CBPM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CBPM_HUMAN
• UniProt AC: P14384
• Protein Name: Carboxypeptidase M
• Gene Name: CPM
• Organism: Homo sapiens (Human).
• Sequence Length: 443
• Subcellular Localization: Cell membrane ; Lipid-anchor, GPI-anchor .
• Protein Description: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins..
• Protein Sequence: MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVLVVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIHIMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKTETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGDECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNNKASLIEYIKQVHLGVKGQVFDQNGNPLPNVIVEVQDRKHICPYRTNKYGEYYLLLLPGSYIINVTVPGHDPHITKVIIPEKSQNFSALKKDILLPFQGQLDSIPVSNPSCPMIPLYRNLPDHSAATKPSLFLFLVSLLHIFFK

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
21	N-linked_Glycosylation	LVAALDFNYHRQEGM HHHHHCCCHHHHHHH	31.22	2753907
21	N-linked_Glycosylation	LVAALDFNYHRQEGM HHHHHCCCHHHHHHH	31.22	2753907
38	N-linked_Glycosylation	FLKTVAQNYSSVTHL HHHHHHHHCCCCEEH	28.99	15066430
115	N-linked_Glycosylation	PEITNLINSTRIHIM HHHHHHHCCCCEEEC	40.26	15066430
124	Phosphorylation	TRIHIMPSMNPDGFE CCEEECCCCCCCCCH	17.51	-
164	N-linked_Glycosylation	PDAFEYNNVSRQPET CCCHHCCCCCCCCCH	32.04	19159218
180	Phosphorylation	AVMKWLKTETFVLSA HEEEHHCCCEEEEEE	37.78	22210691
207	Phosphorylation	FDNGVQATGALYSRS CCCCCCCCCEEECCC	13.09	22210691
212	Phosphorylation	QATGALYSRSLTPDD CCCCEEECCCCCCCC	19.08	24719451
363	N-linked_Glycosylation	LPGSYIINVTVPGHD CCCCEEEEEEECCCC	17.53	UniProtKB CARBOHYD
384	N-linked_Glycosylation	IIPEKSQNFSALKKD ECCCCCCCHHHHCCC	39.67	UniProtKB CARBOHYD
423	GPI-anchor	YRNLPDHSAATKPSL CCCCCCCCCCCCHHH	27.29	12457462

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CBPM_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 CBPM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GTPB3_HUMAN	GTPBP3	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.

Related Literatures of Post-Translational Modification

GPI-anchor

"Modification-specific proteomics of plasma membrane proteins:identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment.";
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,Brodbeck U., Peck S.C., Jensen O.N.;
J. Proteome Res. 5:935-943(2006).
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
PubMed: 16602701

"Proteomic analysis of glycosylphosphatidylinositol-anchored membraneproteins.";
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,Jensen O.N.;
Mol. Cell. Proteomics 2:1261-1270(2003).
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
PubMed: 14517339

"Effect of mutation of two critical glutamic acid residues on theactivity and stability of human carboxypeptidase M andcharacterization of its signal for glycosylphosphatidylinositolanchoring.";
Tan F., Balsitis S., Black J.K., Bloechl A., Mao J.-F., Becker R.P.,Schacht D., Skidgel R.A.;
Biochem. J. 370:567-578(2003).
Cited for: PROTEIN SEQUENCE OF 18-21, GPI-ANCHOR AT SER-423, BIOPHYSICOCHEMICALPROPERTIES, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, ANDMUTAGENESIS OF GLU-277; GLU-281 AND SER-423.
PubMed: 12457462

N-linked Glycosylation

"Crystal structure of human carboxypeptidase M, a membrane-boundenzyme that regulates peptide hormone activity.";
Reverter D., Maskos K., Tan F., Skidgel R.A., Bode W.;
J. Mol. Biol. 338:257-269(2004).
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-443, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-38 AND ASN-115.
PubMed: 15066430

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115 AND ASN-164, AND MASSSPECTROMETRY.
PubMed: 19159218