SDCB1_HUMAN - dbPTM
SDCB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDCB1_HUMAN
UniProt AC O00560
Protein Name Syntenin-1
Gene Name SDCBP
Organism Homo sapiens (Human).
Sequence Length 298
Subcellular Localization Cell junction, focal adhesion . Cell junction, adherens junction . Cell membrane
Peripheral membrane protein . Endoplasmic reticulum membrane
Peripheral membrane protein . Nucleus . Melanosome . Cytoplasm, cytosol . Cytoplasm, cytoskeleton . Secreted,
Protein Description Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. [PubMed: 26291527 Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1]
Protein Sequence MSLYPSLEDLKVDKVIQAQTAFSANPANPAILSEASAPIPHDGNLYPRLYPELSQYMGLSLNEEEIRANVAVVSGAPLQGQLVARPSSINYMVAPVTGNDVGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTITMHKDSTGHVGFIFKNGKITSIVKDSSAARNGLLTEHNICEINGQNVIGLKDSQIADILSTSGTVVTITIMPAFIFEHIIKRMAPSIMKSLMDHTIPEV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSLYPSLED
------CCCCCCHHH
36.2920068231
2Acetylation------MSLYPSLED
------CCCCCCHHH
36.2920068231
4Phosphorylation----MSLYPSLEDLK
----CCCCCCHHHCC
5.4029255136
6Phosphorylation--MSLYPSLEDLKVD
--CCCCCCHHHCCCC
30.7329255136
6 (in isoform 3)Phosphorylation-30.7318578522
11UbiquitinationYPSLEDLKVDKVIQA
CCCHHHCCCCEEEEH
61.79-
14 (in isoform 2)Ubiquitination-44.20-
14UbiquitinationLEDLKVDKVIQAQTA
HHHCCCCEEEEHHHC
44.2021906983
23PhosphorylationIQAQTAFSANPANPA
EEHHHCCCCCCCCHH
25.3628152594
33PhosphorylationPANPAILSEASAPIP
CCCHHHHCCCCCCCC
25.6328152594
36PhosphorylationPAILSEASAPIPHDG
HHHHCCCCCCCCCCC
30.4428152594
46PhosphorylationIPHDGNLYPRLYPEL
CCCCCCCCHHHCHHH
7.1225159151
50PhosphorylationGNLYPRLYPELSQYM
CCCCHHHCHHHHHHC
8.9228348404
54PhosphorylationPRLYPELSQYMGLSL
HHHCHHHHHHCCCCC
20.0127273156
56PhosphorylationLYPELSQYMGLSLNE
HCHHHHHHCCCCCCH
6.9719605366
60PhosphorylationLSQYMGLSLNEEEIR
HHHHCCCCCCHHHHH
24.3421082442
74 (in isoform 2)Phosphorylation-23.7320071362
74PhosphorylationRANVAVVSGAPLQGQ
HHCEEEEECCCCCCE
23.7328450419
86 (in isoform 2)Phosphorylation-23.7728348404
87 (in isoform 2)Phosphorylation-37.9924719451
87PhosphorylationGQLVARPSSINYMVA
CEEEECCCCCCEEEE
37.9928450419
88PhosphorylationQLVARPSSINYMVAP
EEEECCCCCCEEEEC
19.9628450419
91PhosphorylationARPSSINYMVAPVTG
ECCCCCCEEEECCCC
7.4121082442
109UbiquitinationGIRRAEIKQGIREVI
HHCHHHHHCCCCEEE
33.70-
119AcetylationIREVILCKDQDGKIG
CCEEEEEECCCCCEE
55.7826051181
1192-HydroxyisobutyrylationIREVILCKDQDGKIG
CCEEEEEECCCCCEE
55.78-
124AcetylationLCKDQDGKIGLRLKS
EEECCCCCEEEEEEE
41.7225953088
124MalonylationLCKDQDGKIGLRLKS
EEECCCCCEEEEEEE
41.7226320211
124UbiquitinationLCKDQDGKIGLRLKS
EEECCCCCEEEEEEE
41.72-
131PhosphorylationKIGLRLKSIDNGIFV
CEEEEEEEECCCEEE
39.5025850435
145PhosphorylationVQLVQANSPASLVGL
EEEEECCCCHHHEEC
25.5125850435
148PhosphorylationVQANSPASLVGLRFG
EECCCCHHHEECEEC
27.2925850435
170PhosphorylationGENCAGWSSDKAHKV
CCCCCCCCCHHHHHH
27.9527251275
171PhosphorylationENCAGWSSDKAHKVL
CCCCCCCCHHHHHHH
36.3027251275
1732-HydroxyisobutyrylationCAGWSSDKAHKVLKQ
CCCCCCHHHHHHHHH
55.10-
173AcetylationCAGWSSDKAHKVLKQ
CCCCCCHHHHHHHHH
55.1026051181
173UbiquitinationCAGWSSDKAHKVLKQ
CCCCCCHHHHHHHHH
55.10-
178 (in isoform 2)Ubiquitination-3.97-
179 (in isoform 3)Ubiquitination-42.4421890473
1792-HydroxyisobutyrylationDKAHKVLKQAFGEKI
HHHHHHHHHHHCCCE
42.44-
179UbiquitinationDKAHKVLKQAFGEKI
HHHHHHHHHHHCCCE
42.44-
184 (in isoform 2)Ubiquitination-34.53-
185UbiquitinationLKQAFGEKITMTIRD
HHHHHCCCEEEEECC
43.8021890473
185UbiquitinationLKQAFGEKITMTIRD
HHHHHCCCEEEEECC
43.8021890473
185 (in isoform 1)Ubiquitination-43.8021890473
187PhosphorylationQAFGEKITMTIRDRP
HHHCCCEEEEECCCC
21.2320068231
189PhosphorylationFGEKITMTIRDRPFE
HCCCEEEEECCCCCE
12.2920068231
200PhosphorylationRPFERTITMHKDSTG
CCCEEEEEEECCCCC
16.7720068231
205PhosphorylationTITMHKDSTGHVGFI
EEEEECCCCCCEEEE
40.8820068231
205 (in isoform 2)Ubiquitination-40.8821890473
206PhosphorylationITMHKDSTGHVGFIF
EEEECCCCCCEEEEE
41.2520068231
214AcetylationGHVGFIFKNGKITSI
CCEEEEEECCEEEEE
61.0325953088
220PhosphorylationFKNGKITSIVKDSSA
EECCEEEEEECCCHH
28.9422210691
222 (in isoform 2)Ubiquitination-5.89-
223MalonylationGKITSIVKDSSAARN
CEEEEEECCCHHHHC
50.6626320211
223UbiquitinationGKITSIVKDSSAARN
CEEEEEECCCHHHHC
50.662190698
252PhosphorylationNVIGLKDSQIADILS
EEECCCHHHHHHHHH
23.1530576142
260PhosphorylationQIADILSTSGTVVTI
HHHHHHHCCCCEEEE
27.9430576142
266PhosphorylationSTSGTVVTITIMPAF
HCCCCEEEEEEEHHH
14.2030576142
285PhosphorylationIIKRMAPSIMKSLMD
HHHHHCHHHHHHHHH
26.2722210691
289PhosphorylationMAPSIMKSLMDHTIP
HCHHHHHHHHHCCCC
16.1422210691
294PhosphorylationMKSLMDHTIPEV---
HHHHHHCCCCCC---
33.6824719451

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
4YPhosphorylationKinaseSRCP12931
PSP
6SPhosphorylationKinaseULK1O75385
PSP
46YPhosphorylationKinaseSRCP12931
PSP
60SPhosphorylationKinaseULK1O75385
PSP
131SPhosphorylationKinaseAURAO14965
PSP
200TPhosphorylationKinaseAURAO14965
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDCB1_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 SDCB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ULK1_HUMANULK1physical
15014045
RAB5A_HUMANRAB5Aphysical
15014045
SOX4_HUMANSOX4physical
11498591
SDC1_HUMANSDC1physical
11179419
MERL_HUMANNF2physical
11432873
TRAF6_HUMANTRAF6physical
18234474
SET_HUMANSETphysical
25416956
SRSF7_HUMANSRSF7physical
25416956
SIAH1_HUMANSIAH1physical
25416956
SMCA2_HUMANSMARCA2physical
25416956
T23O_HUMANTDO2physical
25416956
TFCP2_HUMANTFCP2physical
25416956
TRAF5_HUMANTRAF5physical
25416956
UBE2A_HUMANUBE2Aphysical
25416956
ZBT14_HUMANZBTB14physical
25416956
CGBP1_HUMANCGGBP1physical
25416956
CAPS1_HUMANCADPSphysical
25416956
SSNA1_HUMANSSNA1physical
25416956
WASL_HUMANWASLphysical
25416956
PPIP1_HUMANPSTPIP1physical
25416956
PNMA1_HUMANPNMA1physical
25416956
SRS11_HUMANSRSF11physical
25416956
RBM39_HUMANRBM39physical
25416956
MYOME_HUMANPDE4DIPphysical
25416956
ABI2_HUMANABI2physical
25416956
CACO2_HUMANCALCOCO2physical
25416956
IKZF1_HUMANIKZF1physical
25416956
CDIPT_HUMANCDIPTphysical
25416956
TRI38_HUMANTRIM38physical
25416956
AN32B_HUMANANP32Bphysical
25416956
PNMA2_HUMANPNMA2physical
25416956
SDCG3_HUMANSDCCAG3physical
25416956
RUN3A_HUMANRUNDC3Aphysical
25416956
TRIM1_HUMANMID2physical
25416956
DMC1_HUMANDMC1physical
25416956
LSM6_HUMANLSM6physical
25416956
KLHL2_HUMANKLHL2physical
25416956
PUF60_HUMANPUF60physical
25416956
MARE3_HUMANMAPRE3physical
25416956
TRI32_HUMANTRIM32physical
25416956
5NTC_HUMANNT5C2physical
25416956
MTUS2_HUMANMTUS2physical
25416956
LDOC1_HUMANLDOC1physical
25416956
TFIP8_HUMANTNFAIP8physical
25416956
TKFC_HUMANDAKphysical
25416956
OSTF1_HUMANOSTF1physical
25416956
GNMT_HUMANGNMTphysical
25416956
ST1B1_HUMANSULT1B1physical
25416956
MED4_HUMANMED4physical
25416956
WASC3_HUMANCCDC53physical
25416956
MTNB_HUMANAPIPphysical
25416956
CUTC_HUMANCUTCphysical
25416956
NO40_HUMANZCCHC17physical
25416956
MBD3_HUMANMBD3physical
25416956
PRR13_HUMANPRR13physical
25416956
NECA2_HUMANNECAB2physical
25416956
LZTL1_HUMANLZTFL1physical
25416956
ROP1A_HUMANROPN1physical
25416956
KCTD9_HUMANKCTD9physical
25416956
ZCH10_HUMANZCCHC10physical
25416956
CA109_HUMANC1orf109physical
25416956
THG1_HUMANTHG1Lphysical
25416956
F118A_HUMANFAM118Aphysical
25416956
ENOX1_HUMANENOX1physical
25416956
CEP55_HUMANCEP55physical
25416956
CK057_HUMANC11orf57physical
25416956
NAGK_HUMANNAGKphysical
25416956
PR40A_HUMANPRPF40Aphysical
25416956
SEPT3_HUMANSEPT3physical
25416956
IF5A2_HUMANEIF5A2physical
25416956
TRI54_HUMANTRIM54physical
25416956
HOMEZ_HUMANHOMEZphysical
25416956
KLH12_HUMANKLHL12physical
25416956
RIC8A_HUMANRIC8Aphysical
25416956
CDCP1_HUMANCDCP1physical
25416956
NADK_HUMANNADKphysical
25416956
P5CR3_HUMANPYCRLphysical
25416956
DCTP1_HUMANDCTPP1physical
25416956
F118B_HUMANFAM118Bphysical
25416956
C102B_HUMANCCDC102Bphysical
25416956
FAD1_HUMANFLAD1physical
25416956
CK068_HUMANC11orf68physical
25416956
TEKT1_HUMANTEKT1physical
25416956
DTBP1_HUMANDTNBP1physical
25416956
EIF1A_HUMANEIF1ADphysical
25416956
PR38A_HUMANPRPF38Aphysical
25416956
EAF1_HUMANEAF1physical
25416956
ANR40_HUMANANKRD40physical
25416956
TIFA_HUMANTIFAphysical
25416956
REEP6_HUMANREEP6physical
25416956
FOXP2_HUMANFOXP2physical
25416956
MR1L1_HUMANMRFAP1L1physical
25416956
CKLF5_HUMANCMTM5physical
25416956
EDAD_HUMANEDARADDphysical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
KCTD6_HUMANKCTD6physical
25416956
KHDR2_HUMANKHDRBS2physical
25416956
GPT11_HUMANGPATCH11physical
25416956
IN80E_HUMANINO80Ephysical
25416956
KCTD1_HUMANKCTD1physical
25416956
ERIC2_HUMANERICH2physical
25416956
SR1IP_HUMANSREK1IP1physical
25416956
IHO1_HUMANCCDC36physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
B2L15_HUMANBCL2L15physical
25416956
CT453_HUMANCT45A3physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
TM239_HUMANTMEM239physical
25416956
PDC6I_HUMANPDCD6IPphysical
22660413
SDC2_HUMANSDC2physical
22660413
SYRC_HUMANRARSphysical
26186194
SYIC_HUMANIARSphysical
26186194
SYQ_HUMANQARSphysical
26186194
SYEP_HUMANEPRSphysical
26186194
AIMP2_HUMANAIMP2physical
26186194
SYDC_HUMANDARSphysical
26186194
SYMC_HUMANMARSphysical
26186194
SYTC2_HUMANTARSL2physical
26186194
AIMP1_HUMANAIMP1physical
26186194
MCA3_HUMANEEF1E1physical
26186194
SYLC_HUMANLARSphysical
26186194
PP6R2_HUMANPPP6R2physical
26186194
ANR28_HUMANANKRD28physical
26186194
SYTC2_HUMANTARSL2physical
28514442
AIMP1_HUMANAIMP1physical
28514442
SYRC_HUMANRARSphysical
28514442
AIMP2_HUMANAIMP2physical
28514442
SYDC_HUMANDARSphysical
28514442
PSME2_HUMANPSME2physical
28514442
SYLC_HUMANLARSphysical
28514442
SYMC_HUMANMARSphysical
28514442
SYIC_HUMANIARSphysical
28514442
SYEP_HUMANEPRSphysical
28514442
MCA3_HUMANEEF1E1physical
28514442
ANR28_HUMANANKRD28physical
28514442
SYQ_HUMANQARSphysical
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 SDCB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.
"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-46 AND TYR-91, AND MASSSPECTROMETRY.

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