dbPTM

DNPEP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNPEP_HUMAN
UniProt AC	Q9ULA0
Protein Name	Aspartyl aminopeptidase
Gene Name	DNPEP
Organism	Homo sapiens (Human).
Sequence Length	475
Subcellular Localization	Cytoplasm .
Protein Description	Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism..
Protein Sequence	MQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1 (in isoform 2)	Acetylation	-	6.98	22814378
1	Acetylation	-------MQVAMNGK -------CCCCCCHH	6.98	22814378
2	Phosphorylation	------MQVAMNGKA ------CCCCCCHHH	31.51	20068231
5	Phosphorylation	---MQVAMNGKARKE ---CCCCCCHHHHHH	7.74	20068231
16	Phosphorylation	ARKEAVQTAAKELLK HHHHHHHHHHHHHHH	23.22	-
19	Ubiquitination	EAVQTAAKELLKFVN HHHHHHHHHHHHHHH	46.56	21890473
19	Succinylation	EAVQTAAKELLKFVN HHHHHHHHHHHHHHH	46.56	23954790
23	Acetylation	TAAKELLKFVNRSPS HHHHHHHHHHHCCCC	60.95	25953088
28	Phosphorylation	LLKFVNRSPSPFHAV HHHHHHCCCCHHHHH	25.24	23312004
29	Ubiquitination	LKFVNRSPSPFHAVA HHHHHCCCCHHHHHH	42.66	-
30	Phosphorylation	KFVNRSPSPFHAVAE HHHHCCCCHHHHHHH	41.25	23312004
33	Ubiquitination	NRSPSPFHAVAECRN HCCCCHHHHHHHHHH	23.76	19608861
33	Acetylation	NRSPSPFHAVAECRN HCCCCHHHHHHHHHH	23.76	19608861
40	Phosphorylation	HAVAECRNRLLQAGF HHHHHHHHHHHHHCC	51.08	-
61	Ubiquitination	EKWNIKPESKYFMTR HHCCCCCHHHCEECC	55.66	-
62	Phosphorylation	KWNIKPESKYFMTRN HCCCCCHHHCEECCC	40.98	-
65	Ubiquitination	IKPESKYFMTRNSST CCCHHHCEECCCCCC	4.66	-
69	Ubiquitination	SKYFMTRNSSTIIAF HHCEECCCCCCEEEE	31.01	-
70	Phosphorylation	KYFMTRNSSTIIAFA HCEECCCCCCEEEEE	26.10	25332170
72	Phosphorylation	FMTRNSSTIIAFAVG EECCCCCCEEEEEEC	19.07	25332170
82	Phosphorylation	AFAVGGQYVPGNGFS EEEECCEECCCCCEE	16.34	18083107
143	Acetylation	LAGRVIVKCPTSGRL ECCEEEEECCCCCCH	24.31	25953088
153	Ubiquitination	TSGRLEQQLVHVERP CCCCHHHHEEEEECC	35.76	-
193	Phosphorylation	HLVPILATAIQEELE HHHHHHHHHHHHHHH	22.35	27251275
203	Phosphorylation	QEELEKGTPEPGPLN HHHHHCCCCCCCCCC	35.23	25849741
213	Phosphorylation	PGPLNAVDERHHSVL CCCCCCCCHHHHHHH	44.81	24275569
231	Phosphorylation	LCAHLGLSPKDIVEM HHHHCCCCHHHHHHH	28.27	24719451
296	Phosphorylation	EPHVRMVTLYDNEEV CCCEEEEEEECCCCC	15.40	-
327	S-nitrosylation	LRRISASCQHPTAFE HHHHHHHCCCCHHHH	4.27	22178444
355	Phosphorylation	AHAVHPNYLDKHEEN HHCCCCCCCHHCCCC	22.26	-
379	Ubiquitination	VIKVNSKQRYASNAV EEECCCCHHHHHHHH	43.36	-
383	Phosphorylation	NSKQRYASNAVSEAL CCCHHHHHHHHHHHH	19.18	27050516
393	Phosphorylation	VSEALIREVANKVKV HHHHHHHHHHHHCCC	38.70	24719451
399	Ubiquitination	REVANKVKVPLQDLM HHHHHHCCCCHHHHC	39.48	-
409	Ubiquitination	LQDLMVRNDTPCGTT HHHHCCCCCCCCCCC	46.20	-
417	Ubiquitination	DTPCGTTIGPILASR CCCCCCCHHHHHHHH	6.58	21906983
434	Phosphorylation	LRVLDLGSPQLAMHS CEEEECCCHHHHHHH	19.44	-

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
109	S	Phosphorylation	Kinase	PAK5	Q9P286	PSP

Functions of PTM Sites

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

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 DNPEP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATL4_HUMAN	ADAMTSL4	physical	16189514
K1H1_HUMAN	KRT31	physical	17353931
KRT36_HUMAN	KRT36	physical	17353931
KRT82_HUMAN	KRT82	physical	17353931
TBCD4_HUMAN	TBC1D4	physical	17353931
KIF4A_HUMAN	KIF4A	physical	17353931
KT33A_HUMAN	KRT33A	physical	17353931
UGPA_HUMAN	UGP2	physical	22939629
ANS1A_HUMAN	ANKS1A	physical	22863883
KCD12_HUMAN	KCTD12	physical	22863883
PLOD2_HUMAN	PLOD2	physical	22863883
PTN12_HUMAN	PTPN12	physical	22863883
TENS3_HUMAN	TNS3	physical	22863883
DNPEP_HUMAN	DNPEP	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
TPIS_HUMAN	TPI1	physical	26344197
SCAF8_HUMAN	SCAF8	physical	28514442
DNJC9_HUMAN	DNAJC9	physical	27173435
XRCC4_HUMAN	XRCC4	physical	27173435
KIF3A_HUMAN	KIF3A	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.

Regulatory Network of DNPEP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, AND MASS SPECTROMETRY.	19608861 [Abstract]