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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