD VGLVAENSRS TQRLMLPPPP LTASGVFSKF RDIARLTGSA
360 370 380 390 400
STAKKIDIIK GLFVACRHSE ARFIARSLSG RLRLGLAEQS VLAALSQAVS
410 420 430 440 450
LTPPGQEFPP AMVDAGKGKT AEARKTWLEE QGMILKQTFC EVPDLDRIIP
460 470 480 490 500
VLLEHGLERL PEHCKLSPGI PLKPMLAHPT RGISEVLKRF EEAAFTCEYK
510 520 530 540 550
YDGQRAQIHA LEGGEVKIFS RNQEDNTGKY PDIISRIPKI KLPSVTSFIL
560 570 580 590 600
DTEAVAWDRE KKQIQPFQVL TTRKRKEVDA SEIQVQVCLY AFDLIYLNGE
610 620 630 640 650
SLVREPLSRR RQLLRENFVE TEGEFVFATS LDTKDIEQIA EFLEQSVKDS
660 670 680 690 700
CEGLMVKTLD VDATYEIAKR SHNWLKLKKD YLDGVGDTLD LVVIGAYLGR
710 720 730 740 750
GKRAGRYGGF LLASYDEDSE ELQAICKLGT GFSDEELEEH HQSLKALVLP
760 770 780 790 800
SPRPYVRIDG AVIPDHWLDP SAVWEVKCAD LSLSPIYPAA RGLVDSDKGI
810 820 830 840 850
SLRFPRFIRV REDKQPEQAT TSAQVACLYR KQSQIQNQQG EDSGSDPEDT

Y
Length:851
Mass (Da):93,948
Last modified:June 28, 2011 - v1
Checksum:i962BAEBE37E672CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011466 Genomic DNA. No translation available.
KC877741 Genomic DNA. No translation available.
RefSeqiNP_001275993.1. NM_001289064.1.
UniGeneiHs.1770.

Genome annotation databases

EnsembliENST00000536218; ENSP00000441531; ENSG00000105486.
GeneIDi3978.
UCSCiuc010xzf.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011466 Genomic DNA. No translation available.
KC877741 Genomic DNA. No translation available.
RefSeqiNP_001275993.1. NM_001289064.1.
UniGeneiHs.1770.

3D structure databases

ProteinModelPortaliF5GZ28.
SMRiF5GZ28. Positions 194-833.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

EPDiF5GZ28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000536218; ENSP00000441531; ENSG00000105486.
GeneIDi3978.
UCSCiuc010xzf.3. human.

Organism-specific databases

CTDi3978.
HGNCiHGNC:6598. LIG1.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00840000129855.

Miscellaneous databases

ChiTaRSiLIG1. human.
GenomeRNAii3978.

Gene expression databases

BgeeiF5GZ28.
ExpressionAtlasiF5GZ28. baseline and differential.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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].
  3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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].
  7. "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].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF5GZ28_HUMAN
AccessioniPrimary (citable) accession number: F5GZ28
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 8, 2016
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.