dbPTM

TSSK4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TSSK4_HUMAN
UniProt AC	Q6SA08
Protein Name	Testis-specific serine/threonine-protein kinase 4
Gene Name	TSSK4
Organism	Homo sapiens (Human).
Sequence Length	328
Subcellular Localization
Protein Description	May be involved in a signaling pathway during male germ cell development or mature sperm function (By similarity). Phosphorylates CREB1 on Ser-133 and stimulates downstream signaling..
Protein Sequence	MGKGDVLEAAPTTTAYHSLMDEYGYEVGKAIGHGSYGSVYEAFYTKQKVMVAVKIISKKKASDDYLNKFLPREIQVMKVLRHKYLINFYRAIESTSRVYIILELAQGGDVLEWIQRYGACSEPLAGKWFSQLTLGIAYLHSKSIVHRDLKLENLLLDKWENVKISDFGFAKMVPSNQPVGCSPSYRQVNCFSHLSQTYCGSFAYACPEILRGLPYNPFLSDTWSMGVILYTLVVAHLPFDDTNLKKLLRETQKEVTFPANHTISQECKNLILQMLRQATKRATILDIIKDSWVLKFQPEQPTHEIRLLEAMCQLHNTTKQHQSLQITT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
62	Phosphorylation	IISKKKASDDYLNKF HHHCCCCCHHHHHHH	39.64	29457462
165	Phosphorylation	KWENVKISDFGFAKM HCCCCEECCCCCCEE	22.59	-
197	Phosphorylation	CFSHLSQTYCGSFAY CCHHHCCHHHHHHHH	19.87	-
251	Phosphorylation	LKKLLRETQKEVTFP HHHHHHHHHCCCCCC	38.21	17525332
256	Phosphorylation	RETQKEVTFPANHTI HHHHCCCCCCCCCCC	25.62	17525332
264	Phosphorylation	FPANHTISQECKNLI CCCCCCCCHHHHHHH	22.53	17525332
283	Phosphorylation	RQATKRATILDIIKD HHHHHHCCHHHHHCC	26.55	-

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
Oops, there are no upstream regulatory protein records of TSSK4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
197	T	Phosphorylation	-
Activated by autophosphorylation on Thr-197.
197	T	Phosphorylation	-
ODF2 potentiates the autophosphorylation activity of TSSK4 at Thr-197.

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 TSSK4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TSSK4_HUMAN !!

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 TSSK4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251; THR-256 ANDSER-264, AND MASS SPECTROMETRY.	17525332 [Abstract]