dbPTM

PDE10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDE10_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	Q9Y233
Protein Name	cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Gene Name	PDE10A
Organism	Homo sapiens (Human).
Sequence Length	779
Subcellular Localization	Cytoplasm. Located mostly to soluble cellular fractions.
Protein Description	Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition..
Protein Sequence	MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MRIEERKSQHLTGLT CCHHHHHHHCCCCCC	29.11	20044836
11	S-palmitoylation	EERKSQHLTGLTDEK HHHHHHCCCCCCHHH	2.93	20610737
16 (in isoform 2)	Phosphorylation	-	59.78	10441464
88	Phosphorylation	YIEQRLDTGGDNQLL HHHHHHCCCCCCEEH	47.89	-
101	Phosphorylation	LLLYELSSIIKIATK EHHHHHHHHHHHHHH	40.74	24719451
115	Phosphorylation	KADGFALYFLGECNN HCCCEEEEEEEECCC	8.04	24043423
123	Phosphorylation	FLGECNNSLCIFTPP EEEECCCEEEEECCC	15.61	24043423
128	Phosphorylation	NNSLCIFTPPGIKEG CCEEEEECCCCCCCC	14.52	24043423
297	Ubiquitination	FQVDHKNKELYSDLF EEECCCCHHHHHHHC	54.63	-
300	Phosphorylation	DHKNKELYSDLFDIG CCCCHHHHHHHCCCC	10.96	26074081
301	Phosphorylation	HKNKELYSDLFDIGE CCCHHHHHHHCCCCC	40.22	26074081
325	Phosphorylation	KTKEIRFSIEKGIAG CCCEEEEEECCCCCC	21.71	24719451
363	Phosphorylation	VDLYTGYTTRNILCM CCCCCCCCCCCEEEE	22.18	-
395	Ubiquitination	ISGSAFSKTDENNFK HCCCCCCCCCCCHHH	54.25	-
490	Phosphorylation	MVHRSCGTSCFELEK EECCCCCCCHHHHHH	27.01	22210691
504	Phosphorylation	KLCRFIMSVKKNYRR HHHHHHHHHHHCCCC	26.43	24719451
639	Phosphorylation	RKQLEEMYQTGSLNL HHHHHHHHHHCCCCC	13.25	-
661	Phosphorylation	RVIGLMMTACDLCSV HHHHHHHHHHHHCCC	15.35	-
669	Phosphorylation	ACDLCSVTKLWPVTK HHHHCCCCCCEECCC	12.25	-
754	Ubiquitination	DNLSQWEKVIRGEET HCHHHHHHHHCCHHH	39.75	-
766	Phosphorylation	EETATWISSPSVAQK HHHCCCCCCHHHHHH	27.97	18691976
767	Phosphorylation	ETATWISSPSVAQKA HHCCCCCCHHHHHHH	16.44	17192257
769	Phosphorylation	ATWISSPSVAQKAAA CCCCCCHHHHHHHHH	31.84	26471730
777	Phosphorylation	VAQKAAASED----- HHHHHHHCCC-----	37.26	19369195

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
16	T	Phosphorylation	Kinase	PKACA	P00517	PSP
16	T	Phosphorylation	Kinase	PKACA	P17612	PSP
16	T	Phosphorylation	Kinase	PRKACA	P27791	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
16	T	Phosphorylation		10441464
[Isoform PDE10A2]: Phosphorylated on Thr-16.

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 PDE10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PDE10_HUMAN !!

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
DB00201	Caffeine
DB00975	Dipyridamole
DB01113	Papaverine
DB08811	Tofisopam
DB08814	Triflusal

Regulatory Network of PDE10_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-767, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-767, AND MASSSPECTROMETRY.	18691976 [Abstract]

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