dbPTM

SDC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SDC1_HUMAN
UniProt AC	P18827
Protein Name	Syndecan-1
Gene Name	SDC1
Organism	Homo sapiens (Human).
Sequence Length	310
Subcellular Localization	Membrane Single-pass type I membrane protein . Secreted . Secreted, exosome . Shedding of the ectodomain produces a soluble form.
Protein Description	Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP. [PubMed: 22660413]
Protein Sequence	MRRAALWLWLCALALSLQPALPQIVATNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPKEGEAVVLPEVEPGLTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFTFETSGENTAVVAVEPDRRNQSPVDQGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	O-linked_Glycosylation	PPEDQDGSGDDSDNF CCCCCCCCCCCCCCC	47.54	8163535
37	O-linked_Glycosylation	PPEDQDGSGDDSDNF CCCCCCCCCCCCCCC	47.54	-
43	N-linked_Glycosylation	GSGDDSDNFSGSGAG CCCCCCCCCCCCCCC	36.61	UniProtKB CARBOHYD
45	O-linked_Glycosylation	GDDSDNFSGSGAGAL CCCCCCCCCCCCCHH	38.00	8163535
45	O-linked_Glycosylation	GDDSDNFSGSGAGAL CCCCCCCCCCCCCHH	38.00	-
47	O-linked_Glycosylation	DSDNFSGSGAGALQD CCCCCCCCCCCHHHE	25.03	-
47	O-linked_Glycosylation	DSDNFSGSGAGALQD CCCCCCCCCCCHHHE	25.03	8163535
61	O-linked_Glycosylation	DITLSQQTPSTWKDT EEECCCCCCCCCCCC	16.15	55826851
72	O-linked_Glycosylation	WKDTQLLTAIPTSPE CCCCEEEEECCCCCC	31.00	55832533
76	O-linked_Glycosylation	QLLTAIPTSPEPTGL EEEEECCCCCCCCCC	51.29	55832539
77	O-linked_Glycosylation	LLTAIPTSPEPTGLE EEEECCCCCCCCCCE	23.16	55832545
81	O-linked_Glycosylation	IPTSPEPTGLEATAA CCCCCCCCCCEEEEE	53.38	55832549
86	O-linked_Glycosylation	EPTGLEATAASTSTL CCCCCEEEEEECCCC	17.24	OGP
89	O-linked_Glycosylation	GLEATAASTSTLPAG CCEEEEEECCCCCCC	22.04	OGP
90	O-linked_Glycosylation	LEATAASTSTLPAGE CEEEEEECCCCCCCC	22.47	OGP
91	O-linked_Glycosylation	EATAASTSTLPAGEG EEEEEECCCCCCCCC	26.00	OGP
92	O-linked_Glycosylation	ATAASTSTLPAGEGP EEEEECCCCCCCCCC	36.53	OGP
122	O-linked_Glycosylation	TAREQEATPRPRETT CHHHCCCCCCCCCCC	21.05	55830737
164	O-linked_Glycosylation	MQPGHHETSTPAGPS CCCCCCCCCCCCCCC	33.28	55826991
165	O-linked_Glycosylation	QPGHHETSTPAGPSQ CCCCCCCCCCCCCCH	29.43	55826997
166	O-linked_Glycosylation	PGHHETSTPAGPSQA CCCCCCCCCCCCCHH	25.28	55827003
171	O-linked_Glycosylation	TSTPAGPSQADLHTP CCCCCCCCHHCCCCC	36.76	55827007
177	O-linked_Glycosylation	PSQADLHTPHTEDGG CCHHCCCCCCCCCCC	24.86	55827011
180	O-linked_Glycosylation	ADLHTPHTEDGGPSA HCCCCCCCCCCCCCH	36.65	55827015
186	O-linked_Glycosylation	HTEDGGPSATERAAE CCCCCCCCHHHHHHH	51.61	55827019
188	O-linked_Glycosylation	EDGGPSATERAAEDG CCCCCCHHHHHHHHC	30.27	55827025
198	O-linked_Glycosylation	AAEDGASSQLPAAEG HHHHCCCCCCCCCCC	34.89	OGP
206	O-linked_Glycosylation	QLPAAEGSGEQDFTF CCCCCCCCCCCCEEE	30.57	8163535
206	O-linked_Glycosylation	QLPAAEGSGEQDFTF CCCCCCCCCCCCEEE	30.57	-
212	O-linked_Glycosylation	GSGEQDFTFETSGEN CCCCCCEEEEECCCC	28.93	OGP
215	Phosphorylation	EQDFTFETSGENTAV CCCEEEEECCCCEEE	37.53	24275569
215	O-linked_Glycosylation	EQDFTFETSGENTAV CCCEEEEECCCCEEE	37.53	OGP
216	Phosphorylation	QDFTFETSGENTAVV CCEEEEECCCCEEEE	36.59	24275569
216	O-linked_Glycosylation	QDFTFETSGENTAVV CCEEEEECCCCEEEE	36.59	8163535
216	O-linked_Glycosylation	QDFTFETSGENTAVV CCEEEEECCCCEEEE	36.59	-
220	O-linked_Glycosylation	FETSGENTAVVAVEP EEECCCCEEEEEECC	19.27	OGP
240	O-linked_Glycosylation	SPVDQGATGASQGLL CCCCCCCCCHHCCCC	39.85	51510761
243	Phosphorylation	DQGATGASQGLLDRK CCCCCCHHCCCCCHH	26.56	32142685
274	Ubiquitination	AVCLVGFMLYRMKKK HHHHHHHHHHHHHCC	2.36	21963094
280	Ubiquitination	FMLYRMKKKDEGSYS HHHHHHHCCCCCCCC	56.99	29901268
281	Ubiquitination	MLYRMKKKDEGSYSL HHHHHHCCCCCCCCC	56.33	29901268
283	Ubiquitination	YRMKKKDEGSYSLEE HHHHCCCCCCCCCCC	59.94	21963094
285	Phosphorylation	MKKKDEGSYSLEEPK HHCCCCCCCCCCCCC	14.97	23927012
286	Ubiquitination	KKKDEGSYSLEEPKQ HCCCCCCCCCCCCCC	28.29	21963094
286	Phosphorylation	KKKDEGSYSLEEPKQ HCCCCCCCCCCCCCC	28.29	25159151
287	Ubiquitination	KKDEGSYSLEEPKQA CCCCCCCCCCCCCCC	30.88	21963094
287	Phosphorylation	KKDEGSYSLEEPKQA CCCCCCCCCCCCCCC	30.88	23927012
292	Ubiquitination	SYSLEEPKQANGGAY CCCCCCCCCCCCCCC	66.38	21963094
296	Ubiquitination	EEPKQANGGAYQKPT CCCCCCCCCCCCCCC	25.73	21963094
299	Phosphorylation	KQANGGAYQKPTKQE CCCCCCCCCCCCCCH	21.97	22461510
299	Ubiquitination	KQANGGAYQKPTKQE CCCCCCCCCCCCCCH	21.97	21963094
301	Ubiquitination	ANGGAYQKPTKQEEF CCCCCCCCCCCCHHC	41.81	21906983
303	Phosphorylation	GGAYQKPTKQEEFYA CCCCCCCCCCHHCCC	53.01	28152594
304	Ubiquitination	GAYQKPTKQEEFYA- CCCCCCCCCHHCCC-	65.33	21906983
309	Phosphorylation	PTKQEEFYA------ CCCCHHCCC------	18.06	27273156
316	Ubiquitination	YA------------- CC-------------		21963094
325	Ubiquitination	---------------------- ----------------------		21963094
328	Ubiquitination	------------------------- -------------------------		21963094

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
286	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SDC1_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 SDC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HGF_HUMAN	HGF	physical	11830493
CATG_HUMAN	CTSG	physical	9565572
A4_HUMAN	APP	physical	21832049
ZN593_HUMAN	ZNF593	physical	22939629
EP300_HUMAN	EP300	physical	25404732
FARP1_HUMAN	FARP1	physical	28514442
DHRS2_HUMAN	DHRS2	physical	28514442
GMEB2_HUMAN	GMEB2	physical	28514442
FGF2_HUMAN	FGF2	physical	28514442
PRD10_HUMAN	PRDM10	physical	28514442
CYHR1_HUMAN	CYHR1	physical	28514442
EPHA2_HUMAN	EPHA2	physical	28514442
KC1G3_HUMAN	CSNK1G3	physical	28514442
OCLN_HUMAN	OCLN	physical	28514442
HMCS1_HUMAN	HMGCS1	physical	28514442
CCNY_HUMAN	CCNY	physical	28514442
EFR3A_HUMAN	EFR3A	physical	28514442
PTPRG_HUMAN	PTPRG	physical	28514442
ARVC_HUMAN	ARVCF	physical	28514442
AMPD2_HUMAN	AMPD2	physical	28514442
RAP2A_HUMAN	RAP2A	physical	28514442
RFTN1_HUMAN	RFTN1	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
EEPD1_HUMAN	EEPD1	physical	28514442
GNAZ_HUMAN	GNAZ	physical	28514442
VANG1_HUMAN	VANGL1	physical	28514442
RRAS_HUMAN	RRAS	physical	28514442
GBB4_HUMAN	GNB4	physical	28514442
GMEB1_HUMAN	GMEB1	physical	28514442
FBX46_HUMAN	FBXO46	physical	28514442
FTO_HUMAN	FTO	physical	28514442
KC1G2_HUMAN	CSNK1G2	physical	28514442
AHNK_HUMAN	AHNAK	physical	28514442
PRRC1_HUMAN	PRRC1	physical	28514442
CGL_HUMAN	CTH	physical	28514442
RASH_HUMAN	HRAS	physical	28514442
NCAM1_HUMAN	NCAM1	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
There are no disease associations of PTM sites.

Regulatory Network of SDC1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASSSPECTROMETRY.	18083107 [Abstract]