TMC6_HUMAN - dbPTM
TMC6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMC6_HUMAN
UniProt AC Q7Z403
Protein Name Transmembrane channel-like protein 6
Gene Name TMC6
Organism Homo sapiens (Human).
Sequence Length 805
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Probable ion channel..
Protein Sequence MAQPLAFILDVPETPGDQGQGPSPYDESEVHDSFQQLIQEQSQCTAQEGLELQQREREVTGSSQQTLWRPEGTQSTATLRILASMPSRTIGRSRGAIISQYYNRTVQLRCRSSRPLLGNFVRSAWPSLRLYDLELDPTALEEEEKQSLLVKELQSLAVAQRDHMLRGMPLSLAEKRSLREKSRTPRGKWRGQPGSGGVCSCCGRLRYACVLALHSLGLALLSALQALMPWRYALKRIGGQFGSSVLSYFLFLKTLLAFNALLLLLLVAFIMGPQVAFPPALPGPAPVCTGLELLTGAGCFTHTVMYYGHYSNATLNQPCGSPLDGSQCTPRVGGLPYNMPLAYLSTVGVSFFITCITLVYSMAHSFGESYRVGSTSGIHAITVFCSWDYKVTQKRASRLQQDNIRTRLKELLAEWQLRHSPRSVCGRLRQAAVLGLVWLLCLGTALGCAVAVHVFSEFMIQSPEAAGQEAVLLVLPLVVGLLNLGAPYLCRVLAALEPHDSPVLEVYVAICRNLILKLAILGTLCYHWLGRRVGVLQGQCWEDFVGQELYRFLVMDFVLMLLDTLFGELVWRIISEKKLKRRRKPEFDIARNVLELIYGQTLTWLGVLFSPLLPAVQIIKLLLVFYVKKTSLLANCQAPRRPWLASHMSTVFLTLLCFPAFLGAAVFLCYAVWQVKPSSTCGPFRTLDTMYEAGRVWVRHLEAAGPRVSWLPWVHRYLMENTFFVFLVSALLLAVIYLNIQVVRGQRKVICLLKEQISNEGEDKIFLINKLHSIYERKEREERSRVGTTEEAAAPPALLTDEQDA
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
48 (in isoform 3)Ubiquitination-64.3821906983
60PhosphorylationQQREREVTGSSQQTL
HHHHHHHCCCCCCEE
26.9630108239
62PhosphorylationREREVTGSSQQTLWR
HHHHHCCCCCCEEEC
18.6630108239
63PhosphorylationEREVTGSSQQTLWRP
HHHHCCCCCCEEECC
27.8730108239
66PhosphorylationVTGSSQQTLWRPEGT
HCCCCCCEEECCCCC
22.2030108239
73PhosphorylationTLWRPEGTQSTATLR
EEECCCCCCCHHHHH
20.0623312004
75PhosphorylationWRPEGTQSTATLRIL
ECCCCCCCHHHHHHH
21.6123312004
76PhosphorylationRPEGTQSTATLRILA
CCCCCCCHHHHHHHH
17.5323312004
78PhosphorylationEGTQSTATLRILASM
CCCCCHHHHHHHHCC
19.3623312004
84PhosphorylationATLRILASMPSRTIG
HHHHHHHCCCCCCCC
27.9928355574
87PhosphorylationRILASMPSRTIGRSR
HHHHCCCCCCCCCCC
33.1530108239
89PhosphorylationLASMPSRTIGRSRGA
HHCCCCCCCCCCCCC
31.9225219547
93PhosphorylationPSRTIGRSRGAIISQ
CCCCCCCCCCCHHHH
29.8325219547
94MethylationSRTIGRSRGAIISQY
CCCCCCCCCCHHHHH
36.8824129315
99PhosphorylationRSRGAIISQYYNRTV
CCCCCHHHHHCCCCE
13.1525219547
101PhosphorylationRGAIISQYYNRTVQL
CCCHHHHHCCCCEEE
8.9125219547
102PhosphorylationGAIISQYYNRTVQLR
CCHHHHHCCCCEEEE
7.1925219547
103N-linked_GlycosylationAIISQYYNRTVQLRC
CHHHHHCCCCEEEEC
28.36UniProtKB CARBOHYD
105PhosphorylationISQYYNRTVQLRCRS
HHHHCCCCEEEECCC
14.6825219547
112PhosphorylationTVQLRCRSSRPLLGN
CEEEECCCCCCCCHH
34.0326657352
113PhosphorylationVQLRCRSSRPLLGNF
EEEECCCCCCCCHHH
20.6826657352
123PhosphorylationLLGNFVRSAWPSLRL
CCHHHHHHHCCCCEE
29.4128450419
127PhosphorylationFVRSAWPSLRLYDLE
HHHHHCCCCEEEEEE
18.5430108239
131PhosphorylationAWPSLRLYDLELDPT
HCCCCEEEEEECCHH
16.4327642862
145 (in isoform 2)Ubiquitination-48.7621906983
145 (in isoform 1)Ubiquitination-48.7621906983
145UbiquitinationTALEEEEKQSLLVKE
HCCCHHHHHHHHHHH
48.7621906983
151UbiquitinationEKQSLLVKELQSLAV
HHHHHHHHHHHHHHH
53.3121906983
151 (in isoform 2)Ubiquitination-53.3121906983
151 (in isoform 1)Ubiquitination-53.3121906983
175UbiquitinationMPLSLAEKRSLREKS
CCCCHHHHHHHHHHC
41.50-
182 (in isoform 4)Ubiquitination-36.3121906983
312N-linked_GlycosylationMYYGHYSNATLNQPC
HHHCCCCCCCCCCCC
29.76UniProtKB CARBOHYD
349 (in isoform 3)Ubiquitination-3.8121906983
406PhosphorylationLQQDNIRTRLKELLA
HHHHCHHHHHHHHHH
36.23-
409 (in isoform 1)Ubiquitination-42.9221906983
409UbiquitinationDNIRTRLKELLAEWQ
HCHHHHHHHHHHHHH
42.9221906983
419 (in isoform 2)Ubiquitination-51.2321906983
420PhosphorylationAEWQLRHSPRSVCGR
HHHHHHCCCHHHHHH
18.6417081983
575PhosphorylationELVWRIISEKKLKRR
HHHHHHHCHHHHHHC
40.7824719451
584UbiquitinationKKLKRRRKPEFDIAR
HHHHHCCCCHHHHHH
47.27-
626PhosphorylationIKLLLVFYVKKTSLL
HHHHHHHHHHHHCHH
12.1330622161
748UbiquitinationQVVRGQRKVICLLKE
HHHCCCCCEEEEEEH
28.23-
754UbiquitinationRKVICLLKEQISNEG
CCEEEEEEHHHCCCC
34.32-
764UbiquitinationISNEGEDKIFLINKL
HCCCCCCCEEHHHHH
30.93-
770UbiquitinationDKIFLINKLHSIYER
CCEEHHHHHHHHHHH
40.352190698
770 (in isoform 1)Ubiquitination-40.3521906983
773PhosphorylationFLINKLHSIYERKER
EHHHHHHHHHHHHHH
36.9825003641
775PhosphorylationINKLHSIYERKEREE
HHHHHHHHHHHHHHH
16.82-
778AcetylationLHSIYERKEREERSR
HHHHHHHHHHHHHHC
49.547378631

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 TMC6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMC6_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 TMC6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PXK_HUMANPXKphysical
28514442
CBARP_HUMANC19orf26physical
28514442

Drug and Disease Associations
Kegg Disease
H00842 Epidermodysplasia verruciformis
OMIM Disease
226400Epidermodysplasia verruciformis (EV)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TMC6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, AND MASSSPECTROMETRY.

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