dbPTM

TM115_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TM115_HUMAN
UniProt AC	Q12893
Protein Name	Transmembrane protein 115 {ECO:0000305}
Gene Name	TMEM115 {ECO:0000312\|HGNC:HGNC:30055}
Organism	Homo sapiens (Human).
Sequence Length	351
Subcellular Localization	Golgi apparatus, Golgi stack membrane Multi-pass membrane protein .
Protein Description	May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum. May indirectly play a role in protein glycosylation in the Golgi..
Protein Sequence	MQRALPGARQHLGAILASASVVVKALCAAVLFLYLLSFAVDTGCLAVTPGYLFPPNFWIWTLATHGLMEQHVWDVAISLTTVVVAGRLLEPLWGALELLIFFSVVNVSVGLLGAFAYLLTYMASFNLVYLFTVRIHGALGFLGGVLVALKQTMGDCVVLRVPQVRVSVMPMLLLALLLLLRLATLLQSPALASYGFGLLSSWVYLRFYQRHSRGRGDMADHFAFATFFPEILQPVVGLLANLVHSLLVKVKICQKTVKRYDVGAPSSITISLPGTDPQDAERRRQLALKALNERLKRVEDQSIWPSMDDDEEESGAKVDSPLPSDKAPTPPGKGAAPESSLITFEAAPPTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	CAAVLFLYLLSFAVD HHHHHHHHHHHHHHH	9.77	26074081
37	Phosphorylation	VLFLYLLSFAVDTGC HHHHHHHHHHHHCCC	14.47	26074081
42	Phosphorylation	LLSFAVDTGCLAVTP HHHHHHHCCCCCCCC	24.16	26074081
48	Phosphorylation	DTGCLAVTPGYLFPP HCCCCCCCCCCCCCC	12.85	26074081
51	Phosphorylation	CLAVTPGYLFPPNFW CCCCCCCCCCCCCCH	13.33	26074081
260	Phosphorylation	CQKTVKRYDVGAPSS HHCCCCCCCCCCCCC	14.84	30576142
266	Phosphorylation	RYDVGAPSSITISLP CCCCCCCCCEEEECC	33.56	28857561
267	Phosphorylation	YDVGAPSSITISLPG CCCCCCCCEEEECCC	23.77	28857561
269	Phosphorylation	VGAPSSITISLPGTD CCCCCCEEEECCCCC	13.37	28857561
271	Phosphorylation	APSSITISLPGTDPQ CCCCEEEECCCCCHH	21.62	28348404
275	Phosphorylation	ITISLPGTDPQDAER EEEECCCCCHHHHHH	42.43	25159151
289	Ubiquitination	RRRQLALKALNERLK HHHHHHHHHHHHHHH	45.26	21890473
289	Ubiquitination	RRRQLALKALNERLK HHHHHHHHHHHHHHH	45.26	21890473
302	Phosphorylation	LKRVEDQSIWPSMDD HHHHHHCCCCCCCCC	38.65	29978859
306	Phosphorylation	EDQSIWPSMDDDEEE HHCCCCCCCCCCHHH	21.61	29507054
314	Phosphorylation	MDDDEEESGAKVDSP CCCCHHHCCCCCCCC	47.53	25159151
320	Phosphorylation	ESGAKVDSPLPSDKA HCCCCCCCCCCCCCC	31.18	29255136
324	Phosphorylation	KVDSPLPSDKAPTPP CCCCCCCCCCCCCCC	60.47	23401153
326	Ubiquitination	DSPLPSDKAPTPPGK CCCCCCCCCCCCCCC	61.68	-
329	Phosphorylation	LPSDKAPTPPGKGAA CCCCCCCCCCCCCCC	47.15	29255136
339	Phosphorylation	GKGAAPESSLITFEA CCCCCCCHHCEEEEE	29.41	24719451
340	Phosphorylation	KGAAPESSLITFEAA CCCCCCHHCEEEEEC	23.33	26074081
343	Phosphorylation	APESSLITFEAAPPT CCCHHCEEEEECCCC	22.25	26074081
350	Phosphorylation	TFEAAPPTL------ EEEECCCCC------	44.00	26074081

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 TM115_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TM115_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 TM115_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SYNE4_HUMAN	SYNE4	physical	25416956

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 TM115_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASSSPECTROMETRY.	19007248 [Abstract]