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P15086 (CBPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase B

EC=3.4.17.2
Alternative name(s):
Pancreas-specific protein
Short name=PASP
Gene names
Name:CPB1
Synonyms:CPB, PCPB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Preferential release of a C-terminal lysine or arginine amino acid.

Cofactor

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the peptidase M14 family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarboxypeptidase activity

Traceable author statement Ref.1. Source: ProtInc

metallocarboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.1 Ref.6
Propeptide16 – 11095Activation peptide
PRO_0000004371
Chain111 – 417307Carboxypeptidase B
PRO_0000004372

Sites

Active site3781Nucleophile By similarity
Metal binding1761Zinc
Metal binding1791Zinc
Metal binding3041Zinc

Amino acid modifications

Disulfide bond173 ↔ 186
Disulfide bond245 ↔ 268
Disulfide bond259 ↔ 273

Natural variations

Natural variant2081D → N. Ref.2
Corresponds to variant rs1059502 [ dbSNP | Ensembl ].
VAR_048598

Experimental info

Sequence conflict161H → A AA sequence Ref.1
Sequence conflict171H → Q AA sequence Ref.1
Sequence conflict371H → Q AA sequence Ref.6
Sequence conflict2451Missing in AAA66973. Ref.1

Secondary structure

.................................................................... 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15086 [UniParc].

Last modified May 10, 2002. Version 4.
Checksum: EBBB98B27F5D5AF9

FASTA41747,368
        10         20         30         40         50         60 
MLALLVLVTV ALASAHHGGE HFEGEKVFRV NVEDENHINI IRELASTTQI DFWKPDSVTQ 

        70         80         90        100        110        120 
IKPHSTVDFR VKAEDTVTVE NVLKQNELQY KVLISNLRNV VEAQFDSRVR ATGHSYEKYN 

       130        140        150        160        170        180 
KWETIEAWTQ QVATENPALI SRSVIGTTFE GRAIYLLKVG KAGQNKPAIF MDCGFHAREW 

       190        200        210        220        230        240 
ISPAFCQWFV REAVRTYGRE IQVTELLDKL DFYVLPVLNI DGYIYTWTKS RFWRKTRSTH 

       250        260        270        280        290        300 
TGSSCIGTDP NRNFDAGWCE IGASRNPCDE TYCGPAAESE KETKALADFI RNKLSSIKAY 

       310        320        330        340        350        360 
LTIHSYSQMM IYPYSYAYKL GENNAELNAL AKATVKELAS LHGTKYTYGP GATTIYPAAG 

       370        380        390        400        410 
GSDDWAYDQG IRYSFTFELR DTGRYGFLLP ESQIRATCEE TFLAIKYVAS YVLEHLY 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a cDNA encoding a human serum marker for acute pancreatitis. Identification of pancreas-specific protein as pancreatic procarboxypeptidase B."
Yamamoto K.K., Pousette A., Chow P., Wilson H., el Shami S., French C.K.
J. Biol. Chem. 267:2575-2581(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-40.
Tissue: Pancreas.
[2]"Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B."
Aloy P., Catasus L., Villegas V., Reverter D., Vendrell J., Aviles F.X.
Biol. Chem. 379:149-155(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-208.
Tissue: Pancreas.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[6]"Purification and properties of five different forms of human procarboxypeptidases."
Pascual R., Burgos F.J., Salva M., Soriano F., Mendez E., Aviles F.X.
Eur. J. Biochem. 179:609-616(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-43.
Tissue: Pancreas.
[7]"Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)."
Barbosa-Pereira P.J., Segura-Martin S., Oliva B., Ferrer-Orta C., Aviles F.X., Coll M., Gomis-Ruth F.X., Vendrell J.
J. Mol. Biol. 321:537-547(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 16-417.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81057 mRNA. Translation: AAA66973.1.
AJ224866 mRNA. Translation: CAA12163.1.
BT009910 mRNA. Translation: AAP88912.1.
CH471052 Genomic DNA. Translation: EAW78903.1.
BC015338 mRNA. Translation: AAH15338.1.
PIRA42332.
RefSeqNP_001862.2. NM_001871.2.
XP_005247181.1. XM_005247124.1.
UniGeneHs.477891.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KWMX-ray1.60A/B16-417[»]
1ZLIX-ray2.09A109-417[»]
ProteinModelPortalP15086.
SMRP15086. Positions 16-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000282957.

Chemistry

BindingDBP15086.
ChEMBLCHEMBL2552.

Protein family/group databases

MEROPSM14.003.

Polymorphism databases

DMDM20532382.

Proteomic databases

PaxDbP15086.
PRIDEP15086.

Protocols and materials databases

DNASU1360.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282957; ENSP00000282957; ENSG00000153002.
ENST00000491148; ENSP00000417222; ENSG00000153002.
GeneID1360.
KEGGhsa:1360.
UCSCuc003ewl.3. human.

Organism-specific databases

CTD1360.
GeneCardsGC03P148508.
HGNCHGNC:2299. CPB1.
MIM114852. gene.
neXtProtNX_P15086.
PharmGKBPA26821.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000252968.
HOVERGENHBG050815.
InParanoidP15086.
KOK01291.
OMAYEKYNKW.
OrthoDBEOG7RZ5Q9.
PhylomeDBP15086.
TreeFamTF317197.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP15086.
BgeeP15086.
CleanExHS_CPB1.
GenevestigatorP15086.

Family and domain databases

Gene3D3.30.70.340. 1 hit.
InterProIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMSSF54897. SSF54897. 1 hit.
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCPB1. human.
EvolutionaryTraceP15086.
GenomeRNAi1360.
NextBio5509.
PMAP-CutDBP15086.
PROP15086.
SOURCESearch...

Entry information

Entry nameCBPB1_HUMAN
AccessionPrimary (citable) accession number: P15086
Secondary accession number(s): O60834, Q53XJ0, Q96BQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 10, 2002
Last modified: February 19, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM