TM45B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TM45B_HUMAN
• UniProt AC: Q96B21
• Protein Name: Transmembrane protein 45B
• Gene Name: TMEM45B
• Organism: Homo sapiens (Human).
• Sequence Length: 275
• Subcellular Localization: Membrane ; Multi-pass membrane protein .
• Protein Sequence: MANFKGHALPGSFFLIIGLCWSVKYPLKYFSHTRKNSPLHYYQRLEIVEAAIRTLFSVTGILAEQFVPDGPHLHLYHENHWIKLMNWQHSTMYLFFAVSGIVDMLTYLVSHVPLGVDRLVMAVAVFMEGFLFYYHVHNRPPLDQHIHSLLLYALFGGCVSISLEVIFRDHIVLELFRTSLIILQGTWFWQIGFVLFPPFGTPEWDQKDDANLMFITMCFCWHYLAALSIVAVNYSLVYCLLTRMKRHGRGEIIGIQKLNSDDTYQTALLSGSDEE

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
263	Phosphorylation	QKLNSDDTYQTALLS EECCCCCCHHHHHHC	23.63	23312004
264	Phosphorylation	KLNSDDTYQTALLSG ECCCCCCHHHHHHCC	15.74	23312004
266	Phosphorylation	NSDDTYQTALLSGSD CCCCCHHHHHHCCCC	14.62	23312004
270	Phosphorylation	TYQTALLSGSDEE-- CHHHHHHCCCCCC--	36.78	20201521
272	Phosphorylation	QTALLSGSDEE---- HHHHHCCCCCC----	38.17	20201521

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

Oops, there are no upstream regulatory protein records of TM45B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TM45B_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 TM45B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UB2G2_HUMAN	UBE2G2	physical	21988832

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-270 AND SER-272, ANDMASS SPECTROMETRY.
PubMed: 18691976