PALM2_HUMAN - dbPTM
PALM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PALM2_HUMAN
UniProt AC Q8IXS6
Protein Name Paralemmin-2
Gene Name PALM2
Organism Homo sapiens (Human).
Sequence Length 379
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side.
Protein Description
Protein Sequence MEMAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTLESEESQISAKEQIILEKLKETEKSFKDFQKGFSSTDGAVYAMEINVEKDKQTGETKILSTSTIGPEGVHQKGVKVYDDGTKVVYEVRSGGTVVENGVHKLSTKDVEELIQKAGQSSLGGGHVSERTVIADGSLSHPKEHMLCKEAKLEMVHKSRKDHSSGNPGQQAQAPSAAGPEANLDQPVTMIFMGYQNIEDEEETKKVLGYDETIKAELVLIDEDDEKSLREKTVTDVSTIDGNAAELVSGRPVSDTTEPSSPEGKEESLATEPAPGTQKKKRCQCCVVM
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
72PhosphorylationEEARRRQSEEDEFRV
HHHHHHHCHHHHHHH		40.9325850435
117PhosphorylationILEKLKETEKSFKDF
HHHHHHHHHHHHHHH		47.3129214152
120PhosphorylationKLKETEKSFKDFQKG
HHHHHHHHHHHHHHC		31.1528258704
126AcetylationKSFKDFQKGFSSTDG
HHHHHHHHCCCCCCC		63.0120167786
136PhosphorylationSSTDGAVYAMEINVE
CCCCCCEEEEEEEEE		10.3327642862
156PhosphorylationGETKILSTSTIGPEG
CCEEEEEECCCCCCC		26.8328674419
157PhosphorylationETKILSTSTIGPEGV
CEEEEEECCCCCCCC		18.0429214152
172PhosphorylationHQKGVKVYDDGTKVV
CCCCCEEECCCCEEE		11.55-
180PhosphorylationDDGTKVVYEVRSGGT
CCCCEEEEEECCCCE		16.2225884760
197PhosphorylationENGVHKLSTKDVEEL
ECCEEECCHHCHHHH		37.9128555341
198PhosphorylationNGVHKLSTKDVEELI
CCEEECCHHCHHHHH		41.5229449344
211PhosphorylationLIQKAGQSSLGGGHV
HHHHHCCCCCCCCCC		26.9828555341
212PhosphorylationIQKAGQSSLGGGHVS
HHHHCCCCCCCCCCC		24.1328555341
219PhosphorylationSLGGGHVSERTVIAD
CCCCCCCCCCEEEEC		18.7128555341
228PhosphorylationRTVIADGSLSHPKEH
CEEEECCCCCCHHHH		27.5228857561
230PhosphorylationVIADGSLSHPKEHML
EEECCCCCCHHHHCC		39.1728857561
300PhosphorylationETKKVLGYDETIKAE
HHHHHHCCCCCEEEE		13.3719664994
318PhosphorylationIDEDDEKSLREKTVT
ECCCCHHHHHHCEEE		30.5230266825
323PhosphorylationEKSLREKTVTDVSTI
HHHHHHCEEEEEEEE		24.7227251275
325PhosphorylationSLREKTVTDVSTIDG
HHHHCEEEEEEEECC		35.6027251275
328PhosphorylationEKTVTDVSTIDGNAA
HCEEEEEEEECCCCC		23.5827251275
329PhosphorylationKTVTDVSTIDGNAAE
CEEEEEEEECCCCCH		23.9627251275
339PhosphorylationGNAAELVSGRPVSDT
CCCCHHHCCCCCCCC		41.5327251275
344PhosphorylationLVSGRPVSDTTEPSS
HHCCCCCCCCCCCCC		31.7429523821
346PhosphorylationSGRPVSDTTEPSSPE
CCCCCCCCCCCCCCC		26.0829523821
347PhosphorylationGRPVSDTTEPSSPEG
CCCCCCCCCCCCCCC		51.3829523821
350PhosphorylationVSDTTEPSSPEGKEE
CCCCCCCCCCCCCHH		52.9029507054
351PhosphorylationSDTTEPSSPEGKEES
CCCCCCCCCCCCHHH		37.3729255136
358PhosphorylationSPEGKEESLATEPAP
CCCCCHHHCCCCCCC		25.1329255136
361PhosphorylationGKEESLATEPAPGTQ
CCHHHCCCCCCCCCC		48.0427732954
373S-palmitoylationGTQKKKRCQCCVVM-
CCCCCCCEEEEEEC-		5.08-
375S-palmitoylationQKKKRCQCCVVM---
CCCCCEEEEEEC---		1.86-
376MethylationKKKRCQCCVVM----
CCCCEEEEEEC----		0.77-
376FarnesylationKKKRCQCCVVM----
CCCCEEEEEEC----		0.77-
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 PALM2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PALM2_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 PALM2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANK3_HUMANANK3physical
26186194
ANK2_HUMANANK2physical
26186194
GPD1L_HUMANGPD1Lphysical
26186194
FOLC_HUMANFPGSphysical
26186194
MSPD2_HUMANMOSPD2physical
26186194
AP3M1_HUMANAP3M1physical
26186194
LACC1_HUMANLACC1physical
26186194
ANK3_HUMANANK3physical
28514442
FOLC_HUMANFPGSphysical
28514442
ANK2_HUMANANK2physical
28514442
LACC1_HUMANLACC1physical
28514442
MSPD2_HUMANMOSPD2physical
28514442
AP3M1_HUMANAP3M1physical
28514442
E2AK4_HUMANEIF2AK4physical
28514442
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 PALM2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND MASSSPECTROMETRY.

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