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P52888

- THOP1_HUMAN

UniProt

P52888 - THOP1_HUMAN

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Protein

Thimet oligopeptidase

Gene
THOP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.

Catalytic activityi

Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi473 – 4731Zinc; catalytic
Active sitei474 – 4741
Metal bindingi477 – 4771Zinc; catalytic
Metal bindingi480 – 4801Zinc; catalytic

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: ProtInc
  3. peptide binding Source: Ensembl
  4. protein binding Source: IntAct

GO - Biological processi

  1. peptide metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM03.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Thimet oligopeptidase (EC:3.4.24.15)
Alternative name(s):
Endopeptidase 24.15
MP78
Gene namesi
Name:THOP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11793. THOP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36505.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 689689Thimet oligopeptidasePRO_0000078153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571N6-acetyllysine1 Publication
Modified residuei278 – 2781Phosphotyrosine By similarity
Modified residuei538 – 5381N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52888.
PaxDbiP52888.
PeptideAtlasiP52888.
PRIDEiP52888.

PTM databases

PhosphoSiteiP52888.

Miscellaneous databases

PMAP-CutDBP52888.

Expressioni

Gene expression databases

ArrayExpressiP52888.
BgeeiP52888.
CleanExiHS_THOP1.
GenevestigatoriP52888.

Organism-specific databases

HPAiCAB025497.

Interactioni

Subunit structurei

Monomer By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Calm3P621612EBI-372399,EBI-397530From a different organism.

Protein-protein interaction databases

BioGridi112921. 34 interactions.
IntActiP52888. 3 interactions.
MINTiMINT-3019782.
STRINGi9606.ENSP00000304467.

Structurei

Secondary structure

1
689
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 5223
Helixi56 – 583
Turni61 – 644
Helixi65 – 8319
Helixi85 – 884
Helixi92 – 11322
Helixi116 – 12813
Helixi136 – 15116
Turni152 – 1554
Helixi158 – 18427
Beta strandi188 – 1914
Turni193 – 1986
Helixi201 – 2044
Beta strandi207 – 2093
Beta strandi215 – 2206
Helixi221 – 23010
Helixi234 – 24411
Turni245 – 2484
Helixi249 – 26921
Helixi275 – 2806
Helixi288 – 32437
Turni334 – 3363
Helixi337 – 34812
Helixi353 – 3564
Helixi357 – 3593
Helixi362 – 37716
Beta strandi379 – 3835
Beta strandi395 – 4017
Turni402 – 4043
Beta strandi407 – 4148
Beta strandi426 – 4316
Beta strandi444 – 4496
Helixi465 – 48319
Helixi489 – 4913
Turni498 – 5025
Helixi503 – 5097
Helixi510 – 5134
Helixi515 – 5206
Turni525 – 5273
Helixi533 – 5419
Helixi542 – 5443
Helixi547 – 56418
Helixi572 – 58211
Helixi594 – 5974
Helixi599 – 6024
Turni606 – 6105
Helixi611 – 63020
Helixi635 – 64410
Turni645 – 6484
Helixi649 – 6513
Helixi654 – 6629
Helixi669 – 6746

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4BX-ray2.00P16-689[»]
2O36X-ray1.95A16-688[»]
ProteinModelPortaliP52888.
SMRiP52888. Positions 24-677.

Miscellaneous databases

EvolutionaryTraceiP52888.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP52888.
KOiK01392.
OMAiGCEPPAC.
OrthoDBiEOG7SR4KW.
PhylomeDBiP52888.
TreeFamiTF300459.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52888-1 [UniParc]FASTAAdd to Basket

« Hide

MKPPAACAGD MADAASPCSV VNDLRWDLSA QQIEERTREL IEQTKRVYDQ    50
VGTQEFEDVS YESTLKALAD VEVTYTVQRN ILDFPQHVSP SKDIRTASTE 100
ADKKLSEFDV EMSMREDVYQ RIVWLQEKVQ KDSLRPEAAR YLERLIKLGR 150
RNGLHLPRET QENIKRIKKK LSLLCIDFNK NLNEDTTFLP FTLQELGGLP 200
EDFLNSLEKM EDGKLKVTLK YPHYFPLLKK CHVPETRRKV EEAFNCRCKE 250
ENCAILKELV TLRAQKSRLL GFHTHADYVL EMNMAKTSQT VATFLDELAQ 300
KLKPLGEQER AVILELKRAE CERRGLPFDG RIRAWDMRYY MNQVEETRYC 350
VDQNLLKEYF PVQVVTHGLL GIYQELLGLA FHHEEGASAW HEDVRLYTAR 400
DAASGEVVGK FYLDLYPREG KYGHAACFGL QPGCLRQDGS RQIAIAAMVA 450
NFTKPTADAP SLLQHDEVET YFHEFGHVMH QLCSQAEFAM FSGTHVERDF 500
VEAPSQMLEN WVWEQEPLLR MSRHYRTGSA VPRELLEKLI ESRQANTGLF 550
NLRQIVLAKV DQALHTQTDA DPAEEYARLC QEILGVPATP GTNMPATFGH 600
LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLNSKVGMD YRSCILRPGG 650
SEDASAMLRR FLGRDPKQDA FLLSKGLQVG GCEPEPQVC 689
Length:689
Mass (Da):78,840
Last modified:January 23, 2007 - v2
Checksum:i092D53DD63B322DE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z50115 mRNA. Translation: CAA90477.1.
U29366 mRNA. Translation: AAA82607.1.
AC006538 Genomic DNA. Translation: AAD13118.1.
BC000135 mRNA. Translation: AAH00135.1.
BC002391 mRNA. Translation: AAH02391.1.
CCDSiCCDS12095.1.
PIRiJC4197. HYHUTH.
RefSeqiNP_003240.1. NM_003249.3.
UniGeneiHs.78769.

Genome annotation databases

EnsembliENST00000307741; ENSP00000304467; ENSG00000172009.
GeneIDi7064.
KEGGihsa:7064.
UCSCiuc002lwj.3. human.

Polymorphism databases

DMDMi1708983.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z50115 mRNA. Translation: CAA90477.1 .
U29366 mRNA. Translation: AAA82607.1 .
AC006538 Genomic DNA. Translation: AAD13118.1 .
BC000135 mRNA. Translation: AAH00135.1 .
BC002391 mRNA. Translation: AAH02391.1 .
CCDSi CCDS12095.1.
PIRi JC4197. HYHUTH.
RefSeqi NP_003240.1. NM_003249.3.
UniGenei Hs.78769.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1S4B X-ray 2.00 P 16-689 [» ]
2O36 X-ray 1.95 A 16-688 [» ]
ProteinModelPortali P52888.
SMRi P52888. Positions 24-677.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112921. 34 interactions.
IntActi P52888. 3 interactions.
MINTi MINT-3019782.
STRINGi 9606.ENSP00000304467.

Protein family/group databases

MEROPSi M03.001.

PTM databases

PhosphoSitei P52888.

Polymorphism databases

DMDMi 1708983.

Proteomic databases

MaxQBi P52888.
PaxDbi P52888.
PeptideAtlasi P52888.
PRIDEi P52888.

Protocols and materials databases

DNASUi 7064.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307741 ; ENSP00000304467 ; ENSG00000172009 .
GeneIDi 7064.
KEGGi hsa:7064.
UCSCi uc002lwj.3. human.

Organism-specific databases

CTDi 7064.
GeneCardsi GC19P002785.
HGNCi HGNC:11793. THOP1.
HPAi CAB025497.
MIMi 601117. gene.
neXtProti NX_P52888.
PharmGKBi PA36505.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0339.
HOGENOMi HOG000245985.
HOVERGENi HBG000238.
InParanoidi P52888.
KOi K01392.
OMAi GCEPPAC.
OrthoDBi EOG7SR4KW.
PhylomeDBi P52888.
TreeFami TF300459.

Miscellaneous databases

EvolutionaryTracei P52888.
GeneWikii THOP1.
GenomeRNAii 7064.
NextBioi 27623.
PMAP-CutDB P52888.
PROi P52888.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52888.
Bgeei P52888.
CleanExi HS_THOP1.
Genevestigatori P52888.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view ]
Pfami PF01432. Peptidase_M3. 1 hit.
[Graphical view ]
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate peptide."
    Thompson A., Huber G., Malherbe P.
    Biochem. Biophys. Res. Commun. 213:66-73(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "cDNA cloning and gene structure of a human gene encoding a highly conserved metalloendopeptidase (EC 3.4.24.15)."
    Taylor G.R., Otulakowski G., Lau C.Y., Munroe D.G.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
  4. "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].
    Tissue: Lung and Placenta.
  5. "Identification of a metalloprotease from Alzheimer's disease brain able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments."
    Papastoitsis G., Siman R., Scott R., Abraham C.R.
    Biochemistry 33:192-199(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 67-78; 181-197 AND 199-200.
    Tissue: Brain.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257 AND LYS-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase."
    Lim E.J., Sampath S., Coll-Rodriguez J., Schmidt J., Ray K., Rodgers D.W.
    J. Biol. Chem. 282:9722-9732(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 16-688, ZINC-BINDING SITES.

Entry informationi

Entry nameiTHOP1_HUMAN
AccessioniPrimary (citable) accession number: P52888
Secondary accession number(s): Q9UCB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 139 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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