STBD1_HUMAN - dbPTM
STBD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STBD1_HUMAN
UniProt AC O95210
Protein Name Starch-binding domain-containing protein 1 {ECO:0000303|PubMed:20810658}
Gene Name STBD1 {ECO:0000303|PubMed:20810658}
Organism Homo sapiens (Human).
Sequence Length 358
Subcellular Localization Preautophagosomal structure membrane
Single-pass type III membrane protein . Endoplasmic reticulum membrane
Single-pass type III membrane protein . Distributed in the transverse tubules and/or near the junctional sarcoplasmic reticulum (PubMed:97
Protein Description Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes..
Protein Sequence MGAVWSALLVGGGLAGALFVWLLRGGPGDTGKDGDAEQEKDAPLGGAAIPGGHQSGSSGLSPGPSGQELVTKPEHLQESNGHLISKTKDLGKLQAASWRLQNPSREVCDNSREHVPSGQFPDTEAPATSETSNSRSYSEVSRNESLESPMGEWGFQKGQEISAKAATCFAEKLPSSNLLKNRAKEEMSLSDLNSQDRVDHEEWEMVPRHSSWGDVGVGGSLKAPVLNLNQGMDNGRSTLVEARGQQVHGKMERVAVMPAGSQQVSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRFLETGHEDKVVHAWWGIH
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
6Phosphorylation--MGAVWSALLVGGG
--CCHHHHHHCCCCH		11.48-
55PhosphorylationAIPGGHQSGSSGLSP
CCCCCCCCCCCCCCC		34.6625627689
57PhosphorylationPGGHQSGSSGLSPGP
CCCCCCCCCCCCCCC		26.8625159151
58PhosphorylationGGHQSGSSGLSPGPS
CCCCCCCCCCCCCCC		47.4825627689
61PhosphorylationQSGSSGLSPGPSGQE
CCCCCCCCCCCCCCC		31.1925627689
65PhosphorylationSGLSPGPSGQELVTK
CCCCCCCCCCCCCCC		60.0524275569
79PhosphorylationKPEHLQESNGHLISK
CHHHHHHHCCCEEEC		34.8424275569
85PhosphorylationESNGHLISKTKDLGK
HHCCCEEECCCCHHH		40.4024275569
97PhosphorylationLGKLQAASWRLQNPS
HHHHHHHHHHCCCCC		18.7529083192
104PhosphorylationSWRLQNPSREVCDNS
HHHCCCCCHHHCCCC		48.9326437602
117PhosphorylationNSREHVPSGQFPDTE
CCCCCCCCCCCCCCC		44.1022798277
128PhosphorylationPDTEAPATSETSNSR
CCCCCCCCCCCCCCC		26.4924275569
129PhosphorylationDTEAPATSETSNSRS
CCCCCCCCCCCCCCC		40.7724275569
132PhosphorylationAPATSETSNSRSYSE
CCCCCCCCCCCCCCC		28.8528555341
136PhosphorylationSETSNSRSYSEVSRN
CCCCCCCCCCCCCCC		32.6020166139
137PhosphorylationETSNSRSYSEVSRNE
CCCCCCCCCCCCCCC		14.0328857561
138PhosphorylationTSNSRSYSEVSRNES
CCCCCCCCCCCCCCC		32.5420166139
141PhosphorylationSRSYSEVSRNESLES
CCCCCCCCCCCCCCC		25.9020166139
145PhosphorylationSEVSRNESLESPMGE
CCCCCCCCCCCCCCC		40.7721712546
148PhosphorylationSRNESLESPMGEWGF
CCCCCCCCCCCCCCC		26.0225159151
175PhosphorylationCFAEKLPSSNLLKNR
HHHHHCCCCHHHHHH		42.1525159151
176PhosphorylationFAEKLPSSNLLKNRA
HHHHCCCCHHHHHHH		29.5620166139
180MalonylationLPSSNLLKNRAKEEM
CCCCHHHHHHHHHHC		47.7832601280
188PhosphorylationNRAKEEMSLSDLNSQ
HHHHHHCCHHHCCCC		28.1824972180
190PhosphorylationAKEEMSLSDLNSQDR
HHHHCCHHHCCCCCC		32.5120166139
194PhosphorylationMSLSDLNSQDRVDHE
CCHHHCCCCCCCCHH		40.5326437602
210PhosphorylationWEMVPRHSSWGDVGV
HEECCCCCCCCCCCC		29.1230266825
211PhosphorylationEMVPRHSSWGDVGVG
EECCCCCCCCCCCCC		29.0230266825
220PhosphorylationGDVGVGGSLKAPVLN
CCCCCCCCEECCEEE		22.2923927012
265PhosphorylationPAGSQQVSVRFQVHY
ECCCCEEEEEEEEEE		11.8428857561
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
175SPhosphorylationKinaseAMPKA1Q13131
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STBD1_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 STBD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBRL1_HUMANGABARAPL1physical
21893048
KASH5_HUMANCCDC155physical
25416956
GLYG_HUMANGYG1physical
26186194
GYS2_HUMANGYS2physical
26186194
GYS1_HUMANGYS1physical
26186194
GBRAP_HUMANGABARAPphysical
26186194
GBRL1_HUMANGABARAPL1physical
26186194
PYGB_HUMANPYGBphysical
26186194
TRI18_HUMANMID1physical
26186194
WDFY1_HUMANWDFY1physical
26186194
GLYG2_HUMANGYG2physical
26186194
EPM2A_HUMANEPM2Aphysical
26186194
CO4A2_HUMANCOL4A2physical
26186194
PPR3D_HUMANPPP1R3Dphysical
26186194
EPM2A_HUMANEPM2Aphysical
28514442
GBRL1_HUMANGABARAPL1physical
28514442
GLYG2_HUMANGYG2physical
28514442
TRI18_HUMANMID1physical
28514442
GLGB_HUMANGBE1physical
28514442
GBRAP_HUMANGABARAPphysical
28514442
GYS1_HUMANGYS1physical
28514442
GLYG_HUMANGYG1physical
28514442
PYGB_HUMANPYGBphysical
28514442
PPR3D_HUMANPPP1R3Dphysical
28514442
WDFY1_HUMANWDFY1physical
28514442
GDE_HUMANAGLphysical
28514442
GYS2_HUMANGYS2physical
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 STBD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-148, AND MASSSPECTROMETRY.

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