dbPTM

TM9S3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TM9S3_MOUSE
UniProt AC	Q9ET30
Protein Name	Transmembrane 9 superfamily member 3
Gene Name	Tm9sf3
Organism	Mus musculus (Mouse).
Sequence Length	587
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description
Protein Sequence	MRPLPGAPGVAAAAALLLLLLPRARSDEHEHTYQDKEEVVLWMNTVGPYHNRQETYKYFSLPFCVGSKKSISHYHETLGEALQGVELEFSGLDIKFKDDVMPGTYCEIDLDKEKRDAFVYAIKNHYWYQMYIDDLPIWGIVGEADENGEDYYLWTYKKLEIGFNGNRIVDVNLTSEGKVKLVPNTKIQMSYSVKWKKSDVKFEDRFDKYLDPSFFQHRIHWFSIFNSFMMVIFLVGLVSMILMRTLRKDYARYSKEEEMDDMDRDLGDEYGWKQVHGDVFRPSSHPLIFSSLIGSGCQIFAVSLIVIIVAMIEDLYTERGSMLSTAIFVYAATSPVNGYFGGSLYARQGGRRWIKQMFIGAFLIPAMVCGTAFFINFIAIYYHASRAIPFGTMVAVCCICFFVILPLNLVGTILGRNLSGQPNFPCRVNAVPRPIPEKKWFMEPAVIVCLGGILPFGSIFIEMYFIFTSFWAYKIYYVYGFMMLVLVILCIVTVCVTIVCTYFLLNAEDYRWQWTSFLSAASTAIYVYMYSFYYYFFKTKMYGLFQTSFYFGYMAVFSTALGIMCGAIGYMGTSAFVRKIYTNVKID

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
64	S-palmitoylation	KYFSLPFCVGSKKSI EEEECCEECCCCCCH	2.98	28526873
115	Dimethylation	IDLDKEKRDAFVYAI EECCHHHHHHHEEEE	41.40	-
115	Methylation	IDLDKEKRDAFVYAI EECCHHHHHHHEEEE	41.40	3980035
172	N-linked_Glycosylation	GNRIVDVNLTSEGKV CCEEEEEEECCCCEE	32.89	19656770
205	Dimethylation	SDVKFEDRFDKYLDP CCCCHHHHHHHHCCH	34.17	-
205	Methylation	SDVKFEDRFDKYLDP CCCCHHHHHHHHCCH	34.17	3980039
270	Phosphorylation	DRDLGDEYGWKQVHG CCCCHHHCCCCCCCC	32.78	-
417	N-linked_Glycosylation	VGTILGRNLSGQPNF HHHHHCCCCCCCCCC	36.44	-
426	Glutathionylation	SGQPNFPCRVNAVPR CCCCCCCCEECCCCC	7.12	24333276
426	S-palmitoylation	SGQPNFPCRVNAVPR CCCCCCCCEECCCCC	7.12	28526873

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 TM9S3_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TM9S3_MOUSE !!

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 TM9S3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TM9S3_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TM9S3_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-172, AND MASSSPECTROMETRY.	19349973 [Abstract]
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-172, AND MASSSPECTROMETRY.	19656770 [Abstract]