dbPTM

SDC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SDC2_HUMAN
UniProt AC	P34741
Protein Name	Syndecan-2
Gene Name	SDC2
Organism	Homo sapiens (Human).
Sequence Length	201
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity)..
Protein Sequence	MRRAWILLTLGLVACVSAESRAELTSDKDMYLDNSSIEEASGVYPIDDDDYASASGSGADEDVESPELTTSRPLPKILLTSAAPKVETTTLNIQNKIPAQTKSPEETDKEKVHLSDSERKMDPAEEDTNVYTEKHSDSLFKRTEVLAAVIAGGVIGFLFAIFLILLLVYRMRKKDEGSYDLGERKPSSAAYQKAPTKEFYA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	RRAWILLTLGLVACV CHHHHHHHHHHHHHH	18.48	24043423
17	Phosphorylation	LGLVACVSAESRAEL HHHHHHHCHHHHHHH	26.63	24043423
20	Phosphorylation	VACVSAESRAELTSD HHHHCHHHHHHHCCC	36.19	24043423
36	Phosphorylation	DMYLDNSSIEEASGV CCCCCCCCHHHHCCC	40.03	29759185
41	Phosphorylation	NSSIEEASGVYPIDD CCCHHHHCCCEECCC	31.88	-
41	O-linked_Glycosylation	NSSIEEASGVYPIDD CCCHHHHCCCEECCC	31.88	-
55	O-linked_Glycosylation	DDDYASASGSGADED CCCCCCCCCCCCCCC	30.88	-
57	O-linked_Glycosylation	DYASASGSGADEDVE CCCCCCCCCCCCCCC	28.45	-
80	O-linked_Glycosylation	PLPKILLTSAAPKVE CCCEEEECCCCCCEE	16.93	55829463
81	O-linked_Glycosylation	LPKILLTSAAPKVET CCEEEECCCCCCEEE	23.54	55829469
88	O-linked_Glycosylation	SAAPKVETTTLNIQN CCCCCEEEEEEECCC	28.24	55826565
89	O-linked_Glycosylation	AAPKVETTTLNIQNK CCCCEEEEEEECCCC	18.77	55826571
90	O-linked_Glycosylation	APKVETTTLNIQNKI CCCEEEEEEECCCCC	25.81	55826575
101	O-linked_Glycosylation	QNKIPAQTKSPEETD CCCCCCCCCCCCCCC	35.28	22171320
107	O-linked_Glycosylation	QTKSPEETDKEKVHL CCCCCCCCCCCCCCC	51.19	55828905
115	O-linked_Glycosylation	DKEKVHLSDSERKMD CCCCCCCCHHHHCCC	24.98	OGP
115	Phosphorylation	DKEKVHLSDSERKMD CCCCCCCCHHHHCCC	24.98	26091039
138	Phosphorylation	YTEKHSDSLFKRTEV CCHHCCCCHHHHHHH	38.43	24719451
174	Ubiquitination	LVYRMRKKDEGSYDL HHHHHHHCCCCCCCC	51.12	-
178	Phosphorylation	MRKKDEGSYDLGERK HHHCCCCCCCCCCCC	17.27	24732914
179	Phosphorylation	RKKDEGSYDLGERKP HHCCCCCCCCCCCCC	26.50	16997272
184	Methylation	GSYDLGERKPSSAAY CCCCCCCCCCCCHHH	55.15	24156243
185	Ubiquitination	SYDLGERKPSSAAYQ CCCCCCCCCCCHHHH	44.97	-
187	Phosphorylation	DLGERKPSSAAYQKA CCCCCCCCCHHHHCC	35.33	30266825
188	Phosphorylation	LGERKPSSAAYQKAP CCCCCCCCHHHHCCC	25.99	30266825
191	Phosphorylation	RKPSSAAYQKAPTKE CCCCCHHHHCCCCCC	15.40	29396449
193	Ubiquitination	PSSAAYQKAPTKEFY CCCHHHHCCCCCCCC	43.59	-
196	Phosphorylation	AAYQKAPTKEFYA-- HHHHCCCCCCCCC--	48.33	29759185
197	Ubiquitination	AYQKAPTKEFYA--- HHHCCCCCCCCC---	44.78	-
200	Phosphorylation	KAPTKEFYA------ CCCCCCCCC------	16.70	29341593

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
115	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
179	Y	Phosphorylation	Kinase	SRC	P12931	PSP
187	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
187	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
188	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
188	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SDC2_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 SDC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E41L1_HUMAN	EPB41L1	physical	12676536
ITPR1_HUMAN	ITPR1	physical	12676536
CSKP_HUMAN	CASK	physical	12676536
CSF2R_HUMAN	CSF2RA	physical	10734053
SDCB1_HUMAN	SDCBP	physical	9391086
FINC_HUMAN	FN1	physical	10772816
SDC2_HUMAN	SDC2	physical	9244383
A1AT_HUMAN	SERPINA1	physical	21988832
SDC2_HUMAN	SDC2	physical	21988832
DHRS2_HUMAN	DHRS2	physical	28514442
FGF2_HUMAN	FGF2	physical	28514442
PDPK1_HUMAN	PDPK1	physical	28514442
GMEB1_HUMAN	GMEB1	physical	28514442
PRD10_HUMAN	PRDM10	physical	28514442
GMEB2_HUMAN	GMEB2	physical	28514442
CAMKV_HUMAN	CAMKV	physical	28514442
SNX33_HUMAN	SNX33	physical	28514442
SULF1_HUMAN	SULF1	physical	28514442
TEFM_HUMAN	TEFM	physical	28514442
NBEL1_HUMAN	NBEAL1	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
DOP2_HUMAN	DOPEY2	physical	28514442
SEM3C_HUMAN	SEMA3C	physical	28514442
FARP1_HUMAN	FARP1	physical	28514442
AMPD2_HUMAN	AMPD2	physical	28514442
TM192_HUMAN	TMEM192	physical	28514442
KLHL7_HUMAN	KLHL7	physical	28514442
SNX18_HUMAN	SNX18	physical	28514442
TF3C2_HUMAN	GTF3C2	physical	28514442
VANG1_HUMAN	VANGL1	physical	28514442
FGRL1_HUMAN	FGFRL1	physical	28514442
FGFR3_HUMAN	FGFR3	physical	28514442
CTR3_HUMAN	SLC7A3	physical	28514442
SULF2_HUMAN	SULF2	physical	28514442
FGFR2_HUMAN	FGFR2	physical	28514442
TMM11_HUMAN	TMEM11	physical	28514442
XPC_HUMAN	XPC	physical	28514442
CKAP5_HUMAN	CKAP5	physical	28514442
OSBL8_HUMAN	OSBPL8	physical	28514442
ZN460_HUMAN	ZNF460	physical	28514442
HEAT6_HUMAN	HEATR6	physical	28514442
ECHB_HUMAN	HADHB	physical	28514442
ZNF92_HUMAN	ZNF92	physical	28514442
RN213_HUMAN	RNF213	physical	28514442
CNDH2_HUMAN	NCAPH2	physical	28514442
CAND2_HUMAN	CAND2	physical	28514442
S10AD_HUMAN	S100A13	physical	28514442
TF3C1_HUMAN	GTF3C1	physical	28514442
MTR1L_HUMAN	GPR50	physical	28514442
VANG2_HUMAN	VANGL2	physical	28514442
TF3C3_HUMAN	GTF3C3	physical	28514442
ECHA_HUMAN	HADHA	physical	28514442
TM186_HUMAN	TMEM186	physical	28514442
EXOC3_HUMAN	EXOC3	physical	28514442
SMC2_HUMAN	SMC2	physical	28514442

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
DB00020	Sargramostim

Regulatory Network of SDC2_HUMAN

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT THR-101, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]