DPP6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPP6_HUMAN
• UniProt AC: P42658
• Protein Name: Dipeptidyl aminopeptidase-like protein 6
• Gene Name: DPP6
• Organism: Homo sapiens (Human).
• Sequence Length: 865
• Subcellular Localization: Cell membrane ; Single-pass type II membrane protein .
• Protein Description: Promotes cell surface expression of the potassium channel KCND2. [PubMed: 15454437]
• Protein Sequence: MASLYQRFTGKINTSRSFPAPPEASHLLGGQGPEEDGGAGAKPLGPRAQAAAPRERGGGGGGAGGRPRFQYQARSDGDEEDELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAEDNSLSQKKKVTVEDLFSEDFKIHDPEAKWISDTEFIYREQKGTVRLWNVETNTSTVLIEGKKIESLRAIRYEISPDREYALFSYNVEPIYQHSYTGYYVLSKIPHGDPQSLDPPEVSNAKLQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKTHIAHWWSPDGTRLAYAAINDSRVPIMELPTYTGSIYPTVKPYHYPKAGSENPSISLHVIGLNGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKKHEDESEAWLHRQNEEPVFSKDGRKFFFIRAIPQGGRGKFYHITVSSSQPNSSNDNIQSITSGDWDVTKILAYDEKGNKIYFLSTEDLPRRRQLYSANTVGNFNRQCLSCDLVENCTYFSASFSHSMDFFLLKCEGPGVPMVTVHNTTDKKKMFDLETNEHVKKAINDRQMPKVEYRDIEIDDYNLPMQILKPATFTDTTHYPLLLVVDGTPGSQSVAEKFEVSWETVMVSSHGAVVVKCDGRGSGFQGTKLLHEVRRRLGLLEEKDQMEAVRTMLKEQYIDRTRVAVFGKDYGGYLSTYILPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKVAHRVSALEEQQFLIIHPTADEKIHFQHTAELITQLIRGKANYSLQIYPDESHYFTSSSLKQHLYRSIINFFVECFRIQDKLLTVTAKEDEEED

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
2 (in isoform 2)	Phosphorylation	-	14.29	26471730
3 (in isoform 2)	Phosphorylation	-	26.72	26471730
8 (in isoform 2)	Phosphorylation	-	6.61	26471730
10 (in isoform 2)	Phosphorylation	-	26.57	26471730
13 (in isoform 2)	Phosphorylation	-	35.17	26471730
22	Phosphorylation	SRSFPAPPEASHLLG CCCCCCCCCHHHHCC	52.47	-
66	Methylation	GGGGAGGRPRFQYQA CCCCCCCCCCCEEEC	20.50	-
68	Methylation	GGAGGRPRFQYQARS CCCCCCCCCEEECCC	29.91	-
173	N-linked_Glycosylation	RLWNVETNTSTVLIE EEEEEECCCEEEEEC	20.66	15476821
186	Phosphorylation	IEGKKIESLRAIRYE ECCEEEEEEEEEEEE	26.99	24702127
195	Phosphorylation	RAIRYEISPDREYAL EEEEEEECCCCCEEE	14.60	24260401
238	Phosphorylation	SLDPPEVSNAKLQYA HCCCCCCCCCEEEEC	29.43	-
263	Phosphorylation	FIFENNIYYCAHVGK EEEECCEEEEEECCC	8.46	-
264	Phosphorylation	IFENNIYYCAHVGKQ EEECCEEEEEECCCC	4.56	-
277	Phosphorylation	KQAIRVVSTGKEGVI CCEEEEEECCCCCEE	28.69	-
278	Phosphorylation	QAIRVVSTGKEGVIY CEEEEEECCCCCEEE	40.43	-
300	Phosphorylation	YEEEILKTHIAHWWS CHHHHHHHHCCEEEC	18.31	26074081
307	Phosphorylation	THIAHWWSPDGTRLA HHCCEEECCCCCEEE	14.12	26074081
311	Phosphorylation	HWWSPDGTRLAYAAI EEECCCCCEEEEEEE	29.86	26074081
315	Phosphorylation	PDGTRLAYAAINDSR CCCCEEEEEEECCCC	10.93	26074081
319	N-linked_Glycosylation	RLAYAAINDSRVPIM EEEEEEECCCCCCEE	36.16	15476821
321	Phosphorylation	AYAAINDSRVPIMEL EEEEECCCCCCEEEC	30.59	26074081
332	Phosphorylation	IMELPTYTGSIYPTV EEECCCCCCCCCCCC	27.25	20049867
334	Phosphorylation	ELPTYTGSIYPTVKP ECCCCCCCCCCCCCC	15.91	20049867
338	Phosphorylation	YTGSIYPTVKPYHYP CCCCCCCCCCCCCCC	24.96	20049867
342	Phosphorylation	IYPTVKPYHYPKAGS CCCCCCCCCCCCCCC	14.31	20049867
349	Phosphorylation	YHYPKAGSENPSISL CCCCCCCCCCCCEEE	38.77	20049867
397	Phosphorylation	TSTKVAVTWLNRAQN CCCCHHHHHHHHCCC	17.94	19053533
404	N-linked_Glycosylation	TWLNRAQNVSILTLC HHHHHCCCEEEEEEE	28.63	15476821
406	Phosphorylation	LNRAQNVSILTLCDA HHHCCCEEEEEEEEC	21.30	19053533
419	Phosphorylation	DATTGVCTKKHEDES ECCCCCCCCCCCCCC	40.50	19053533
471	N-linked_Glycosylation	TVSSSQPNSSNDNIQ EEECCCCCCCCCCCC	50.89	UniProtKB CARBOHYD
535	N-linked_Glycosylation	LSCDLVENCTYFSAS HCCCCCCCCEEEEEE	18.89	15476821
566	N-linked_Glycosylation	VPMVTVHNTTDKKKM CCEEEEECCCCCCCC	40.10	15476821
671	Acetylation	GSGFQGTKLLHEVRR CCCCCHHHHHHHHHH	56.74	7823017
697	Acetylation	EAVRTMLKEQYIDRT HHHHHHHHHHHCCCE	31.76	22368373
791	Phosphorylation	FLIIHPTADEKIHFQ EEEECCCCCCCCCHH	27.67	-
793	Phosphorylation	IIHPTADEKIHFQHT EECCCCCCCCCHHHH	51.99	-
813	N-linked_Glycosylation	QLIRGKANYSLQIYP HHHHCCCCEEEEECC	30.34	15476821
815	O-linked_Glycosylation	IRGKANYSLQIYPDE HHCCCCEEEEECCCC	17.38	29351928
855	Phosphorylation	RIQDKLLTVTAKEDE CCCCEEEEEEECCCC	26.67	-
857	Phosphorylation	QDKLLTVTAKEDEEE CCEEEEEEECCCCCC	27.12	-

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

Oops, there are no upstream regulatory protein records of DPP6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPP6_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 DPP6_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of DPP6_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• 612956: Familial paroxysmal ventricular fibrillation 2 (VF2)
• 616311: Mental retardation, autosomal dominant 33 (MRD33)
• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structure of a human A-type potassium channel interacting proteinDPPX, a member of the dipeptidyl aminopeptidase family.";
Strop P., Bankovich A.J., Hansen K.C., Garcia K.C., Brunger A.T.;
J. Mol. Biol. 343:1055-1065(2004).
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 127-849, FUNCTION, SUBUNIT,DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-173; ASN-319; ASN-404;ASN-535; ASN-566 AND ASN-813.
PubMed: 15476821