PALM_MOUSE - dbPTM
PALM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PALM_MOUSE
UniProt AC Q9Z0P4
Protein Name Paralemmin-1
Gene Name Palm
Organism Mus musculus (Mouse).
Sequence Length 383
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side. Cell projection, filopodium membrane
Lipid-anchor. Cell projection, axon. Cell projection, dendrite. Cell projection, dendritic spine. Basolateral cell membrane
Lipid-anchor. Apicolateral cell membrane
Lip
Protein Description Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner..
Protein Sequence MEVLATDTASQQERLQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARGLEESITRLEKEIDVLEFGESAPAASKENSAAPSPGRPQSASPAKEEQKSETLVNAQQTPLGTPKENRTSTPVRSPGGSTMMKAAMYSVEITVEKDKVTGETRVLSSTTVLPRDPLPQGVKVYEDETKVVHAVDGIAENGIQPLSSSEVDELIHKADEVTLSEAGSTAGPAEPRGLAEDVTRTTPSRREITGVEAQPGEATSGPPGIQPGQEPPVTMVFMGYQNVEDEAETKKVLGLQDTIKAELVVIEDAATPREPAPLNGSAAELPATKEENQTGPTTTPSDTQDLDMKKPRCRCCSVM
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-------MEVLATDT
-------CCCCCCCC		7.88-
8PhosphorylationMEVLATDTASQQERL
CCCCCCCCCHHHHHH		24.6928066266
10PhosphorylationVLATDTASQQERLQA
CCCCCCCHHHHHHHH		34.1928066266
30PhosphorylationRKQAEIESKRRQLED
HHHHHHHHHHHHHHH		36.8025266776
44PhosphorylationDDRRQLQYLKSKALR
HHHHHHHHHHHHHHH		25.3729514104
47PhosphorylationRQLQYLKSKALRERW
HHHHHHHHHHHHHHH		22.14-
59PhosphorylationERWLLEGTPSSASEG
HHHHHCCCCCCCCCC		15.6028066266
61PhosphorylationWLLEGTPSSASEGDE
HHHCCCCCCCCCCCH		38.0719060867
62PhosphorylationLLEGTPSSASEGDED
HHCCCCCCCCCCCHH		36.7019060867
64PhosphorylationEGTPSSASEGDEDMR
CCCCCCCCCCCHHHH		44.0221183079
87PhosphorylationKARGLEESITRLEKE
HHHHHHHHHHHHHHH		21.6426824392
89PhosphorylationRGLEESITRLEKEID
HHHHHHHHHHHHHHC		38.1828066266
103PhosphorylationDVLEFGESAPAASKE
CEEECCCCCCCCCCC		39.6728066266
108PhosphorylationGESAPAASKENSAAP
CCCCCCCCCCCCCCC		42.4825521595
112PhosphorylationPAASKENSAAPSPGR
CCCCCCCCCCCCCCC		27.2225521595
116PhosphorylationKENSAAPSPGRPQSA
CCCCCCCCCCCCCCC		34.9525521595
122PhosphorylationPSPGRPQSASPAKEE
CCCCCCCCCCCCCHH		33.1425521595
124PhosphorylationPGRPQSASPAKEEQK
CCCCCCCCCCCHHHH		30.5525521595
132PhosphorylationPAKEEQKSETLVNAQ
CCCHHHHCHHHHCCC		35.1925619855
134PhosphorylationKEEQKSETLVNAQQT
CHHHHCHHHHCCCCC		43.0025619855
141PhosphorylationTLVNAQQTPLGTPKE
HHHCCCCCCCCCCCC		14.3825521595
145PhosphorylationAQQTPLGTPKENRTS
CCCCCCCCCCCCCCC		38.5824925903
147UbiquitinationQTPLGTPKENRTSTP
CCCCCCCCCCCCCCC		68.4122790023
151PhosphorylationGTPKENRTSTPVRSP
CCCCCCCCCCCCCCC		48.8425521595
152 (in isoform 2)Phosphorylation-27.7229514104
152PhosphorylationTPKENRTSTPVRSPG
CCCCCCCCCCCCCCC		27.7225521595
153PhosphorylationPKENRTSTPVRSPGG
CCCCCCCCCCCCCCH		25.7825521595
153 (in isoform 2)Phosphorylation-25.7829514104
157PhosphorylationRTSTPVRSPGGSTMM
CCCCCCCCCCHHHHH		28.2925521595
157 (in isoform 2)Phosphorylation-28.2929514104
161PhosphorylationPVRSPGGSTMMKAAM
CCCCCCHHHHHHEEE		21.0325521595
161 (in isoform 2)Phosphorylation-21.0329514104
162PhosphorylationVRSPGGSTMMKAAMY
CCCCCHHHHHHEEEE		25.2624925903
169PhosphorylationTMMKAAMYSVEITVE
HHHHEEEEEEEEEEE		12.5829514104
170PhosphorylationMMKAAMYSVEITVEK
HHHEEEEEEEEEEEE		10.53-
188PhosphorylationTGETRVLSSTTVLPR
CCCEEEEEECEEECC		23.8426824392
190PhosphorylationETRVLSSTTVLPRDP
CEEEEEECEEECCCC		19.9722802335
191PhosphorylationTRVLSSTTVLPRDPL
EEEEEECEEECCCCC		23.2222802335
205PhosphorylationLPQGVKVYEDETKVV
CCCCCEEEECCCEEE		16.3729514104
209PhosphorylationVKVYEDETKVVHAVD
CEEEECCCEEEEEEC		41.2729514104
242PhosphorylationIHKADEVTLSEAGST
HHHCCEEECCCCCCC		23.6325619855
244PhosphorylationKADEVTLSEAGSTAG
HCCEEECCCCCCCCC		18.9425521595
248PhosphorylationVTLSEAGSTAGPAEP
EECCCCCCCCCCCCC		23.3325521595
249PhosphorylationTLSEAGSTAGPAEPR
ECCCCCCCCCCCCCC		34.4125619855
263PhosphorylationRGLAEDVTRTTPSRR
CCCCCCCCCCCCCCC		34.3222324799
265PhosphorylationLAEDVTRTTPSRREI
CCCCCCCCCCCCCEE		33.4222324799
266PhosphorylationAEDVTRTTPSRREIT
CCCCCCCCCCCCEEC		18.9022324799
268PhosphorylationDVTRTTPSRREITGV
CCCCCCCCCCEECCE		41.7122324799
315UbiquitinationEDEAETKKVLGLQDT
CCHHHHHHHHCCHHH		50.5422790023
322PhosphorylationKVLGLQDTIKAELVV
HHHCCHHHEEEEEEE		16.0622324799
335PhosphorylationVVIEDAATPREPAPL
EEEECCCCCCCCCCC		25.3025338131
345PhosphorylationEPAPLNGSAAELPAT
CCCCCCCCCCCCCCC		24.1925521595
352PhosphorylationSAAELPATKEENQTG
CCCCCCCCCCCCCCC		36.7325619855
358PhosphorylationATKEENQTGPTTTPS
CCCCCCCCCCCCCCC		57.6324925903
361PhosphorylationEENQTGPTTTPSDTQ
CCCCCCCCCCCCCCC		44.6525521595
362PhosphorylationENQTGPTTTPSDTQD
CCCCCCCCCCCCCCC		39.5825521595
363PhosphorylationNQTGPTTTPSDTQDL
CCCCCCCCCCCCCCC		24.2325521595
365PhosphorylationTGPTTTPSDTQDLDM
CCCCCCCCCCCCCCC		51.7225521595
367PhosphorylationPTTTPSDTQDLDMKK
CCCCCCCCCCCCCCC		28.4625521595
377S-palmitoylationLDMKKPRCRCCSVM-
CCCCCCCCCCCCCC-		5.46-
379S-palmitoylationMKKPRCRCCSVM---
CCCCCCCCCCCC---		2.02-
380MethylationKKPRCRCCSVM----
CCCCCCCCCCC----		1.45-
380FarnesylationKKPRCRCCSVM----
CCCCCCCCCCC----		1.45-
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 PALM_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; THR-141; THR-145;SER-157 AND SER-345, AND MASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-145; SER-152AND SER-157, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-145; SER-345;THR-363 AND SER-365, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND THR-145, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND THR-145, ANDMASS SPECTROMETRY.

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