SC23B_HUMAN - dbPTM
SC23B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC23B_HUMAN
UniProt AC Q15437
Protein Name Protein transport protein Sec23B {ECO:0000305}
Gene Name SEC23B {ECO:0000312|HGNC:HGNC:10702}
Organism Homo sapiens (Human).
Sequence Length 767
Subcellular Localization Cytoplasmic vesicle, COPII-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytosol .
Protein Description Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex..
Protein Sequence MATYLEFIQQNEERDGVRFSWNVWPSSRLEATRMVVPLACLLTPLKERPDLPPVQYEPVLCSRPTCKAVLNPLCQVDYRAKLWACNFCFQRNQFPPAYGGISEVNQPAELMPQFSTIEYVIQRGAQSPLIFLYVVDTCLEEDDLQALKESLQMSLSLLPPDALVGLITFGRMVQVHELSCEGISKSYVFRGTKDLTAKQIQDMLGLTKPAMPMQQARPAQPQEHPFASSRFLQPVHKIDMNLTDLLGELQRDPWPVTQGKRPLRSTGVALSIAVGLLEGTFPNTGARIMLFTGGPPTQGPGMVVGDELKIPIRSWHDIEKDNARFMKKATKHYEMLANRTAANGHCIDIYACALDQTGLLEMKCCANLTGGYMVMGDSFNTSLFKQTFQRIFTKDFNGDFRMAFGATLDVKTSRELKIAGAIGPCVSLNVKGPCVSENELGVGGTSQWKICGLDPTSTLGIYFEVVNQHNTPIPQGGRGAIQFVTHYQHSSTQRRIRVTTIARNWADVQSQLRHIEAAFDQEAAAVLMARLGVFRAESEEGPDVLRWLDRQLIRLCQKFGQYNKEDPTSFRLSDSFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFARQDLTQSLIMIQPILYSYSFHGPPEPVLLDSSSILADRILLMDTFFQIVIYLGETIAQWRKAGYQDMPEYENFKHLLQAPLDDAQEILQARFPMPRYINTEHGGSQARFLLSKVNPSQTHNNLYAWGQETGAPILTDDVSLQVFMDHLKKLAVSSAC
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
2Acetylation------MATYLEFIQ
------CCCHHHHHH		12.6422223895
3Phosphorylation-----MATYLEFIQQ
-----CCCHHHHHHH		27.6020068231
4Phosphorylation----MATYLEFIQQN
----CCCHHHHHHHH		8.4923607784
32PhosphorylationPSSRLEATRMVVPLA
CHHHHHHHHHHHHHH		15.2123401153
34SulfoxidationSRLEATRMVVPLACL
HHHHHHHHHHHHHHH		2.8628465586
43PhosphorylationVPLACLLTPLKERPD
HHHHHHHHCCCCCCC		17.3923401153
67UbiquitinationLCSRPTCKAVLNPLC
ECCCCCHHHHHCCCC		43.97-
81UbiquitinationCQVDYRAKLWACNFC
CCCHHHHHHHHHHHH		35.25-
150PhosphorylationDLQALKESLQMSLSL
HHHHHHHHHHHHHHH		23.4725599653
154PhosphorylationLKESLQMSLSLLPPD
HHHHHHHHHHHCCHH		11.2225599653
168PhosphorylationDALVGLITFGRMVQV
HHHHHHHHHCCCEEE		25.6925599653
185UbiquitinationLSCEGISKSYVFRGT
EEECCCCHHHEECCC		43.83-
186PhosphorylationSCEGISKSYVFRGTK
EECCCCHHHEECCCC		21.53-
187PhosphorylationCEGISKSYVFRGTKD
ECCCCHHHEECCCCC		13.8224719451
193UbiquitinationSYVFRGTKDLTAKQI
HHEECCCCCCCHHHH		54.27-
198UbiquitinationGTKDLTAKQIQDMLG
CCCCCCHHHHHHHHC		42.57-
208UbiquitinationQDMLGLTKPAMPMQQ
HHHHCCCCCCCCHHH		35.50-
237UbiquitinationRFLQPVHKIDMNLTD
HCCCCCHHCCCCHHH		40.41-
260UbiquitinationPWPVTQGKRPLRSTG
CCCCCCCCCCCHHHC		40.8121906983
309UbiquitinationMVVGDELKIPIRSWH
EECCCEEECCCCCHH		44.3721890473
320UbiquitinationRSWHDIEKDNARFMK
CCHHHHHHHHHHHHH		57.5319608861
320AcetylationRSWHDIEKDNARFMK
CCHHHHHHHHHHHHH		57.5323749302
328UbiquitinationDNARFMKKATKHYEM
HHHHHHHHHHHHHHH		49.88-
331UbiquitinationRFMKKATKHYEMLAN
HHHHHHHHHHHHHHC		49.39-
333PhosphorylationMKKATKHYEMLANRT
HHHHHHHHHHHHCCC		12.46-
363AcetylationQTGLLEMKCCANLTG
CCCCHHCEECCCCCC		19.457696041
381PhosphorylationVMGDSFNTSLFKQTF
EECCCCCHHHHHHHH		25.46-
382PhosphorylationMGDSFNTSLFKQTFQ
ECCCCCHHHHHHHHH		32.6724719451
393PhosphorylationQTFQRIFTKDFNGDF
HHHHHHHCCCCCCCE		27.6020068231
394UbiquitinationTFQRIFTKDFNGDFR
HHHHHHCCCCCCCEE		49.9621890473
407PhosphorylationFRMAFGATLDVKTSR
EEEHEECEEECCCCC		24.7020068231
412PhosphorylationGATLDVKTSRELKIA
ECEEECCCCCCEEEC		32.6320068231
413PhosphorylationATLDVKTSRELKIAG
CEEECCCCCCEEECC		20.3129759185
431UbiquitinationPCVSLNVKGPCVSEN
CCEEEECCCCEECCC		56.9421890473
485PhosphorylationRGAIQFVTHYQHSST
CCCEEEEEEECCCCC		19.0229978859
487PhosphorylationAIQFVTHYQHSSTQR
CEEEEEEECCCCCCC		9.8829978859
490PhosphorylationFVTHYQHSSTQRRIR
EEEEECCCCCCCEEE		21.3929978859
491PhosphorylationVTHYQHSSTQRRIRV
EEEECCCCCCCEEEE		26.8329978859
492PhosphorylationTHYQHSSTQRRIRVT
EEECCCCCCCEEEEE		29.1629978859
558AcetylationQLIRLCQKFGQYNKE
HHHHHHHHHCCCCCC		50.9325953088
558UbiquitinationQLIRLCQKFGQYNKE
HHHHHHHHHCCCCCC		50.93-
564AcetylationQKFGQYNKEDPTSFR
HHHCCCCCCCCCCEE		59.57-
564UbiquitinationQKFGQYNKEDPTSFR
HHHCCCCCCCCCCEE		59.5721890473
671UbiquitinationETIAQWRKAGYQDMP
HHHHHHHHCCCCCCC		43.1121890473
680PhosphorylationGYQDMPEYENFKHLL
CCCCCCCCCCHHHHH		15.4227642862
684UbiquitinationMPEYENFKHLLQAPL
CCCCCCHHHHHHCCC		44.95-
707PhosphorylationARFPMPRYINTEHGG
HHCCCCCEEECCCCC		7.8328152594
710PhosphorylationPMPRYINTEHGGSQA
CCCCEEECCCCCHHH		21.5727732954
715PhosphorylationINTEHGGSQARFLLS
EECCCCCHHHHHHHC		25.8427732954
734PhosphorylationSQTHNNLYAWGQETG
HHCCCCCEECCHHCC		11.4827642862
760UbiquitinationVFMDHLKKLAVSSAC
HHHHHHHHHHHHHCC		48.30-
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
186SPhosphorylationKinaseULK1O75385
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC23B_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 SC23B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC24B_HUMANSEC24Bphysical
22939629
SRSF3_HUMANSRSF3physical
22939629
TMED9_HUMANTMED9physical
9472029
TMEDA_HUMANTMED10physical
9472029
TMED1_HUMANTMED1physical
9472029
TMED2_HUMANTMED2physical
9472029
ERD21_HUMANKDELR1physical
9472029
UD11_HUMANUGT1A1physical
9472029
GALT1_HUMANGALNT1physical
9472029
MA2A1_HUMANMAN2A1physical
9472029
PAXI_HUMANPXNphysical
22863883
SC24C_HUMANSEC24Cphysical
22863883
SC23B_HUMANSEC23Bphysical
25416956
CPSF7_HUMANCPSF7physical
25416956
FATE1_HUMANFATE1physical
25416956
DTX2_HUMANDTX2physical
25416956
PRRC1_HUMANPRRC1physical
25416956
SYNE4_HUMANSYNE4physical
25416956
CPNE2_HUMANCPNE2physical
26344197
SEC13_HUMANSEC13physical
26344197
SC24A_HUMANSEC24Aphysical
26344197
SC24B_HUMANSEC24Bphysical
26344197
PRRC1_HUMANPRRC1physical
21516116
HXA3_HUMANHOXA3physical
21516116
SC24D_HUMANSEC24Dphysical
21516116
Drug and Disease Associations
Kegg Disease
H00917 Congenital dyserythropoietic anemias (CDAs)
OMIM Disease
224100Anemia, congenital dyserythropoietic, 2 (CDAN2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SC23B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-320, AND MASS SPECTROMETRY.

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