SC24D_HUMAN - dbPTM
SC24D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC24D_HUMAN
UniProt AC O94855
Protein Name Protein transport protein Sec24D {ECO:0000305}
Gene Name SEC24D {ECO:0000312|HGNC:HGNC:10706}
Organism Homo sapiens (Human).
Sequence Length 1032
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. [PubMed: 17499046]
Protein Sequence MSQQGYVATPPYSQPQPGIGLSPPHYGHYGDPSHTASPTGMMKPAGPLGATATRGMLPPGPPPPGPHQFGQNGAHATGHPPQRFPGPPPVNNVASSHAPYQPSAQSSYPGPISTSSVTQLGSQLSAMQINSYGSGMAPPSQGPPGPLSATSLQTPPRPPQPSILQPGSQVLPPPPTTLNGPGASPLPLPMYRPDGLSGPPPPNAQYQPPPLPGQTLGAGYPPQQANSGPQMAGAQLSYPGGFPGGPAQMAGPPQPQKKLDPDSIPSPIQVIENDRASRGGQVYATNTRGQIPPLVTTDCMIQDQGNASPRFIRCTTYCFPCTSDMAKQAQIPLAAVIKPFATIPSNESPLYLVNHGESGPVRCNRCKAYMCPFMQFIEGGRRYQCGFCNCVNDVPPFYFQHLDHIGRRLDHYEKPELSLGSYEYVATLDYCRKSKPPNPPAFIFMIDVSYSNIKNGLVKLICEELKTMLEKIPKEEQEETSAIRVGFITYNKVLHFFNVKSNLAQPQMMVVTDVGEVFVPLLDGFLVNYQESQSVIHNLLDQIPDMFADSNENETVFAPVIQAGMEALKAADCPGKLFIFHSSLPTAEAPGKLKNRDDKKLVNTDKEKILFQPQTNVYDSLAKDCVAHGCSVTLFLFPSQYVDVASLGLVPQLTGGTLYKYNNFQMHLDRQQFLNDLRNDIEKKIGFDAIMRVRTSTGFRATDFFGGILMNNTTDVEMAAIDCDKAVTVEFKHDDKLSEDSGALIQCAVLYTTISGQRRLRIHNLGLNCSSQLADLYKSCETDALINFFAKSAFKAVLHQPLKVIREILVNQTAHMLACYRKNCASPSAASQLILPDSMKVLPVYMNCLLKNCVLLSRPEISTDERAYQRQLVMTMGVADSQLFFYPQLLPIHTLDVKSTMLPAAVRCSESRLSEEGIFLLANGLHMFLWLGVSSPPELIQGIFNVPSFAHINTDMTLLPEVGNPYSQQLRMIMGIIQQKRPYSMKLTIVKQREQPEMVFRQFLVEDKGLYGGSSYVDFLCCVHKEICQLLN
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------MSQQGYVAT
------CCCCCCCCC
42.3823401153
6Phosphorylation--MSQQGYVATPPYS
--CCCCCCCCCCCCC
5.2026074081
9PhosphorylationSQQGYVATPPYSQPQ
CCCCCCCCCCCCCCC
18.1123401153
12PhosphorylationGYVATPPYSQPQPGI
CCCCCCCCCCCCCCC
22.5726074081
13PhosphorylationYVATPPYSQPQPGIG
CCCCCCCCCCCCCCC
40.9526074081
22PhosphorylationPQPGIGLSPPHYGHY
CCCCCCCCCCCCCCC
31.0425159151
26PhosphorylationIGLSPPHYGHYGDPS
CCCCCCCCCCCCCCC
16.0426074081
29PhosphorylationSPPHYGHYGDPSHTA
CCCCCCCCCCCCCCC
20.8926074081
33PhosphorylationYGHYGDPSHTASPTG
CCCCCCCCCCCCCCC
37.9023401153
35PhosphorylationHYGDPSHTASPTGMM
CCCCCCCCCCCCCCC
32.9228348404
37PhosphorylationGDPSHTASPTGMMKP
CCCCCCCCCCCCCCC
24.9328348404
140PhosphorylationGSGMAPPSQGPPGPL
CCCCCCCCCCCCCCC
46.8623879269
148PhosphorylationQGPPGPLSATSLQTP
CCCCCCCCCCCCCCC
32.4123879269
154PhosphorylationLSATSLQTPPRPPQP
CCCCCCCCCCCCCCC
40.3223879269
258UbiquitinationGPPQPQKKLDPDSIP
CCCCCCCCCCCCCCC
53.53-
263PhosphorylationQKKLDPDSIPSPIQV
CCCCCCCCCCCCEEE
41.6130266825
266PhosphorylationLDPDSIPSPIQVIEN
CCCCCCCCCEEEEEC
32.7230266825
278MethylationIENDRASRGGQVYAT
EECCCCCCCCCEEEE
52.88115493563
283PhosphorylationASRGGQVYATNTRGQ
CCCCCCEEEECCCCC
10.3821253578
300SulfoxidationPLVTTDCMIQDQGNA
CCEEECCEECCCCCC
3.2530846556
315PhosphorylationSPRFIRCTTYCFPCT
CCCEEEEEEEEEECC
15.7924114839
317PhosphorylationRFIRCTTYCFPCTSD
CEEEEEEEEEECCHH
3.6424114839
322PhosphorylationTTYCFPCTSDMAKQA
EEEEEECCHHHHHHC
28.1824114839
323PhosphorylationTYCFPCTSDMAKQAQ
EEEEECCHHHHHHCC
31.9124114839
338UbiquitinationIPLAAVIKPFATIPS
CCCEEEECCCCCCCC
27.73-
339 (in isoform 2)Ubiquitination-17.00-
466UbiquitinationKLICEELKTMLEKIP
HHHHHHHHHHHHHCC
34.86-
471UbiquitinationELKTMLEKIPKEEQE
HHHHHHHHCCHHHHH
61.42-
480PhosphorylationPKEEQEETSAIRVGF
CHHHHHHHCCEEEEE
23.7829083192
481PhosphorylationKEEQEETSAIRVGFI
HHHHHHHCCEEEEEE
25.6129083192
576AcetylationKAADCPGKLFIFHSS
HHCCCCCCEEEEECC
25.9326051181
576UbiquitinationKAADCPGKLFIFHSS
HHCCCCCCEEEEECC
25.93-
577 (in isoform 2)Ubiquitination-5.02-
594UbiquitinationAEAPGKLKNRDDKKL
CCCCCCCCCCCCCCC
54.12-
595 (in isoform 2)Ubiquitination-64.15-
600UbiquitinationLKNRDDKKLVNTDKE
CCCCCCCCCCCCCHH
65.74-
608UbiquitinationLVNTDKEKILFQPQT
CCCCCHHHHCCCCCC
50.91-
639PhosphorylationVTLFLFPSQYVDVAS
EEEEECCHHHCCHHH
27.1522210691
646PhosphorylationSQYVDVASLGLVPQL
HHHCCHHHHCCCCCC
23.8722210691
666SulfoxidationYKYNNFQMHLDRQQF
EEECCEEEEECHHHH
2.7230846556
684UbiquitinationLRNDIEKKIGFDAIM
HHHHHHHHHCHHHEE
34.96-
685 (in isoform 2)Ubiquitination-11.15-
702PhosphorylationTSTGFRATDFFGGIL
CCCCCCCCCCCCCEE
29.1423532336
728PhosphorylationIDCDKAVTVEFKHDD
ECCCCCEEEEEECCC
21.1223532336
770PhosphorylationHNLGLNCSSQLADLY
ECCCCCCHHHHHHHH
21.7527732954
771PhosphorylationNLGLNCSSQLADLYK
CCCCCCHHHHHHHHH
31.2627732954
779PhosphorylationQLADLYKSCETDALI
HHHHHHHHHCHHHHH
12.0221712546
791 (in isoform 1)Ubiquitination-36.8421890473
791UbiquitinationALINFFAKSAFKAVL
HHHHHHHHHHHHHHH
36.8421906983
792 (in isoform 2)Ubiquitination-35.1921890473
795UbiquitinationFFAKSAFKAVLHQPL
HHHHHHHHHHHHCHH
36.982189047
795AcetylationFFAKSAFKAVLHQPL
HHHHHHHHHHHHCHH
36.9825953088
795 (in isoform 1)Ubiquitination-36.9821890473
796 (in isoform 2)Ubiquitination-11.5821890473
803MalonylationAVLHQPLKVIREILV
HHHHCHHHHHHHHHC
42.1526320211
803UbiquitinationAVLHQPLKVIREILV
HHHHCHHHHHHHHHC
42.15-
804 (in isoform 2)Ubiquitination-7.03-
816SulfoxidationLVNQTAHMLACYRKN
HCHHHHHHHHHHHHC
2.0530846556
826PhosphorylationCYRKNCASPSAASQL
HHHHCCCCHHHHHHH
22.9125850435
828PhosphorylationRKNCASPSAASQLIL
HHCCCCHHHHHHHHC
33.6925850435
831PhosphorylationCASPSAASQLILPDS
CCCHHHHHHHHCCCH
25.8221712546
851UbiquitinationVYMNCLLKNCVLLSR
HHHHHHHHCCHHHCC
35.04-
852 (in isoform 2)Ubiquitination-22.54-
857PhosphorylationLKNCVLLSRPEISTD
HHCCHHHCCCCCCCC
41.4429449344
862PhosphorylationLLSRPEISTDERAYQ
HHCCCCCCCCHHHHH
28.3029449344
863PhosphorylationLSRPEISTDERAYQR
HCCCCCCCCHHHHHH
47.7629449344
875PhosphorylationYQRQLVMTMGVADSQ
HHHHHHHHHCCCCHH
11.8624043423
881PhosphorylationMTMGVADSQLFFYPQ
HHHCCCCHHEEECCC
21.0325332170
886PhosphorylationADSQLFFYPQLLPIH
CCHHEEECCCCCCCE
5.2424043423
894PhosphorylationPQLLPIHTLDVKSTM
CCCCCCEECCCCCCC
25.9324043423
899PhosphorylationIHTLDVKSTMLPAAV
CEECCCCCCCCCHHH
20.9225690035
901SulfoxidationTLDVKSTMLPAAVRC
ECCCCCCCCCHHHHC
5.6421406390
911PhosphorylationAAVRCSESRLSEEGI
HHHHCCCCCCCHHHE
23.40-
981 (in isoform 2)Ubiquitination-30.93-
988PhosphorylationRPYSMKLTIVKQREQ
CCCCCEEEEEECCCC
20.43-
991UbiquitinationSMKLTIVKQREQPEM
CCEEEEEECCCCCCH
39.52-
992 (in isoform 2)Ubiquitination-43.16-

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 SC24D_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC24D_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 SC24D_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC23B_HUMANSEC23Bphysical
16189514
RSU1_HUMANRSU1physical
22863883
GLYM_HUMANSHMT2physical
22863883
SF3B4_HUMANSF3B4physical
25416956
SC23B_HUMANSEC23Bphysical
25416956
ARFP1_HUMANARFIP1physical
26344197
CD2AP_HUMANCD2APphysical
26344197
SC23A_HUMANSEC23Aphysical
26344197
SC23B_HUMANSEC23Bphysical
26344197
SC24A_HUMANSEC24Aphysical
26344197
SC24C_HUMANSEC24Cphysical
26344197
SH3K1_HUMANSH3KBP1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616294Cole-Carpenter syndrome 2 (CLCRP2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SC24D_HUMAN

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Related Literatures of Post-Translational Modification

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