dbPTM

CBPB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBPB2_HUMAN
UniProt AC	Q96IY4
Protein Name	Carboxypeptidase B2
Gene Name	CPB2
Organism	Homo sapiens (Human).
Sequence Length	423
Subcellular Localization	Secreted.
Protein Description	Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin..
Protein Sequence	MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTADLIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYYEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGIHAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNINQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKISKNTRYTHGHGSETLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	N-linked_Glycosylation	RQVQVLQNLTTTYEI HHHHHHHHCCCEEEE	34.88	16445295
73	N-linked_Glycosylation	KQVHFFVNASDVDNV CEEEEEEEHHHCCCH	28.68	17623646
73	N-linked_Glycosylation	KQVHFFVNASDVDNV CEEEEEEEHHHCCCH	28.68	16335952
85	N-linked_Glycosylation	DNVKAHLNVSGIPCS CCHHHHCCCCCCCHH	18.95	18559974
108	N-linked_Glycosylation	LIQQQISNDTVSPRA HHHHHHCCCCCCCCC	51.07	22171320
156	Phosphorylation	IGSSFEKYPLYVLKV ECCCCCCCCEEEEEE	7.41	22817900
159	Phosphorylation	SFEKYPLYVLKVSGK CCCCCCEEEEEECCC	10.14	22817900
241	N-linked_Glycosylation	KNRMWRKNRSFYANN HCCCCCCCCCCCCCC	35.93	16445295
294	Phosphorylation	PEVKAVASFLRRNIN HHHHHHHHHHHHCHH	20.44	24719451
338	Phosphorylation	EELSLVASEAVRAIE HHHHHHHHHHHHHHH	20.71	24505115
380	Phosphorylation	IYDLGIKYSFTIELR EEECCCEEEEEEEEE	13.70	-
383	Phosphorylation	LGIKYSFTIELRDTG CCCEEEEEEEEECCC	13.96	-

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
Oops, there are no upstream regulatory protein records of CBPB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CBPB2_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
159	Phosphorylation	169 (10)	A ⇒ T	rs3742264	Blood protein levels	28240269

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A2MG_HUMAN	A2M	physical	8662763
CO5_HUMAN	C5	physical	11939578
TINAG_HUMAN	TINAG	physical	21988832

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 CBPB2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structures of TAFI elucidate the inactivation mechanism ofactivated TAFI: a novel mechanism for enzyme autoregulation."; Marx P.F., Brondijk T.H., Plug T., Romijn R.A., Hemrika W.,Meijers J.C., Huizinga E.G.; Blood 112:2803-2809(2008). Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-423 ALONE AND IN COMPLEXWITH INHIBITOR, GLYCOSYLATION AT ASN-44; ASN-73; ASN-85 AND ASN-108,ACTIVE SITE, ZINC-BINDING SITES, ENZYME REGULATION, AND DISULFIDEBONDS.	18559974 [Abstract]
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT ASN-108, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]
"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-108, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Post-translational modifications of human thrombin-activatablefibrinolysis inhibitor (TAFI): evidence for a large shift in theisoelectric point and reduced solubility upon activation."; Valnickova Z., Christensen T., Skottrup P., Thogersen I.B., Hojrup P.,Enghild J.J.; Biochemistry 45:1525-1535(2006). Cited for: GLYCOSYLATION AT ASN-44; ASN-73; ASN-85; ASN-108 AND ASN-241, ANDDISULFIDE BONDS.	16445295 [Abstract]
"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-44; ASN-73 AND ASN-108,AND MASS SPECTROMETRY.	16335952 [Abstract]