TM38B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TM38B_HUMAN
• UniProt AC: Q9NVV0
• Protein Name: Trimeric intracellular cation channel type B
• Gene Name: TMEM38B
• Organism: Homo sapiens (Human).
• Sequence Length: 291
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores..
• Protein Sequence: MDSPWDELALAFSRTSMFPFFDIAHYLVSVMAVKRQPGAAALAWKNPISSWFTAMLHCFGGGILSCLLLAEPPLKFLANHTNILLASSIWYITFFCPHDLVSQGYSYLPVQLLASGMKEVTRTWKIVGGVTHANSYYKNGWIVMIAIGWARGAGGTIITNFERLVKGDWKPEGDEWLKMSYPAKVTLLGSVIFTFQHTQHLAISKHNLMFLYTIFIVATKITMMTTQTSTMTFAPFEDTLSWMLFGWQQPFSSCEKKSEAKSPSNGVGSLASKPVDVASDNVKKKHTKKNE

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
121	Phosphorylation	ASGMKEVTRTWKIVG HCCCCHHHEEEEEEC	24.39	29116813
123	Phosphorylation	GMKEVTRTWKIVGGV CCCHHHEEEEEECCE	23.03	29116813
135	Phosphorylation	GGVTHANSYYKNGWI CCEECCCEECCCCEE	30.53	29116813
136	Phosphorylation	GVTHANSYYKNGWIV CEECCCEECCCCEEE	20.47	29116813
166	Ubiquitination	TNFERLVKGDWKPEG ECHHHHHCCCCCCCC	56.60	21890473
170	Ubiquitination	RLVKGDWKPEGDEWL HHHCCCCCCCCCCCC	37.62	-
186	Phosphorylation	MSYPAKVTLLGSVIF CCCCEEEEEEEEEEE	18.63	-
190	Phosphorylation	AKVTLLGSVIFTFQH EEEEEEEEEEEEEEC	16.41	-
232	Phosphorylation	TTQTSTMTFAPFEDT CCCCCEEEEECHHHH	19.41	28985074
239	Phosphorylation	TFAPFEDTLSWMLFG EEECHHHHHHHHHHC	18.59	28985074
258	Phosphorylation	FSSCEKKSEAKSPSN CCCCCCHHCCCCCCC	54.58	21712546
262	Phosphorylation	EKKSEAKSPSNGVGS CCHHCCCCCCCCCHH	40.38	30266825
264	Phosphorylation	KSEAKSPSNGVGSLA HHCCCCCCCCCHHHC	53.99	30266825
269	Phosphorylation	SPSNGVGSLASKPVD CCCCCCHHHCCCCCC	20.53	30266825
272	Phosphorylation	NGVGSLASKPVDVAS CCCHHHCCCCCCCCC	42.67	30266825
273	Ubiquitination	GVGSLASKPVDVASD CCHHHCCCCCCCCCC	43.37	2190698
279	Phosphorylation	SKPVDVASDNVKKKH CCCCCCCCCCCCCCC	29.57	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TM38B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TM38B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TM38B_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TM38B_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 615066: Osteogenesis imperfecta 14 (OI14)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASSSPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262 AND SER-264, ANDMASS SPECTROMETRY.
PubMed: 18691976

"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-279, AND MASSSPECTROMETRY.
PubMed: 19007248