TCHP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TCHP_HUMAN
• UniProt AC: Q9BT92
• Protein Name: Trichoplein keratin filament-binding protein
• Gene Name: TCHP {ECO:0000312|EMBL:AAH04285.1}
• Organism: Homo sapiens (Human).
• Sequence Length: 498
• Subcellular Localization: Cytoplasm, cytoskeleton . Cytoplasm . Cell membrane . Mitochondrion . Cell junction, desmosome .
• Protein Description: Tumor suppressor which has the ability to inhibit cell growth and be pro-apoptotic during cell stress. Inhibits cell growth in bladder and prostate cancer cells by a down-regulation of HSPB1 by inhibiting its phosphorylation. May act as a 'capping' or 'branching' protein for keratin filaments in the cell periphery. May regulate K8/K18 filament and desmosome organization mainly at the apical or peripheral regions of simple epithelial cells. [PubMed: 15731013]
• Protein Sequence: MALPTLPSYWCSQQRLNQQLARQREQEARLRQQWEQNSRYFRMSDICSSKQAEWSSKTSYQRSMHAYQREKMKEEKRRSLEARREKLRQLMQEEQDLLARELEELRLSMNLQERRIREQHGKLKSAKEEQRKLIAEQLLYEHWKKNNPKLREMELDLHQKHVVNSWEMQKEEKKQQEATAEQENKRYENEYERARREALERMKAEEERRQLEDKLQAEALLQQMEELKLKEVEATKLKKEQENLLKQRWELERLEEERKQMEAFRQKAELGRFLRHQYNAQLSRRTQQIQEELEADRRILQALLEKEDESQRLHLARREQVMADVAWMKQAIEEQLQLERAREAELQMLLREEAKEMWEKREAEWARERSARDRLMSEVLTGRQQQIQEKIEQNRRAQEESLKHREQLIRNLEEVRELARREKEESEKLKSARKQELEAQVAERRLQAWEADQQEEEEEEEARRVEQLSDALLQQEAETMAEQGYRPKPYGHPKIAWN

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
50	Ubiquitination	MSDICSSKQAEWSSK HHHHCCCCCCCCCCC	36.91	PubMed
57	Ubiquitination	KQAEWSSKTSYQRSM CCCCCCCCHHHHHHH	35.65	PubMed
71	Acetylation	MHAYQREKMKEEKRR HHHHHHHHHHHHHHH	58.42	12649993
122	Ubiquitination	RIREQHGKLKSAKEE HHHHHHCCHHCHHHH	51.09	-
132	Ubiquitination	SAKEEQRKLIAEQLL CHHHHHHHHHHHHHH	43.89	-
140	Phosphorylation	LIAEQLLYEHWKKNN HHHHHHHHHHHHHHC	17.84	28796482
144	Ubiquitination	QLLYEHWKKNNPKLR HHHHHHHHHHCHHHH	47.75	-
170	Ubiquitination	VNSWEMQKEEKKQQE HHHHHHHHHHHHHHH	67.54	-
214	Ubiquitination	ERRQLEDKLQAEALL HHHHHHHHHHHHHHH	32.88	-
228	Ubiquitination	LQQMEELKLKEVEAT HHHHHHHCCHHHHHH	61.87	-
246	Ubiquitination	KEQENLLKQRWELER HHHHHHHHHHHHHHH	40.77	-
259	Ubiquitination	ERLEEERKQMEAFRQ HHHHHHHHHHHHHHH	58.22	-
278	Phosphorylation	GRFLRHQYNAQLSRR HHHHHHHHHHHHHHH	13.31	22817900
283	Phosphorylation	HQYNAQLSRRTQQIQ HHHHHHHHHHHHHHH	13.98	-
306	Ubiquitination	ILQALLEKEDESQRL HHHHHHHCCCHHHHH	71.13	-
390	Ubiquitination	RQQQIQEKIEQNRRA HHHHHHHHHHHHHHH	34.86	-
469	Phosphorylation	ARRVEQLSDALLQQE HHHHHHHHHHHHHHH	22.11	27050516
488	Ubiquitination	AEQGYRPKPYGHPKI HHCCCCCCCCCCCCC	41.70	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	KCTD17	Q8N5Z5	PMID:25270598

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TCHP_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 TCHP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LZTS2_HUMAN	LZTS2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
DYDC1_HUMAN	DYDC1	physical	25416956
MIPO1_HUMAN	MIPOL1	physical	25416956
CC172_HUMAN	CCDC172	physical	25416956

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.