POPD1_HUMAN - dbPTM
POPD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POPD1_HUMAN
UniProt AC Q8NE79
Protein Name Blood vessel epicardial substance {ECO:0000312|HGNC:HGNC:1152}
Gene Name BVES {ECO:0000312|HGNC:HGNC:1152}
Organism Homo sapiens (Human).
Sequence Length 360
Subcellular Localization Lateral cell membrane . Cell junction, tight junction . Membrane
Multi-pass membrane protein . Cell membrane, sarcolemma . Membrane, caveola . Colocalizes with VAMP3 at the cell-cell contact in cardiac and skeletal muscle (By similarity). Its movem
Protein Description Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. [PubMed: 16188940 Plays a role in VAMP3-mediated vesicular transport and recycling of different receptor molecules through its interaction with VAMP3. Plays a role in the regulation of cell shape and movement by modulating the Rho-family GTPase activity through its interaction with ARHGEF25/GEFT. Induces primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. Also involved in striated muscle regeneration and repair and in the regulation of cell spreading (By similarity Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density]
Protein Sequence MNYTESSPLRESTAIGFTPELESIIPVPSNKTTCENWREIHHLVFHVANICFAVGLVIPTTLHLHMIFLRGMLTLGCTLYIVWATLYRCALDIMIWNSVFLGVNILHLSYLLYKKRPVKIEKELSGMYRRLFEPLRVPPDLFRRLTGQFCMIQTLKKGQTYAAEDKTSVDDRLSILLKGKMKVSYRGHFLHNIYPCAFIDSPEFRSTQMHKGEKFQVTIIADDNCRFLCWSRERLTYFLESEPFLYEIFRYLIGKDITNKLYSLNDPTLNDKKAKKLEHQLSLCTQISMLEMRNSIASSSDSDDGLHQFLRGTSSMSSLHVSSPHQRASAKMKPIEEGAEDDDDVFEPASPNTLKVHQLP
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
2N-linked_Glycosylation------MNYTESSPL
------CCCCCCCCC
53.05UniProtKB CARBOHYD
3Phosphorylation-----MNYTESSPLR
-----CCCCCCCCCC
15.58-
6Phosphorylation--MNYTESSPLREST
--CCCCCCCCCCCCC
29.4722210691
7Phosphorylation-MNYTESSPLRESTA
-CCCCCCCCCCCCCC
23.0122210691
30N-linked_GlycosylationSIIPVPSNKTTCENW
HCEECCCCCCCCCCH
39.35UniProtKB CARBOHYD
122AcetylationKRPVKIEKELSGMYR
CCCCCCHHHHCHHHH
68.3819813459
194PhosphorylationGHFLHNIYPCAFIDS
CCCHHCCCCCEEECC
9.51-
295PhosphorylationSMLEMRNSIASSSDS
HHHHHHHHHHCCCCC
14.7930177828
298PhosphorylationEMRNSIASSSDSDDG
HHHHHHHCCCCCCCC
28.8025850435
299PhosphorylationMRNSIASSSDSDDGL
HHHHHHCCCCCCCCH
29.1925850435
300PhosphorylationRNSIASSSDSDDGLH
HHHHHCCCCCCCCHH
38.3425850435
302PhosphorylationSIASSSDSDDGLHQF
HHHCCCCCCCCHHHH
39.2825850435
313PhosphorylationLHQFLRGTSSMSSLH
HHHHHHCCCCCCCCC
15.9322210691
314PhosphorylationHQFLRGTSSMSSLHV
HHHHHCCCCCCCCCC
27.2024117733
315PhosphorylationQFLRGTSSMSSLHVS
HHHHCCCCCCCCCCC
23.6324117733
317PhosphorylationLRGTSSMSSLHVSSP
HHCCCCCCCCCCCCH
31.5324117733
318PhosphorylationRGTSSMSSLHVSSPH
HCCCCCCCCCCCCHH
17.5324117733
322PhosphorylationSMSSLHVSSPHQRAS
CCCCCCCCCHHHHHC
27.6624117733
323PhosphorylationMSSLHVSSPHQRASA
CCCCCCCCHHHHHCC
25.8824117733
350PhosphorylationDDVFEPASPNTLKVH
CCCCCCCCCCCEEEE
29.4226657352
353PhosphorylationFEPASPNTLKVHQLP
CCCCCCCCEEEECCC
31.1922673903

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 POPD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POPD1_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 POPD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBAC1_HUMANUBAC1physical
26186194
RN123_HUMANRNF123physical
26186194
RN123_HUMANRNF123physical
28514442
UBAC1_HUMANUBAC1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POPD1_HUMAN

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Related Literatures of Post-Translational Modification

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