dbPTM

TICN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TICN2_HUMAN
UniProt AC	Q92563
Protein Name	Testican-2
Gene Name	SPOCK2
Organism	Homo sapiens (Human).
Sequence Length	424
Subcellular Localization	Secreted, extracellular space, extracellular matrix .
Protein Description	May participate in diverse steps of neurogenesis. Binds calcium..
Protein Sequence	MRAPGCGRLVLPLLLLAAAALAEGDAKGLKEGETPGNFMEDEQWLSSISQYSGKIKHWNRFRDEVEDDYIKSWEDNQQGDEALDTTKDPCQKVKCSRHKVCIAQGYQRAMCISRKKLEHRIKQPTVKLHGNKDSICKPCHMAQLASVCGSDGHTYSSVCKLEQQACLSSKQLAVRCEGPCPCPTEQAATSTADGKPETCTGQDLADLGDRLRDWFQLLHENSKQNGSASSVAGPASGLDKSLGASCKDSIGWMFSKLDTSADLFLDQTELAAINLDKYEVCIRPFFNSCDTYKDGRVSTAEWCFCFWREKPPCLAELERIQIQEAAKKKPGIFIPSCDEDGYYRKMQCDQSSGDCWCVDQLGLELTGTRTHGSPDCDDIVGFSGDFGSGVGWEDEEEKETEEAGEEAEEEEGEAGEADDGGYIW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
69	Phosphorylation	RDEVEDDYIKSWEDN HHHCHHHHHHCCCCC	23.67	29759185
72	Phosphorylation	VEDDYIKSWEDNQQG CHHHHHHCCCCCCCC	26.58	14702039
85	Phosphorylation	QGDEALDTTKDPCQK CCCHHHHCCCCHHHH	36.27	29759185
86	Phosphorylation	GDEALDTTKDPCQKV CCHHHHCCCCHHHHC	32.87	22817900
125	Phosphorylation	EHRIKQPTVKLHGNK HHHCCCCCEEECCCC	27.98	29083192
154	Phosphorylation	VCGSDGHTYSSVCKL HHCCCCCCHHHHHHH	30.54	-
155	Phosphorylation	CGSDGHTYSSVCKLE HCCCCCCHHHHHHHH	8.02	-
156	Phosphorylation	GSDGHTYSSVCKLEQ CCCCCCHHHHHHHHH	19.90	-
184	O-linked_Glycosylation	EGPCPCPTEQAATST CCCCCCCCHHHCCCC	47.66	OGP
189	O-linked_Glycosylation	CPTEQAATSTADGKP CCCHHHCCCCCCCCC	29.62	OGP
225	N-linked_Glycosylation	LHENSKQNGSASSVA HHHHCCCCCCCCCCC	50.56	UniProtKB CARBOHYD
230	O-linked_Glycosylation	KQNGSASSVAGPASG CCCCCCCCCCCCCCC	18.72	OGP
383	O-linked_Glycosylation	CDDIVGFSGDFGSGV HHHEEEECCCCCCCC	31.37	-
383	O-linked_Glycosylation	CDDIVGFSGDFGSGV HHHEEEECCCCCCCC	31.37	10386950
388	O-linked_Glycosylation	GFSGDFGSGVGWEDE EECCCCCCCCCCCCH	30.24	-
388	O-linked_Glycosylation	GFSGDFGSGVGWEDE EECCCCCCCCCCCCH	30.24	10386950

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
72	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TICN2_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 TICN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TICN3_HUMAN	SPOCK3	physical	12810672

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 TICN2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND MASSSPECTROMETRY.	17081983 [Abstract]