ARVC_HUMAN - dbPTM
ARVC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARVC_HUMAN
UniProt AC O00192
Protein Name Armadillo repeat protein deleted in velo-cardio-facial syndrome
Gene Name ARVCF
Organism Homo sapiens (Human).
Sequence Length 962
Subcellular Localization
Protein Description Involved in protein-protein interactions at adherens junctions..
Protein Sequence MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMVSGGMGSGQPLPMAWQQLVLQEQSPGSQASLATMPEAPDVLEETVTVEEDPGTPTSHVSIVTSEDGTTRRTETKVTKTVKTVTTRTVRQVPVGPDGLPLLDGGPPLGPFADGALDRHFLLRGGGPVATLSRAYLSSGGGFPEGPEPRDSPSYGSLSRGLGMRPPRAGPLGPGPGDGCFTLPGHREAFPVGPEPGPPGGRSLPERFQAEPYGLEDDTRSLAADDEGGPELEPDYGTATRRRPECGRGLHTRAYEDTADDGGELADERPAFPMVTAPLAQPERGSMGSLDRLVRRSPSVDSARKEPRWRDPELPEVLAMLRHPVDPVKANAAAYLQHLCFENEGVKRRVRQLRGLPLLVALLDHPRAEVRRRACGALRNLSYGRDTDNKAAIRDCGGVPALVRLLRAARDNEVRELVTGTLWNLSSYEPLKMVIIDHGLQTLTHEVIVPHSGWEREPNEDSKPRDAEWTTVFKNTSGCLRNVSSDGAEARRRLRECEGLVDALLHALQSAVGRKDTDNKSVENCVCIMRNLSYHVHKEVPGADRYQEAEPGPLGSAVGSQRRRRDDASCFGGKKAKEEWFHQGKKDGEMDRNFDTLDLPKRTEAAKGFELLYQPEVVRLYLSLLTESRNFNTLEAAAGALQNLSAGNWMWATYIRATVRKERGLPVLVELLQSETDKVVRAVAIALRNLSLDRRNKDLIGSYAMAELVRNVRNAQAPPRPGACLEEDTVVAVLNTIHEIVSDSLDNARSLLQARGVPALVALVASSQSVREAKAASHVLQTVWSYKELRGTLQKDGWTKARFQSAAATAKGPKGALSPGGFDDSTLPLVDKSLEGEKTGSRDVIPMDALGPDGYSTVDRRERRPRGASSAGEASEKEPLKLDPSRKAPPPGPSRPAVRLVDAVGDAKPQPVDSWV
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
102PhosphorylationTVEEDPGTPTSHVSI
EEECCCCCCCCCEEE		28.8724275569
104PhosphorylationEEDPGTPTSHVSIVT
ECCCCCCCCCEEEEE		31.1624275569
105PhosphorylationEDPGTPTSHVSIVTS
CCCCCCCCCEEEEEC		24.0824275569
108PhosphorylationGTPTSHVSIVTSEDG
CCCCCCEEEEECCCC		13.1024275569
111PhosphorylationTSHVSIVTSEDGTTR
CCCEEEEECCCCCEE		25.4024275569
170MethylationLDRHFLLRGGGPVAT
HHHCCHHCCCCHHHE		43.80-
177PhosphorylationRGGGPVATLSRAYLS
CCCCHHHEECHHHHH		26.0424173317
179PhosphorylationGGPVATLSRAYLSSG
CCHHHEECHHHHHCC		15.5423403867
182PhosphorylationVATLSRAYLSSGGGF
HHEECHHHHHCCCCC		13.1525002506
184PhosphorylationTLSRAYLSSGGGFPE
EECHHHHHCCCCCCC		17.7927732954
185PhosphorylationLSRAYLSSGGGFPEG
ECHHHHHCCCCCCCC		38.5727732954
198PhosphorylationEGPEPRDSPSYGSLS
CCCCCCCCCCCCCCC		19.6121815630
200PhosphorylationPEPRDSPSYGSLSRG
CCCCCCCCCCCCCCC		46.1828796482
201PhosphorylationEPRDSPSYGSLSRGL
CCCCCCCCCCCCCCC		17.7025884760
203PhosphorylationRDSPSYGSLSRGLGM
CCCCCCCCCCCCCCC		18.2230266825
205PhosphorylationSPSYGSLSRGLGMRP
CCCCCCCCCCCCCCC		26.4630266825
228PhosphorylationGPGDGCFTLPGHREA
CCCCCCCCCCCCCCC		35.8024719451
249PhosphorylationPGPPGGRSLPERFQA
CCCCCCCCCCHHHHC		52.10-
259PhosphorylationERFQAEPYGLEDDTR
HHHHCCCCCCCCCCC		26.3325884760
265PhosphorylationPYGLEDDTRSLAADD
CCCCCCCCCCCCCCC		34.1828102081
267PhosphorylationGLEDDTRSLAADDEG
CCCCCCCCCCCCCCC		25.1819664994
282PhosphorylationGPELEPDYGTATRRR
CCCCCCCCCCCCCCC		27.3924702127
284PhosphorylationELEPDYGTATRRRPE
CCCCCCCCCCCCCCC		20.7325072903
286PhosphorylationEPDYGTATRRRPECG
CCCCCCCCCCCCCCC		25.2524702127
301PhosphorylationRGLHTRAYEDTADDG
CCCCCCCCCCCCCCC		15.8527251275
304PhosphorylationHTRAYEDTADDGGEL
CCCCCCCCCCCCCCC		21.7525219547
322PhosphorylationRPAFPMVTAPLAQPE
CCCCCEEECCCCCCC		19.1225219547
332PhosphorylationLAQPERGSMGSLDRL
CCCCCCCCCCHHHHH		26.6230266825
335PhosphorylationPERGSMGSLDRLVRR
CCCCCCCHHHHHHHH		20.6030266825
343PhosphorylationLDRLVRRSPSVDSAR
HHHHHHHCCCHHHHC		15.8030266825
345PhosphorylationRLVRRSPSVDSARKE
HHHHHCCCHHHHCCC		39.5430266825
348PhosphorylationRRSPSVDSARKEPRW
HHCCCHHHHCCCCCC		28.0230266825
428PhosphorylationCGALRNLSYGRDTDN
HHHHHHHHCCCCCCC		29.1427174698
429PhosphorylationGALRNLSYGRDTDNK
HHHHHHHCCCCCCCC		21.2427174698
433PhosphorylationNLSYGRDTDNKAAIR
HHHCCCCCCCCHHHH		39.8627174698
465PhosphorylationNEVRELVTGTLWNLS
CHHHHHHHHHCCCCC		36.7529759185
467PhosphorylationVRELVTGTLWNLSSY
HHHHHHHHCCCCCCC		21.1629759185
474PhosphorylationTLWNLSSYEPLKMVI
HCCCCCCCCCCEEEE		20.4229759185
478UbiquitinationLSSYEPLKMVIIDHG
CCCCCCCEEEEEECC		41.66-
591MethylationKEVPGADRYQEAEPG
CCCCCCCCCCCCCCC		34.20-
592PhosphorylationEVPGADRYQEAEPGP
CCCCCCCCCCCCCCC		15.9724927040
602PhosphorylationAEPGPLGSAVGSQRR
CCCCCCCCCCCCCCC		27.7120068231
606PhosphorylationPLGSAVGSQRRRRDD
CCCCCCCCCCCCCCC		17.5720068231
642PhosphorylationEMDRNFDTLDLPKRT
CCCCCCCCCCCCCCH		20.3119664994
647UbiquitinationFDTLDLPKRTEAAKG
CCCCCCCCCHHHHCC		78.30-
699PhosphorylationAGNWMWATYIRATVR
CCCCCHHHHHHHHHH		12.1722210691
700PhosphorylationGNWMWATYIRATVRK
CCCCHHHHHHHHHHH		4.8122210691
704PhosphorylationWATYIRATVRKERGL
HHHHHHHHHHHHCCC		15.8222210691
797 (in isoform 2)Ubiquitination-3.2421906983
815 (in isoform 2)Ubiquitination-25.7021906983
821 (in isoform 2)Ubiquitination-22.65-
838PhosphorylationSYKELRGTLQKDGWT
CHHHHHCCCCCCCCH		21.4130266825
841AcetylationELRGTLQKDGWTKAR
HHHCCCCCCCCHHHH		62.4112432251
860 (in isoform 1)Ubiquitination-66.5421906983
860UbiquitinationAATAKGPKGALSPGG
HHHCCCCCCCCCCCC		66.5421906983
864PhosphorylationKGPKGALSPGGFDDS
CCCCCCCCCCCCCCC		22.4430266825
871PhosphorylationSPGGFDDSTLPLVDK
CCCCCCCCCCCCCCH		33.4230266825
872PhosphorylationPGGFDDSTLPLVDKS
CCCCCCCCCCCCCHH		39.1130266825
878 (in isoform 1)Ubiquitination-49.8421906983
878UbiquitinationSTLPLVDKSLEGEKT
CCCCCCCHHCCCCCC		49.842190698
879PhosphorylationTLPLVDKSLEGEKTG
CCCCCCHHCCCCCCC		27.4730266825
885PhosphorylationKSLEGEKTGSRDVIP
HHCCCCCCCCCCCCC		35.7728857561
887PhosphorylationLEGEKTGSRDVIPMD
CCCCCCCCCCCCCHH		30.4525849741
901PhosphorylationDALGPDGYSTVDRRE
HHCCCCCCCCCCHHH		14.4624719451
902PhosphorylationALGPDGYSTVDRRER
HCCCCCCCCCCHHHC		27.7324719451
903PhosphorylationLGPDGYSTVDRRERR
CCCCCCCCCCHHHCC		20.2423312004
915PhosphorylationERRPRGASSAGEASE
HCCCCCCCCCCCCCC		24.4429255136
916PhosphorylationRRPRGASSAGEASEK
CCCCCCCCCCCCCCC		39.5029255136
921PhosphorylationASSAGEASEKEPLKL
CCCCCCCCCCCCCCC		44.9223403867
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 ARVC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARVC_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 ARVC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAD15_HUMANCDH15physical
11058098
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARVC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642; SER-871 ANDTHR-872, AND MASS SPECTROMETRY.
"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-642 AND SER-864, ANDMASS SPECTROMETRY.

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