PLLP_HUMAN - dbPTM
PLLP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLLP_HUMAN
UniProt AC Q9Y342
Protein Name Plasmolipin
Gene Name PLLP
Organism Homo sapiens (Human).
Sequence Length 182
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective (By similarity)..
Protein Sequence MAEFPSKVSTRTSSPAQGAEASVSALRPDLGFVRSRLGALMLLQLVLGLLVWALIADTPYHLYPAYGWVMFVAVFLWLVTIVLFNLYLFQLHMKLYMVPWPLVLMIFNISATVLYITAFIACSAAVDLTSLRGTRPYNQRAAASFFACLVMIAYGVSAFFSYQAWRGVGSNAATSQMAGGYA
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
6Phosphorylation--MAEFPSKVSTRTS
--CCCCCCCCCCCCC
51.5128857561
7Ubiquitination-MAEFPSKVSTRTSS
-CCCCCCCCCCCCCC
40.20-
9PhosphorylationAEFPSKVSTRTSSPA
CCCCCCCCCCCCCHH
18.8628355574
10PhosphorylationEFPSKVSTRTSSPAQ
CCCCCCCCCCCCHHC
40.7423186163
12PhosphorylationPSKVSTRTSSPAQGA
CCCCCCCCCCHHCCC
33.3825850435
13PhosphorylationSKVSTRTSSPAQGAE
CCCCCCCCCHHCCCC
30.9126657352
14PhosphorylationKVSTRTSSPAQGAEA
CCCCCCCCHHCCCCH
24.5221082442
22PhosphorylationPAQGAEASVSALRPD
HHCCCCHHHHHHCCC
14.2223322592
24PhosphorylationQGAEASVSALRPDLG
CCCCHHHHHHCCCHH
21.0624719451
170PhosphorylationQAWRGVGSNAATSQM
HHHCCCCCCHHHHHH
22.3822461510
181PhosphorylationTSQMAGGYA------
HHHHCCCCC------
14.2827642862

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 PLLP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLLP_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 PLLP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M4A12_HUMANMS4A12physical
25416956

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 PLLP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.

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