GPM6A_HUMAN - dbPTM
GPM6A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPM6A_HUMAN
UniProt AC P51674
Protein Name Neuronal membrane glycoprotein M6-a
Gene Name GPM6A
Organism Homo sapiens (Human).
Sequence Length 278
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cell projection, axon. Cell projection, dendritic spine. Cell projection, filopodium. Localizes to cholesterol-rich lipid rafts of the plasma membrane of hippocampal neurons. Localized to plasma membrane of
Protein Description Involved in neuronal differentiation, including differentiation and migration of neuronal stem cells. Plays a role in neuronal plasticity and is involved in neurite and filopodia outgrowth, filopodia motility and probably synapse formation. GPM6A-induced filopodia formation involves mitogen-activated protein kinase (MAPK) and Src signaling pathways. May be involved in neuronal NGF-dependent Ca(2+) influx. May be involved in regulation of endocytosis and intracellular trafficking of G-protein-coupled receptors (GPCRs); enhances internalization and recycling of mu-type opioid receptor..
Protein Sequence MEENMEEGQTQKGCFECCIKCLGGIPYASLIATILLYAGVALFCGCGHEALSGTVNILQTYFEMARTAGDTLDVFTMIDIFKYVIYGIAAAFFVYGILLMVEGFFTTGAIKDLYGDFKITTCGRCVSAWFIMLTYLFMLAWLGVTAFTSLPVYMYFNLWTICRNTTLVEGANLCLDLRQFGIVTIGEEKKICTVSENFLRMCESTELNMTFHLFIVALAGAGAAVIAMVHYLMVLSANWAYVKDACRMQKYEDIKSKEEQELHDIHSTRSKERLNAYT
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-------MEENMEEG
-------CCCCCCCC
15.2722223895
10PhosphorylationENMEEGQTQKGCFEC
CCCCCCCCCCCHHHH
43.0012359212
164N-linked_GlycosylationNLWTICRNTTLVEGA
HHHHHHCCCCCCCCC
32.76UniProtKB CARBOHYD
208N-linked_GlycosylationMCESTELNMTFHLFI
HHHCCCCHHHHHHHH
22.63UniProtKB CARBOHYD
220UbiquitinationLFIVALAGAGAAVIA
HHHHHHHHCHHHHHH
25.9532142685
222UbiquitinationIVALAGAGAAVIAMV
HHHHHHCHHHHHHHH
17.1032142685
244UbiquitinationANWAYVKDACRMQKY
CCCHHHHHHHHCCCH
40.6432142685
246UbiquitinationWAYVKDACRMQKYED
CHHHHHHHHCCCHHH
5.5132142685
248UbiquitinationYVKDACRMQKYEDIK
HHHHHHHCCCHHHHC
3.9732142685
250UbiquitinationKDACRMQKYEDIKSK
HHHHHCCCHHHHCCH
41.0632142685
251PhosphorylationDACRMQKYEDIKSKE
HHHHCCCHHHHCCHH
11.2725332170
255UbiquitinationMQKYEDIKSKEEQEL
CCCHHHHCCHHHHHH
68.7332142685
256PhosphorylationQKYEDIKSKEEQELH
CCHHHHCCHHHHHHH
45.7118510355
257UbiquitinationKYEDIKSKEEQELHD
CHHHHCCHHHHHHHH
61.3432142685
267PhosphorylationQELHDIHSTRSKERL
HHHHHHHHCCCHHHH
26.3315822905
268PhosphorylationELHDIHSTRSKERLN
HHHHHHHCCCHHHHH
25.4628270605
270PhosphorylationHDIHSTRSKERLNAY
HHHHHCCCHHHHHCC
38.6728270605
277PhosphorylationSKERLNAYT------
CHHHHHCCC------
16.3524927040
278PhosphorylationKERLNAYT-------
HHHHHCCC-------
29.71-

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
10TPhosphorylationKinasePRKCAP17252
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPM6A_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 GPM6A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZDH17_HUMANZDHHC17physical
24705354
CC126_HUMANCCDC126physical
26186194
MGT5A_HUMANMGAT5physical
26186194
RMD3_HUMANRMDN3physical
26186194
S35B2_HUMANSLC35B2physical
26186194
PLCC_HUMANAGPAT3physical
26186194
FITM2_HUMANFITM2physical
26186194
ERMP1_HUMANERMP1physical
26186194
HAX1_HUMANHAX1physical
26186194
IKIP_HUMANIKBIPphysical
26186194
RFT1_HUMANRFT1physical
26186194
QCR9_HUMANUQCR10physical
26186194
YIPF3_HUMANYIPF3physical
26186194
F189B_HUMANFAM189Bphysical
26186194
SCAM2_HUMANSCAMP2physical
26186194
PXMP2_HUMANPXMP2physical
26186194
GP1BB_HUMANGP1BBphysical
26186194
VKORL_HUMANVKORC1L1physical
26186194
ZDH18_HUMANZDHHC18physical
26186194
CC126_HUMANCCDC126physical
28514442
MGT5A_HUMANMGAT5physical
28514442
HAX1_HUMANHAX1physical
28514442
IKIP_HUMANIKBIPphysical
28514442
FITM2_HUMANFITM2physical
28514442
TSN3_HUMANTSPAN3physical
28514442
YIPF3_HUMANYIPF3physical
28514442
ZDH18_HUMANZDHHC18physical
28514442
ERMP1_HUMANERMP1physical
28514442
GP1BB_HUMANGP1BBphysical
28514442
FKRP_HUMANFKRPphysical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPM6A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex.";
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.;
J. Proteome Res. 4:306-315(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASSSPECTROMETRY.

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