SC23A_HUMAN - dbPTM
SC23A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC23A_HUMAN
UniProt AC Q15436
Protein Name Protein transport protein Sec23A {ECO:0000305}
Gene Name SEC23A {ECO:0000312|HGNC:HGNC:10701}
Organism Homo sapiens (Human).
Sequence Length 765
Subcellular Localization Cytoplasmic vesicle, COPII-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytosol . Enriched at endoplasmic reticulum exit sites.
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 MTTYLEFIQQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCSRTTCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPSYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPLTQATRGPQVQQPPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGGRGAIQFVTQYQHSSGQRRIRVTTIARNWADAQTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESGAPILTDDVSLQVFMDHLKKLAVSSAA
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------MTTYLEFIQ
------CCCHHHHHH		24.9322223895
43PhosphorylationVPVAALFTPLKERPD
HHHHHHHCCCCCCCC		28.67-
46UbiquitinationAALFTPLKERPDLPP
HHHHCCCCCCCCCCC		53.5321963094
62PhosphorylationQYEPVLCSRTTCRAV
CCCCEECCHHHHHHH		28.62-
81UbiquitinationCQVDYRAKLWACNFC
CCCHHHHHHHHHHHH		35.25-
105UbiquitinationYAGISELNQPAELLP
CCCHHHCCCCHHHHH		41.56-
116UbiquitinationELLPQFSSIEYVVLR
HHHHCCCCCEEEEEC		22.26-
137O-linked_GlycosylationIFLYVVDTCMEDEDL
EEEEEHHHCCCHHHH		11.3523301498
150PhosphorylationDLQALKESMQMSLSL
HHHHHHHHHHHHHHH		16.84-
168O-linked_GlycosylationTALVGLITFGRMVQV
HHHHHHHHHCCCEEE		25.6923301498
184O-linked_GlycosylationELGCEGISKSYVFRG
ECCCCCCCHHHEECC		26.8023301498
185AcetylationLGCEGISKSYVFRGT
CCCCCCCHHHEECCC		43.8325953088
185MalonylationLGCEGISKSYVFRGT
CCCCCCCHHHEECCC		43.8326320211
185UbiquitinationLGCEGISKSYVFRGT
CCCCCCCHHHEECCC		43.83-
187PhosphorylationCEGISKSYVFRGTKD
CCCCCHHHEECCCCC		13.8224719451
193UbiquitinationSYVFRGTKDLSAKQL
HHEECCCCCCCHHHH		60.5422817900
1932-HydroxyisobutyrylationSYVFRGTKDLSAKQL
HHEECCCCCCCHHHH		60.54-
198UbiquitinationGTKDLSAKQLQEMLG
CCCCCCHHHHHHHHC		48.4421906983
203SulfoxidationSAKQLQEMLGLSKVP
CHHHHHHHHCCCCCC		2.0130846556
207PhosphorylationLQEMLGLSKVPLTQA
HHHHHCCCCCCCCCC		29.79-
208UbiquitinationQEMLGLSKVPLTQAT
HHHHCCCCCCCCCCC		53.5721906983
215PhosphorylationKVPLTQATRGPQVQQ
CCCCCCCCCCCCCCC		26.7528857561
226O-linked_GlycosylationQVQQPPPSNRFLQPV
CCCCCCCCCCCCCCC		46.5423301498
238SulfoxidationQPVQKIDMNLTDLLG
CCCCCCCCCHHHHHH		5.1521406390
241O-linked_GlycosylationQKIDMNLTDLLGELQ
CCCCCCHHHHHHHHH		21.4223301498
307UbiquitinationMVVGDELKTPIRSWH
CCCCCCCCCCCCCCC		50.6521906983
308PhosphorylationVVGDELKTPIRSWHD
CCCCCCCCCCCCCCC		36.2527551091
312PhosphorylationELKTPIRSWHDIDKD
CCCCCCCCCCCCCCC		29.4920873877
318UbiquitinationRSWHDIDKDNAKYVK
CCCCCCCCCCHHHHH		53.89-
326UbiquitinationDNAKYVKKGTKHFEA
CCHHHHHHHHHHHHH		62.8629967540
329UbiquitinationKYVKKGTKHFEALAN
HHHHHHHHHHHHHHH		55.7733845483
329MalonylationKYVKKGTKHFEALAN
HHHHHHHHHHHHHHH		55.7726320211
360SulfoxidationDQTGLLEMKCCPNLT
CCCCCCEEEECCCCC		3.9830846556
360UbiquitinationDQTGLLEMKCCPNLT
CCCCCCEEEECCCCC		3.98-
379PhosphorylationVMGDSFNTSLFKQTF
EECCCCCHHHHHHHH		25.46-
380PhosphorylationMGDSFNTSLFKQTFQ
ECCCCCHHHHHHHHH		32.6724719451
392UbiquitinationTFQRVFTKDMHGQFK
HHHHHHCCCCCCCEE		41.4029967540
3922-HydroxyisobutyrylationTFQRVFTKDMHGQFK
HHHHHHCCCCCCCEE		41.40-
405PhosphorylationFKMGFGGTLEIKTSR
EEECCCCEEEEEECC		22.9221406692
425PhosphorylationGAIGPCVSLNSKGPC
EEECCCEECCCCCCC		28.6620873877
428PhosphorylationGPCVSLNSKGPCVSE
CCCEECCCCCCCCCC		44.2620873877
429AcetylationPCVSLNSKGPCVSEN
CCEECCCCCCCCCCC		66.8426051181
429UbiquitinationPCVSLNSKGPCVSEN
CCEECCCCCCCCCCC		66.8429967540
432UbiquitinationSLNSKGPCVSENEIG
ECCCCCCCCCCCCCC		7.78-
449UbiquitinationGTCQWKICGLSPTTT
CCCEEEECCCCCCCE		3.89-
467UbiquitinationYFEVVNQHNAPIPQG
EEEHHHHCCCCCCCC		27.50-
508O-linked_GlycosylationRNWADAQTQIQNIAA
CCHHHHHHHHHHHHH		29.3823301498
516O-linked_GlycosylationQIQNIAASFDQEAAA
HHHHHHHCCCHHHHH		21.9723301498
556MalonylationQLIRLCQKFGEYHKD
HHHHHHHHHCHHCCC		55.1026320211
562UbiquitinationQKFGEYHKDDPSSFR
HHHCHHCCCCHHHCC		64.0321906983
566PhosphorylationEYHKDDPSSFRFSET
HHCCCCHHHCCCCCC		49.4520873877
567PhosphorylationYHKDDPSSFRFSETF
HCCCCHHHCCCCCCC		26.3220873877
587PhosphorylationFMFHLRRSSFLQVFN
HHHHCCHHCCHHHHC		21.0025849741
588PhosphorylationMFHLRRSSFLQVFNN
HHHCCHHCCHHHHCC		28.3225849741
600PhosphorylationFNNSPDESSYYRHHF
HCCCCCCHHHHHHHH		30.9028857561
601PhosphorylationNNSPDESSYYRHHFM
CCCCCCHHHHHHHHH		24.9228857561
602PhosphorylationNSPDESSYYRHHFMR
CCCCCHHHHHHHHHC		17.5028857561
603PhosphorylationSPDESSYYRHHFMRQ
CCCCHHHHHHHHHCC		12.8628857561
613PhosphorylationHFMRQDLTQSLIMIQ
HHHCCCHHHHHHHHH		25.1324043423
615PhosphorylationMRQDLTQSLIMIQPI
HCCCHHHHHHHHHHH		18.0324043423
624PhosphorylationIMIQPILYAYSFSGP
HHHHHHHHHHHCCCC		12.2924043423
626PhosphorylationIQPILYAYSFSGPPE
HHHHHHHHHCCCCCC		9.1924043423
627PhosphorylationQPILYAYSFSGPPEP
HHHHHHHHCCCCCCC		12.5524043423
627O-linked_GlycosylationQPILYAYSFSGPPEP
HHHHHHHHCCCCCCC		12.5523301498
629PhosphorylationILYAYSFSGPPEPVL
HHHHHHCCCCCCCEE		44.4424043423
629O-linked_GlycosylationILYAYSFSGPPEPVL
HHHHHHCCCCCCCEE		44.4423301498
639PhosphorylationPEPVLLDSSSILADR
CCCEEECCHHHHHHH		26.4224043423
639O-linked_GlycosylationPEPVLLDSSSILADR
CCCEEECCHHHHHHH		26.4223301498
640O-linked_GlycosylationEPVLLDSSSILADRI
CCEEECCHHHHHHHH		22.5123301498
640PhosphorylationEPVLLDSSSILADRI
CCEEECCHHHHHHHH		22.5124043423
641O-linked_GlycosylationPVLLDSSSILADRIL
CEEECCHHHHHHHHH		26.1023301498
641PhosphorylationPVLLDSSSILADRIL
CEEECCHHHHHHHHH		26.1024043423
669UbiquitinationETIAQWRKSGYQDMP
HHHHHHHHCCCCCCH		45.3223000965
669UbiquitinationETIAQWRKSGYQDMP
HHHHHHHHCCCCCCH		45.3221890473
670PhosphorylationTIAQWRKSGYQDMPE
HHHHHHHCCCCCCHH		33.8728857561
672PhosphorylationAQWRKSGYQDMPEYE
HHHHHCCCCCCHHHH		14.3928555341
675SulfoxidationRKSGYQDMPEYENFR
HHCCCCCCHHHHCHH		1.2830846556
678PhosphorylationGYQDMPEYENFRHLL
CCCCCHHHHCHHHHH		15.4227642862
693UbiquitinationQAPVDDAQEILHSRF
CCCCCCHHHHHHHCC		45.3021890473
705PhosphorylationSRFPMPRYIDTEHGG
HCCCCCCEEECCCCC		9.4027251275
708PhosphorylationPMPRYIDTEHGGSQA
CCCCEEECCCCCHHH		21.9627251275
713PhosphorylationIDTEHGGSQARFLLS
EECCCCCHHHHHHHH		25.8428857561
732PhosphorylationSQTHNNMYAWGQESG
CCCCCCCCCCCCCCC		11.0027642862
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
207SPhosphorylationKinaseULK1O75385
PSP
405TPhosphorylationKinaseULK1O75385
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC23A_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 SC23A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC24C_HUMANSEC24Cphysical
22939629
SC24B_HUMANSEC24Bphysical
22939629
SEC13_HUMANSEC13physical
22939629
SC24A_HUMANSEC24Aphysical
22939629
CHIP_HUMANSTUB1physical
22939629
TACC3_HUMANTACC3physical
22939629
TTL12_HUMANTTLL12physical
22939629
UBE2B_HUMANUBE2Bphysical
22939629
USP9X_HUMANUSP9Xphysical
22939629
THADA_HUMANTHADAphysical
22939629
SP100_HUMANSP100physical
22939629
UB2V2_HUMANUBE2V2physical
22939629
TTC1_HUMANTTC1physical
22939629
UBXN7_HUMANUBXN7physical
22939629
SNX3_HUMANSNX3physical
22939629
SERPH_HUMANSERPINH1physical
22939629
UBQL2_HUMANUBQLN2physical
22939629
TPM1_HUMANTPM1physical
22939629
STMN2_HUMANSTMN2physical
22939629
SGTA_HUMANSGTAphysical
22939629
CTNA1_HUMANCTNNA1physical
22863883
SYCC_HUMANCARSphysical
22863883
IF4B_HUMANEIF4Bphysical
22863883
GARS_HUMANGARSphysical
22863883
GFPT1_HUMANGFPT1physical
22863883
HIRP3_HUMANHIRIP3physical
22863883
HS74L_HUMANHSPA4Lphysical
22863883
HSP74_HUMANHSPA4physical
22863883
HS105_HUMANHSPH1physical
22863883
DPYL3_HUMANDPYSL3physical
22863883
PLOD2_HUMANPLOD2physical
22863883
ANM3_HUMANPRMT3physical
22863883
SAMH1_HUMANSAMHD1physical
22863883
RO60_HUMANTROVE2physical
22863883
TTC1_HUMANTTC1physical
22863883
XPO7_HUMANXPO7physical
22863883
ARMC1_HUMANARMC1physical
26344197
SEC13_HUMANSEC13physical
26344197
SC23B_HUMANSEC23Bphysical
26344197
SC24A_HUMANSEC24Aphysical
26344197
SC24B_HUMANSEC24Bphysical
26344197
SUMO3_HUMANSUMO3physical
26344197
Drug and Disease Associations
Kegg Disease
H01105 Cranio-lenticulo-sutural dysplasia (CLSD); Boyadjiev-Jabs syndrome
OMIM Disease
607812Craniolenticulosutural dysplasia (CLSD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SC23A_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 THR-308, AND MASSSPECTROMETRY.

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