dbPTM

THOP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THOP1_HUMAN
UniProt AC	P52888
Protein Name	Thimet oligopeptidase
Gene Name	THOP1
Organism	Homo sapiens (Human).
Sequence Length	689
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..
Protein Sequence	MKPPAACAGDMADAASPCSVVNDLRWDLSAQQIEERTRELIEQTKRVYDQVGTQEFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPSKDIRTASTEADKKLSEFDVEMSMREDVYQRIVWLQEKVQKDSLRPEAARYLERLIKLGRRNGLHLPRETQENIKRIKKKLSLLCIDFNKNLNEDTTFLPFTLQELGGLPEDFLNSLEKMEDGKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEENCAILKELVTLRAQKSRLLGFHTHADYVLEMNMAKTSQTVATFLDELAQKLKPLGEQERAVILELKRAECERRGLPFDGRIRAWDMRYYMNQVEETRYCVDQNLLKEYFPVQVVTHGLLGIYQELLGLAFHHEEGASAWHEDVRLYTARDAASGEVVGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQIAIAAMVANFTKPTADAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFVEAPSQMLENWVWEQEPLLRMSRHYRTGSAVPRELLEKLIESRQANTGLFNLRQIVLAKVDQALHTQTDADPAEEYARLCQEILGVPATPGTNMPATFGHLAGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLNSKVGMDYRSCILRPGGSEDASAMLRRFLGRDPKQDAFLLSKGLQVGGCEPEPQVC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Ubiquitination	------MKPPAACAG ------CCCCCCCCC	60.76	24816145
2	Acetylation	------MKPPAACAG ------CCCCCCCCC	60.76	25953088
7	Ubiquitination	-MKPPAACAGDMADA -CCCCCCCCCCCCCC	4.77	22817900
11	Ubiquitination	PAACAGDMADAASPC CCCCCCCCCCCCCCC	3.39	21890473
16	Phosphorylation	GDMADAASPCSVVND CCCCCCCCCCHHHHH	28.32	23401153
19	Phosphorylation	ADAASPCSVVNDLRW CCCCCCCHHHHHHHC	32.27	29255136
30	Ubiquitination	DLRWDLSAQQIEERT HHHCCCCHHHHHHHH	16.76	24816145
45	Ubiquitination	RELIEQTKRVYDQVG HHHHHHHHHHHHHHC	39.29	21890473
49	Ubiquitination	EQTKRVYDQVGTQEF HHHHHHHHHHCCCCC	33.56	21890473
49	Acetylation	EQTKRVYDQVGTQEF HHHHHHHHHHCCCCC	33.56	-
70	Ubiquitination	STLKALADVEVTYTV HHHHHHCCCEEEEEE	37.65	21890473
89	Phosphorylation	LDFPQHVSPSKDIRT CCCCCCCCCCCCHHH	22.72	28450419
91	Phosphorylation	FPQHVSPSKDIRTAS CCCCCCCCCCHHHCC	35.14	28450419
92	Ubiquitination	PQHVSPSKDIRTAST CCCCCCCCCHHHCCH	61.63	29967540
92	Acetylation	PQHVSPSKDIRTAST CCCCCCCCCHHHCCH	61.63	25953088
99	Phosphorylation	KDIRTASTEADKKLS CCHHHCCHHHHHHHH	32.50	-
103	Ubiquitination	TASTEADKKLSEFDV HCCHHHHHHHHHCCC	63.76	-
104	Ubiquitination	ASTEADKKLSEFDVE CCHHHHHHHHHCCCC	58.77	24816145
108	Ubiquitination	ADKKLSEFDVEMSMR HHHHHHHCCCCHHHC	13.17	21963094
128	Ubiquitination	RIVWLQEKVQKDSLR HHHHHHHHHHHCCCC	36.68	29967540
131	Ubiquitination	WLQEKVQKDSLRPEA HHHHHHHHCCCCHHH	52.88	29967540
139	Ubiquitination	DSLRPEAARYLERLI CCCCHHHHHHHHHHH	10.05	-
141	Phosphorylation	LRPEAARYLERLIKL CCHHHHHHHHHHHHH	14.27	-
147	Ubiquitination	RYLERLIKLGRRNGL HHHHHHHHHHHHCCC	49.86	27667366
165	Acetylation	RETQENIKRIKKKLS HHHHHHHHHHHHHHC	60.70	25953088
170	Ubiquitination	NIKRIKKKLSLLCID HHHHHHHHHCCEEEE	38.00	-
172	Phosphorylation	KRIKKKLSLLCIDFN HHHHHHHCCEEEECC	28.33	28450419
216	Ubiquitination	KMEDGKLKVTLKYPH HCCCCCEEEEEECCC	36.34	22817900
220	Ubiquitination	GKLKVTLKYPHYFPL CCEEEEEECCCHHHH	47.58	21963094
221	Phosphorylation	KLKVTLKYPHYFPLL CEEEEEECCCHHHHH	9.80	20090780
224	Phosphorylation	VTLKYPHYFPLLKKC EEEECCCHHHHHHHC	11.46	28152594
229	Acetylation	PHYFPLLKKCHVPET CCHHHHHHHCCCCHH	62.12	19608861
230	Ubiquitination	HYFPLLKKCHVPETR CHHHHHHHCCCCHHH	29.55	-
236	Ubiquitination	KKCHVPETRRKVEEA HHCCCCHHHHHHHHH	29.69	-
239	Acetylation	HVPETRRKVEEAFNC CCCHHHHHHHHHHHC	51.19	19811663
239	Ubiquitination	HVPETRRKVEEAFNC CCCHHHHHHHHHHHC	51.19	24816145
244	Ubiquitination	RRKVEEAFNCRCKEE HHHHHHHHHCCCCHH	11.38	-
249	Acetylation	EAFNCRCKEENCAIL HHHHCCCCHHHHHHH	49.03	23749302
257	Ubiquitination	EENCAILKELVTLRA HHHHHHHHHHHHHHH	42.78	19608861
257	Acetylation	EENCAILKELVTLRA HHHHHHHHHHHHHHH	42.78	19608861
267	Phosphorylation	VTLRAQKSRLLGFHT HHHHHHHHHHCCCCC	18.97	23663014
274	Phosphorylation	SRLLGFHTHADYVLE HHHCCCCCCHHHHHH	19.25	23663014
278	Phosphorylation	GFHTHADYVLEMNMA CCCCCHHHHHHHHHH	14.02	23663014
287	Phosphorylation	LEMNMAKTSQTVATF HHHHHHCCHHHHHHH	19.27	30624053
288	Phosphorylation	EMNMAKTSQTVATFL HHHHHCCHHHHHHHH	24.13	30624053
290	Phosphorylation	NMAKTSQTVATFLDE HHHCCHHHHHHHHHH	16.33	30624053
293	Phosphorylation	KTSQTVATFLDELAQ CCHHHHHHHHHHHHH	22.01	30624053
301	Ubiquitination	FLDELAQKLKPLGEQ HHHHHHHHHHCCCHH	53.52	30230243
303	Ubiquitination	DELAQKLKPLGEQER HHHHHHHHCCCHHHH	45.27	29967540
317	Ubiquitination	RAVILELKRAECERR HHHHHHHHHHHHHHC	39.94	21963094
329	Ubiquitination	ERRGLPFDGRIRAWD HHCCCCCCCCEEHHH	43.45	21890473
339	Phosphorylation	IRAWDMRYYMNQVEE EEHHHHHHHHHHHHH	10.63	21406692
340	Phosphorylation	RAWDMRYYMNQVEET EHHHHHHHHHHHHHH	4.53	21406692
347	Phosphorylation	YMNQVEETRYCVDQN HHHHHHHHHEECCHH	17.27	20068231
350	Ubiquitination	QVEETRYCVDQNLLK HHHHHHEECCHHHHH	2.15	21963094
412	Phosphorylation	GEVVGKFYLDLYPRE CCEEEEEEEECCCCC	11.64	20068231
416	Phosphorylation	GKFYLDLYPREGKYG EEEEEECCCCCCCCC	10.42	28152594
419	Ubiquitination	YLDLYPREGKYGHAA EEECCCCCCCCCCCH	56.38	27667366
421	Ubiquitination	DLYPREGKYGHAACF ECCCCCCCCCCCHHC	43.22	-
422	Phosphorylation	LYPREGKYGHAACFG CCCCCCCCCCCHHCC	25.63	28152594
427	Ubiquitination	GKYGHAACFGLQPGC CCCCCCHHCCCCCCC	2.63	24816145
527	Phosphorylation	RMSRHYRTGSAVPRE HHCHHHCCCCCCCHH	28.46	29449344
529	Phosphorylation	SRHYRTGSAVPRELL CHHHCCCCCCCHHHH	26.02	29449344
538	Ubiquitination	VPRELLEKLIESRQA CCHHHHHHHHHHCCC	55.52	22053931
538	Acetylation	VPRELLEKLIESRQA CCHHHHHHHHHHCCC	55.52	19608861
559	Ubiquitination	LRQIVLAKVDQALHT HHHHHHHHHHHHHHC	42.03	21906983
628	Ubiquitination	DMFHTRFKQEGVLNS CCCCHHHHHCCCCCC	44.12	27667366
628	Acetylation	DMFHTRFKQEGVLNS CCCCHHHHHCCCCCC	44.12	26051181
636	Ubiquitination	QEGVLNSKVGMDYRS HCCCCCCCCCCCHHH	41.56	24816145
641	Phosphorylation	NSKVGMDYRSCILRP CCCCCCCHHHCCCCC	8.78	-
643	Phosphorylation	KVGMDYRSCILRPGG CCCCCHHHCCCCCCC	10.16	10969067
667	Ubiquitination	RFLGRDPKQDAFLLS HHHCCCCCCCCCHHH	66.16	29967540
675	Ubiquitination	QDAFLLSKGLQVGGC CCCCHHHCCCCCCCC	64.71	-

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
643	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
643	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of THOP1_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VAV2_HUMAN	VAV2	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
TT39C_HUMAN	TTC39C	physical	22939629
XYLB_HUMAN	XYLB	physical	22939629
UBE2H_HUMAN	UBE2H	physical	22939629
UAP1_HUMAN	UAP1	physical	22939629
UNG_HUMAN	UNG	physical	22939629
PURA2_HUMAN	ADSS	physical	22863883
ANXA6_HUMAN	ANXA6	physical	22863883
CHRC1_HUMAN	CHRAC1	physical	22863883
CH60_HUMAN	HSPD1	physical	22863883
CH10_HUMAN	HSPE1	physical	22863883
IDHC_HUMAN	IDH1	physical	22863883
NDKA_HUMAN	NME1	physical	22863883
6PGD_HUMAN	PGD	physical	22863883
PLST_HUMAN	PLS3	physical	22863883
PTMS_HUMAN	PTMS	physical	22863883
RBBP7_HUMAN	RBBP7	physical	22863883
DHSO_HUMAN	SORD	physical	22863883
TALDO_HUMAN	TALDO1	physical	22863883
WDR1_HUMAN	WDR1	physical	22863883
TRAF2_HUMAN	TRAF2	physical	25416956
SYNE2_HUMAN	SYNE2	physical	26344197
TRXR1_HUMAN	TXNRD1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of THOP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257 AND LYS-538, AND MASSSPECTROMETRY.	19608861 [Abstract]