THOP1_MOUSE - dbPTM
THOP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOP1_MOUSE
UniProt AC Q8C1A5
Protein Name Thimet oligopeptidase
Gene Name Thop1
Organism Mus musculus (Mouse).
Sequence Length 687
Subcellular Localization Cytoplasm.
Protein Description Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the amyloid-beta precursor protein and generate amyloidogenic fragments (By similarity)..
Protein Sequence MKPPAACAGDVVDAASPASTVNHLRWDLSAQQIRALTTQLIEQTKCVYDRVGAQNFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPCKDIRAASTEADKKLSEFDVEMSMRQDVYQRVVWLQEKTPKNSLKPEAARYLERLIKLGRRNGLHLPQDTQEKIKNIKKRLSLLCIDFNKNLNEDTTFLPFTREELGGLPEDFLSSLEKAEDGKLKVTLKYPHYFPLLKKCHVPETRRLLEEAFNCRCKEENCAILKELVSLRAQKSSLLGFHTHADYVLEMNMAKTSQTVATFLDELAQKLKPLGEQERAVILELKEAECAKRGLPFDGRIHAWDMRYYMNQVEETRYRVDQNLLKEYFPMQVVTRGLLAIYQELLGLTFTLEEGAAAWHEDVRLYSVRDAASGEEIGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQLAVAAMVANFTKPTPDAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFVEAPSQMLENWVWEKEPLMRMSQHYRTGSEAPQDLLEKLIKSRQANAGLFNLRQIVLAKVDQVLHTQTDADPAEEYARLCQEILGVPATPGTNMPATFGHLAGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLSPKVGMDYRTSILRPGGSEDASAMLKQFLGRDPKQDAFLLSKGLQVEGSEAPAC
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MKPPAACAG
------CCCCCCCCC		60.7622826441
7Glutathionylation-MKPPAACAGDVVDA
-CCCCCCCCCCCCCC		4.7724333276
16PhosphorylationGDVVDAASPASTVNH
CCCCCCCCCCHHHCH		23.7924453211
19PhosphorylationVDAASPASTVNHLRW
CCCCCCCHHHCHHHC		35.9523984901
20PhosphorylationDAASPASTVNHLRWD
CCCCCCHHHCHHHCC		27.6823984901
45AcetylationTQLIEQTKCVYDRVG
HHHHHHHCCHHHCCC		22.7722826441
60PhosphorylationAQNFEDVSYESTLKA
CCCCCCCCHHHHHHH		35.19-
89PhosphorylationLDFPQHVSPCKDIRA
CCCCCCCCCCCCHHH		23.5828494245
92UbiquitinationPQHVSPCKDIRAAST
CCCCCCCCCHHHHCC		60.6222790023
128AcetylationRVVWLQEKTPKNSLK
HHHHHHCCCCCCCCC		58.1122826441
131UbiquitinationWLQEKTPKNSLKPEA
HHHCCCCCCCCCHHH		65.48-
147AcetylationRYLERLIKLGRRNGL
HHHHHHHHHHHHCCC		49.8622826441
172PhosphorylationKNIKKRLSLLCIDFN
HHHHHHHHEEEEECC		24.2726745281
186PhosphorylationNKNLNEDTTFLPFTR
CCCCCCCCCCCCCCH		17.1726060331
187PhosphorylationKNLNEDTTFLPFTRE
CCCCCCCCCCCCCHH		35.1826060331
192PhosphorylationDTTFLPFTREELGGL
CCCCCCCCHHHHCCC		34.9226060331
205PhosphorylationGLPEDFLSSLEKAED
CCCHHHHHHHHHCCC		32.6327149854
206PhosphorylationLPEDFLSSLEKAEDG
CCHHHHHHHHHCCCC		42.5727149854
220AcetylationGKLKVTLKYPHYFPL
CCEEEEEECCCHHHH		47.5822826441
229AcetylationPHYFPLLKKCHVPET
CCHHHHHHHCCCHHH		62.1222826441
257AcetylationEENCAILKELVSLRA
HHHHHHHHHHHHHHH		42.7822826441
278PhosphorylationGFHTHADYVLEMNMA
CCCCCHHHHHHHHHH		14.0218034455
303AcetylationDELAQKLKPLGEQER
HHHHHHHHCCCHHHH		45.2722826441
359PhosphorylationDQNLLKEYFPMQVVT
CHHHHHHHCCHHHHH		16.0524759943
366PhosphorylationYFPMQVVTRGLLAIY
HCCHHHHHHHHHHHH		21.8424759943
373PhosphorylationTRGLLAIYQELLGLT
HHHHHHHHHHHHCCE		7.1324759943
380PhosphorylationYQELLGLTFTLEEGA
HHHHHCCEEEECCCH		16.8724759943
382PhosphorylationELLGLTFTLEEGAAA
HHHCCEEEECCCHHH		28.2024759943
398PhosphorylationHEDVRLYSVRDAASG
CCCEEEEEEEECCCC		18.4424759943
421AcetylationDLYPREGKYGHAACF
ECCCCCCCCCCCHHC		43.2222826441
527PhosphorylationRMSQHYRTGSEAPQD
HHHHHHCCCCCCCHH		37.5824759943
529PhosphorylationSQHYRTGSEAPQDLL
HHHHCCCCCCCHHHH		29.9427841257
538UbiquitinationAPQDLLEKLIKSRQA
CCHHHHHHHHHHCHH		56.3222790023
538AcetylationAPQDLLEKLIKSRQA
CCHHHHHHHHHHCHH		56.32-
628AcetylationDMFHTRFKQEGVLSP
CCCCHHHHCCCCCCC		44.1222826441
634PhosphorylationFKQEGVLSPKVGMDY
HHCCCCCCCCCCCCC		21.9225266776
636UbiquitinationQEGVLSPKVGMDYRT
CCCCCCCCCCCCCCC		48.3122790023
644PhosphorylationVGMDYRTSILRPGGS
CCCCCCCCCCCCCCC		15.6124719451
667AcetylationQFLGRDPKQDAFLLS
HHHCCCCCCCCHHHH		66.1622826441
667UbiquitinationQFLGRDPKQDAFLLS
HHHCCCCCCCCHHHH		66.1622790023
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
644SPhosphorylationKinasePKA-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THOP1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of THOP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of THOP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THOP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278, AND MASSSPECTROMETRY.

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