SCAM3_HUMAN - dbPTM
SCAM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCAM3_HUMAN
UniProt AC O14828
Protein Name Secretory carrier-associated membrane protein 3
Gene Name SCAMP3
Organism Homo sapiens (Human).
Sequence Length 347
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface..
Protein Sequence MAQSRDGGNPFAEPSELDNPFQDPAVIQHRPSRQYATLDVYNPFETREPPPAYEPPAPAPLPPPSAPSLQPSRKLSPTEPKNYGSYSTQASAAAATAELLKKQEELNRKAEELDRRERELQHAALGGTATRQNNWPPLPSFCPVQPCFFQDISMEIPQEFQKTVSTMYYLWMCSTLALLLNFLACLASFCVETNNGAGFGLSILWVLLFTPCSFVCWYRPMYKAFRSDSSFNFFVFFFIFFVQDVLFVLQAIGIPGWGFSGWISALVVPKGNTAVSVLMLLVALLFTGIAVLGIVMLKRIHSLYRRTGASFQKAQQEFAAGVFSNPAVRTAAANAAAGAAENAFRAP
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
4Phosphorylation----MAQSRDGGNPF
----CCCCCCCCCCC		23.8526074081
15PhosphorylationGNPFAEPSELDNPFQ
CCCCCCHHHCCCCCC		42.1528152594
27 (in isoform 2)Phosphorylation-2.8728796482
32PhosphorylationAVIQHRPSRQYATLD
HHHCCCCCCCEEEEE		31.7929255136
34UbiquitinationIQHRPSRQYATLDVY
HCCCCCCCEEEEEEC		36.2323000965
35UbiquitinationQHRPSRQYATLDVYN
CCCCCCCEEEEEECC		10.6323000965
35PhosphorylationQHRPSRQYATLDVYN
CCCCCCCEEEEEECC		10.6321945579
37PhosphorylationRPSRQYATLDVYNPF
CCCCCEEEEEECCCC		20.6821945579
39 (in isoform 2)Phosphorylation-36.1826434776
41PhosphorylationQYATLDVYNPFETRE
CEEEEEECCCCCCCC		19.4521945579
42UbiquitinationYATLDVYNPFETREP
EEEEEECCCCCCCCC		34.3322053931
42 (in isoform 2)Phosphorylation-34.3326434776
46PhosphorylationDVYNPFETREPPPAY
EECCCCCCCCCCCCC		40.4921945579
46 (in isoform 2)Phosphorylation-40.4926434776
48UbiquitinationYNPFETREPPPAYEP
CCCCCCCCCCCCCCC		70.3627667366
48 (in isoform 2)Ubiquitination-70.3621890473
50PhosphorylationPFETREPPPAYEPPA
CCCCCCCCCCCCCCC		22.7732645325
53PhosphorylationTREPPPAYEPPAPAP
CCCCCCCCCCCCCCC		34.4421945579
55 (in isoform 2)Ubiquitination-20.0621890473
55UbiquitinationEPPPAYEPPAPAPLP
CCCCCCCCCCCCCCC		20.0623000965
65PhosphorylationPAPLPPPSAPSLQPS
CCCCCCCCCCCCCCC		59.5921945579
68PhosphorylationLPPPSAPSLQPSRKL
CCCCCCCCCCCCCCC		39.0821945579
72PhosphorylationSAPSLQPSRKLSPTE
CCCCCCCCCCCCCCC		29.1421945579
74 (in isoform 1)Ubiquitination-58.6221890473
74UbiquitinationPSLQPSRKLSPTEPK
CCCCCCCCCCCCCCC		58.6227667366
75 (in isoform 2)Ubiquitination-7.8221890473
75UbiquitinationSLQPSRKLSPTEPKN
CCCCCCCCCCCCCCC		7.8223000965
75NeddylationSLQPSRKLSPTEPKN
CCCCCCCCCCCCCCC		7.8232015554
76UbiquitinationLQPSRKLSPTEPKNY
CCCCCCCCCCCCCCC		32.5823000965
76PhosphorylationLQPSRKLSPTEPKNY
CCCCCCCCCCCCCCC		32.5829255136
76 (in isoform 2)Ubiquitination-32.5821890473
78PhosphorylationPSRKLSPTEPKNYGS
CCCCCCCCCCCCCCC		62.6430266825
81UbiquitinationKLSPTEPKNYGSYST
CCCCCCCCCCCCHHH		57.4823000965
81 (in isoform 1)Ubiquitination-57.4821890473
83 (in isoform 2)Ubiquitination-17.3621890473
83UbiquitinationSPTEPKNYGSYSTQA
CCCCCCCCCCHHHHH		17.3622053931
83PhosphorylationSPTEPKNYGSYSTQA
CCCCCCCCCCHHHHH		17.3621945579
85PhosphorylationTEPKNYGSYSTQASA
CCCCCCCCHHHHHHH		12.9221945579
86PhosphorylationEPKNYGSYSTQASAA
CCCCCCCHHHHHHHH		16.0421945579
87PhosphorylationPKNYGSYSTQASAAA
CCCCCCHHHHHHHHH		18.7521945579
88PhosphorylationKNYGSYSTQASAAAA
CCCCCHHHHHHHHHH		21.6621945579
91PhosphorylationGSYSTQASAAAATAE
CCHHHHHHHHHHHHH		14.5021945579
96PhosphorylationQASAAAATAELLKKQ
HHHHHHHHHHHHHHH		18.8821945579
101 (in isoform 1)Ubiquitination-66.1021890473
101UbiquitinationAATAELLKKQEELNR
HHHHHHHHHHHHHHH		66.1023000965
101NeddylationAATAELLKKQEELNR
HHHHHHHHHHHHHHH		66.1032015554
102 (in isoform 1)Ubiquitination-64.0121890473
102UbiquitinationATAELLKKQEELNRK
HHHHHHHHHHHHHHH		64.0123000965
109 (in isoform 1)Ubiquitination-60.1121890473
109UbiquitinationKQEELNRKAEELDRR
HHHHHHHHHHHHHHH		60.1121906983
128PhosphorylationQHAALGGTATRQNNW
HHHHHCCCCCCCCCC		24.0625867546
130PhosphorylationAALGGTATRQNNWPP
HHHCCCCCCCCCCCC		32.4025867546
190S-palmitoylationLACLASFCVETNNGA
HHHHHHHHHHCCCCC		2.2129575903
212S-palmitoylationWVLLFTPCSFVCWYR
HHHHHCCCHHHHHHH		4.4729575903
216S-palmitoylationFTPCSFVCWYRPMYK
HCCCHHHHHHHHHHH		2.2029575903
246UbiquitinationIFFVQDVLFVLQAIG
HHHHHHHHHHHHHHC		3.1023000965
287 (in isoform 2)Ubiquitination-27.8721890473
287UbiquitinationLLVALLFTGIAVLGI
HHHHHHHHHHHHHHH		27.8723000965
299UbiquitinationLGIVMLKRIHSLYRR
HHHHHHHHHHHHHHH		28.0823000965
302PhosphorylationVMLKRIHSLYRRTGA
HHHHHHHHHHHHHCC		25.4024719451
304PhosphorylationLKRIHSLYRRTGASF
HHHHHHHHHHHCCHH		10.8924719451
313UbiquitinationRTGASFQKAQQEFAA
HHCCHHHHHHHHHHH		46.2623000965
313 (in isoform 1)Ubiquitination-46.2621890473
313SumoylationRTGASFQKAQQEFAA
HHCCHHHHHHHHHHH		46.2625114211
324PhosphorylationEFAAGVFSNPAVRTA
HHHHCCCCCHHHHHH		39.2320860994
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

Oops, there are no upstream regulatory protein records of SCAM3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCAM3_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 SCAM3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEDD4_HUMANNEDD4physical
19158374
WWP2_HUMANWWP2physical
19158374
YAP1_HUMANYAP1physical
19158374
TS101_HUMANTSG101physical
19158374
A4_HUMANAPPphysical
21832049
VATE1_HUMANATP6V1E1physical
22939629
TIAR_HUMANTIAL1physical
22939629
SRPRB_HUMANSRPRBphysical
22939629
SLIRP_HUMANSLIRPphysical
22939629
SUGP1_HUMANSUGP1physical
22939629
TPX2_HUMANTPX2physical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
BAP31_HUMANBCAP31physical
26344197
OST48_HUMANDDOSTphysical
26344197
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 SCAM3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-85, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-76, 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-76, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASSSPECTROMETRY.
"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-76, AND MASSSPECTROMETRY.
"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-83, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND MASSSPECTROMETRY.

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