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Protein

DNA topoisomerase 1

Gene

TOP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter.By similarity5 Publications

Miscellaneous

Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.

Catalytic activityi

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.PROSITE-ProRule annotation3 Publications

Activity regulationi

Specifically inhibited by camptothecin (CPT), a plant alkaloid with antitumor activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei723O-(3'-phospho-DNA)-tyrosine intermediatePROSITE-ProRule annotation7 Publications1

GO - Molecular functioni

GO - Biological processi

  • chromatin remodeling Source: UniProtKB
  • chromosome segregation Source: GO_Central
  • circadian regulation of gene expression Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • DNA replication Source: GO_Central
  • DNA topological change Source: UniProtKB
  • embryonic cleavage Source: Ensembl
  • peptidyl-serine phosphorylation Source: CAFA
  • phosphorylation Source: UniProtKB
  • programmed cell death Source: UniProtKB
  • response to drug Source: UniProtKB
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionDNA-binding, Isomerase, Topoisomerase
Biological processBiological rhythms, Host-virus interaction

Enzyme and pathway databases

BRENDAi5.99.1.2 2681
ReactomeiR-HSA-4615885 SUMOylation of DNA replication proteins
SIGNORiP11387

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 1 (EC:5.99.1.2)
Alternative name(s):
DNA topoisomerase I
Gene namesi
Name:TOP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000198900.5
HGNCiHGNC:11986 TOP1
MIMi126420 gene
neXtProtiNX_P11387

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TOP1 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with NUP98.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103K → 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. 1 Publication1
Mutagenesisi117K → 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. 1 Publication1
Mutagenesisi153K → 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. 1 Publication1
Mutagenesisi532K → A: Almost abolishes enzyme activity. 1 Publication1
Mutagenesisi532K → R: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi723Y → F: No change in CPT-induced clearing from nuclei. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi7150
OpenTargetsiENSG00000198900
PharmGKBiPA353

Chemistry databases

ChEMBLiCHEMBL1781
DrugBankiDB05806 BNP 1350
DB04690 Camptothecin
DB04882 Edotecarin
DB05129 Elsamitrucin
DB00762 Irinotecan
DB05482 LE-SN38
DB04967 Lucanthone
DB05630 Sodium stibogluconate
DB01030 Topotecan
DB06069 XMT-1001

Polymorphism and mutation databases

BioMutaiTOP1
DMDMi12644118

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001452012 – 765DNA topoisomerase 1Add BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
Modified residuei57PhosphoserineCombined sources1
Cross-linki101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei112PhosphoserineCombined sources1
Cross-linki117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated
Cross-linki153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei172N6-acetyllysine; alternateBy similarity1
Cross-linki172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei280N6-acetyllysineCombined sources1
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei506Phosphoserine; by CK21 Publication1
Cross-linki549Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki642Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki700Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki712Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

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.1 Publication
Phosphorylation at Ser-506 by CK2 increases binding to supercoiled DNA and sensitivity to camptothecin.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP11387
MaxQBiP11387
PaxDbiP11387
PeptideAtlasiP11387
PRIDEiP11387
ProteomicsDBi52766

2D gel databases

SWISS-2DPAGEiP11387

PTM databases

iPTMnetiP11387
PhosphoSitePlusiP11387
SwissPalmiP11387

Miscellaneous databases

PMAP-CutDBiP11387

Expressioni

Tissue specificityi

Endothelial cells.1 Publication

Gene expression databases

BgeeiENSG00000198900 Expressed in 232 organ(s), highest expression level in trabecular bone tissue
CleanExiHS_TOP1
GenevisibleiP11387 HS

Organism-specific databases

HPAiCAB009058
HPA019039

Interactioni

Subunit structurei

Monomer.7 Publications
(Microbial infection) Interacts with SV40 Large T antigen; this interactions allows viral DNA replication.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei316Interaction with DNA1
Sitei364Interaction with DNA1
Sitei412Interaction with DNA1
Sitei443Interaction with DNA1
Sitei501Interaction with DNA1
Sitei532Interaction with DNA1
Sitei574Interaction with DNA1
Sitei632Interaction with DNA1
Sitei650Interaction with DNA1

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113003, 185 interactors
CORUMiP11387
DIPiDIP-36356N
ELMiP11387
IntActiP11387, 74 interactors
MINTiP11387
STRINGi9606.ENSP00000354522

Chemistry databases

BindingDBiP11387

Structurei

Secondary structure

1765
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00075
ProteinModelPortaliP11387
SMRiP11387
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11387

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni425 – 426Interaction with DNA2
Regioni488 – 493Interaction with DNA6
Regioni585 – 587Interaction with DNA3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi23 – 204Lys-richAdd BLAST182

Sequence similaritiesi

Belongs to the type IB topoisomerase family.Curated

Phylogenomic databases

eggNOGiKOG0981 Eukaryota
COG3569 LUCA
GeneTreeiENSGT00390000016347
HOVERGENiHBG007988
InParanoidiP11387
KOiK03163
OMAiCSLKYEH
OrthoDBiEOG091G02KT
PhylomeDBiP11387
TreeFamiTF105281

Family and domain databases

CDDicd00659 Topo_IB_C, 1 hit
Gene3Di1.10.10.41, 1 hit
1.10.132.10, 1 hit
2.170.11.10, 1 hit
3.90.15.10, 1 hit
InterProiView protein in InterPro
IPR011010 DNA_brk_join_enz
IPR013034 DNA_topo_DNA_db_N_dom1
IPR013030 DNA_topo_DNA_db_N_dom2
IPR001631 TopoI
IPR018521 TopoI_AS
IPR025834 TopoI_C_dom
IPR014711 TopoI_cat_a-hlx-sub_euk
IPR014727 TopoI_cat_a/b-sub_euk
IPR013500 TopoI_cat_euk
IPR008336 TopoI_DNA-bd_euk
IPR036202 TopoI_DNA-bd_euk_N_sf
IPR013499 TopoI_euk
PANTHERiPTHR10290 PTHR10290, 1 hit
PfamiView protein in Pfam
PF14370 Topo_C_assoc, 1 hit
PF01028 Topoisom_I, 1 hit
PF02919 Topoisom_I_N, 1 hit
PRINTSiPR00416 EUTPISMRASEI
SMARTiView protein in SMART
SM00435 TOPEUc, 1 hit
SUPFAMiSSF56349 SSF56349, 1 hit
SSF56741 SSF56741, 1 hit
PROSITEiView protein in PROSITE
PS00176 TOPOISOMERASE_I_EUK, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11387-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK EKDREKSKHS
60 70 80 90 100
NSEHKDSEKK HKEKEKTKHK DGSSEKHKDK HKDRDKEKRK EEKVRASGDA
110 120 130 140 150
KIKKEKENGF SSPPQIKDEP EDDGYFVPPK EDIKPLKRPR DEDDADYKPK
160 170 180 190 200
KIKTEDTKKE KKRKLEEEED GKLKKPKNKD KDKKVPEPDN KKKKPKKEEE
210 220 230 240 250
QKWKWWEEER YPEGIKWKFL EHKGPVFAPP YEPLPENVKF YYDGKVMKLS
260 270 280 290 300
PKAEEVATFF AKMLDHEYTT KEIFRKNFFK DWRKEMTNEE KNIITNLSKC
310 320 330 340 350
DFTQMSQYFK AQTEARKQMS KEEKLKIKEE NEKLLKEYGF CIMDNHKERI
360 370 380 390 400
ANFKIEPPGL FRGRGNHPKM GMLKRRIMPE DIIINCSKDA KVPSPPPGHK
410 420 430 440 450
WKEVRHDNKV TWLVSWTENI QGSIKYIMLN PSSRIKGEKD WQKYETARRL
460 470 480 490 500
KKCVDKIRNQ YREDWKSKEM KVRQRAVALY FIDKLALRAG NEKEEGETAD
510 520 530 540 550
TVGCCSLRVE HINLHPELDG QEYVVEFDFL GKDSIRYYNK VPVEKRVFKN
560 570 580 590 600
LQLFMENKQP EDDLFDRLNT GILNKHLQDL MEGLTAKVFR TYNASITLQQ
610 620 630 640 650
QLKELTAPDE NIPAKILSYN RANRAVAILC NHQRAPPKTF EKSMMNLQTK
660 670 680 690 700
IDAKKEQLAD ARRDLKSAKA DAKVMKDAKT KKVVESKKKA VQRLEEQLMK
710 720 730 740 750
LEVQATDREE NKQIALGTSK LNYLDPRITV AWCKKWGVPI EKIYNKTQRE
760
KFAWAIDMAD EDYEF
Length:765
Mass (Da):90,726
Last modified:December 1, 2000 - v2
Checksum:i6FBED540BCF7BE28
GO

Sequence cautioni

The sequence CAA36834 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145A → V in AAA61207 (PubMed:2833744).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052592214G → S. Corresponds to variant dbSNP:rs6029542Ensembl.1
Natural variantiVAR_036555326K → R in breast cancer; somatic mutation. 1 Publication1
Natural variantiVAR_010666370M → T in CPT-resistant leukemia. 1 Publication1
Natural variantiVAR_007530533D → G in CPT-resistant leukemia. 1 PublicationCorresponds to variant dbSNP:rs267607131EnsemblClinVar.1
Natural variantiVAR_010667722N → S in CPT-resistant leukemia. 1 Publication1
Natural variantiVAR_007531729T → A in CPT-resistant lung cancer. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 Genomic DNA No translation available.
AL022394 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75994.1
CH471077 Genomic DNA Translation: EAW75995.1
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
CCDSiCCDS13312.1
PIRiA30887 ISHUT1
RefSeqiNP_003277.1, NM_003286.3
UniGeneiHs.472737

Genome annotation databases

EnsembliENST00000361337; ENSP00000354522; ENSG00000198900
GeneIDi7150
KEGGihsa:7150
UCSCiuc002xjl.4 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 Genomic DNA No translation available.
AL022394 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75994.1
CH471077 Genomic DNA Translation: EAW75995.1
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
CCDSiCCDS13312.1
PIRiA30887 ISHUT1
RefSeqiNP_003277.1, NM_003286.3
UniGeneiHs.472737

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A31X-ray2.10A175-765[»]
1A35X-ray2.50A175-765[»]
1A36X-ray2.80A175-765[»]
1EJ9X-ray2.60A203-765[»]
1K4SX-ray3.20A174-765[»]
1K4TX-ray2.10A174-765[»]
1LPQX-ray3.14A202-765[»]
1NH3X-ray3.10A203-765[»]
1R49X-ray3.13A174-765[»]
1RR8X-ray2.60C203-765[»]
1RRJX-ray2.30A201-765[»]
1SC7X-ray3.00A174-765[»]
1SEUX-ray3.00A174-765[»]
1T8IX-ray3.00A174-765[»]
1TL8X-ray3.10A174-765[»]
DisProtiDP00075
ProteinModelPortaliP11387
SMRiP11387
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113003, 185 interactors
CORUMiP11387
DIPiDIP-36356N
ELMiP11387
IntActiP11387, 74 interactors
MINTiP11387
STRINGi9606.ENSP00000354522

Chemistry databases

BindingDBiP11387
ChEMBLiCHEMBL1781
DrugBankiDB05806 BNP 1350
DB04690 Camptothecin
DB04882 Edotecarin
DB05129 Elsamitrucin
DB00762 Irinotecan
DB05482 LE-SN38
DB04967 Lucanthone
DB05630 Sodium stibogluconate
DB01030 Topotecan
DB06069 XMT-1001

PTM databases

iPTMnetiP11387
PhosphoSitePlusiP11387
SwissPalmiP11387

Polymorphism and mutation databases

BioMutaiTOP1
DMDMi12644118

2D gel databases

SWISS-2DPAGEiP11387

Proteomic databases

EPDiP11387
MaxQBiP11387
PaxDbiP11387
PeptideAtlasiP11387
PRIDEiP11387
ProteomicsDBi52766

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361337; ENSP00000354522; ENSG00000198900
GeneIDi7150
KEGGihsa:7150
UCSCiuc002xjl.4 human

Organism-specific databases

CTDi7150
DisGeNETi7150
EuPathDBiHostDB:ENSG00000198900.5
GeneCardsiTOP1
H-InvDBiHIX0015818
HIX0040702
HGNCiHGNC:11986 TOP1
HPAiCAB009058
HPA019039
MIMi126420 gene
neXtProtiNX_P11387
OpenTargetsiENSG00000198900
PharmGKBiPA353
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0981 Eukaryota
COG3569 LUCA
GeneTreeiENSGT00390000016347
HOVERGENiHBG007988
InParanoidiP11387
KOiK03163
OMAiCSLKYEH
OrthoDBiEOG091G02KT
PhylomeDBiP11387
TreeFamiTF105281

Enzyme and pathway databases

BRENDAi5.99.1.2 2681
ReactomeiR-HSA-4615885 SUMOylation of DNA replication proteins
SIGNORiP11387

Miscellaneous databases

ChiTaRSiTOP1 human
EvolutionaryTraceiP11387
GeneWikiiTOP1
GenomeRNAii7150
PMAP-CutDBiP11387
PROiPR:P11387
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198900 Expressed in 232 organ(s), highest expression level in trabecular bone tissue
CleanExiHS_TOP1
GenevisibleiP11387 HS

Family and domain databases

CDDicd00659 Topo_IB_C, 1 hit
Gene3Di1.10.10.41, 1 hit
1.10.132.10, 1 hit
2.170.11.10, 1 hit
3.90.15.10, 1 hit
InterProiView protein in InterPro
IPR011010 DNA_brk_join_enz
IPR013034 DNA_topo_DNA_db_N_dom1
IPR013030 DNA_topo_DNA_db_N_dom2
IPR001631 TopoI
IPR018521 TopoI_AS
IPR025834 TopoI_C_dom
IPR014711 TopoI_cat_a-hlx-sub_euk
IPR014727 TopoI_cat_a/b-sub_euk
IPR013500 TopoI_cat_euk
IPR008336 TopoI_DNA-bd_euk
IPR036202 TopoI_DNA-bd_euk_N_sf
IPR013499 TopoI_euk
PANTHERiPTHR10290 PTHR10290, 1 hit
PfamiView protein in Pfam
PF14370 Topo_C_assoc, 1 hit
PF01028 Topoisom_I, 1 hit
PF02919 Topoisom_I_N, 1 hit
PRINTSiPR00416 EUTPISMRASEI
SMARTiView protein in SMART
SM00435 TOPEUc, 1 hit
SUPFAMiSSF56349 SSF56349, 1 hit
SSF56741 SSF56741, 1 hit
PROSITEiView protein in PROSITE
PS00176 TOPOISOMERASE_I_EUK, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTOP1_HUMAN
AccessioniPrimary (citable) accession number: P11387
Secondary accession number(s): A8KA78
, E1P5W3, O43256, Q12855, Q12856, Q15610, Q5TFY3, Q9UJN0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 2000
Last modified: November 7, 2018
This is version 212 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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