dbPTM

CN37_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CN37_HUMAN
UniProt AC	P09543
Protein Name	2',3'-cyclic-nucleotide 3'-phosphodiesterase
Gene Name	CNP
Organism	Homo sapiens (Human).
Sequence Length	421
Subcellular Localization	Membrane Lipid-anchor. Melanosome. Firmly bound to membrane structures of brain white matter. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin..
Protein Sequence	MNRGFSRKSHTFLPKIFFRKMSSSGAKDKPELQFPFLQDEDTVATLLECKTLFILRGLPGSGKSTLARVIVDKYRDGTKMVSADAYKITPGARGAFSEEYKRLDEDLAAYCRRRDIRILVLDDTNHERERLEQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRQFVPGDEPREKMDLVTYFGKRPPGVLHCTTKFCDYGKAPGAEEYAQQDVLKKSYSKAFTLTISALFVTPKTTGARVELSEQQLQLWPSDVDKLSPTDNLPRGSRAHITLGCAADVEAVQTGLDLLEILRQEKGGSRGEEVGELSRGKLYSLGNGRWMLTLAKNMEVRAIFTGYYGKGKPVPTQGSRKGGALQSCTII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MNRGFSRKSHTFL --CCCCCCCCCCCHH	41.44	23403867
8	Ubiquitination	MNRGFSRKSHTFLPK CCCCCCCCCCCHHHH	45.45	-
9	Phosphorylation	NRGFSRKSHTFLPKI CCCCCCCCCCHHHHH	27.01	22617229
11	Phosphorylation	GFSRKSHTFLPKIFF CCCCCCCCHHHHHHH	33.68	23403867
15	Ubiquitination	KSHTFLPKIFFRKMS CCCCHHHHHHHHHCC	55.05	21890473
15 (in isoform 1)	Ubiquitination	-	55.05	21890473
22	Phosphorylation	KIFFRKMSSSGAKDK HHHHHHCCCCCCCCC	25.12	26657352
23	Phosphorylation	IFFRKMSSSGAKDKP HHHHHCCCCCCCCCC	29.32	28464451
24	Phosphorylation	FFRKMSSSGAKDKPE HHHHCCCCCCCCCCC	35.15	28464451
27	Methylation	KMSSSGAKDKPELQF HCCCCCCCCCCCCCC	70.57	12692561
29	Methylation	SSSGAKDKPELQFPF CCCCCCCCCCCCCCC	39.42	12692561
29	Ubiquitination	SSSGAKDKPELQFPF CCCCCCCCCCCCCCC	39.42	-
42	Phosphorylation	PFLQDEDTVATLLEC CCCCCHHHHHHHHHC	15.25	26552605
49	Glutathionylation	TVATLLECKTLFILR HHHHHHHCCEEEHHC	4.04	22555962
51	Phosphorylation	ATLLECKTLFILRGL HHHHHCCEEEHHCCC	38.26	23882029
53 (in isoform 2)	Ubiquitination	-	6.30	21890473
63	Ubiquitination	RGLPGSGKSTLARVI CCCCCCCCHHHHHHH	41.80	-
64	Phosphorylation	GLPGSGKSTLARVIV CCCCCCCHHHHHHHH	31.98	24076635
65	Phosphorylation	LPGSGKSTLARVIVD CCCCCCHHHHHHHHH	28.11	25332170
67 (in isoform 2)	Ubiquitination	-	12.09	21890473
73	Ubiquitination	LARVIVDKYRDGTKM HHHHHHHCCCCCCEE	31.15	21890473
73 (in isoform 1)	Ubiquitination	-	31.15	21890473
79	Acetylation	DKYRDGTKMVSADAY HCCCCCCEEEECEEE	42.72	25953088
79	Malonylation	DKYRDGTKMVSADAY HCCCCCCEEEECEEE	42.72	26320211
79	Ubiquitination	DKYRDGTKMVSADAY HCCCCCCEEEECEEE	42.72	-
81 (in isoform 2)	Ubiquitination	-	4.56	21890473
82	Phosphorylation	RDGTKMVSADAYKIT CCCCEEEECEEEECC	19.55	28258704
86	Phosphorylation	KMVSADAYKITPGAR EEEECEEEECCCCCC	11.94	21253578
87	Ubiquitination	MVSADAYKITPGARG EEECEEEECCCCCCC	41.65	21890473
87 (in isoform 1)	Ubiquitination	-	41.65	21890473
89	Phosphorylation	SADAYKITPGARGAF ECEEEECCCCCCCCC	16.12	20049867
97	Phosphorylation	PGARGAFSEEYKRLD CCCCCCCCHHHHHCC	29.05	25332170
100	Phosphorylation	RGAFSEEYKRLDEDL CCCCCHHHHHCCHHH	9.43	21253578
101	Ubiquitination	GAFSEEYKRLDEDLA CCCCHHHHHCCHHHH	50.17	21890473
101 (in isoform 1)	Ubiquitination	-	50.17	21890473
110	Phosphorylation	LDEDLAAYCRRRDIR CCHHHHHHHHHCCCE	4.85	20007894
124	Phosphorylation	RILVLDDTNHERERL EEEEECCCCHHHHHH	37.83	25332170
141	Phosphorylation	LFEMADQYQYQVVLV HHHHHHHCCEEEEEE	15.10	-
155 (in isoform 2)	Ubiquitination	-	20.41	21890473
162	Acetylation	RLDCAQLKEKNQWQL EECHHHHHHHCCEEC	55.34	25953088
162	Malonylation	RLDCAQLKEKNQWQL EECHHHHHHHCCEEC	55.34	26320211
162	Ubiquitination	RLDCAQLKEKNQWQL EECHHHHHHHCCEEC	55.34	-
164	Ubiquitination	DCAQLKEKNQWQLSA CHHHHHHHCCEECCH	53.50	-
170	Phosphorylation	EKNQWQLSADDLKKL HHCCEECCHHHHHHH	17.98	19664994
175	2-Hydroxyisobutyrylation	QLSADDLKKLKPGLE ECCHHHHHHHCCCCC	64.15	-
175	Acetylation	QLSADDLKKLKPGLE ECCHHHHHHHCCCCC	64.15	23236377
175	Malonylation	QLSADDLKKLKPGLE ECCHHHHHHHCCCCC	64.15	26320211
175	Succinylation	QLSADDLKKLKPGLE ECCHHHHHHHCCCCC	64.15	23954790
175	Ubiquitination	QLSADDLKKLKPGLE ECCHHHHHHHCCCCC	64.15	21890473
175 (in isoform 1)	Ubiquitination	-	64.15	21890473
176	Ubiquitination	LSADDLKKLKPGLEK CCHHHHHHHCCCCCC	69.87	-
178	Malonylation	ADDLKKLKPGLEKDF HHHHHHHCCCCCCCC	46.01	26320211
178	Succinylation	ADDLKKLKPGLEKDF HHHHHHHCCCCCCCC	46.01	27452117
197	Ubiquitination	FGWFLTKKSSETLRK HHHHHCCCCHHHHHH	54.71	-
197 (in isoform 2)	Ubiquitination	-	54.71	21890473
204	Malonylation	KSSETLRKAGQVFLE CCHHHHHHHHHHHHH	61.04	26320211
204	Ubiquitination	KSSETLRKAGQVFLE CCHHHHHHHHHHHHH	61.04	-
217	Ubiquitination	LEELGNHKAFKKELR HHHHCCCHHHHHHHH	60.56	21890473
217 (in isoform 1)	Ubiquitination	-	60.56	21890473
220	Ubiquitination	LGNHKAFKKELRQFV HCCCHHHHHHHHHHC	50.64	-
221	Ubiquitination	GNHKAFKKELRQFVP CCCHHHHHHHHHHCC	56.37	-
235	2-Hydroxyisobutyrylation	PGDEPREKMDLVTYF CCCCCHHHCCEEHHC	38.71	-
235	Ubiquitination	PGDEPREKMDLVTYF CCCCCHHHCCEEHHC	38.71	-
240	Phosphorylation	REKMDLVTYFGKRPP HHHCCEEHHCCCCCC	22.04	21406692
241	Phosphorylation	EKMDLVTYFGKRPPG HHCCEEHHCCCCCCC	11.67	21406692
241 (in isoform 2)	Ubiquitination	-	11.67	21890473
244	Ubiquitination	DLVTYFGKRPPGVLH CEEHHCCCCCCCEEE	52.40	-
255	Acetylation	GVLHCTTKFCDYGKA CEEEEECCCCCCCCC	26.33	26051181
255	Ubiquitination	GVLHCTTKFCDYGKA CEEEEECCCCCCCCC	26.33	-
255 (in isoform 2)	Ubiquitination	-	26.33	21890473
261	Ubiquitination	TKFCDYGKAPGAEEY CCCCCCCCCCCHHHH	45.22	22053931
275	Ubiquitination	YAQQDVLKKSYSKAF HHHHHHHHHHHHHCE	39.25	21890473
275 (in isoform 1)	Ubiquitination	-	39.25	21890473
276	Ubiquitination	AQQDVLKKSYSKAFT HHHHHHHHHHHHCEE	50.93	-
277	Phosphorylation	QQDVLKKSYSKAFTL HHHHHHHHHHHCEEE	32.81	21406692
278	Phosphorylation	QDVLKKSYSKAFTLT HHHHHHHHHHCEEEE	24.07	21406692
279	Phosphorylation	DVLKKSYSKAFTLTI HHHHHHHHHCEEEEE	25.30	21406692
283	Phosphorylation	KSYSKAFTLTISALF HHHHHCEEEEEEEEE	28.05	21406692
285	Phosphorylation	YSKAFTLTISALFVT HHHCEEEEEEEEEEC	15.16	21406692
287	Phosphorylation	KAFTLTISALFVTPK HCEEEEEEEEEECCC	17.43	21406692
292	Phosphorylation	TISALFVTPKTTGAR EEEEEEECCCCCCCE	16.25	21406692
295	Phosphorylation	ALFVTPKTTGARVEL EEEECCCCCCCEEEE	31.50	21406692
296	Phosphorylation	LFVTPKTTGARVELS EEECCCCCCCEEEEC	34.66	21406692
296 (in isoform 2)	Ubiquitination	-	34.66	21890473
303	Phosphorylation	TGARVELSEQQLQLW CCCEEEECHHHHHHC	21.61	24076635
312	Phosphorylation	QQLQLWPSDVDKLSP HHHHHCCCCCHHCCC	38.39	18510355
316	Ubiquitination	LWPSDVDKLSPTDNL HCCCCCHHCCCCCCC	51.19	22053931
316 (in isoform 1)	Ubiquitination	-	51.19	21890473
318	Phosphorylation	PSDVDKLSPTDNLPR CCCCHHCCCCCCCCC	31.34	30266825
320	Phosphorylation	DVDKLSPTDNLPRGS CCHHCCCCCCCCCCC	33.86	30266825
327	Phosphorylation	TDNLPRGSRAHITLG CCCCCCCCCEEEEEC	27.81	24076635
356	Ubiquitination	LEILRQEKGGSRGEE HHHHHHHCCCCCCCC	61.30	-
359	Phosphorylation	LRQEKGGSRGEEVGE HHHHCCCCCCCCCCC	45.86	-
366 (in isoform 2)	Ubiquitination	-	49.07	-
368	Phosphorylation	GEEVGELSRGKLYSL CCCCCCCCCCEEEEE	34.38	25332170
371	Ubiquitination	VGELSRGKLYSLGNG CCCCCCCEEEEECCC	43.04	-
373	Phosphorylation	ELSRGKLYSLGNGRW CCCCCEEEEECCCCE	12.82	22817900
383	Phosphorylation	GNGRWMLTLAKNMEV CCCCEEEEEECCCEE	14.47	19664995
406	Phosphorylation	GKGKPVPTQGSRKGG CCCCCCCCCCCCCCC	45.88	28857561
409	Phosphorylation	KPVPTQGSRKGGALQ CCCCCCCCCCCCCCC	22.47	28857561
418	Farnesylation	KGGALQSCTII---- CCCCCCCCEEC----	1.72	-
418	Methylation	KGGALQSCTII---- CCCCCCCCEEC----	1.72	-

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
9	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
9	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CN37_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 CN37_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SIR3_HUMAN	SIRT3	physical	26186194
SIR3_HUMAN	SIRT3	physical	28514442

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 CN37_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-170, AND MASSSPECTROMETRY.	19413330 [Abstract]