EMB_HUMAN - dbPTM
EMB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EMB_HUMAN
UniProt AC Q6PCB8
Protein Name Embigin
Gene Name EMB
Organism Homo sapiens (Human).
Sequence Length 327
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell junction, synapse . Localizes to the neuromuscular junctions.
Protein Description Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays the retraction of terminal sprouts following re-innervation of denervated endplates. May play a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane (By similarity)..
Protein Sequence MRALPGLLEARARTPRLLLLQCLLAAARPSSADGSAPDSPFTSPPLREEIMANNFSLESHNISLTEHSSMPVEKNITLERPSNVNLTCQFTTSGDLNAVNVTWKKDGEQLENNYLVSATGSTLYTQYRFTIINSKQMGSYSCFFREEKEQRGTFNFKVPELHGKNKPLISYVGDSTVLTCKCQNCFPLNWTWYSSNGSVKVPVGVQMNKYVINGTYANETKLKITQLLEEDGESYWCRALFQLGESEEHIELVVLSYLVPLKPFLVIVAEVILLVATILLCEKYTQKKKKHSDEGKEFEQIEQLKSDDSNGIENNVPRHRKNESLGQ
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
54N-linked_GlycosylationREEIMANNFSLESHN
HHHHHHCCCCCEECC		20.53UniProtKB CARBOHYD
55UbiquitinationEEIMANNFSLESHNI
HHHHHCCCCCEECCE		9.89-
61N-linked_GlycosylationNFSLESHNISLTEHS
CCCCEECCEECCCCC		34.52UniProtKB CARBOHYD
75N-linked_GlycosylationSSMPVEKNITLERPS
CCCCEEECEEEECCC		20.97UniProtKB CARBOHYD
85N-linked_GlycosylationLERPSNVNLTCQFTT
EECCCCEEEEEEEEC		33.61UniProtKB CARBOHYD
85UbiquitinationLERPSNVNLTCQFTT
EECCCCEEEEEEEEC		33.61-
100N-linked_GlycosylationSGDLNAVNVTWKKDG
CCCCCEEEEEEECCH		24.08UniProtKB CARBOHYD
105UbiquitinationAVNVTWKKDGEQLEN
EEEEEEECCHHHCCC		63.63-
107UbiquitinationNVTWKKDGEQLENNY
EEEEECCHHHCCCCE		33.17-
116UbiquitinationQLENNYLVSATGSTL
HCCCCEEEECCCCEE		2.30-
135UbiquitinationRFTIINSKQMGSYSC
EEEEEECCCCEEEEE		39.55-
157UbiquitinationQRGTFNFKVPELHGK
HCCEEEEECCHHCCC		58.9729967540
166UbiquitinationPELHGKNKPLISYVG
CHHCCCCCCCEEEEC		44.69-
189N-linked_GlycosylationCQNCFPLNWTWYSSN
ECCEEECCEEEECCC		34.08UniProtKB CARBOHYD
196N-linked_GlycosylationNWTWYSSNGSVKVPV
CEEEECCCCCEEEEE		40.60UniProtKB CARBOHYD
213N-linked_GlycosylationQMNKYVINGTYANET
EECEEEECCEECCCC		27.0619349973
213N-linked_GlycosylationQMNKYVINGTYANET
EECEEEECCEECCCC		27.0619349973
218N-linked_GlycosylationVINGTYANETKLKIT
EECCEECCCCEEEEE		47.2419349973
218N-linked_GlycosylationVINGTYANETKLKIT
EECCEECCCCEEEEE		47.2419349973
246UbiquitinationALFQLGESEEHIELV
HHHHCCCCHHHEEEE		46.6222817900
246UbiquitinationALFQLGESEEHIELV
HHHHCCCCHHHEEEE		46.62-
255UbiquitinationEHIELVVLSYLVPLK
HHEEEEHHHHHCCCH		1.8622817900
255UbiquitinationEHIELVVLSYLVPLK
HHEEEEHHHHHCCCH		1.86-
296UbiquitinationKKHSDEGKEFEQIEQ
HHCCCCCHHHHHHHH		58.1221906983
305UbiquitinationFEQIEQLKSDDSNGI
HHHHHHHCCCCCCCC		52.0821906983
306PhosphorylationEQIEQLKSDDSNGIE
HHHHHHCCCCCCCCC		56.0730266825
309PhosphorylationEQLKSDDSNGIENNV
HHHCCCCCCCCCCCC		41.7823401153
324PhosphorylationPRHRKNESLGQ----
CCHHCCCCCCC----		47.39-
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 EMB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of EMB_HUMAN !!
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 EMB_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-213 AND ASN-218, AND MASSSPECTROMETRY.

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