dbPTM

ACPH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACPH_HUMAN
UniProt AC	P13798
Protein Name	Acylamino-acid-releasing enzyme
Gene Name	APEH
Organism	Homo sapiens (Human).
Sequence Length	732
Subcellular Localization	Cytoplasm.
Protein Description	This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser..
Protein Sequence	MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGQYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGGTGPGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDDEIARLKKPDQAIKGDQFVFYEDWGENMVSKSIPVLCVLDVESGNISVLEGVPENVSPGQAFWAPGDAGVVFVGWWHEPFRLGIRFCTNRRSALYYVDLIGGKCELLSDDSLAVSSPRLSPDQCRIVYLQYPSLIPHHQCSQLCLYDWYTKVTSVVVDVVPRQLGENFSGIYCSLLPLGCWSADSQRVVFDSAQRSRQDLFAVDTQVGTVTSLTAGGSGGSWKLLTIDQDLMVAQFSTPSLPPTLKVGFLPSAGKEQSVLWVSLEEAEPIPDIHWGIRVLQPPPEQENVQYAGLDFEAILLQPGSPPDKTQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVEQVLQEEHFDASHVALMGGSHGGFISCHLIGQYPETYRACVARNPVINIASMLGSTDIPDWCVVEAGFPFSSDCLPDLSVWAEMLDKSPIRYIPQVKTPLLLMLGQEDRRVPFKQGMEYYRALKTRNVPVRLLLYPKSTHALSEVEVESDSFMNAVLWLRTHLGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MERQVLLS -------CCCEECCC	9.63	10395453
2	Ubiquitination	------MERQVLLSE ------CCCEECCCC	52.39	22817900
7	Ubiquitination	-MERQVLLSEPEEAA -CCCEECCCCHHHHH	5.99	22817900
8	Phosphorylation	MERQVLLSEPEEAAA CCCEECCCCHHHHHH	47.12	-
17	Ubiquitination	PEEAAALYRGLSRQP HHHHHHHHHCCCCCC	9.63	22817900
25	Ubiquitination	RGLSRQPALSAACLG HCCCCCCCHHHHHHC	13.05	22817900
27	Phosphorylation	LSRQPALSAACLGPE CCCCCCHHHHHHCCC	18.87	21406692
28	Ubiquitination	SRQPALSAACLGPEV CCCCCHHHHHHCCCE	11.75	22817900
30	Ubiquitination	QPALSAACLGPEVTT CCCHHHHHHCCCEEE	4.52	21890473
36	Phosphorylation	ACLGPEVTTQYGGQY HHHCCCEEECCCCEE	13.40	21406692
37	Phosphorylation	CLGPEVTTQYGGQYR HHCCCEEECCCCEEE	25.60	21406692
39	Phosphorylation	GPEVTTQYGGQYRTV CCCEEECCCCEEEEE	22.56	21406692
43	Phosphorylation	TTQYGGQYRTVHTEW EECCCCEEEEEECCC	16.13	21406692
45	Phosphorylation	QYGGQYRTVHTEWTQ CCCCEEEEEECCCCH	16.23	26437602
51	Phosphorylation	RTVHTEWTQRDLERM EEEECCCCHHHHHHH	13.90	26437602
79	Ubiquitination	DGDSVVFAGPAGNSV CCCEEEEEECCCCCC	16.08	27667366
94	Ubiquitination	ETRGELLSRESPSGT CCCHHHHHCCCCCCC	46.77	21963094
94	Phosphorylation	ETRGELLSRESPSGT CCCHHHHHCCCCCCC	46.77	24719451
95	Ubiquitination	TRGELLSRESPSGTM CCHHHHHCCCCCCCH	48.67	22817900
96	Ubiquitination	RGELLSRESPSGTMK CHHHHHCCCCCCCHH	64.72	21963094
101	Ubiquitination	SRESPSGTMKAVLRK HCCCCCCCHHHHHHH	21.60	21963094
103	Ubiquitination	ESPSGTMKAVLRKAG CCCCCCHHHHHHHCC	34.87	22817900
108	Ubiquitination	TMKAVLRKAGGTGPG CHHHHHHHCCCCCCC	47.42	21906983
118	Ubiquitination	GTGPGEEKQFLEVWE CCCCCHHHHHHHHHH	41.89	21906983
126	Ubiquitination	QFLEVWEKNRKLKSF HHHHHHHHCCCCHHC	46.47	22817900
129	Ubiquitination	EVWEKNRKLKSFNLS HHHHHCCCCHHCCHH	70.43	22817900
131	Ubiquitination	WEKNRKLKSFNLSAL HHHCCCCHHCCHHHH	56.91	21906983
132	Phosphorylation	EKNRKLKSFNLSALE HHCCCCHHCCHHHHH	29.78	21712546
136	Ubiquitination	KLKSFNLSALEKHGP CCHHCCHHHHHHHCC	31.73	22817900
136	Phosphorylation	KLKSFNLSALEKHGP CCHHCCHHHHHHHCC	31.73	21712546
144	Ubiquitination	ALEKHGPVYEDDCFG HHHHHCCCCCCCCCC	10.93	21963094
146	Ubiquitination	EKHGPVYEDDCFGCL HHHCCCCCCCCCCCC	47.83	22817900
148	Ubiquitination	HGPVYEDDCFGCLSW HCCCCCCCCCCCCCC	20.08	22817900
153	Ubiquitination	EDDCFGCLSWSHSET CCCCCCCCCCCCCCE	6.34	22817900
154	Ubiquitination	DDCFGCLSWSHSETH CCCCCCCCCCCCCEE	30.52	22817900
157	Ubiquitination	FGCLSWSHSETHLLY CCCCCCCCCCEEEEE	24.32	22817900
159	Ubiquitination	CLSWSHSETHLLYVA CCCCCCCCEEEEEEE	34.52	21890473
163	Ubiquitination	SHSETHLLYVAEKKR CCCCEEEEEEEECCC	2.22	22817900
171	Ubiquitination	YVAEKKRPKAESFFQ EEEECCCCCCHHHHC	49.43	22817900
172	Ubiquitination	VAEKKRPKAESFFQT EEECCCCCCHHHHCC	69.67	29967540
174	Ubiquitination	EKKRPKAESFFQTKA ECCCCCCHHHHCCCC	54.96	22817900
175	Phosphorylation	KKRPKAESFFQTKAL CCCCCCHHHHCCCCC	35.90	28555341
176	Ubiquitination	KRPKAESFFQTKALD CCCCCHHHHCCCCCC	3.86	21890473
180	Ubiquitination	AESFFQTKALDVSAS CHHHHCCCCCCCCCC	35.85	21906983
185	Phosphorylation	QTKALDVSASDDEIA CCCCCCCCCCHHHHH	23.01	29255136
187	Phosphorylation	KALDVSASDDEIARL CCCCCCCCHHHHHHC	37.78	19664994
190	Ubiquitination	DVSASDDEIARLKKP CCCCCHHHHHHCCCC	43.47	21963094
195	Ubiquitination	DDEIARLKKPDQAIK HHHHHHCCCCCCCCC	57.62	21906983
196	Ubiquitination	DEIARLKKPDQAIKG HHHHHCCCCCCCCCC	59.42	22817900
202	Ubiquitination	KKPDQAIKGDQFVFY CCCCCCCCCCEEEEE	60.49	21963094
208	Ubiquitination	IKGDQFVFYEDWGEN CCCCEEEEECCCCCC	6.12	27667366
209	Phosphorylation	KGDQFVFYEDWGENM CCCEEEEECCCCCCC	14.00	-
223	Ubiquitination	MVSKSIPVLCVLDVE CCCCCCCEEEEEECC	6.53	21963094
224	Ubiquitination	VSKSIPVLCVLDVES CCCCCCEEEEEECCC	1.08	22817900
225	Ubiquitination	SKSIPVLCVLDVESG CCCCCEEEEEECCCC	2.66	27667366
230	Ubiquitination	VLCVLDVESGNISVL EEEEEECCCCCEEEE	53.23	21963094
240	Ubiquitination	NISVLEGVPENVSPG CEEEEECCCCCCCCC	3.82	21963094
241	Ubiquitination	ISVLEGVPENVSPGQ EEEEECCCCCCCCCC	38.00	22817900
245	Ubiquitination	EGVPENVSPGQAFWA ECCCCCCCCCCCEEC	34.59	21963094
247	Ubiquitination	VPENVSPGQAFWAPG CCCCCCCCCCEECCC	24.76	21963094
276	Phosphorylation	RLGIRFCTNRRSALY CCCEEECCCCCCEEE	29.11	24719451
280	Phosphorylation	RFCTNRRSALYYVDL EECCCCCCEEEEEEC	21.27	21712546
283	Phosphorylation	TNRRSALYYVDLIGG CCCCCEEEEEECCCC	10.93	24719451
290	Ubiquitination	YYVDLIGGKCELLSD EEEECCCCEEEECCC	25.17	21963094
291	Ubiquitination	YVDLIGGKCELLSDD EEECCCCEEEECCCC	21.23	21963094
296	Phosphorylation	GGKCELLSDDSLAVS CCEEEECCCCCCCCC	52.58	25332170
299	Phosphorylation	CELLSDDSLAVSSPR EEECCCCCCCCCCCC	24.18	30576142
303	Phosphorylation	SDDSLAVSSPRLSPD CCCCCCCCCCCCCHH	29.08	25332170
308	Phosphorylation	AVSSPRLSPDQCRIV CCCCCCCCHHHEEEE	27.92	30576142
319	Ubiquitination	CRIVYLQYPSLIPHH EEEEEEECCCCCCHH	7.68	21963094
336	Ubiquitination	SQLCLYDWYTKVTSV HHHHHHHHHHCCEEE	6.80	21963094
434	Ubiquitination	PSLPPTLKVGFLPSA CCCCCCEEEEECCCC	42.67	29967540
440	Phosphorylation	LKVGFLPSAGKEQSV EEEEECCCCCCCEEE	52.37	26437602
469	Ubiquitination	HWGIRVLQPPPEQEN CEEEEECCCCCCCCC	45.67	21963094
486	Ubiquitination	YAGLDFEAILLQPGS ECCCCEEEEEECCCC	9.56	23000965
493	Phosphorylation	AILLQPGSPPDKTQV EEEECCCCCCCCCCC	39.69	22468782
516	Phosphorylation	GPHSSFVTAWMLFPA CCCCHHHHHHHHHHH	16.76	23879269
517	Ubiquitination	PHSSFVTAWMLFPAM CCCHHHHHHHHHHHH	5.60	21963094
534	Ubiquitination	KMGFAVLLVNYRGST HHCCEEEEEECCCCC	1.56	23000965
563	Ubiquitination	GHQDVKDVQFAVEQV CCCCHHHHHHHHHHH	4.12	21963094
580	Ubiquitination	EEHFDASHVALMGGS HHCCCHHEEEECCCC	15.58	23000965
618	Ubiquitination	NPVINIASMLGSTDI CCCEEHHHHHCCCCC	15.67	21963094
635	Ubiquitination	WCVVEAGFPFSSDCL CEEEECCCCCCCCCC	7.71	23000965
663	Ubiquitination	PIRYIPQVKTPLLLM CCCCCCCCCCCEEEE	6.64	21963094
664	Ubiquitination	IRYIPQVKTPLLLML CCCCCCCCCCEEEEC	38.90	21906983
665	Phosphorylation	RYIPQVKTPLLLMLG CCCCCCCCCEEEECC	21.95	21712546
670	Sulfoxidation	VKTPLLLMLGQEDRR CCCCEEEECCCCCCC	3.89	21406390
676	Methylation	LMLGQEDRRVPFKQG EECCCCCCCCCHHHH	40.52	-
680	Ubiquitination	QEDRRVPFKQGMEYY CCCCCCCHHHHHHHH	9.38	23000965
681	Ubiquitination	EDRRVPFKQGMEYYR CCCCCCHHHHHHHHH	39.61	23000965
681	Methylation	EDRRVPFKQGMEYYR CCCCCCHHHHHHHHH	39.61	-
692	Phosphorylation	EYYRALKTRNVPVRL HHHHHHHHCCCCEEE	28.46	-
692	Ubiquitination	EYYRALKTRNVPVRL HHHHHHHHCCCCEEE	28.46	21963094
709	Ubiquitination	YPKSTHALSEVEVES CCCCCCCCCEEEECC	3.30	23000965
726	Ubiquitination	FMNAVLWLRTHLGS- HHHHHHHHHHHCCC-	3.86	23000965

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACPH_HUMAN	APEH	physical	16189514
UBA5_HUMAN	UBA5	physical	16189514
IST1_HUMAN	IST1	physical	16189514
PPCEL_HUMAN	PREPL	physical	22939629
CAND1_HUMAN	CAND1	physical	22863883
SRC8_HUMAN	CTTN	physical	22863883
SYCC_HUMAN	CARS	physical	22863883
GARS_HUMAN	GARS	physical	22863883
H12_HUMAN	HIST1H1C	physical	22863883
HS74L_HUMAN	HSPA4L	physical	22863883
IPO7_HUMAN	IPO7	physical	22863883
SYK_HUMAN	KARS	physical	22863883
LAMP2_HUMAN	LAMP2	physical	22863883
NMI_HUMAN	NMI	physical	22863883
PPM1G_HUMAN	PPM1G	physical	22863883
GDN_HUMAN	SERPINE2	physical	22863883
SNX6_HUMAN	SNX6	physical	22863883
ZYX_HUMAN	ZYX	physical	22863883
ACPH_HUMAN	APEH	physical	25416956
LEG8_HUMAN	LGALS8	physical	25416956
IST1_HUMAN	IST1	physical	25416956
CNOT7_HUMAN	CNOT7	physical	26344197
SNUT2_HUMAN	USP39	physical	26344197

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 ACPH_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Structural investigations on human erythrocyte acylpeptide hydrolaseby mass spectrometric procedures."; Scaloni A., Ingallinella P., Andolfo A., Jones W., Marino G.,Manning J.M.; J. Protein Chem. 18:349-360(1999). Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND ACETYLATION AT MET-1.	10395453 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND MASSSPECTROMETRY.	18669648 [Abstract]