SC31A_RAT - dbPTM
SC31A_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC31A_RAT
UniProt AC Q9Z2Q1
Protein Name Protein transport protein Sec31A
Gene Name Sec31a
Organism Rattus norvegicus (Rat).
Sequence Length 1249
Subcellular Localization Cytoplasm . Cytoplasmic vesicle, COPII-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Endoplasmic reticulum membrane
Peripheral membrane protein. Associates with membranes in a GTP-dependent manner (PubMed:10574704).
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..
Protein Sequence MKLKEIDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPHKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQKDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVVQMWDLRFASSPLRVLENHARGILAIAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASFDGRIRVYSIMGGSIDGLRQKQVDKLSSSFGNLDPFGTGQPLPPLQIPQQTSQHSIVLPLKKPPKWIRRPVGASFSFGGKLVTFENVTGQPQQGAEQPRRQPVFISQVVTEKDFLSRSEQLQHVVQSQGFISYCQKKIDASQTDFEKNVWSFLKVNFEEDSRGKYLELLGYRREDLGEKIALALNRVDGSDVALKDSDRVAQSDGEESPAEEGQLLGERIKEEKQECDFLPSAGGGTFNISVSGDIDGLITRALLTGNFESAVDLCLHDNRMADAIILAIAGGQELLAQTQKKYFAKSQSKITRLITAVVMKNWKEIVESCDLKNWREALAAVLTYAKPDEFSALCDLLGARLESEGDSLLRTQACLCYICAGNVERLVACWTKAQDGSNPLSLQDLIEKVVILRKAVQLTQALDTNTVGALLAEKMSQYANLLAAQGSIAAALAFLPDNTNQPDIVQLRDRLCRAQGRSVPGQESSRSSYEGQPLPKGGPGPLAGHPQVSRVQSQQYYPQVRIAPTVTTWSDRTPTALPSHPPAACPSDTQGGNPPPPGFIMHGNVVPNSPAPLPTSPGHMHSQPPPYPQPQPYQPAQQYSLGTGGSAVYRPQQPVAPPASKRYPNAPYVSPVASYSGQPHMYTAQPASSPTSSSAPLPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTGPQNGWNDPPALNRVPKKKKLPENFMPPVPITSPIMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHLAGGQPFHGIQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKKPIPDEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLECLYDKLRDQTLSPTIISGLHSIARSIETRNYSEGLTVHTHIVSTSNFSETSAFMPVLKVVLSQASKLGV
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------MKLKEIDRT
------CCHHHCCHH
78.5422902405
323PhosphorylationPAVLSAASFDGRIRV
HHHEEEEECCCCEEE
24.4827097102
337PhosphorylationVYSIMGGSIDGLRQK
EEEECCCCCCHHHHH
16.2727097102
350PhosphorylationQKQVDKLSSSFGNLD
HHHHHHHHHCCCCCC
29.6723984901
351PhosphorylationKQVDKLSSSFGNLDP
HHHHHHHHCCCCCCC
39.8723984901
352PhosphorylationQVDKLSSSFGNLDPF
HHHHHHHCCCCCCCC
33.5223984901
361PhosphorylationGNLDPFGTGQPLPPL
CCCCCCCCCCCCCCC
32.7823984901
374PhosphorylationPLQIPQQTSQHSIVL
CCCCCCCCCCCEEEE
25.7123984901
375PhosphorylationLQIPQQTSQHSIVLP
CCCCCCCCCCEEEEE
22.8923984901
378PhosphorylationPQQTSQHSIVLPLKK
CCCCCCCEEEEECCC
13.5223984901
397PhosphorylationIRRPVGASFSFGGKL
CCCCCCCEEEECCEE
18.5923984901
399PhosphorylationRPVGASFSFGGKLVT
CCCCCEEEECCEEEE
22.0823984901
423Asymmetric dimethylarginineQGAEQPRRQPVFISQ
CCCCCCCCCCCEEEE
52.41-
423MethylationQGAEQPRRQPVFISQ
CCCCCCCCCCCEEEE
52.41-
464PhosphorylationCQKKIDASQTDFEKN
HHHHCCCCCCCHHHH
29.8422817900
513PhosphorylationALNRVDGSDVALKDS
HHHCCCCCCEECCCC
25.1729779826
520PhosphorylationSDVALKDSDRVAQSD
CCEECCCCCHHCCCC
26.2321738781
526PhosphorylationDSDRVAQSDGEESPA
CCCHHCCCCCCCCHH
37.5319700791
531PhosphorylationAQSDGEESPAEEGQL
CCCCCCCCHHHHCHH
25.7119700791
793PhosphorylationLCRAQGRSVPGQESS
HHHHCCCCCCCCCCC
39.2225575281
799PhosphorylationRSVPGQESSRSSYEG
CCCCCCCCCCCCCCC
24.1425575281
800PhosphorylationSVPGQESSRSSYEGQ
CCCCCCCCCCCCCCC
35.1128689409
802PhosphorylationPGQESSRSSYEGQPL
CCCCCCCCCCCCCCC
38.9428432305
803PhosphorylationGQESSRSSYEGQPLP
CCCCCCCCCCCCCCC
26.5422108457
804PhosphorylationQESSRSSYEGQPLPK
CCCCCCCCCCCCCCC
25.8928689409
828PhosphorylationPQVSRVQSQQYYPQV
CCCCCCCCCCCCCEE
19.1829779826
831PhosphorylationSRVQSQQYYPQVRIA
CCCCCCCCCCEEEEC
14.9623984901
1050PhosphorylationFMPPVPITSPIMNPG
CCCCCCCCCCCCCCC
23.5223984901
1051PhosphorylationMPPVPITSPIMNPGG
CCCCCCCCCCCCCCC
17.1023984901
1070PhosphorylationQGLQQQPSASGPRSS
CCCCCCCCCCCCCCC
30.6327097102
1072PhosphorylationLQQQPSASGPRSSHA
CCCCCCCCCCCCCCC
54.3827097102
1185AcetylationRLECLYDKLRDQTLS
HHHHHHHHHHHCCCC
31.6822902405
1190PhosphorylationYDKLRDQTLSPTIIS
HHHHHHCCCCHHHHH
33.2325403869
1192PhosphorylationKLRDQTLSPTIISGL
HHHHCCCCHHHHHHH
24.3127097102
1194PhosphorylationRDQTLSPTIISGLHS
HHCCCCHHHHHHHHH
27.8027097102
1197PhosphorylationTLSPTIISGLHSIAR
CCCHHHHHHHHHHHH
31.3027097102
1201PhosphorylationTIISGLHSIARSIET
HHHHHHHHHHHHHHC
24.0027097102
1242PhosphorylationPVLKVVLSQASKLGV
HHHHHHHHHHHHHCC
16.4628689409
1245PhosphorylationKVVLSQASKLGV---
HHHHHHHHHHCC---
22.3028689409

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 SC31A_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC31A_RAT !!

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 SC31A_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SC31A_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SC31A_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-531, ANDMASS SPECTROMETRY.

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