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P15086

- CBPB1_HUMAN

UniProt

P15086 - CBPB1_HUMAN

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Protein
Carboxypeptidase B
Gene
CPB1, CPB, PCPB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi176 – 1761Zinc
Metal bindingi179 – 1791Zinc
Metal bindingi304 – 3041Zinc
Active sitei378 – 3781Nucleophile By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: ProtInc
  2. metallocarboxypeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Protein family/group databases

    MEROPSiM14.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase B (EC:3.4.17.2)
    Alternative name(s):
    Pancreas-specific protein
    Short name:
    PASP
    Gene namesi
    Name:CPB1
    Synonyms:CPB, PCPB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:2299. CPB1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26821.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15152 Publications
    Add
    BLAST
    Propeptidei16 – 11095Activation peptide
    PRO_0000004371Add
    BLAST
    Chaini111 – 417307Carboxypeptidase B
    PRO_0000004372Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi173 ↔ 186
    Disulfide bondi245 ↔ 268
    Disulfide bondi259 ↔ 273

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    MaxQBiP15086.
    PaxDbiP15086.
    PRIDEiP15086.

    Miscellaneous databases

    PMAP-CutDBP15086.

    Expressioni

    Tissue specificityi

    Pancreas.

    Gene expression databases

    ArrayExpressiP15086.
    BgeeiP15086.
    CleanExiHS_CPB1.
    GenevestigatoriP15086.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000282957.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 224
    Beta strandi26 – 327
    Helixi35 – 4713
    Beta strandi50 – 578
    Helixi58 – 603
    Beta strandi63 – 719
    Helixi73 – 753
    Helixi76 – 8510
    Beta strandi90 – 956
    Helixi97 – 1037
    Beta strandi111 – 1133
    Helixi122 – 13514
    Turni137 – 1393
    Beta strandi140 – 1478
    Beta strandi153 – 1608
    Beta strandi168 – 1725
    Helixi181 – 19616
    Turni197 – 1993
    Helixi201 – 2099
    Beta strandi211 – 2166
    Helixi220 – 2289
    Helixi250 – 2523
    Beta strandi254 – 2574
    Beta strandi260 – 2623
    Helixi281 – 29212
    Turni293 – 2964
    Beta strandi297 – 3048
    Beta strandi309 – 3135
    Beta strandi315 – 3184
    Helixi324 – 34219
    Beta strandi347 – 3504
    Helixi351 – 3544
    Helixi362 – 3687
    Beta strandi372 – 3787
    Beta strandi382 – 3854
    Helixi386 – 3883
    Helixi391 – 3933
    Helixi394 – 41320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KWMX-ray1.60A/B16-417[»]
    1ZLIX-ray2.09A109-417[»]
    ProteinModelPortaliP15086.
    SMRiP15086. Positions 16-417.

    Miscellaneous databases

    EvolutionaryTraceiP15086.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2866.
    HOGENOMiHOG000252968.
    HOVERGENiHBG050815.
    InParanoidiP15086.
    KOiK01291.
    OMAiYEKYNKW.
    OrthoDBiEOG7RZ5Q9.
    PhylomeDBiP15086.
    TreeFamiTF317197.

    Family and domain databases

    Gene3Di3.30.70.340. 1 hit.
    InterProiIPR000834. Peptidase_M14.
    IPR003146. Prot_inh_M14A.
    IPR009020. Prot_inh_propept.
    [Graphical view]
    PfamiPF00246. Peptidase_M14. 1 hit.
    PF02244. Propep_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00631. Zn_pept. 1 hit.
    [Graphical view]
    SUPFAMiSSF54897. SSF54897. 1 hit.
    PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15086-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLALLVLVTV ALASAHHGGE HFEGEKVFRV NVEDENHINI IRELASTTQI    50
    DFWKPDSVTQ IKPHSTVDFR VKAEDTVTVE NVLKQNELQY KVLISNLRNV 100
    VEAQFDSRVR ATGHSYEKYN KWETIEAWTQ QVATENPALI SRSVIGTTFE 150
    GRAIYLLKVG KAGQNKPAIF MDCGFHAREW ISPAFCQWFV REAVRTYGRE 200
    IQVTELLDKL DFYVLPVLNI DGYIYTWTKS RFWRKTRSTH TGSSCIGTDP 250
    NRNFDAGWCE IGASRNPCDE TYCGPAAESE KETKALADFI RNKLSSIKAY 300
    LTIHSYSQMM IYPYSYAYKL GENNAELNAL AKATVKELAS LHGTKYTYGP 350
    GATTIYPAAG GSDDWAYDQG IRYSFTFELR DTGRYGFLLP ESQIRATCEE 400
    TFLAIKYVAS YVLEHLY 417
    Length:417
    Mass (Da):47,368
    Last modified:May 10, 2002 - v4
    Checksum:iEBBB98B27F5D5AF9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti208 – 2081D → N.1 Publication
    Corresponds to variant rs1059502 [ dbSNP | Ensembl ].
    VAR_048598

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161H → A AA sequence 1 Publication
    Sequence conflicti17 – 171H → Q AA sequence 1 Publication
    Sequence conflicti37 – 371H → Q AA sequence 1 Publication
    Sequence conflicti245 – 2451Missing in AAA66973. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS33874.1.
    PIRiA42332.
    RefSeqiNP_001862.2. NM_001871.2.
    XP_005247181.1. XM_005247124.1.
    UniGeneiHs.477891.

    Genome annotation databases

    EnsembliENST00000282957; ENSP00000282957; ENSG00000153002.
    ENST00000491148; ENSP00000417222; ENSG00000153002.
    GeneIDi1360.
    KEGGihsa:1360.
    UCSCiuc003ewl.3. human.

    Polymorphism databases

    DMDMi20532382.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS33874.1.
    PIRi A42332.
    RefSeqi NP_001862.2. NM_001871.2.
    XP_005247181.1. XM_005247124.1.
    UniGenei Hs.477891.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KWM X-ray 1.60 A/B 16-417 [» ]
    1ZLI X-ray 2.09 A 109-417 [» ]
    ProteinModelPortali P15086.
    SMRi P15086. Positions 16-417.
    ModBasei Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000282957.

    Chemistry

    BindingDBi P15086.
    ChEMBLi CHEMBL2552.

    Protein family/group databases

    MEROPSi M14.003.

    Polymorphism databases

    DMDMi 20532382.

    Proteomic databases

    MaxQBi P15086.
    PaxDbi P15086.
    PRIDEi P15086.

    Protocols and materials databases

    DNASUi 1360.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282957 ; ENSP00000282957 ; ENSG00000153002 .
    ENST00000491148 ; ENSP00000417222 ; ENSG00000153002 .
    GeneIDi 1360.
    KEGGi hsa:1360.
    UCSCi uc003ewl.3. human.

    Organism-specific databases

    CTDi 1360.
    GeneCardsi GC03P148508.
    HGNCi HGNC:2299. CPB1.
    MIMi 114852. gene.
    neXtProti NX_P15086.
    PharmGKBi PA26821.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2866.
    HOGENOMi HOG000252968.
    HOVERGENi HBG050815.
    InParanoidi P15086.
    KOi K01291.
    OMAi YEKYNKW.
    OrthoDBi EOG7RZ5Q9.
    PhylomeDBi P15086.
    TreeFami TF317197.

    Enzyme and pathway databases

    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    ChiTaRSi CPB1. human.
    EvolutionaryTracei P15086.
    GenomeRNAii 1360.
    NextBioi 5509.
    PMAP-CutDB P15086.
    PROi P15086.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15086.
    Bgeei P15086.
    CleanExi HS_CPB1.
    Genevestigatori P15086.

    Family and domain databases

    Gene3Di 3.30.70.340. 1 hit.
    InterProi IPR000834. Peptidase_M14.
    IPR003146. Prot_inh_M14A.
    IPR009020. Prot_inh_propept.
    [Graphical view ]
    Pfami PF00246. Peptidase_M14. 1 hit.
    PF02244. Propep_M14. 1 hit.
    [Graphical view ]
    PRINTSi PR00765. CRBOXYPTASEA.
    SMARTi SM00631. Zn_pept. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54897. SSF54897. 1 hit.
    PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    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. 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.

    Entry informationi

    Entry nameiCBPB1_HUMAN
    AccessioniPrimary (citable) accession number: P15086
    Secondary accession number(s): O60834, Q53XJ0, Q96BQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: May 10, 2002
    Last modified: September 3, 2014
    This is version 158 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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