TM104_HUMAN - dbPTM
TM104_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM104_HUMAN
UniProt AC Q8NE00
Protein Name Transmembrane protein 104
Gene Name TMEM104
Organism Homo sapiens (Human).
Sequence Length 496
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MAGEITETGELYSSYVGLVYMFNLIVGTGALTMPKAFATAGWLVSLVLLVFLGFMSFVTTTFVIEAMAAANAQLHWKRMENLKEEEDDDSSTASDSDVLIRDNYERAEKRPILSVQRRGSPNPFEITDRVEMGQMASMFFNKVGVNLFYFCIIVYLYGDLAIYAAAVPFSLMQVTCSATGNDSCGVEADTKYNDTDRCWGPLRRVDAYRIYLAIFTLLLGPFTFFDVQKTKYLQILTSLMRWIAFAVMIVLALIRIGHGQGEGHPPLADFSGVRNLFGVCVYSFMCQHSLPSLITPVSSKRHLTRLVFLDYVLILAFYGLLSFTAIFCFRGDSLMDMYTLNFARCDVVGLAAVRFFLGLFPVFTISTNFPIIAVTLRNNWKTLFHREGGTYPWVVDRVVFPTITLVPPVLVAFCTHDLESLVGITGAYAGTGIQYVIPAFLVYHCRRDTQLAFGCGVSNKHRSPFRHTFWVGFVLLWAFSCFIFVTANIILSETKL
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
83 (in isoform 2)Ubiquitination-74.7421906983
83 (in isoform 1)Ubiquitination-74.7421890473
83UbiquitinationWKRMENLKEEEDDDS
HHHHHCCCCCCCCCC
74.7421906983
90PhosphorylationKEEEDDDSSTASDSD
CCCCCCCCCCCCHHC
36.2629255136
91PhosphorylationEEEDDDSSTASDSDV
CCCCCCCCCCCHHCE
34.6829255136
92PhosphorylationEEDDDSSTASDSDVL
CCCCCCCCCCHHCEE
33.8529255136
94PhosphorylationDDDSSTASDSDVLIR
CCCCCCCCHHCEEEE
37.4229255136
96PhosphorylationDSSTASDSDVLIRDN
CCCCCCHHCEEEECC
27.4229255136
104PhosphorylationDVLIRDNYERAEKRP
CEEEECCHHHHHHCC
15.8723090842
109 (in isoform 2)Ubiquitination-63.5921906983
109 (in isoform 1)Ubiquitination-63.5921890473
109UbiquitinationDNYERAEKRPILSVQ
CCHHHHHHCCEEEEE
63.5921906983
114PhosphorylationAEKRPILSVQRRGSP
HHHCCEEEEECCCCC
19.5429978859
120PhosphorylationLSVQRRGSPNPFEIT
EEEECCCCCCCCCCC
21.4929255136
127PhosphorylationSPNPFEITDRVEMGQ
CCCCCCCCCCHHHHH
15.5629978859
193N-linked_GlycosylationVEADTKYNDTDRCWG
CCCCCCCCCCCCCCC
47.46UniProtKB CARBOHYD
208PhosphorylationPLRRVDAYRIYLAIF
CCCHHHHHHHHHHHH
7.9622210691
211PhosphorylationRVDAYRIYLAIFTLL
HHHHHHHHHHHHHHH
4.8922210691
216PhosphorylationRIYLAIFTLLLGPFT
HHHHHHHHHHHCCCC
15.4722210691
232PhosphorylationFDVQKTKYLQILTSL
CCCCHHHHHHHHHHH
14.7429083192
237PhosphorylationTKYLQILTSLMRWIA
HHHHHHHHHHHHHHH
22.8029083192
238PhosphorylationKYLQILTSLMRWIAF
HHHHHHHHHHHHHHH
19.4029083192
381UbiquitinationVTLRNNWKTLFHREG
EEECCCEEEEEECCC
37.1621890473
381 (in isoform 1)Ubiquitination-37.1621890473
460UbiquitinationFGCGVSNKHRSPFRH
EECCCCCCCCCCCCH
32.65-

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 TM104_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM104_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 TM104_HUMAN !!

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

Oops, there are no PPI records of TM104_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 TM104_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-91; THR-92 AND SER-94,AND MASS SPECTROMETRY.

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