SC31A_MOUSE - dbPTM
SC31A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC31A_MOUSE
UniProt AC Q3UPL0
Protein Name Protein transport protein Sec31A
Gene Name Sec31a
Organism Mus musculus (Mouse).
Sequence Length 1230
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..
Protein Description Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (By similarity). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity)..
Protein Sequence MKLKEIDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPHKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQKDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVIQMWDLRFASSPLRVLENHARGILAVAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASFDGRISVYSIMGGSIDGLRQKQVDKLSSSFGNLDPFGTGQPLPPLQIPQQSAQHSIVLPLKKPPKWIRRPVGASFSFGGKLVTFESVAVPLQQGAEQQRRQPVFISQVVTEKDFLNRSAQLQHAVQSQGFIGYCQKKIEASQTEFEKNVWSFLKVNFEEDSRGKYLELLGYRKEDLGQKIALALNKVDGPDVALKDSDQVAQSDGEESPAAEEQLLGERIKEEKQECDFLPSAGGTFNISVSGDIDGLITRALLTGNFESAVDLCLHDNRMADAIILAIAGGQELLAQTQKKYFAKSQSKITRLITAVVMKNWREIVESCDLKNWREALAAVLTYAKPDEFSALCDLLGTRLEREGDSLLRTQACLCYICAGNVERLVACWTKAQDGSSPLSLQDLIEKVVILRKAVQLTQALDTNTVGALLAEKMSQYASLLAAQGSIAAALAFLPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFIMQGNVIPNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTENQSFQDQASILEGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKKPIPEEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLEFLYDKLREQTLSPTIINGLHSIARSIETRNYSEGLSVHTHIVSTSNFSETSAFMPVLKVVLSQASKLGV
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
71AcetylationSSSHRYHKLIWGPHK
CCHHCCEEEECCCCC		32.5022826441
111MalonylationSKIIAGDKEVVIAQK
HHEEECCCEEEEEEC		52.0326320211
111UbiquitinationSKIIAGDKEVVIAQK
HHEEECCCEEEEEEC		52.03-
118AcetylationKEVVIAQKDKHTGPV
CEEEEEECCCCCCCE		60.7723954790
118SuccinylationKEVVIAQKDKHTGPV
CEEEEEECCCCCCCE		60.7723954790
135PhosphorylationLDVNIFQTNLVASGA
EEEEEEEECEEECCC		21.5529109428
206UbiquitinationRKNEPIIKVSDHSNR
CCCCCEEEECCCCCC		36.0822790023
323PhosphorylationPAVLSAASFDGRISV
HHHEEEEEECCCEEE		24.4829514104
350PhosphorylationQKQVDKLSSSFGNLD
HHHHHHHHHCCCCCC		29.6726643407
351PhosphorylationKQVDKLSSSFGNLDP
HHHHHHHHCCCCCCC		39.8723984901
352PhosphorylationQVDKLSSSFGNLDPF
HHHHHHHCCCCCCCC		33.5223984901
361PhosphorylationGNLDPFGTGQPLPPL
CCCCCCCCCCCCCCC		32.7826060331
397PhosphorylationIRRPVGASFSFGGKL
CCCCCCCEEEECCEE		18.5929899451
423Asymmetric dimethylarginineQGAEQQRRQPVFISQ
HCHHHHHCCCEEEEE		40.59-
423MethylationQGAEQQRRQPVFISQ
HCHHHHHCCCEEEEE		40.5924129315
433PhosphorylationVFISQVVTEKDFLNR
EEEEEECCHHHHCCH		38.16-
435UbiquitinationISQVVTEKDFLNRSA
EEEECCHHHHCCHHH		44.4022790023
457S-palmitoylationSQGFIGYCQKKIEAS
HCCHHHHHHHHHHHH		3.9428526873
470UbiquitinationASQTEFEKNVWSFLK
HHHHHHHHHHHHHHC		63.2222790023
477UbiquitinationKNVWSFLKVNFEEDS
HHHHHHHCCCCCCCC		32.87-
487UbiquitinationFEEDSRGKYLELLGY
CCCCCCCCCHHHCCC		45.6222790023
494PhosphorylationKYLELLGYRKEDLGQ
CCHHHCCCCHHHHHH		20.6222871156
502UbiquitinationRKEDLGQKIALALNK
CHHHHHHHHHHHHHC		28.3122790023
509UbiquitinationKIALALNKVDGPDVA
HHHHHHHCCCCCCEE		42.4222790023
520PhosphorylationPDVALKDSDQVAQSD
CCEECCCHHHHHHCC		28.4924925903
526PhosphorylationDSDQVAQSDGEESPA
CHHHHHHCCCCCCHH		37.5327087446
531PhosphorylationAQSDGEESPAAEEQL
HHCCCCCCHHHHHHH		18.6124925903
614UbiquitinationELLAQTQKKYFAKSQ
HHHHHHHHHHHHHCH		53.48-
619MalonylationTQKKYFAKSQSKITR
HHHHHHHHCHHHHHH		38.8526320211
620PhosphorylationQKKYFAKSQSKITRL
HHHHHHHCHHHHHHH		35.9422807455
646UbiquitinationIVESCDLKNWREALA
HHHHCCCCCHHHHHH		41.0122790023
706UbiquitinationRLVACWTKAQDGSSP
HEEEEEEECCCCCCC		21.3922790023
711PhosphorylationWTKAQDGSSPLSLQD
EEECCCCCCCCCHHH		36.7520415495
712PhosphorylationTKAQDGSSPLSLQDL
EECCCCCCCCCHHHH		35.0820415495
715PhosphorylationQDGSSPLSLQDLIEK
CCCCCCCCHHHHHHH		27.6327566939
722UbiquitinationSLQDLIEKVVILRKA
CHHHHHHHHHHHHHH		34.5022790023
728UbiquitinationEKVVILRKAVQLTQA
HHHHHHHHHHHHHHH		49.8422790023
771UbiquitinationAALAFLPDNTNQPNI
HHHHHCCCCCCCCCH		76.3927667366
784UbiquitinationNIVQLRDRLCKAQGK
CHHHHHHHHHHHCCC		35.2427667366
791MalonylationRLCKAQGKPVSGQES
HHHHHCCCCCCCCCC		30.1126320211
791UbiquitinationRLCKAQGKPVSGQES
HHHHHCCCCCCCCCC		30.11-
794PhosphorylationKAQGKPVSGQESSQS
HHCCCCCCCCCCCCC		43.2025619855
798O-linked_GlycosylationKPVSGQESSQSPYER
CCCCCCCCCCCCCCC		26.2830059200
798PhosphorylationKPVSGQESSQSPYER
CCCCCCCCCCCCCCC		26.2825619855
799PhosphorylationPVSGQESSQSPYERQ
CCCCCCCCCCCCCCC		33.6525168779
801PhosphorylationSGQESSQSPYERQPL
CCCCCCCCCCCCCCC		31.2527087446
803PhosphorylationQESSQSPYERQPLSK
CCCCCCCCCCCCCCC		29.0525168779
809PhosphorylationPYERQPLSKGRPGPV
CCCCCCCCCCCCCCC		39.4826160508
810UbiquitinationYERQPLSKGRPGPVA
CCCCCCCCCCCCCCC		67.6227667366
820PhosphorylationPGPVAGHSQMPRVQT
CCCCCCCCCCCCCCC		27.5324899341
1171PhosphorylationYDKLREQTLSPTIIN
HHHHHHCCCCHHHHH		25.1730372032
1173PhosphorylationKLREQTLSPTIINGL
HHHHCCCCHHHHHHH		24.3126824392
1175PhosphorylationREQTLSPTIINGLHS
HHCCCCHHHHHHHHH		30.9823984901
1223PhosphorylationPVLKVVLSQASKLGV
HHHHHHHHHHHHHCC		16.4629472430
1226PhosphorylationKVVLSQASKLGV---
HHHHHHHHHHCC---		22.3029514104
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC31A_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SC31A_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SC31A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.

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