MYLIP_HUMAN - dbPTM
MYLIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYLIP_HUMAN
UniProt AC Q8WY64
Protein Name E3 ubiquitin-protein ligase MYLIP
Gene Name MYLIP
Organism Homo sapiens (Human).
Sequence Length 445
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein .
Protein Description E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR..
Protein Sequence MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKEALLAGHLLCSPEQAVELSALLAQTKFGDYNQNTAKYNYEELCAKELSSATLNSIVAKHKELEGTSQASAEYQVLQIVSAMENYGIEWHSVRDSEGQKLLIGVGPEGISICKDDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRNNQSPSHSPLKSSESSMNCSSCEGLSCQQTRVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI
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
4Phosphorylation----MLCYVTRPDAV
----CCEEEECCCEE
10.8223663014
6Phosphorylation--MLCYVTRPDAVLM
--CCEEEECCCEEEE
15.2623663014
47PhosphorylationDYFGLQFTGSKGESL
EEEEEEEECCCCCEE
27.82-
49PhosphorylationFGLQFTGSKGESLWL
EEEEEECCCCCEEHH
34.14-
137UbiquitinationDYNQNTAKYNYEELC
CCCCCHHCCCHHHHH
31.80-
146UbiquitinationNYEELCAKELSSATL
CHHHHHHHHHHHHHH
59.18-
149PhosphorylationELCAKELSSATLNSI
HHHHHHHHHHHHHHH
21.0125159151
150PhosphorylationLCAKELSSATLNSIV
HHHHHHHHHHHHHHH
37.5926074081
152PhosphorylationAKELSSATLNSIVAK
HHHHHHHHHHHHHHH
28.5526074081
159UbiquitinationTLNSIVAKHKELEGT
HHHHHHHHHHHHCCC
44.29-
257PhosphorylationVLLFKMISTRAASGL
EEEEEHHHHHHHHHH
14.3522210691
258PhosphorylationLLFKMISTRAASGLY
EEEEHHHHHHHHHHH
17.2522210691
269PhosphorylationSGLYRAITETHAFYR
HHHHHHHHHCCCCCC
33.5730576142
279PhosphorylationHAFYRCDTVTSAVMM
CCCCCCCHHHHHHHH
29.3429759185
281PhosphorylationFYRCDTVTSAVMMQY
CCCCCHHHHHHHHHH
17.0429759185
282PhosphorylationYRCDTVTSAVMMQYS
CCCCHHHHHHHHHHC
17.9630576142
318PhosphorylationYVFDIKRTSKEVYDH
EEEEEECCCHHHHHH
38.87-
319PhosphorylationVFDIKRTSKEVYDHA
EEEEECCCHHHHHHH
30.74-
323PhosphorylationKRTSKEVYDHARRAL
ECCCHHHHHHHHHHH
11.78-
377UbiquitinationQTRVLQEKLRKLKEA
HHHHHHHHHHHHHHH
40.40-

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
-KUbiquitinationE3 ubiquitin ligaseMYLIPQ8WY64
PMID:14550572

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYLIP_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 MYLIP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNPY2_HUMANCNPY2physical
12826659
MYLIP_HUMANMYLIPphysical
12826659
LDLR_HUMANLDLRphysical
21734303
MYLIP_HUMANMYLIPphysical
21685362
LDLR_HUMANLDLRphysical
21685362
UB2D1_HUMANUBE2D1physical
21685362
LDLR_HUMANLDLRphysical
22109552
VLDLR_HUMANVLDLRphysical
22109552
LRP8_HUMANLRP8physical
22109552
ML12B_HUMANMYL12Bphysical
10593918
UB2D2_HUMANUBE2D2physical
21685362
UB2D3_HUMANUBE2D3physical
21685362
UB2D4_HUMANUBE2D4physical
21685362
UB2D1_HUMANUBE2D1physical
21734303
UBE2N_HUMANUBE2Nphysical
21734303
KDM1A_HUMANKDM1Aphysical
23455924
T22D4_HUMANTSC22D4physical
25416956
RASF5_HUMANRASSF5physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
LDLR_HUMANLDLRphysical
23382078
CTR9_HUMANCTR9physical
28514442
WDFY1_HUMANWDFY1physical
28514442
MYCB2_HUMANMYCBP2physical
28514442
PAF1_HUMANPAF1physical
28514442
UBA6_HUMANUBA6physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYLIP_HUMAN

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Related Literatures of Post-Translational Modification

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