ST32C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ST32C_HUMAN
• UniProt AC: Q86UX6
• Protein Name: Serine/threonine-protein kinase 32C
• Gene Name: STK32C {ECO:0000312|EMBL:AAH45760.1}
• Organism: Homo sapiens (Human).
• Sequence Length: 486
• Protein Sequence: MRSGAERRGSSAAASPGSPPPGRARPAGSDAPSALPPPAAGQPRARDSGDVRSQPRPLFQWSKWKKRMGSSMSAATARRPVFDDKEDVNFDHFQILRAIGKGSFGKVCIVQKRDTEKMYAMKYMNKQQCIERDEVRNVFRELEILQEIEHVFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQQNVQFSEDTVRLYICEMALALDYLRGQHIIHRDVKPDNILLDERGHAHLTDFNIATIIKDGERATALAGTKPYMAPEIFHSFVNGGTGYSFEVDWWSVGVMAYELLRGWRPYDIHSSNAVESLVQLFSTVSVQYVPTWSKEMVALLRKLLTVNPEHRLSSLQDVQAAPALAGVLWDHLSEKRVEPGFVPNKGRLHCDPTFELEEMILESRPLHKKKKRLAKNKSRDNSRDSSQSENDYLQDCLDAIQQDFVIFNREKLKRSQDLPREPLPAPESRDAAEPVEDEAERSALPMCGPICPSAGSG

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
8	Methylation	MRSGAERRGSSAAAS CCCCCCCCCCCCCCC	40.63	115920153
10	Phosphorylation	SGAERRGSSAAASPG CCCCCCCCCCCCCCC	18.26	23927012
11	Phosphorylation	GAERRGSSAAASPGS CCCCCCCCCCCCCCC	25.42	23927012
15	Phosphorylation	RGSSAAASPGSPPPG CCCCCCCCCCCCCCC	25.68	29255136
18	Phosphorylation	SAAASPGSPPPGRAR CCCCCCCCCCCCCCC	37.30	29255136
29	Phosphorylation	GRARPAGSDAPSALP CCCCCCCCCCCCCCC	32.48	25850435
33	Phosphorylation	PAGSDAPSALPPPAA CCCCCCCCCCCCCCC	44.13	25850435
70	Phosphorylation	KWKKRMGSSMSAATA HHHHHHCCCCCHHHC	17.33	23312004
71	Phosphorylation	WKKRMGSSMSAATAR HHHHHCCCCCHHHCC	15.84	28857561
73	Phosphorylation	KRMGSSMSAATARRP HHHCCCCCHHHCCCC	19.39	28857561
76	Phosphorylation	GSSMSAATARRPVFD CCCCCHHHCCCCCCC	22.03	23312004
101 (in isoform 2)	Ubiquitination	-	45.31	21906983
119	Phosphorylation	KRDTEKMYAMKYMNK CCCHHHHHHHHHCCH	18.02	-
218	Ubiquitination	HIIHRDVKPDNILLD CEECCCCCCCCEEEC	51.44	21906983
218 (in isoform 1)	Ubiquitination	-	51.44	21906983
247 (in isoform 2)	Ubiquitination	-	7.91	21906983
299	Phosphorylation	WRPYDIHSSNAVESL CCCCCCCCCCHHHHH	26.14	27251275
320	Phosphorylation	VSVQYVPTWSKEMVA CCCEECCCCCHHHHH	32.12	27251275
322	Phosphorylation	VQYVPTWSKEMVALL CEECCCCCHHHHHHH	22.63	27251275
364	Ubiquitination	LWDHLSEKRVEPGFV HHHHHHCCCCCCCCC	59.37	21906983
364 (in isoform 1)	Ubiquitination	-	59.37	21906983
374	Ubiquitination	EPGFVPNKGRLHCDP CCCCCCCCCCCCCCC	39.06	-
407	Phosphorylation	KRLAKNKSRDNSRDS HHHHHCCCCCCCCCC	55.02	22617229
411	Phosphorylation	KNKSRDNSRDSSQSE HCCCCCCCCCCCHHH	41.58	22617229

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ST32C_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ST32C_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ST32C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FDFT_HUMAN	FDFT1	physical	26186194
CDC37_HUMAN	CDC37	physical	26186194
MCM5_HUMAN	MCM5	physical	26186194

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15 AND SER-18,AND MASS SPECTROMETRY.
PubMed: 18669648