PALMD_HUMAN - dbPTM
PALMD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PALMD_HUMAN
UniProt AC Q9NP74
Protein Name Palmdelphin
Gene Name PALMD
Organism Homo sapiens (Human).
Sequence Length 551
Subcellular Localization Cytoplasm . Cell projection, dendrite . Cell projection, dendritic spine.
Protein Description
Protein Sequence MEEAELVKGRLQAITDKRKIQEEISQKRLKIEEDKLKHQHLKKKALREKWLLDGISSGKEQEEMKKQNQQDQHQIQVLEQSILRLEKEIQDLEKAELQISTKEEAILKKLKSIERTTEDIIRSVKVEREERAEESIEDIYANIPDLPKSYIPSRLRKEINEEKEDDEQNRKALYAMEIKVEKDLKTGESTVLSSIPLPSDDFKGTGIKVYDDGQKSVYAVSSNHSAAYNGTDGLAPVEVEELLRQASERNSKSPTEYHEPVYANPFYRPTTPQRETVTPGPNFQERIKIKTNGLGIGVNESIHNMGNGLSEERGNNFNHISPIPPVPHPRSVIQQAEEKLHTPQKRLMTPWEESNVMQDKDAPSPKPRLSPRETIFGKSEHQNSSPTCQEDEEDVRYNIVHSLPPDINDTEPVTMIFMGYQQAEDSEEDKKFLTGYDGIIHAELVVIDDEEEEDEGEAEKPSYHPIAPHSQVYQPAKPTPLPRKRSEASPHENTNHKSPHKNSISLKEQEESLGSPVHHSPFDAQTTGDGTEDPSLTALRMRMAKLGKKVI
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
1Acetylation-------MEEAELVK
-------CHHHHHHH		10.6822814378
56PhosphorylationKWLLDGISSGKEQEE
HHHHHHHCCHHHHHH		38.27-
81PhosphorylationQIQVLEQSILRLEKE
HHHHHHHHHHHHHHH		17.7620068231
112PhosphorylationAILKKLKSIERTTED
HHHHHHHHCCCCHHH		39.8725159151
125SumoylationEDIIRSVKVEREERA
HHHHHHHHHHHHHHH		39.3628112733
135PhosphorylationREERAEESIEDIYAN
HHHHHHHHHHHHHHC		23.8421712546
140PhosphorylationEESIEDIYANIPDLP
HHHHHHHHHCCCCCC		13.1025884760
153PhosphorylationLPKSYIPSRLRKEIN
CCHHHCCHHHHHHHH		34.10-
174PhosphorylationEQNRKALYAMEIKVE
HHHHHHHHHHEEEEE		14.5725159151
179SumoylationALYAMEIKVEKDLKT
HHHHHEEEEEECCCC		30.91-
179SumoylationALYAMEIKVEKDLKT
HHHHHEEEEEECCCC		30.9125114211
193PhosphorylationTGESTVLSSIPLPSD
CCCCEEEECCCCCCC		23.1427251275
194PhosphorylationGESTVLSSIPLPSDD
CCCEEEECCCCCCCC		24.8627251275
210PhosphorylationKGTGIKVYDDGQKSV
CCCCEEEEECCCCEE		11.87-
218PhosphorylationDDGQKSVYAVSSNHS
ECCCCEEEEEECCCC		14.3722817900
221PhosphorylationQKSVYAVSSNHSAAY
CCEEEEEECCCCCCC		19.7630576142
228PhosphorylationSSNHSAAYNGTDGLA
ECCCCCCCCCCCCCC		17.5330576142
231PhosphorylationHSAAYNGTDGLAPVE
CCCCCCCCCCCCCHH		24.2130576142
247PhosphorylationEELLRQASERNSKSP
HHHHHHHHHHCCCCC		28.84-
251PhosphorylationRQASERNSKSPTEYH
HHHHHHCCCCCCCCC		40.5126055452
253PhosphorylationASERNSKSPTEYHEP
HHHHCCCCCCCCCCC		36.5521945579
255PhosphorylationERNSKSPTEYHEPVY
HHCCCCCCCCCCCCC		57.1621945579
257PhosphorylationNSKSPTEYHEPVYAN
CCCCCCCCCCCCCCC		17.6021945579
262PhosphorylationTEYHEPVYANPFYRP
CCCCCCCCCCCCCCC		16.0421945579
267PhosphorylationPVYANPFYRPTTPQR
CCCCCCCCCCCCCCC		19.5521945579
270PhosphorylationANPFYRPTTPQRETV
CCCCCCCCCCCCCCC		41.9521945579
271PhosphorylationNPFYRPTTPQRETVT
CCCCCCCCCCCCCCC		21.8021945579
276PhosphorylationPTTPQRETVTPGPNF
CCCCCCCCCCCCCCH		31.6925159151
278PhosphorylationTPQRETVTPGPNFQE
CCCCCCCCCCCCHHH		29.9221815630
301PhosphorylationLGIGVNESIHNMGNG
CCCCCCHHHHCCCCC		24.7628555341
321PhosphorylationGNNFNHISPIPPVPH
CCCCCCCCCCCCCCC		14.8222167270
331PhosphorylationPPVPHPRSVIQQAEE
CCCCCCHHHHHHHHH		28.2027251275
339UbiquitinationVIQQAEEKLHTPQKR
HHHHHHHHHCCCCHH		36.75-
342PhosphorylationQAEEKLHTPQKRLMT
HHHHHHCCCCHHCCC		37.5424732914
354PhosphorylationLMTPWEESNVMQDKD
CCCCCHHHCCCCCCC		24.1822210691
364PhosphorylationMQDKDAPSPKPRLSP
CCCCCCCCCCCCCCC		47.4822167270
370PhosphorylationPSPKPRLSPRETIFG
CCCCCCCCCCCCCCC		24.1625159151
378AcetylationPRETIFGKSEHQNSS
CCCCCCCCCCCCCCC		41.7526051181
379PhosphorylationRETIFGKSEHQNSSP
CCCCCCCCCCCCCCC		40.4622167270
384PhosphorylationGKSEHQNSSPTCQED
CCCCCCCCCCCCCCC		30.9922167270
385PhosphorylationKSEHQNSSPTCQEDE
CCCCCCCCCCCCCCH		31.6025463755
387PhosphorylationEHQNSSPTCQEDEED
CCCCCCCCCCCCHHH		28.8622167270
486PhosphorylationTPLPRKRSEASPHEN
CCCCCCCCCCCCCCC		40.3220068231
489PhosphorylationPRKRSEASPHENTNH
CCCCCCCCCCCCCCC		23.8020068231
494PhosphorylationEASPHENTNHKSPHK
CCCCCCCCCCCCCCC		35.4023403867
498PhosphorylationHENTNHKSPHKNSIS
CCCCCCCCCCCCCCC		25.3726055452
503PhosphorylationHKSPHKNSISLKEQE
CCCCCCCCCCHHHHH		20.5426055452
505PhosphorylationSPHKNSISLKEQEES
CCCCCCCCHHHHHHH		32.9623312004
512PhosphorylationSLKEQEESLGSPVHH
CHHHHHHHHCCCCCC		36.9625159151
515PhosphorylationEQEESLGSPVHHSPF
HHHHHHCCCCCCCCC		29.1025159151
520PhosphorylationLGSPVHHSPFDAQTT
HCCCCCCCCCCCCCC		16.6325159151
526PhosphorylationHSPFDAQTTGDGTED
CCCCCCCCCCCCCCC		34.1730576142
527PhosphorylationSPFDAQTTGDGTEDP
CCCCCCCCCCCCCCH		22.6130576142
531PhosphorylationAQTTGDGTEDPSLTA
CCCCCCCCCCHHHHH		41.7927251275
535PhosphorylationGDGTEDPSLTALRMR
CCCCCCHHHHHHHHH		51.1520068231
537PhosphorylationGTEDPSLTALRMRMA
CCCCHHHHHHHHHHH		28.1620068231
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 PALMD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of PALMD_HUMAN !!
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 PALMD_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-135 AND SER-321, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND MASSSPECTROMETRY.

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