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P52888 (THOP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thimet oligopeptidase
EC=3.4.24.15
Alternative name(s):
Endopeptidase 24.15
MP78
Gene names
Name:THOP1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length689 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MPHOSPH6Q995471EBI-372399,EBI-373187

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 689688Thimet oligopeptidase
PRO_0000078153

Sites

Active site4741 By similarity
Metal binding4731Zinc; catalytic By similarity
Metal binding4771Zinc; catalytic By similarity
Metal binding4801Zinc; catalytic By similarity

Amino acid modifications

Modified residue2571N6-acetyllysine Ref.6
Modified residue2781Phosphotyrosine By similarity
Modified residue5381N6-acetyllysine Ref.6

Secondary structure

1 ........................................................................................... 689
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52888 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 092D53DD63B322DE

FASTA68978,840
        10         20         30         40         50         60 
MKPPAACAGD MADAASPCSV VNDLRWDLSA QQIEERTREL IEQTKRVYDQ VGTQEFEDVS 

        70         80         90        100        110        120 
YESTLKALAD VEVTYTVQRN ILDFPQHVSP SKDIRTASTE ADKKLSEFDV EMSMREDVYQ 

       130        140        150        160        170        180 
RIVWLQEKVQ KDSLRPEAAR YLERLIKLGR RNGLHLPRET QENIKRIKKK LSLLCIDFNK 

       190        200        210        220        230        240 
NLNEDTTFLP FTLQELGGLP EDFLNSLEKM EDGKLKVTLK YPHYFPLLKK CHVPETRRKV 

       250        260        270        280        290        300 
EEAFNCRCKE ENCAILKELV TLRAQKSRLL GFHTHADYVL EMNMAKTSQT VATFLDELAQ 

       310        320        330        340        350        360 
KLKPLGEQER AVILELKRAE CERRGLPFDG RIRAWDMRYY MNQVEETRYC VDQNLLKEYF 

       370        380        390        400        410        420 
PVQVVTHGLL GIYQELLGLA FHHEEGASAW HEDVRLYTAR DAASGEVVGK FYLDLYPREG 

       430        440        450        460        470        480 
KYGHAACFGL QPGCLRQDGS RQIAIAAMVA NFTKPTADAP SLLQHDEVET YFHEFGHVMH 

       490        500        510        520        530        540 
QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEQEPLLR MSRHYRTGSA VPRELLEKLI 

       550        560        570        580        590        600 
ESRQANTGLF NLRQIVLAKV DQALHTQTDA DPAEEYARLC QEILGVPATP GTNMPATFGH 

       610        620        630        640        650        660 
LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLNSKVGMD YRSCILRPGG SEDASAMLRR 

       670        680 
FLGRDPKQDA FLLSKGLQVG GCEPEPQVC

« Hide

References

« Hide 'large scale' references
[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: 7639763] [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. expand/collapse author list , 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: 15057824] [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: 15489334] [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: 8286339] [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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257 AND LYS-538, MASS SPECTROMETRY.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00549189.
PIRHYHUTH. JC4197.
RefSeqNP_003240.1. NM_003249.3.
UniGeneHs.78769.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4BX-ray2.00P16-688[»]
2O36X-ray1.95A16-688[»]
ProteinModelPortalP52888.
SMRP52888. Positions 24-677.
ModBaseSearch...

Protein-protein interaction databases

IntActP52888. 1 interaction.
MINTMINT-3019782.
STRINGP52888.

Protein family/group databases

MEROPSM03.001.

PTM databases

PhosphoSiteP52888.

Polymorphism databases

DMDM1708983.

Proteomic databases

PeptideAtlasP52888.
PRIDEP52888.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307741; ENSP00000304467; ENSG00000172009.
GeneID7064.
KEGGhsa:7064.
UCSCuc002lwj.1. human.

Organism-specific databases

CTD7064.
GeneCardsGC19P002785.
H-InvDBHIX0014625.
HGNCHGNC:11793. THOP1.
HPACAB025497.
MIM601117. gene.
neXtProtNX_P52888.
PharmGKBPA36505.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG678447.
HOVERGENHBG000238.
InParanoidP52888.
OMARNMLDFP.
OrthoDBEOG4CG07P.
PhylomeDBP52888.

Gene expression databases

ArrayExpressP52888.
BgeeP52888.
CleanExHS_THOP1.
GenevestigatorP52888.
GermOnlineENSG00000172009. Homo sapiens.

Family and domain databases

InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
Gene3DG3DSA:1.10.1370.10. G3DSA:1.10.1370.10. 2 hits.
G3DSA:1.20.1050.40. G3DSA:1.20.1050.40. 1 hit.
G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
KOK01392.
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio27623.
PMAP-CutDBP52888.
SOURCESearch...

Entry information

Entry nameTHOP1_HUMAN
AccessionPrimary (citable) accession number: P52888
Secondary accession number(s): Q9UCB3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents