TTYH2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TTYH2_HUMAN
• UniProt AC: Q9BSA4
• Protein Name: Protein tweety homolog 2
• Gene Name: TTYH2
• Organism: Homo sapiens (Human).
• Sequence Length: 534
• Subcellular Localization: Cell membrane; Multi-pass membrane protein.
• Protein Description: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction. May be involved in cell proliferation and cell aggregation..
• Protein Sequence: MQAARVDYIAPWWVVWLHSVPHVGLRLQPVNSTFSPGDESYQESLLFLGLVAAVCLGLNLIFLVAYLVCACHCRRDDAVQTKQHHSCCITWTAVVAGLICCAAVGVGFYGNSETNDGAYQLMYSLDDANHTFSGIDALVSGTTQKMKVDLEQHLARLSEIFAARGDYLQTLKFIQQMAGSVVVQLSGLPVWREVTMELTKLSDQTGYVEYYRWLSYLLLFILDLVICLIACLGLAKRSKCLLASMLCCGALSLLLSWASLAADGSAAVATSDFCVAPDTFILNVTEGQISTEVTRYYLYCSQSGSSPFQQTLTTFQRALTTMQIQVAGLLQFAVPLFSTAEEDLLAIQLLLNSSESSLHQLTAMVDCRGLHKDYLDALAGICYDGLQGLLYLGLFSFLAALAFSTMICAGPRAWKHFTTRNRDYDDIDDDDPFNPQAWRMAAHSPPRGQLHSFCSYSSGLGSQTSLQPPAQTISNAPVSEYMNQAMLFGRNPRYENVPLIGRASPPPTYSPSMRATYLSVADEHLRHYGNQFPA

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
31	N-linked_Glycosylation	GLRLQPVNSTFSPGD EEEEECCCCCCCCCC	41.85	UniProtKB CARBOHYD
195	Phosphorylation	LPVWREVTMELTKLS CCCHHEHHHHHHHHC	10.52	-
199	Phosphorylation	REVTMELTKLSDQTG HEHHHHHHHHCCCCC	19.34	22817900
205	Phosphorylation	LTKLSDQTGYVEYYR HHHHCCCCCHHHHHH	35.16	22468782
283	N-linked_Glycosylation	APDTFILNVTEGQIS CCCEEEEEECCCCCC	33.57	UniProtKB CARBOHYD
424	Phosphorylation	FTTRNRDYDDIDDDD CCCCCCCCCCCCCCC	16.57	27642862
444	Phosphorylation	AWRMAAHSPPRGQLH HHHHHCCCCCCCCCC	31.69	30266825
494	Phosphorylation	LFGRNPRYENVPLIG HHCCCCCCCCCCCCC	17.08	24927040
504	Phosphorylation	VPLIGRASPPPTYSP CCCCCCCCCCCCCCH	36.26	30266825
508	Phosphorylation	GRASPPPTYSPSMRA CCCCCCCCCCHHHHH	42.26	29255136
509	Phosphorylation	RASPPPTYSPSMRAT CCCCCCCCCHHHHHE	25.10	27732954
510	Phosphorylation	ASPPPTYSPSMRATY CCCCCCCCHHHHHEE	16.99	27732954
512	Phosphorylation	PPPTYSPSMRATYLS CCCCCCHHHHHEEEH	18.24	27732954
516	Phosphorylation	YSPSMRATYLSVADE CCHHHHHEEEHHHHH	18.03	28796482
517	Phosphorylation	SPSMRATYLSVADEH CHHHHHEEEHHHHHH	8.94	20007894
519	Phosphorylation	SMRATYLSVADEHLR HHHHEEEHHHHHHHH	12.58	28796482
528	Phosphorylation	ADEHLRHYGNQFPA- HHHHHHHCCCCCCC-	16.02	27470641

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
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:18577513
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:18577513

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TTYH2_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 TTYH2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NEDD4_HUMAN	NEDD4	physical	18577513

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

"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 THR-199, AND MASSSPECTROMETRY.
PubMed: 17081983