dbPTM

PCNP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCNP_HUMAN
UniProt AC	Q8WW12
Protein Name	PEST proteolytic signal-containing nuclear protein
Gene Name	PCNP
Organism	Homo sapiens (Human).
Sequence Length	178
Subcellular Localization	Nucleus .
Protein Description	May be involved in cell cycle regulation..
Protein Sequence	MADGKAGDEKPEKSQRAGAAGGPEEEAEKPVKTKTVSSSNGGESSSRSAEKRSAEEEAADLPTKPTKISKFGFAIGSQTTKKASAISIKLGSSKPKETVPTLAPKTLSVAAAFNEDEDSEPEEMPPEAKMRMKNIGRDTPTSAGPNSFNKGKHGFSDNQKLWERNIKSHLGNVHDQDN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADGKAGDE ------CCCCCCCCC	33.97	20154145
5	Acetylation	---MADGKAGDEKPE ---CCCCCCCCCCCH	50.14	22424773
10	Ubiquitination	DGKAGDEKPEKSQRA CCCCCCCCCHHHHHC	64.32	24816145
14	Phosphorylation	GDEKPEKSQRAGAAG CCCCCHHHHHCCCCC	24.20	-
16	Methylation	EKPEKSQRAGAAGGP CCCHHHHHCCCCCCC	41.92	115486695
29	Acetylation	GPEEEAEKPVKTKTV CCHHHHCCCCCCCEE	63.26	23954790
29	Ubiquitination	GPEEEAEKPVKTKTV CCHHHHCCCCCCCEE	63.26	33845483
32	Ubiquitination	EEAEKPVKTKTVSSS HHHCCCCCCCEEECC	53.48	24816145
32	Acetylation	EEAEKPVKTKTVSSS HHHCCCCCCCEEECC	53.48	25953088
35	Phosphorylation	EKPVKTKTVSSSNGG CCCCCCCEEECCCCC	30.74	22468782
37	Phosphorylation	PVKTKTVSSSNGGES CCCCCEEECCCCCCC	33.03	26657352
38	Phosphorylation	VKTKTVSSSNGGESS CCCCEEECCCCCCCC	24.40	26657352
39	Phosphorylation	KTKTVSSSNGGESSS CCCEEECCCCCCCCC	31.80	22468782
44	Ubiquitination	SSSNGGESSSRSAEK ECCCCCCCCCCHHHH	36.57	33845483
44	Phosphorylation	SSSNGGESSSRSAEK ECCCCCCCCCCHHHH	36.57	28102081
45	Phosphorylation	SSNGGESSSRSAEKR CCCCCCCCCCHHHHH	26.01	30576142
46	Phosphorylation	SNGGESSSRSAEKRS CCCCCCCCCHHHHHH	39.26	24719451
47	Ubiquitination	NGGESSSRSAEKRSA CCCCCCCCHHHHHHH	41.66	32015554
48	Phosphorylation	GGESSSRSAEKRSAE CCCCCCCHHHHHHHH	42.60	26657352
53	Phosphorylation	SRSAEKRSAEEEAAD CCHHHHHHHHHHHCC	51.61	29255136
63	Phosphorylation	EEAADLPTKPTKISK HHHCCCCCCCCEEHH	57.88	20071362
64	Ubiquitination	EAADLPTKPTKISKF HHCCCCCCCCEEHHC	49.07	33845483
64	Acetylation	EAADLPTKPTKISKF HHCCCCCCCCEEHHC	49.07	19608861
64	Malonylation	EAADLPTKPTKISKF HHCCCCCCCCEEHHC	49.07	26320211
66	Phosphorylation	ADLPTKPTKISKFGF CCCCCCCCEEHHCCE	42.43	25159151
66	O-linked_Glycosylation	ADLPTKPTKISKFGF CCCCCCCCEEHHCCE	42.43	OGP
67	Ubiquitination	DLPTKPTKISKFGFA CCCCCCCEEHHCCEE	54.21	32015554
67	Acetylation	DLPTKPTKISKFGFA CCCCCCCEEHHCCEE	54.21	21466224
69	Phosphorylation	PTKPTKISKFGFAIG CCCCCEEHHCCEECC	24.40	20068231
69	Ubiquitination	PTKPTKISKFGFAIG CCCCCEEHHCCEECC	24.40	33845483
70	Methylation	TKPTKISKFGFAIGS CCCCEEHHCCEECCC	53.64	90767
70	Acetylation	TKPTKISKFGFAIGS CCCCEEHHCCEECCC	53.64	25953088
76	Ubiquitination	SKFGFAIGSQTTKKA HHCCEECCCCCCCCE	15.40	33845483
77	O-linked_Glycosylation	KFGFAIGSQTTKKAS HCCEECCCCCCCCEE	20.45	OGP
77	Phosphorylation	KFGFAIGSQTTKKAS HCCEECCCCCCCCEE	20.45	23401153
79	O-linked_Glycosylation	GFAIGSQTTKKASAI CEECCCCCCCCEEEE	42.13	OGP
79	Phosphorylation	GFAIGSQTTKKASAI CEECCCCCCCCEEEE	42.13	25159151
80	O-linked_Glycosylation	FAIGSQTTKKASAIS EECCCCCCCCEEEEE	23.94	OGP
80	Phosphorylation	FAIGSQTTKKASAIS EECCCCCCCCEEEEE	23.94	25159151
81	Acetylation	AIGSQTTKKASAISI ECCCCCCCCEEEEEE	50.13	25953088
82	Ubiquitination	IGSQTTKKASAISIK CCCCCCCCEEEEEEE	45.54	29967540
84	O-linked_Glycosylation	SQTTKKASAISIKLG CCCCCCEEEEEEECC	34.71	30059200
84	Phosphorylation	SQTTKKASAISIKLG CCCCCCEEEEEEECC	34.71	30266825
86	Phosphorylation	TTKKASAISIKLGSS CCCCEEEEEEECCCC	3.97	32142685
87	Phosphorylation	TKKASAISIKLGSSK CCCEEEEEEECCCCC	17.25	23401153
89	Ubiquitination	KASAISIKLGSSKPK CEEEEEEECCCCCCC	39.75	33845483
89	Acetylation	KASAISIKLGSSKPK CEEEEEEECCCCCCC	39.75	25953088
92	Phosphorylation	AISIKLGSSKPKETV EEEEECCCCCCCCCC	45.70	-
94	Acetylation	SIKLGSSKPKETVPT EEECCCCCCCCCCCC	62.90	25953088
96	Ubiquitination	KLGSSKPKETVPTLA ECCCCCCCCCCCCCC	70.52	33845483
98	Phosphorylation	GSSKPKETVPTLAPK CCCCCCCCCCCCCCC	37.60	20068231
99	Phosphorylation	SSKPKETVPTLAPKT CCCCCCCCCCCCCCC	3.41	32142685
101	O-linked_Glycosylation	KPKETVPTLAPKTLS CCCCCCCCCCCCCHH	31.08	30059200
101	Phosphorylation	KPKETVPTLAPKTLS CCCCCCCCCCCCCHH	31.08	20068231
106	Phosphorylation	VPTLAPKTLSVAAAF CCCCCCCCHHHHHHH	24.17	30278072
108	Phosphorylation	TLAPKTLSVAAAFNE CCCCCCHHHHHHHCC	18.23	29255136
108 (in isoform 2)	Phosphorylation	-	18.23	19053533
114	Phosphorylation	LSVAAAFNEDEDSEP HHHHHHHCCCCCCCC	51.59	32142685
117	Ubiquitination	AAAFNEDEDSEPEEM HHHHCCCCCCCCCCC	58.20	32015554
118	Phosphorylation	AAFNEDEDSEPEEMP HHHCCCCCCCCCCCC	71.30	32142685
119	Ubiquitination	AFNEDEDSEPEEMPP HHCCCCCCCCCCCCH	53.67	29967540
119	Phosphorylation	AFNEDEDSEPEEMPP HHCCCCCCCCCCCCH	53.67	19664994
120 (in isoform 2)	Phosphorylation	-	69.88	19053533
121 (in isoform 2)	Phosphorylation	-	46.96	19053533
125	Ubiquitination	DSEPEEMPPEAKMRM CCCCCCCCHHHHHHH	27.19	32015554
127	Ubiquitination	EPEEMPPEAKMRMKN CCCCCCHHHHHHHHH	55.86	32015554
130	Ubiquitination	EMPPEAKMRMKNIGR CCCHHHHHHHHHCCC	6.97	32142685
133	Methylation	PEAKMRMKNIGRDTP HHHHHHHHHCCCCCC	34.74	116253289
134	Ubiquitination	EAKMRMKNIGRDTPT HHHHHHHHCCCCCCC	32.38	29967540
135	Ubiquitination	AKMRMKNIGRDTPTS HHHHHHHCCCCCCCC	3.90	32015554
138	Phosphorylation	RMKNIGRDTPTSAGP HHHHCCCCCCCCCCC	52.39	32142685
139	Phosphorylation	MKNIGRDTPTSAGPN HHHCCCCCCCCCCCC	27.40	29255136
140	Ubiquitination	KNIGRDTPTSAGPNS HHCCCCCCCCCCCCC	28.75	32015554
141	Phosphorylation	NIGRDTPTSAGPNSF HCCCCCCCCCCCCCC	33.05	22167270
142	O-linked_Glycosylation	IGRDTPTSAGPNSFN CCCCCCCCCCCCCCC	32.22	30059200
142	Ubiquitination	IGRDTPTSAGPNSFN CCCCCCCCCCCCCCC	32.22	29967540
142	Phosphorylation	IGRDTPTSAGPNSFN CCCCCCCCCCCCCCC	32.22	30266825
147	Phosphorylation	PTSAGPNSFNKGKHG CCCCCCCCCCCCCCC	33.07	29255136
149	Ubiquitination	SAGPNSFNKGKHGFS CCCCCCCCCCCCCCC	52.57	32015554
150	Ubiquitination	AGPNSFNKGKHGFSD CCCCCCCCCCCCCCC	68.29	32015554
150	Acetylation	AGPNSFNKGKHGFSD CCCCCCCCCCCCCCC	68.29	19608861
150	Methylation	AGPNSFNKGKHGFSD CCCCCCCCCCCCCCC	68.29	19608861
151	Ubiquitination	GPNSFNKGKHGFSDN CCCCCCCCCCCCCCH	28.44	29967540
152	Ubiquitination	PNSFNKGKHGFSDNQ CCCCCCCCCCCCCHH	42.01	19608861
152	Methylation	PNSFNKGKHGFSDNQ CCCCCCCCCCCCCHH	42.01	19608861
152	Acetylation	PNSFNKGKHGFSDNQ CCCCCCCCCCCCCHH	42.01	19608861
156	Phosphorylation	NKGKHGFSDNQKLWE CCCCCCCCCHHHHHH	40.00	30576142
159	Ubiquitination	KHGFSDNQKLWERNI CCCCCCHHHHHHHHH	47.40	32015554
160	Ubiquitination	HGFSDNQKLWERNIK CCCCCHHHHHHHHHH	62.92	32015554
160	Acetylation	HGFSDNQKLWERNIK CCCCCHHHHHHHHHH	62.92	25953088
166	Ubiquitination	QKLWERNIKSHLGNV HHHHHHHHHHHHCCC	6.40	29967540
167	Ubiquitination	KLWERNIKSHLGNVH HHHHHHHHHHHCCCC	35.06	29967540
167	Acetylation	KLWERNIKSHLGNVH HHHHHHHHHHHCCCC	35.06	25953088

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
-	K	Ubiquitination	E3 ubiquitin ligase	UHRF2	Q96PU4	PMID:14741369

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
UHRF2_HUMAN	UHRF2	physical	14741369

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 PCNP_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-64; LYS-150 AND LYS-152, ANDMASS SPECTROMETRY.	19608861 [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-119 AND SER-147, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.	19413330 [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-87; SER-119 AND THR-139,AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-66; SER-69; SER-77;THR-139; SER-142 AND SER-147, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND MASSSPECTROMETRY.	17924679 [Abstract]