CBPA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CBPA4_HUMAN
• UniProt AC: Q9UI42
• Protein Name: Carboxypeptidase A4
• Gene Name: CPA4
• Organism: Homo sapiens (Human).
• Sequence Length: 421
• Subcellular Localization: Secreted.
• Protein Description: Metalloprotease that could be involved in the histone hyperacetylation pathway. [PubMed: 10383164 Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val]
• Protein Sequence: MRWILFIGALIGSSICGQEKFFGDQVLRINVRNGDEISKLSQLVNSNNLKLNFWKSPSSFNRPVDVLVPSVSLQAFKSFLRSQGLEYAVTIEDLQALLDNEDDEMQHNEGQERSSNNFNYGAYHSLEAIYHEMDNIAADFPDLARRVKIGHSFENRPMYVLKFSTGKGVRRPAVWLNAGIHSREWISQATAIWTARKIVSDYQRDPAITSILEKMDIFLLPVANPDGYVYTQTQNRLWRKTRSRNPGSSCIGADPNRNWNASFAGKGASDNPCSEVYHGPHANSEVEVKSVVDFIQKHGNFKGFIDLHSYSQLLMYPYGYSVKKAPDAEELDKVARLAAKALASVSGTEYQVGPTCTTVYPASGSSIDWAYDNGIKFAFTFELRDTGTYGFLLPANQIIPTAEETWLGLKTIMEHVRDNLY

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
38	Phosphorylation	VRNGDEISKLSQLVN ECCHHHHHHHHHHHH	26.04	-
78	Phosphorylation	VSLQAFKSFLRSQGL HHHHHHHHHHHHCCC	24.06	24719451
210	Phosphorylation	QRDPAITSILEKMDI CCCHHHHHHHHHCCE	21.04	24719451
260	N-linked_Glycosylation	ADPNRNWNASFAGKG CCCCCCCCCCCCCCC	29.29	15738388

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

Oops, there are no upstream regulatory protein records of CBPA4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CBPA4_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 CBPA4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LXN_HUMAN	LXN	physical	15738388
NUCG_HUMAN	ENDOG	physical	26186194

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

"Structure of human carboxypeptidase A4 with its endogenous proteininhibitor, latexin.";
Pallares I., Bonet R., Garcia-Castellanos R., Ventura S., Aviles F.X.,Vendrell J., Gomis-Rueth F.-X.;
Proc. Natl. Acad. Sci. U.S.A. 102:3978-3983(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 114-421 IN COMPLEX WITH LXN,GLYCOSYLATION AT ASN-260, AND DISULFIDE BOND.
PubMed: 15738388

"Detailed molecular comparison between the inhibition mode of A/B-typecarboxypeptidases in the zymogen state and by the endogenous inhibitorlatexin.";
Garcia-Castellanos R., Bonet-Figueredo R., Pallares I., Ventura S.,Aviles F.X., Vendrell J., Gomis-Rueth F.-X.;
Cell. Mol. Life Sci. 62:1996-2014(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-421 IN COMPLEX WITH LXNAND ZINC IONS, GLYCOSYLATION AT ASN-260, AND DISULFIDE BOND.
PubMed: 16091843