TM168_HUMAN - dbPTM
TM168_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM168_HUMAN
UniProt AC Q9H0V1
Protein Name Transmembrane protein 168
Gene Name TMEM168
Organism Homo sapiens (Human).
Sequence Length 697
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MCKSLRYCFSHCLYLAMTRLEEVNREVNMHSSVRYLGYLARINLLVAICLGLYVRWEKTANSLILVIFILGLFVLGIASILYYYFSMEAASLSLSNLWFGFLLGLLCFLDNSSFKNDVKEESTKYLLLTSIVLRILCSLVERISGYVRHRPTLLTTVEFLELVGFAIASTTMLVEKSLSVILLVVALAMLIIDLRMKSFLAIPNLVIFAVLLFFSSLETPKNPIAFACFFICLITDPFLDIYFSGLSVTERWKPFLYRGRICRRLSVVFAGMIELTFFILSAFKLRDTHLWYFVIPGFSIFGIFWMICHIIFLLTLWGFHTKLNDCHKVYFTHRTDYNSLDRIMASKGMRHFCLISEQLVFFSLLATAILGAVSWQPTNGIFLSMFLIVLPLESMAHGLFHELGNCLGGTSVGYAIVIPTNFCSPDGQPTLLPPEHVQELNLRSTGMLNAIQRFFAYHMIETYGCDYSTSGLSFDTLHSKLKAFLELRTVDGPRHDTYILYYSGHTHGTGEWALAGGDTLRLDTLIEWWREKNGSFCSRLIIVLDSENSTPWVKEVRKINDQYIAVQGAELIKTVDIEEADPPQLGDFTKDWVEYNCNSSNNICWTEKGRTVKAVYGVSKRWSDYTLHLPTGSDVAKHWMLHFPRITYPLVHLANWLCGLNLFWICKTCFRCLKRLKMSWFLPTVLDTGQGFKLVKS
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
31PhosphorylationNREVNMHSSVRYLGY
HHHCCCCHHHHHHHH
21.54-
35PhosphorylationNMHSSVRYLGYLARI
CCCHHHHHHHHHHHH
11.4324043423
38PhosphorylationSSVRYLGYLARINLL
HHHHHHHHHHHHHHH
8.4624043423
53PhosphorylationVAICLGLYVRWEKTA
HHHHHHHHHHHHHHH
6.0324043423
111N-linked_GlycosylationGLLCFLDNSSFKNDV
HHHHHHCCCCCCCCC
41.52UniProtKB CARBOHYD
125PhosphorylationVKEESTKYLLLTSIV
CCHHHHHHHHHHHHH
11.5824505115
198PhosphorylationIIDLRMKSFLAIPNL
HHHHHHHHHCCCHHH
19.02-
219PhosphorylationLFFSSLETPKNPIAF
HHHHCCCCCCCHHHH
44.8721964256
253UbiquitinationLSVTERWKPFLYRGR
CCCHHCCCCCHHHCH
31.92-
276PhosphorylationFAGMIELTFFILSAF
HHHHHHHHHHHHHHH
12.05-
281PhosphorylationELTFFILSAFKLRDT
HHHHHHHHHHCCCCC
27.18-
330PhosphorylationLNDCHKVYFTHRTDY
HHCCCEEEEECCCCH
13.94-
337PhosphorylationYFTHRTDYNSLDRIM
EEECCCCHHHHHHHH
13.16-
339PhosphorylationTHRTDYNSLDRIMAS
ECCCCHHHHHHHHHC
25.97-
346PhosphorylationSLDRIMASKGMRHFC
HHHHHHHCCCCCCHH
16.62-
445PhosphorylationQELNLRSTGMLNAIQ
HHCCCCCCCHHHHHH
21.85-
533N-linked_GlycosylationIEWWREKNGSFCSRL
HHHHHHHCCCCCEEE
46.73UniProtKB CARBOHYD
535PhosphorylationWWREKNGSFCSRLII
HHHHHCCCCCEEEEE
32.26-
598N-linked_GlycosylationDWVEYNCNSSNNICW
CCHHHCCCCCCCEEE
44.85UniProtKB CARBOHYD
623PhosphorylationYGVSKRWSDYTLHLP
EECCCCCCCEEEECC
25.4424961811
625PhosphorylationVSKRWSDYTLHLPTG
CCCCCCCEEEECCCC
12.99-
626PhosphorylationSKRWSDYTLHLPTGS
CCCCCCEEEECCCCC
16.82-
631PhosphorylationDYTLHLPTGSDVAKH
CEEEECCCCCHHHHH
56.53-
679PhosphorylationCLKRLKMSWFLPTVL
HHHHHCHHHCCCEEE
17.06-

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 TM168_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM168_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 TM168_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TM168_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TM168_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP