CPN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPN2_HUMAN
• UniProt AC: P22792
• Protein Name: Carboxypeptidase N subunit 2
• Gene Name: CPN2
• Organism: Homo sapiens (Human).
• Sequence Length: 545
• Subcellular Localization: Secreted.
• Protein Description: The 83 kDa subunit binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit..
• Protein Sequence: MLPGAWLLWTSLLLLARPAQPCPMGCDCFVQEVFCSDEELATVPLDIPPYTKNIIFVETSFTTLETRAFGSNPNLTKVVFLNTQLCQFRPDAFGGLPRLEDLEVTGSSFLNLSTNIFSNLTSLGKLTLNFNMLEALPEGLFQHLAALESLHLQGNQLQALPRRLFQPLTHLKTLNLAQNLLAQLPEELFHPLTSLQTLKLSNNALSGLPQGVFGKLGSLQELFLDSNNISELPPQVFSQLFCLERLWLQRNAITHLPLSIFASLGNLTFLSLQWNMLRVLPAGLFAHTPCLVGLSLTHNQLETVAEGTFAHLSNLRSLMLSYNAITHLPAGIFRDLEELVKLYLGSNNLTALHPALFQNLSKLELLSLSKNQLTTLPEGIFDTNYNLFNLALHGNPWQCDCHLAYLFNWLQQYTDRLLNIQTYCAGPAYLKGQVVPALNEKQLVCPVTRDHLGFQVTWPDESKAGGSWDLAVQERAARSQCTYSNPEGTVVLACDQAQCRWLNVQLSPQQGSLGLQYNASQEWDLRSSCGSLRLTVSIEARAAGP

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
71	Phosphorylation	LETRAFGSNPNLTKV CCCCCCCCCCCCCEE	42.53	-
74	N-linked_Glycosylation	RAFGSNPNLTKVVFL CCCCCCCCCCEEEEE	65.67	17623646
76	Phosphorylation	FGSNPNLTKVVFLNT CCCCCCCCEEEEECC	28.56	-
111	N-linked_Glycosylation	VTGSSFLNLSTNIFS ECCCCHHHCCCCHHH	29.90	UniProtKB CARBOHYD
119	N-linked_Glycosylation	LSTNIFSNLTSLGKL CCCCHHHCCCCCCCE	36.27	UniProtKB CARBOHYD
228	N-linked_Glycosylation	ELFLDSNNISELPPQ HHHCCCCCHHHCCHH	43.02	16335952
266	N-linked_Glycosylation	SIFASLGNLTFLSLQ HHHHHCCCCEEHHHH	41.00	UniProtKB CARBOHYD
313	Phosphorylation	EGTFAHLSNLRSLML HHHHHHHHHHHHHHH	24.77	24719451
348	N-linked_Glycosylation	KLYLGSNNLTALHPA HHHHCCCCCHHHCHH	40.23	14760718
359	N-linked_Glycosylation	LHPALFQNLSKLELL HCHHHHHCCCHHHHH	38.66	14760718
367	Phosphorylation	LSKLELLSLSKNQLT CCHHHHHHCCCCCCC	43.13	24719451
457	O-linked_Glycosylation	DHLGFQVTWPDESKA CCCEEEEECCCHHCC	22.09	OGP
467	Phosphorylation	DESKAGGSWDLAVQE CHHCCCCCEEHHHHH	19.25	24505115
518	N-linked_Glycosylation	GSLGLQYNASQEWDL CCCCCEEECCCCEEC	21.83	16335952

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

Oops, there are no upstream regulatory protein records of CPN2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CPN2_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 CPN2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CPN2_HUMAN !!

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228 AND ASN-518, AND MASSSPECTROMETRY.
PubMed: 16335952

"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348 AND ASN-359, AND MASSSPECTROMETRY.
PubMed: 14760718