HVCN1_HUMAN - dbPTM
HVCN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HVCN1_HUMAN
UniProt AC Q96D96
Protein Name Voltage-gated hydrogen channel 1
Gene Name HVCN1
Organism Homo sapiens (Human).
Sequence Length 273
Subcellular Localization Membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein. Detected mainly at intracellular membranes upon overexpression in HeLa cells (PuMed:20147290), but not in other cell types.
Protein Description Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis..
Protein Sequence MATWDEKAVTRRAKVAPAERMSKFLRHFTVVGDDYHAWNINYKKWENEEEEEEEEQPPPTPVSGEEGRAAAPDVAPAPGPAPRAPLDFRGMLRKLFSSHRFQVIIICLVVLDALLVLAELILDLKIIQPDKNNYAAMVFHYMSITILVFFMMEIIFKLFVFRLEFFHHKFEILDAVVVVVSFILDIVLLFQEHQFEALGLLILLRLWRVARIINGIIISVKTRSERQLLRLKQMNVQLAAKIQHLEFSCSEKEQEIERLNKLLRQHGLLGEVN
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
7Ubiquitination-MATWDEKAVTRRAK
-CCCCCHHHHHHHHC
45.76-
15 (in isoform 4)Phosphorylation-8.2327155012
23UbiquitinationAPAERMSKFLRHFTV
CCHHHHHHHHHHCEE
38.7921890473
29PhosphorylationSKFLRHFTVVGDDYH
HHHHHHCEEECCCCH
14.2528857561
35PhosphorylationFTVVGDDYHAWNINY
CEEECCCCHHHCCCC
9.7429978859
42PhosphorylationYHAWNINYKKWENEE
CHHHCCCCCCCCCHH
15.3322817900
43UbiquitinationHAWNINYKKWENEEE
HHHCCCCCCCCCHHH
47.0921890473
43UbiquitinationHAWNINYKKWENEEE
HHHCCCCCCCCCHHH
47.0921890473
43 (in isoform 1)Ubiquitination-47.0921890473
43 (in isoform 2)Ubiquitination-47.0921890473
43 (in isoform 3)Ubiquitination-47.0921890473
60PhosphorylationEEEQPPPTPVSGEEG
HHCCCCCCCCCCCCC
41.9422617229
63PhosphorylationQPPPTPVSGEEGRAA
CCCCCCCCCCCCCCC
41.5130576142
90UbiquitinationRAPLDFRGMLRKLFS
CCCCCHHHHHHHHHC
21.3321890473
97PhosphorylationGMLRKLFSSHRFQVI
HHHHHHHCCCCHHHH
35.3514702039
232UbiquitinationERQLLRLKQMNVQLA
HHHHHHHHHHCHHHH
40.8629967540
252AcetylationLEFSCSEKEQEIERL
HHHCCCHHHHHHHHH
48.6923749302
252UbiquitinationLEFSCSEKEQEIERL
HHHCCCHHHHHHHHH
48.6929967540

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
9TPhosphorylationKinasePKCDQ05655
PSP
29TPhosphorylationKinasePRKCDQ05655
GPS
77SPhosphorylationKinasePKCDQ05655
PSP
97SPhosphorylationKinasePRKCDQ05655
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HVCN1_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 HVCN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUCL1_HUMANMUCL1physical
26186194
PIGR_HUMANPIGRphysical
26186194
OXLD1_HUMANOXLD1physical
26186194
CYTN_HUMANCST1physical
26186194
CYTT_HUMANCST2physical
26186194
DOK2_HUMANDOK2physical
26186194
OXLD1_HUMANOXLD1physical
28514442
CYTN_HUMANCST1physical
28514442
DOK2_HUMANDOK2physical
28514442
IGJ_HUMANIGJphysical
28514442
PIGR_HUMANPIGRphysical
28514442
MUCL1_HUMANMUCL1physical
28514442

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 HVCN1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP