Reviewed, UniProtKB/Swiss-Prot P11387 (TOP1_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA topoisomerase 1
    EC=5.99.1.2
Alternative name(s):
    DNA topoisomerase I

Gene names

Name:

TOP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	765 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another.
Catalytic activity	ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Enzyme regulation	Specifically inhibited by camptothecin (CPT), a plant alkaloid with antitumor activity.
Subunit structure	Monomer. Interacts with SV40 Large T antigen; this interactions allows viral DNA replication. Ref.14
Subcellular location	Nucleus › nucleolus. Nucleus › nucleoplasm. Note: Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumolyated forms found in both nucleoplasm and nucleoli. Ref.13
Post-translational modification	Sumoylated. Lys-117 is the main site of sumoylation. Sumoylation plays a role in partitioning TOP1 between nucleoli and nucleoplasm. Levels are dramatically increased on camptothecin (CPT) treatment. Ref.13
Involvement in disease	A chromosomal aberration involving TOP1 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with NUP98.
Miscellaneous	Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils. When a topoisomerase transiently breaks a DNA backbone bond, it simultaneously forms a protein-DNA link, in which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus at one end of the enzyme-severed DNA strand.
Sequence similarities	Belongs to the eukaryotic type I topoisomerase family.
Sequence caution	The sequence CAA36834.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA unwinding during replication Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Non-traceable author statement. Source: UniProtKB programmed cell death Non-traceable author statement. Source: UniProtKB response to drug Inferred from expression pattern. Source: UniProtKB
Cellular component	chromosome Inferred from electronic annotation. Source: InterPro nucleolus Inferred from direct assay. Source: UniProtKB nucleoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: InterPro DNA topoisomerase type I activity Inferred from mutant phenotype. Source: UniProtKB chromatin binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NKX3-1	Q99801	3	EBI-876302,EBI-1385894

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 765

764

DNA topoisomerase 1

PRO_0000145201

Regions

Compositional bias

23 – 204

182

Lys-rich

Sites

Active site

723

1

O-(3'-phospho-DNA)-tyrosine intermediate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.7

Modified residue

280

1

N6-acetyllysine Ref.16

Cross-link

103

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Cross-link

117

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Cross-link

153

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Natural variations

Natural variant

214

1

G → S: dbSNP rs6029542.

VAR_052592

Natural variant

326

1

K → R in breast cancer; somatic mutation. Ref.22

VAR_036555

Natural variant

370

1

M → T in CPT-resistant leukemia. Ref.8

VAR_010666

Natural variant

533

1

D → G in CPT-resistant leukemia. Ref.20

VAR_007530

Natural variant

722

1

N → S in CPT-resistant leukemia. Ref.8

VAR_010667

Natural variant

729

1

T → A in CPT-resistant lung cancer. Ref.21

VAR_007531

Experimental info

Mutagenesis

103

1

K → R: Localizes in both nucleoplasm and nucleoli; when associated with R-117 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-117 and R-153. Ref.13

Mutagenesis

117

1

K → R: 5-fold decrease in sumoylation. Localizes in both nucleoplasm and nucleoli; when associated with or without R-103 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-153. Ref.13

Mutagenesis

153

1

K → R: Localizes in both nucleoplasm and nucleoli; when associated with R-103 or R-117. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-117. Ref.13

Mutagenesis

723

1

Y → F: No change in CPT-induced clearing from nuclei. Ref.13

Sequence conflict

145

1

A → V in AAA61207. Ref.1

Secondary structure

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765

Helix Strand Turn

Details...

Helix

205 – 207

3

Helix

251 – 261

11

Turn

262 – 265

4

Helix

267 – 270

4

Helix

272 – 285

14

Helix

288 – 293

6

Helix

297 – 299

3

Helix

303 – 317

15

Helix

321 – 338

18

Beta strand

339 – 343

5

Beta strand

346 – 351

6

Beta strand

358 – 360

3

Beta strand

364 – 366

3

Turn

368 – 371

4

Helix

379 – 381

3

Beta strand

383 – 385

3

Beta strand

402 – 405

4

Beta strand

413 – 417

5

Turn

419 – 421

3

Beta strand

424 – 427

4

Helix

434 – 464

31

Helix

470 – 485

16

Turn

495 – 497

3

Helix

504 – 506

3

Helix

509 – 511

3

Beta strand

514 – 518

5

Beta strand

521 – 530

10

Helix

532 – 534

3

Beta strand

536 – 542

7

Helix

545 – 553

9

Turn

554 – 557

4

Turn

564 – 567

4

Helix

570 – 580

11

Helix

586 – 605

20

Helix

612 – 625

14

Turn

721 – 723

3

Helix

726 – 735

10

Helix

740 – 742

3

Helix

746 – 751

6

Helix

753 – 758

6

Sequences

	Sequence		Length	Mass (Da)
	P11387-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 6FBED540BCF7BE28	FASTA	765	90,726
	10 20 30 40 50 60 MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK EKDREKSKHS NSEHKDSEKK 70 80 90 100 110 120 HKEKEKTKHK DGSSEKHKDK HKDRDKEKRK EEKVRASGDA KIKKEKENGF SSPPQIKDEP 130 140 150 160 170 180 EDDGYFVPPK EDIKPLKRPR DEDDADYKPK KIKTEDTKKE KKRKLEEEED GKLKKPKNKD 190 200 210 220 230 240 KDKKVPEPDN KKKKPKKEEE QKWKWWEEER YPEGIKWKFL EHKGPVFAPP YEPLPENVKF 250 260 270 280 290 300 YYDGKVMKLS PKAEEVATFF AKMLDHEYTT KEIFRKNFFK DWRKEMTNEE KNIITNLSKC 310 320 330 340 350 360 DFTQMSQYFK AQTEARKQMS KEEKLKIKEE NEKLLKEYGF CIMDNHKERI ANFKIEPPGL 370 380 390 400 410 420 FRGRGNHPKM GMLKRRIMPE DIIINCSKDA KVPSPPPGHK WKEVRHDNKV TWLVSWTENI 430 440 450 460 470 480 QGSIKYIMLN PSSRIKGEKD WQKYETARRL KKCVDKIRNQ YREDWKSKEM KVRQRAVALY 490 500 510 520 530 540 FIDKLALRAG NEKEEGETAD TVGCCSLRVE HINLHPELDG QEYVVEFDFL GKDSIRYYNK 550 560 570 580 590 600 VPVEKRVFKN LQLFMENKQP EDDLFDRLNT GILNKHLQDL MEGLTAKVFR TYNASITLQQ 610 620 630 640 650 660 QLKELTAPDE NIPAKILSYN RANRAVAILC NHQRAPPKTF EKSMMNLQTK IDAKKEQLAD 670 680 690 700 710 720 ARRDLKSAKA DAKVMKDAKT KKVVESKKKA VQRLEEQLMK LEVQATDREE NKQIALGTSK 730 740 750 760 LNYLDPRITV AWCKKWGVPI EKIYNKTQRE KFAWAIDMAD EDYEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of human DNA topoisomerase I: catalytic activity of a 67.7-kDa carboxyl-terminal fragment." D'Arpa P., Machlin P.S., Ratrie H. III, Rothfield N.F., Cleveland D.W., Earnshaw W.C. Proc. Natl. Acad. Sci. U.S.A. 85:2543-2547(1988) [PubMed: 2833744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of the human type I DNA topoisomerase gene." Kunze N., Yang G., Dolberg M., Sundarp R., Knippers R., Richter A. J. Biol. Chem. 266:9610-9616(1991) [PubMed: 1851751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Structural characterisation of the human DNA topoisomerase I gene promoter." Kunze N., Klein M., Richter A., Knippers R. Eur. J. Biochem. 194:323-330(1990) [PubMed: 2176592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
[7]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17; 107-117; 224-239; 253-262; 292-299; 355-362; 426-434; 476-484; 509-532; 550-587; 591-615; 625-634; 656-663; 694-712; 721-734 AND 736-742, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[8]	"Mutation at the catalytic site of topoisomerase I in CEM/C2, a human leukemia cell line resistant to camptothecin." Fujimori A., Harker W.G., Kohlhagen G., Hoki Y., Pommier Y. Cancer Res. 55:1339-1346(1995) [PubMed: 7882333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-765, VARIANTS CPT-RESISTNAT LEUKEMIA THR-370 AND SER-722. Tissue: Peripheral blood.
[9]	"Monoclonal antibodies neutralizing mammalian DNA topoisomerase I activity." Oddou P., Schmidt U., Knippers R., Richter A. Eur. J. Biochem. 177:523-529(1988) [PubMed: 2461859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 344-765.
[10]	"Characterization of the 3' region of the human DNA topoisomerase I gene." Zhou B.S., Bastow K.F., Cheng Y.C. Cancer Res. 49:3922-3927(1989) [PubMed: 2544263] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 541-765.
[11]	"Determination of an epitope of the diffuse systemic sclerosis marker antigen DNA topoisomerase I: sequence similarity with retroviral p30gag protein suggests a possible cause for autoimmunity in systemic sclerosis." Maul G.G., Jimenez S.A., Riggs E., Ziemnicka-Kotula D. Proc. Natl. Acad. Sci. U.S.A. 86:8492-8496(1989) [PubMed: 2479024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 657-765.
[12]	"The t(11;20)(p15;q11) chromosomal translocation associated with therapy-related myelodysplastic syndrome results in an NUP98-TOP1 fusion." Ahuja H.G., Felix C.A., Aplan P.D. Blood 94:3258-3261(1999) [PubMed: 10556215] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98.
[13]	"Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin." Rallabhandi P., Hashimoto K., Mo Y.-Y., Beck W.T., Moitra P.K., D'Arpa P. J. Biol. Chem. 277:40020-40026(2002) [PubMed: 12149243] [Abstract] Cited for: SUMOYLATION AT LYS-117, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-103; LYS-117; LYS-153 AND TYR-723.
[14]	"Simian virus 40 DNA replication is dependent on an interaction between topoisomerase I and the C-terminal end of T antigen." Khopde S., Simmons D.T. J. Virol. 82:1136-1145(2008) [PubMed: 18003733] [Abstract] Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, MASS SPECTROMETRY.
[17]	"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA." Redinbo M.R., Stewart L., Kuhn P., Champoux J.J., Hol W.G.J. Science 279:1504-1513(1998) [PubMed: 9488644] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 215-765.
[18]	"A model for the mechanism of human topoisomerase I." Stewart L., Redinbo M.R., Qiu X., Hol W.G.J., Champoux J.J. Science 279:1534-1541(1998) [PubMed: 9488652] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 215-765.
[19]	"Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA." Redinbo M.R., Champoux J.J., Hol W.G.J. Biochemistry 39:6832-6840(2000) [PubMed: 10841763] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 203-903 IN COMPLEX WITH DNA.
[20]	"Molecular cloning of a cDNA of a camptothecin-resistant human DNA topoisomerase I and identification of mutation sites." Tamura H., Kohchi C., Yamada R., Ikeda T., Koiwai O., Patterson E., Keene J.D., Okada K., Kjeldsen E., Nishikawa K. Nucleic Acids Res. 19:69-75(1991) [PubMed: 1849260] [Abstract] Cited for: VARIANT CPT-RESISTANT LEUKEMIA GLY-533.
[21]	"Detection of topoisomerase I gene point mutation in CPT-11 resistant lung cancer cell line." Kubota N., Kanzawa F., Nishio K., Takeda Y., Ohmori T., Fujiwara Y., Terashima Y., Saijo N. Biochem. Biophys. Res. Commun. 188:571-577(1992) [PubMed: 1332703] [Abstract] Cited for: VARIANT CPT-RESISTANT LUNG CANCER ALA-729.
[22]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] BREAST CANCER ARG-326.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

J03250 mRNA. Translation: AAA61207.1.
M60706 , M60688, M60689, M60690, M60691, M60692, M60693, M60694, M60695, M60696, M60697, M60698, M60699, M60700, M60701, M60702, M60703, M60704, M60705 Genomic DNA. Translation: AAA61206.1.
AK292943 mRNA. Translation: BAF85632.1.
AL035652, AL022394 Genomic DNA. Translation: CAI19767.1.
AL022394, AL035652 Genomic DNA. Translation: CAI42886.1.
CH471077 Genomic DNA. Translation: EAW75994.1.
X52601 Genomic DNA. Translation: CAA36834.1. Sequence problems.
U07804 mRNA. Translation: AAB60379.1.
U07806 mRNA. Translation: AAB60380.1.
X16479 mRNA. Translation: CAA34500.2.
M27913 mRNA. Translation: AAA61208.1.

IPI

IPI00413611.

PIR

ISHUT1. A30887.

RefSeq

NP_003277.1.

UniGene

Hs.472737
Hs.712686

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A31	X-ray	2.10	A	175-765	[»]
1A35	X-ray	2.50	A	175-765	[»]
1A36	X-ray	2.80	A	175-765	[»]
1EJ9	X-ray	2.60	A	203-765	[»]
1K4S	X-ray	3.20	A	174-765	[»]
1K4T	X-ray	2.10	A	174-765	[»]
1LPQ	X-ray	3.14	A	202-765	[»]
1NH3	X-ray	3.10	A	203-764	[»]
1R49	X-ray	3.13	A	174-765	[»]
1RR8	X-ray	2.60	C	203-765	[»]
1RRJ	X-ray	2.30	A	201-765	[»]
1SC7	X-ray	3.00	A	174-765	[»]
1SEU	X-ray	3.00	A	174-765	[»]
1T8I	X-ray	3.00	A	174-765	[»]
1TL8	X-ray	3.10	A	174-765	[»]

DisProt

DP00075.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11387. 40 interactions.

STRING

P11387.

PTM databases

PhosphoSite

P11387.

2-D gel databases

SWISS-2DPAGE

P11387.

Aarhus/Ghent-2DPAGE

610. NEPHGE.

Proteomic databases

PeptideAtlas

P11387.

PRIDE

P11387.

Genome annotation databases

Ensembl

ENST00000361337; ENSP00000354522; ENSG00000198900; Homo sapiens. [Genome view]

GeneID

7150.

KEGG

hsa:7150.

UCSC

uc002xjl.1. human.

Organism-specific databases

CTD

7150.

GeneCards

GC20P039090.

HGNC

HGNC:11986. TOP1.

HPA

CAB009058.
HPA019039.

MIM

126420. gene.

PharmGKB

PA134883507.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P11387.

Enzyme and pathway databases

BRENDA

5.99.1.2. 247.

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.

Gene expression databases

ArrayExpress

P11387.

Bgee

P11387.

CleanEx

HS_TOP1.

Genevestigator

P11387.

GermOnline

ENSG00000198900. Homo sapiens.

Family and domain databases

InterPro

IPR018521. TopoI_AS.
IPR001631. TopoI_C.
IPR013499. TopoI_C_euk.
IPR014711. TopoI_cat_a-hlx-sub_euk.
IPR014727. TopoI_cat_a/b-sub_euk.
IPR013500. TopoI_cat_euk.
IPR013030. TopoI_DNA-bd_mixed-a/b_euk.
IPR008336. TopoI_DNA_bd_euk.
[Graphical view]

Gene3D

G3DSA:3.90.15.10. TopoI_cat_a-hlx-sub_euk. 1 hit.
G3DSA:1.10.132.10. TopoI_cat_a/b-sub_euk. 1 hit.
G3DSA:2.170.11.10. TopoI_DNA-bd_mixed-a/b_euk. 1 hit.

Pfam

PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view]

PRINTS

PR00416. EUTPISMRASEI.

SMART

SM00435. TOPEUc. 1 hit.
[Graphical view]

PROSITE

PS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00762. Irinotecan.
DB04967. Lucanthone.
DB01030. Topotecan.

NextBio

27982.

PMAP-CutDB

P11387.

SOURCE

Search...

Entry information

Entry name

TOP1_HUMAN

Accession

Primary (citable) accession number: P11387
Secondary accession number(s): A8KA78 , O43256, Q12855, Q12856, Q15610, Q5TFY3, Q9UJN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	December 1, 2000
Last modified:	November 3, 2009
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.