VMA5A_MOUSE - dbPTM
VMA5A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VMA5A_MOUSE
UniProt AC Q99KC8
Protein Name von Willebrand factor A domain-containing protein 5A
Gene Name Vwa5a
Organism Mus musculus (Mouse).
Sequence Length 793
Subcellular Localization
Protein Description May play a role in tumorigenesis as a tumor suppressor. Altered expression of this protein and disruption of the molecular pathway it is involved in may contribute directly to or modify tumorigenesis (By similarity)..
Protein Sequence MEHHCGLITSNKETVPLKNISVTLSINEFVAAVVATLNYENEEKVPLEATFVFPMDEDSAVYSFEALVDGKKIVAELQDKMKAHSEYEEALSQGHQAYLLEEDDYSRDVFSCNVGNLQPGAKVAVTLRYVQELPLETDGALRYLLPAILNPRYQLSEQSANSCLNIQKPTVPLEDLPYTLNMTATITSQHGIERVQSNCSLSPIQYLTDDKTSAQVSLTEGHKFDRDVELLIYYNEVHSPSVAVEMGMLDMKPDSLMGAPSAMVSFYPDIPEVEASKACGEFVFLMDRSGSMDSPMSTENNSQLRIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEKFFPESVKYTQDTMEDAVKRVKALKANLGGTEILTPLCNIYKASSIPGHPLQLFVFTDGEVSDTFSVIREVKLNSKKHRCFSFGIGQGASTSLIKNIARVSGGTAVFITGKDRMQTKALGSLKFALQCAVDNISLSWDLPPGLSVKMLSPEQLTIFRGQRLIIYAQLTGLMPQVESTGAVCLKHILQGRSLENRVTFSLQPKANDNFTIHRLAAKSLIQTKDFGSQEASKEEKEDVMNISLQSGVLSSFTAFIAINKELNKPVQGPLAHRVIPRPVMAGSSSMRFYSSFSGGFKGPQPRSLRVPAYDLCSAESANLVLKKSACSAIQKKKTNSSTNKSNLKKEHKAFGENAVVQLISLQKANGSWELDEDLTKILGTKSKDIKAANPAKHEDPSAWSTVLAVVWLHANGTDLKCEWELLERKAVAWLHDHAGSSIPMLVQAANSLLKLSVNPAVFGV
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
85PhosphorylationQDKMKAHSEYEEALS
HHHHHHCHHHHHHHH		46.8925367039
87PhosphorylationKMKAHSEYEEALSQG
HHHHCHHHHHHHHCC		23.2925367039
92PhosphorylationSEYEEALSQGHQAYL
HHHHHHHHCCHHEEE		40.96-
105PhosphorylationYLLEEDDYSRDVFSC
EECCCCCCCCCCEEE		20.2325367039
106PhosphorylationLLEEDDYSRDVFSCN
ECCCCCCCCCCEEEE		29.0625367039
111PhosphorylationDYSRDVFSCNVGNLQ
CCCCCCEEEECCCCC		12.4825367039
279S-nitrosocysteineEVEASKACGEFVFLM
HHHHHHHCCEEEEEE		6.53-
279S-nitrosylationEVEASKACGEFVFLM
HHHHHHHCCEEEEEE		6.5321278135
279GlutathionylationEVEASKACGEFVFLM
HHHHHHHCCEEEEEE		6.5324333276
310UbiquitinationQLRIEAAKETLLLLL
HHHHHHHHHHHHHHH		59.2822790023
319PhosphorylationTLLLLLKSLPMGCYF
HHHHHHHHCCCCCEE		37.3629109428
325PhosphorylationKSLPMGCYFNIYGFG
HHCCCCCEEEECCCC		8.2429109428
355UbiquitinationDTMEDAVKRVKALKA
HHHHHHHHHHHHHHH		53.8727667366
374S-nitrosylationTEILTPLCNIYKASS
CEEHHHHHHHHHHCC		2.8321278135
374GlutathionylationTEILTPLCNIYKASS
CEEHHHHHHHHHHCC		2.8324333276
374S-nitrosocysteineTEILTPLCNIYKASS
CEEHHHHHHHHHHCC		2.83-
453MalonylationGKDRMQTKALGSLKF
CCCHHHCHHHHHHHH		25.4026320211
490PhosphorylationMLSPEQLTIFRGQRL
ECCHHHEEEECCCEE		20.1227566939
538UbiquitinationVTFSLQPKANDNFTI
EEEEECCCCCCCEEE		47.0322790023
544PhosphorylationPKANDNFTIHRLAAK
CCCCCCEEEEEHHHH		23.3329176673
551UbiquitinationTIHRLAAKSLIQTKD
EEEEHHHHHHHHHCC		39.9422790023
557UbiquitinationAKSLIQTKDFGSQEA
HHHHHHHCCCCCCCC		34.3822790023
565PhosphorylationDFGSQEASKEEKEDV
CCCCCCCCHHHHHHH		39.59-
566UbiquitinationFGSQEASKEEKEDVM
CCCCCCCHHHHHHHH		76.5527667366
597MalonylationAINKELNKPVQGPLA
HHHHHCCCCCCCCCC		60.2226320211
616PhosphorylationPRPVMAGSSSMRFYS
CCCEECCCCCCEEEC		15.0929472430
617PhosphorylationRPVMAGSSSMRFYSS
CCEECCCCCCEEECC		27.5119060867
618PhosphorylationPVMAGSSSMRFYSSF
CEECCCCCCEEECCC		18.7019060867
622PhosphorylationGSSSMRFYSSFSGGF
CCCCCEEECCCCCCC		7.9522817900
623PhosphorylationSSSMRFYSSFSGGFK
CCCCEEECCCCCCCC		23.3826643407
624PhosphorylationSSMRFYSSFSGGFKG
CCCEEECCCCCCCCC		16.4421930439
626PhosphorylationMRFYSSFSGGFKGPQ
CEEECCCCCCCCCCC		39.7021930439
630UbiquitinationSSFSGGFKGPQPRSL
CCCCCCCCCCCCCCC		73.3222790023
630AcetylationSSFSGGFKGPQPRSL
CCCCCCCCCCCCCCC		73.3222826441
636PhosphorylationFKGPQPRSLRVPAYD
CCCCCCCCCCCCHHH		27.4926824392
642PhosphorylationRSLRVPAYDLCSAES
CCCCCCHHHHCCHHH		11.9020116462
645GlutathionylationRVPAYDLCSAESANL
CCCHHHHCCHHHHHH		3.1124333276
656MalonylationSANLVLKKSACSAIQ
HHHHEECHHHHHHHH		38.8426320211
659GlutathionylationLVLKKSACSAIQKKK
HEECHHHHHHHHHHH		3.4924333276
664AcetylationSACSAIQKKKTNSST
HHHHHHHHHHCCCCC		50.5623806337
664SuccinylationSACSAIQKKKTNSST
HHHHHHHHHHCCCCC		50.5623806337
664MalonylationSACSAIQKKKTNSST
HHHHHHHHHHCCCCC		50.5626320211
666AcetylationCSAIQKKKTNSSTNK
HHHHHHHHCCCCCCH		61.0319860239
673MalonylationKTNSSTNKSNLKKEH
HCCCCCCHHHHHHHH		40.5932601280
677AcetylationSTNKSNLKKEHKAFG
CCCHHHHHHHHHHHH		61.4419860245
678AcetylationTNKSNLKKEHKAFGE
CCHHHHHHHHHHHHC		69.1219860251
693PhosphorylationNAVVQLISLQKANGS
CHHHHHHEEEECCCC		33.0822942356
709AcetylationELDEDLTKILGTKSK
ECCHHHHHHHCCCCC		43.1423954790
719MalonylationGTKSKDIKAANPAKH
CCCCCCCCCCCCCCC		52.1326320211
769PhosphorylationWLHDHAGSSIPMLVQ
HHHHCCCCCHHHHHH		26.3625777480
770PhosphorylationLHDHAGSSIPMLVQA
HHHCCCCCHHHHHHH		29.7825777480
780PhosphorylationMLVQAANSLLKLSVN
HHHHHHHHHHHHCCC		30.2825777480
785PhosphorylationANSLLKLSVNPAVFG
HHHHHHHCCCHHHHC		20.4725777480
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 VMA5A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VMA5A_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 VMA5A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VMA5A_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VMA5A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-622, AND MASSSPECTROMETRY.

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