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Description:
DNA ligase 1 (EC 6.5.1.1) (DNA ligase I) (Polydeoxyribonucleotidesynthase [ATP] 1).
Molecular weight: 10173
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
07-FEB-2006, entry version 62.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein DNL1_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M36067 | AAA59518.1 | - |
| EMBL | AF527418 | AAM77697.1 | - |
| PIR | A36048 | A41275. | |
| PDB | 1X9N | X-ray | A=233-919. |
| Ensembl | ENSG00000105486 | Homo sapiens.1 | |
| HGNC | HGNC:6598 | LIG1.1 | |
| MIM | 126391 | gene. | |
| Reactome | P18858 | -.1 | |
| GO | GO:0005634 | C:nucleus | TAS. |
| GO | GO:0003677 | F:DNA binding | TAS. |
| GO | GO:0003909 | F:DNA ligase activity | TAS. |
| GO | GO:0006281 | P:DNA repair | TAS. |
| GO | GO:0009653 | P:morphogenesis | TAS. |
| InterPro | IPR000977 | DNA_ligase. | |
| InterPro | IPR012309 | DNA_ligase_A_C. | |
| InterPro | IPR012310 | DNA_ligase_A_M. | |
| InterPro | IPR012308 | DNA_ligase_A_N. | |
| PANTHER | PTHR10459 | DNA_ligase.1 | 1. |
| Pfam | PF04679 | DNA_ligase_A_C | 1. |
| Pfam | PF01068 | DNA_ligase_A_M | 1. |
| Pfam | PF04675 | DNA_ligase_A_N | 1. |
| TIGRFAMs | TIGR00574 | dnl1 | 1. |
| PROSITE | PS00697 | DNA_LIGASE_A1 | 1. |
| PROSITE | PS00333 | DNA_LIGASE_A2 | 1. |
| PROSITE | PS50160 | DNA_LIGASE_A3 | 1. |
Keywords:
3D-structure; ATP-binding; Cell cycle; Cell division; Disease mutation; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nuclear protein; Nucleotide-binding; Phosphorylation; Polymorphism.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=T lymphoblast;
RX MEDLINE=90370849; PubMed=2204063;
RA Barnes D.E., Johnston L.H., Kodama K., Tomkinson A.E., Lasko D.D.,
RA Lindahl T.;
RT "Human DNA ligase I cDNA: cloning and functional expression in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6679-6683(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-24; TRP-62;
RP GLU-249; SER-267; MET-349; ILE-369; VAL-480; ILE-614 AND LEU-677.
RA Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W.,
RA Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D.,
RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE OF 716-753.
RX MEDLINE=91352039; PubMed=1881902;
RA Petrini J.H.J., Huwiler K.G., Weaver D.T.;
RT "A wild-type DNA ligase I gene is expressed in Bloom's syndrome
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7615-7619(1991).
RN [4]
RP PHOSPHORYLATION SITES SER-66; SER-76; SER-141; THR-195 AND SER-911.
RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN [5]
RP VARIANTS LYS-566 AND TRP-771.
RX MEDLINE=92257590; PubMed=1581963; DOI=10.1016/0092-8674(92)90450-Q;
RA Barnes D.E., Tomkinson A.E., Lehmann A.R., Webster A.D.B., Lindahl T.;
RT "Mutations in the DNA ligase I gene of an individual with
RT immunodeficiencies and cellular hypersensitivity to DNA-damaging
RT agents.";
RL Cell 69:495-503(1992).
Feature:
CHAIN 1 919 DNA ligase 1.
/FTId=PRO_0000059570.
ACT_SITE 568 568 N6-AMP-lysine intermediate (By
similarity).
MOD_RES 66 66 Phosphoserine.
MOD_RES 76 76 Phosphoserine.
MOD_RES 141 141 Phosphoserine.
MOD_RES 195 195 Phosphothreonine.
MOD_RES 911 911 Phosphoserine.
VARIANT 24 24 A -> V (in dbSNP:3730855).
/FTId=VAR_018802.
VARIANT 52 52 P -> L (in dbSNP:4987181).
/FTId=VAR_020194.
VARIANT 62 62 R -> W (in dbSNP:3730863).
/FTId=VAR_018803.
VARIANT 72 72 D -> G (in dbSNP:4987070).
/FTId=VAR_020195.
VARIANT 249 249 G -> E (in dbSNP:3730911).
/FTId=VAR_016766.
VARIANT 267 267 N -> S (in dbSNP:3730933).
/FTId=VAR_016767.
VARIANT 349 349 V -> M (in dbSNP:3730947).
/FTId=VAR_018804.
VARIANT 369 369 V -> I (in dbSNP:3730966).
/FTId=VAR_018805.
VARIANT 409 409 R -> H (in dbSNP:4987068).
/FTId=VAR_016768.
VARIANT 480 480 M -> V (in dbSNP:3730980).
/FTId=VAR_016769.
VARIANT 566 566 E -> K (in LIG1 deficiency).
/FTId=VAR_002262.
VARIANT 614 614 T -> I (in dbSNP:3731003).
/FTId=VAR_016770.
VARIANT 677 677 R -> L (in dbSNP:3731008).
/FTId=VAR_018806.
VARIANT 771 771 R -> W (in LIG1 deficiency).
/FTId=VAR_002263.
HELIX 263 265
TURN 268 269
STRAND 271 272
HELIX 275 278
STRAND 281 281
TURN 283 284
STRAND 285 285
STRAND 288 288
HELIX 289 300
TURN 301 301
HELIX 305 322
HELIX 324 335
TURN 336 336
STRAND 338 339
HELIX 341 343
HELIX 351 362
TURN 363 363
HELIX 366 376
TURN 377 377
HELIX 379 382
TURN 383 383
STRAND 397 397
STRAND 400 400
HELIX 401 413
STRAND 416 416
TURN 417 418
HELIX 419 433
STRAND 436 436
TURN 437 437
HELIX 438 446
TURN 447 448
STRAND 453 453
HELIX 456 469
STRAND 470 470
TURN 472 473
STRAND 476 477
STRAND 479 479
STRAND 481 481
TURN 483 486
STRAND 487 487
HELIX 489 509
STRAND 510 510
HELIX 513 527
TURN 528 528
HELIX 529 531
TURN 536 537
STRAND 538 538
STRAND 544 550
HELIX 551 557
TURN 558 560
STRAND 561 561
STRAND 563 578
TURN 580 581
STRAND 582 582
STRAND 584 587
TURN 589 590
STRAND 591 591
STRAND 593 593
TURN 595 597
HELIX 599 603
TURN 604 604
STRAND 605 605
HELIX 606 608
STRAND 609 609
TURN 611 612
STRAND 616 625
TURN 627 629
STRAND 631 632
HELIX 635 638
TURN 639 640
STRAND 641 641
STRAND 643 644
HELIX 648 650
STRAND 653 665
TURN 666 667
STRAND 668 669
TURN 671 672
STRAND 673 673
HELIX 675 685
STRAND 686 686
STRAND 689 689
TURN 690 692
STRAND 693 695
STRAND 698 699
HELIX 704 716
TURN 717 717
STRAND 718 730
STRAND 732 733
TURN 735 737
STRAND 739 746
HELIX 747 751
STRAND 752 753
STRAND 755 767
TURN 769 770
STRAND 771 772
TURN 773 773
STRAND 774 784
TURN 785 788
STRAND 789 796
STRAND 799 799
HELIX 802 814
TURN 815 815
STRAND 816 819
TURN 822 823
STRAND 824 825
STRAND 827 829
STRAND 833 836
STRAND 838 838
STRAND 841 854
TURN 857 861
STRAND 862 862
STRAND 864 865
STRAND 867 872
STRAND 874 878
TURN 880 881
HELIX 884 886
STRAND 887 887
STRAND 889 889
HELIX 890 900
Comments:
-!- FUNCTION: This protein seals, during DNA replication, DNA
recombination and DNA repair, nicks in double-stranded DNA.
-!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
(deoxyribonucleotide)(m) = AMP + diphosphate +
(deoxyribonucleotide)(n+m).
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Phosphorylated in vivo.
-!- DISEASE: Defects in LIG1 seem to cause immunodeficiencies and
cellular hypersensitivity to DNA-damaging agents.
-!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
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Sequence length: 919
MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD SPVKRPGRKA
ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE NNASLSDTSP MDSSPSGIPK
RRTARKQLPK RTIQEVLEEQ SEDEDREAKR KKEEEEEETP KESLTEAEVA TEKEGEDGDQ
PTTPPKPLKT SKAETPTESV SEPEVATKQE LQEEEEQTKP PRRAPKTLSS FFTPRKPAVK
KEVKEEEPGA PGKEGAAEGP LDPSGYNPAK NNYHPVEDAC WKPGQKVPYL AVARTFEKIE
EVSARLRMVE TLSNLLRSVV ALSPPDLLPV LYLSLNHLGP PQQGLELGVG DGVLLKAVAQ
ATGRQLESVR AEAAEKGDVG LVAENSRSTQ RLMLPPPPLT ASGVFSKFRD IARLTGSAST
AKKIDIIKGL FVACRHSEAR FIARSLSGRL RLGLAEQSVL AALSQAVSLT PPGQEFPPAM
VDAGKGKTAE ARKTWLEEQG MILKQTFCEV PDLDRIIPVL LEHGLERLPE HCKLSPGIPL
KPMLAHPTRG ISEVLKRFEE AAFTCEYKYD GQRAQIHALE GGEVKIFSRN QEDNTGKYPD
IISRIPKIKL PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE IQVQVCLYAF
DLIYLNGESL VREPLSRRRQ LLRENFVETE GEFVFATSLD TKDIEQIAEF LEQSVKDSCE
GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL DGVGDTLDLV VIGAYLGRGK RAGRYGGFLL
ASYDEDSEEL QAICKLGTGF SDEELEEHHQ SLKALVLPSP RPYVRIDGAV IPDHWLDPSA
VWEVKCADLS LSPIYPAARG LVDSDKGISL RFPRFIRVRE DKQPEQATTS AQVACLYRKQ
SQIQNQQGED SGSDPEDTY