dbPTM

TACD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TACD2_HUMAN
UniProt AC	P09758
Protein Name	Tumor-associated calcium signal transducer 2
Gene Name	TACSTD2
Organism	Homo sapiens (Human).
Sequence Length	323
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	May function as a growth factor receptor..
Protein Sequence	MARGPGLAPPPLRLPLLLLVLAAVTGHTAAQDNCTCPTNKMTVCSPDGPGGRCQCRALGSGMAVDCSTLTSKCLLLKARMSAPKNARTLVRPSEHALVDNDGLYDPDCDPEGRFKARQCNQTSVCWCVNSVGVRRTDKGDLSLRCDELVRTHHILIDLRHRPTAGAFNHSDLDAELRRLFRERYRLHPKFVAAVHYEQPTIQIELRQNTSQKAAGDVDIGDAAYYFERDIKGESLFQGRGGLDLRVRGEPLQVERTLIYYLDEIPPKFSMKRLTAGLIAVIVVVVVALVAGMAVLVITNRRKSGKYKKVEIKELGELRKEPSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	N-linked_Glycosylation	GHTAAQDNCTCPTNK CCHHHHCCCCCCCCC	15.77	UniProtKB CARBOHYD
41	Sulfoxidation	CTCPTNKMTVCSPDG CCCCCCCEEEECCCC	3.54	28465586
60	Phosphorylation	CQCRALGSGMAVDCS CEEEECCCCCEEEHH	26.67	28102081
67	Phosphorylation	SGMAVDCSTLTSKCL CCCEEEHHHHHHHHH	23.22	28102081
68	Phosphorylation	GMAVDCSTLTSKCLL CCEEEHHHHHHHHHH	40.15	28102081
70	Phosphorylation	AVDCSTLTSKCLLLK EEEHHHHHHHHHHHH	26.65	28102081
71	Phosphorylation	VDCSTLTSKCLLLKA EEHHHHHHHHHHHHH	25.20	28102081
93	O-linked_Glycosylation	ARTLVRPSEHALVDN CCCCCCCCCCEEECC	31.30	55825165
120	N-linked_Glycosylation	RFKARQCNQTSVCWC CEECEECCCCEEEEE	39.57	UniProtKB CARBOHYD
130	Phosphorylation	SVCWCVNSVGVRRTD EEEEEEECCCCCCCC	10.39	-
142	Phosphorylation	RTDKGDLSLRCDELV CCCCCCCEEEHHHHH	20.64	24719451
168	N-linked_Glycosylation	RPTAGAFNHSDLDAE CCCCCCCCHHHHHHH	32.97	UniProtKB CARBOHYD
208	N-linked_Glycosylation	IQIELRQNTSQKAAG EEEEEECCCCCCCCC	34.95	UniProtKB CARBOHYD
212	Acetylation	LRQNTSQKAAGDVDI EECCCCCCCCCCCCC	39.72	7960403
224	Phosphorylation	VDIGDAAYYFERDIK CCCCHHHEEEEECCC	15.48	-
225	Phosphorylation	DIGDAAYYFERDIKG CCCHHHEEEEECCCC	8.34	-
231	Ubiquitination	YYFERDIKGESLFQG EEEEECCCCCCCCCC	62.00	29901268
259	Phosphorylation	QVERTLIYYLDEIPP EEEEEEEEHHHCCCC	10.90	-
269	Phosphorylation	DEIPPKFSMKRLTAG HCCCCCCCHHHHHHH	29.53	24719451
303	Phosphorylation	VITNRRKSGKYKKVE HHCCCCCCCCCEEEE	38.41	22817900
307	Ubiquitination	RRKSGKYKKVEIKEL CCCCCCCEEEEHHHH	54.55	23503661
308	Ubiquitination	RKSGKYKKVEIKELG CCCCCCEEEEHHHHH	41.85	29901268
312	Ubiquitination	KYKKVEIKELGELRK CCEEEEHHHHHHHCC	33.12	29901268
319	Ubiquitination	KELGELRKEPSL--- HHHHHHCCCCCC---	83.22	29967540
322	Phosphorylation	GELRKEPSL------ HHHCCCCCC------	48.04	28355574

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
303	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
322	S	Phosphorylation	Kinase	PKCA	P17252	PSP
322	S	Phosphorylation	Kinase	PKCD	Q05655	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TACD2_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 TACD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TACD2_HUMAN !!

Drug and Disease Associations

Kegg Disease
H00953	Gelatinous drop-like corneal dystrophy (GDCD); Subepithelial amyloidosis; Primary familial amyloidos
OMIM Disease
204870	Corneal dystrophy, gelatinous drop-like (GDLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TACD2_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 SER-322, AND MASSSPECTROMETRY.	17081983 [Abstract]