DPYL5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPYL5_HUMAN
• UniProt AC: Q9BPU6
• Protein Name: Dihydropyrimidinase-related protein 5
• Gene Name: DPYSL5
• Organism: Homo sapiens (Human).
• Sequence Length: 564
• Subcellular Localization: Cytoplasm .
• Protein Description: May have a function in neuronal differentiation and/or axon growth..
• Protein Sequence: MLANSASVRILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAALVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITWWAPKVKAEMETLVREKGVNSFQMFMTYKDLYMLRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHATLTGLHYYHQDWSHAAAYVTVPPLRLDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCPLRSFPDTVYKKLVQREKTLKVRGVDRTPYLGDVAVVVHPGKKEMGTPLADTPTRPVTRHGGMRDLHESSFSLSGSQIDDHVPKRASARILAPPGGRSSGIW

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
5	Phosphorylation	---MLANSASVRILI ---CCCCCCEEEEEE	19.13	28634298
7	Phosphorylation	-MLANSASVRILIKG -CCCCCCEEEEEEEC	16.26	28634298
49	Ubiquitination	LMIPGGAKVIDATGK EEECCCCEEEECCCC	42.89	30230243
163	Phosphorylation	SFQMFMTYKDLYMLR CEEEEEEHHHHHCCC	7.24	-
167	Phosphorylation	FMTYKDLYMLRDSEL EEEHHHHHCCCHHHH	12.30	-
172	Phosphorylation	DLYMLRDSELYQVLH HHHCCCHHHHHHHHH	24.06	24076635
343	Methylation	MGKEDFTKIPHGVSG CCCCCHHCCCCCCCC	54.99	-
343	"N6,N6-dimethyllysine"	MGKEDFTKIPHGVSG CCCCCHHCCCCCCCC	54.99	-
361	Methylation	RMSVIWERGVVGGKM HHHHHHHCCCCCCCC	28.36	-
383	Ubiquitination	VTSSNAAKLLNLYPR EECCCHHHHHCCCCC	51.61	30230243
388	Phosphorylation	AAKLLNLYPRKGRII HHHHHCCCCCCCCCC	10.42	-
481	Phosphorylation	KLVQREKTLKVRGVD HHHHCCCCCCCCCCC	27.36	-
490	Phosphorylation	KVRGVDRTPYLGDVA CCCCCCCCCCCCCEE	16.30	29214152
504	Ubiquitination	AVVVHPGKKEMGTPL EEEECCCCCCCCCCC	50.43	32142685
505	Ubiquitination	VVVHPGKKEMGTPLA EEECCCCCCCCCCCC	59.87	30230243
509	Phosphorylation	PGKKEMGTPLADTPT CCCCCCCCCCCCCCC	17.51	21712546
514	Phosphorylation	MGTPLADTPTRPVTR CCCCCCCCCCCCCCC	22.43	21712546
516	Phosphorylation	TPLADTPTRPVTRHG CCCCCCCCCCCCCCC	50.09	29396449
520	Phosphorylation	DTPTRPVTRHGGMRD CCCCCCCCCCCCCCC	21.45	29496963
531	Phosphorylation	GMRDLHESSFSLSGS CCCCCCCCCEECCCC	26.40	24117733
532	Phosphorylation	MRDLHESSFSLSGSQ CCCCCCCCEECCCCC	18.83	25307156
534	Phosphorylation	DLHESSFSLSGSQID CCCCCCEECCCCCCC	24.47	21712546
536	Phosphorylation	HESSFSLSGSQIDDH CCCCEECCCCCCCCC	34.89	29978859
538	Phosphorylation	SSFSLSGSQIDDHVP CCEECCCCCCCCCCC	22.16	29978859
549	Phosphorylation	DHVPKRASARILAPP CCCCCCCCCEEECCC	23.32	24719451
559	Methylation	ILAPPGGRSSGIW-- EECCCCCCCCCCC--	33.30	-
560	Phosphorylation	LAPPGGRSSGIW--- ECCCCCCCCCCC---	35.87	22496350
561	Phosphorylation	APPGGRSSGIW---- CCCCCCCCCCC----	32.70	24117733

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
516	T	Phosphorylation	Kinase	GSK3B	P49841	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPYL5_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 DPYL5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBB5_BOVIN	TUBB	physical	12134159
DPYL3_HUMAN	DPYSL3	physical	28514442
DPYL4_HUMAN	DPYSL4	physical	28514442
DPYL2_HUMAN	DPYSL2	physical	28514442
SHIP2_HUMAN	INPPL1	physical	28514442
LONF2_HUMAN	LONRF2	physical	28514442
CF161_HUMAN	C15orf26	physical	27173435

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 proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509; THR-514; THR-516AND SER-534, AND MASS SPECTROMETRY.
PubMed: 17287340