Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96IY4

- CBPB2_HUMAN

UniProt

Q96IY4 - CBPB2_HUMAN

Protein

Carboxypeptidase B2

Gene

CPB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.1 Publication

    Catalytic activityi

    Release of C-terminal Arg and Lys from a polypeptide.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.

    Enzyme regulationi

    TAFI/CPB2 is unique among carboxypeptidases in that it spontaneously inactivates with a short half-life, a property that is crucial for its role in controlling blood clot lysis. The zymogen is stabilized by interactions with the activation peptide. Release of the activation peptide increases a dynamic flap mobility and in time this leads to conformational changes that disrupt the catalytic site and expose a cryptic thrombin-cleavage site present at Arg-324.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi181 – 1811Zinc; catalytic
    Metal bindingi184 – 1841Zinc; catalytic
    Metal bindingi310 – 3101Zinc; catalytic
    Sitei324 – 3252Cleavage; by thrombin
    Active sitei385 – 3851Nucleophile1 Publication

    GO - Molecular functioni

    1. metallocarboxypeptidase activity Source: ProtInc
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW
    2. cellular response to glucose stimulus Source: Ensembl
    3. fibrinolysis Source: UniProtKB-KW
    4. liver regeneration Source: Ensembl
    5. negative regulation of fibrinolysis Source: Ensembl
    6. negative regulation of hepatocyte proliferation Source: Ensembl
    7. negative regulation of plasminogen activation Source: Ensembl
    8. positive regulation of extracellular matrix constituent secretion Source: Ensembl
    9. proteolysis Source: ProtInc
    10. response to drug Source: Ensembl
    11. response to heat Source: Ensembl

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Blood coagulation, Fibrinolysis, Hemostasis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Protein family/group databases

    MEROPSiM14.009.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase B2 (EC:3.4.17.20)
    Alternative name(s):
    Carboxypeptidase U
    Short name:
    CPU
    Plasma carboxypeptidase B
    Short name:
    pCPB
    Thrombin-activable fibrinolysis inhibitor
    Short name:
    TAFI
    Gene namesi
    Name:CPB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:2300. CPB2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26822.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 11492Activation peptidePRO_0000004377Add
    BLAST
    Chaini115 – 423309Carboxypeptidase B2PRO_0000004378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi44 – 441N-linked (GlcNAc...)3 Publications
    Glycosylationi73 – 731N-linked (GlcNAc...)3 Publications
    Glycosylationi85 – 851N-linked (GlcNAc...)2 Publications
    Glycosylationi108 – 1081N-linked (GlcNAc...) (complex)5 Publications
    Disulfide bondi178 ↔ 191
    Glycosylationi241 – 2411N-linked (GlcNAc...); partial1 Publication
    Disulfide bondi250 ↔ 274
    Disulfide bondi265 ↔ 279

    Post-translational modificationi

    N-glycosylated. N-glycan at Asn-108: Hex5HexNAc4.5 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ96IY4.
    PaxDbiQ96IY4.
    PRIDEiQ96IY4.

    PTM databases

    PhosphoSiteiQ96IY4.

    Miscellaneous databases

    PMAP-CutDBA8K464.

    Expressioni

    Tissue specificityi

    Plasma; synthesized in the liver.

    Gene expression databases

    BgeeiQ96IY4.
    CleanExiHS_CPB2.
    GenevestigatoriQ96IY4.

    Organism-specific databases

    HPAiHPA004146.

    Interactioni

    Protein-protein interaction databases

    BioGridi107753. 7 interactions.
    IntActiQ96IY4. 1 interaction.
    STRINGi9606.ENSP00000181383.

    Structurei

    Secondary structure

    1
    423
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 317
    Helixi36 – 4813
    Beta strandi49 – 5810
    Helixi59 – 613
    Beta strandi68 – 736
    Helixi74 – 8613
    Beta strandi91 – 966
    Helixi98 – 10710
    Helixi108 – 1103
    Helixi118 – 1214
    Helixi126 – 13914
    Turni141 – 1433
    Beta strandi144 – 1518
    Beta strandi157 – 1637
    Beta strandi172 – 1787
    Helixi186 – 20015
    Turni201 – 2044
    Helixi206 – 2149
    Beta strandi215 – 2217
    Helixi225 – 2339
    Helixi255 – 2573
    Turni262 – 2654
    Beta strandi269 – 2713
    Helixi287 – 29812
    Turni299 – 3024
    Beta strandi303 – 3108
    Beta strandi312 – 3198
    Beta strandi321 – 3255
    Helixi330 – 34718
    Beta strandi354 – 3574
    Helixi358 – 3614
    Helixi369 – 3757
    Beta strandi380 – 3856
    Beta strandi389 – 3924
    Helixi393 – 3953
    Helixi398 – 4003
    Helixi401 – 42222

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3D66X-ray3.10A/B/C24-423[»]
    3D67X-ray3.40A/B/C24-423[»]
    3D68X-ray2.80A/B/C24-423[»]
    3LMSX-ray2.50A115-423[»]
    ProteinModelPortaliQ96IY4.
    SMRiQ96IY4. Positions 24-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96IY4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2866.
    HOGENOMiHOG000252968.
    HOVERGENiHBG050815.
    InParanoidiQ96IY4.
    KOiK01300.
    OMAiEIYSWIE.
    OrthoDBiEOG7RZ5Q9.
    PhylomeDBiQ96IY4.
    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.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96IY4-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKLCSLAVLV PIVLFCEQHV FAFQSGQVLA ALPRTSRQVQ VLQNLTTTYE    50
    IVLWQPVTAD LIVKKKQVHF FVNASDVDNV KAHLNVSGIP CSVLLADVED 100
    LIQQQISNDT VSPRASASYY EQYHSLNEIY SWIEFITERH PDMLTKIHIG 150
    SSFEKYPLYV LKVSGKEQAA KNAIWIDCGI HAREWISPAF CLWFIGHITQ 200
    FYGIIGQYTN LLRLVDFYVM PVVNVDGYDY SWKKNRMWRK NRSFYANNHC 250
    IGTDLNRNFA SKHWCEEGAS SSSCSETYCG LYPESEPEVK AVASFLRRNI 300
    NQIKAYISMH SYSQHIVFPY SYTRSKSKDH EELSLVASEA VRAIEKISKN 350
    TRYTHGHGSE TLYLAPGGGD DWIYDLGIKY SFTIELRDTG TYGFLLPERY 400
    IKPTCREAFA AVSKIAWHVI RNV 423
    Length:423
    Mass (Da):48,424
    Last modified:January 11, 2011 - v2
    Checksum:iB4D20E03ECDD55EF
    GO
    Isoform 2 (identifier: Q96IY4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-234: Missing.
         384-423: IELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV → SNPPVEKLLPLSLK

    Show »
    Length:360
    Mass (Da):40,922
    Checksum:i2C011F6D4265F4B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251S → T in BAA90475. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti169 – 1691A → T.2 Publications
    Corresponds to variant rs3742264 [ dbSNP | Ensembl ].
    VAR_032565
    Natural varianti347 – 3471I → T.5 Publications
    Corresponds to variant rs1926447 [ dbSNP | Ensembl ].
    VAR_022258

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei198 – 23437Missing in isoform 2. 1 PublicationVSP_013446Add
    BLAST
    Alternative sequencei384 – 42340IELRD…VIRNV → SNPPVEKLLPLSLK in isoform 2. 1 PublicationVSP_013447Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75106 mRNA. Translation: AAA60042.1.
    AB011969 mRNA. Translation: BAA90475.1.
    BT006936 mRNA. Translation: AAP35582.1.
    AK290829 mRNA. Translation: BAF83518.1.
    AY714780 Genomic DNA. Translation: AAT97987.1.
    AL157758, AL137141 Genomic DNA. Translation: CAI10904.1.
    AL157758, AL137141 Genomic DNA. Translation: CAI10905.1.
    AL137141, AL157758 Genomic DNA. Translation: CAI12170.1.
    AL137141, AL157758 Genomic DNA. Translation: CAI12171.1.
    BC007057 mRNA. Translation: AAH07057.1.
    CCDSiCCDS9401.1. [Q96IY4-1]
    PIRiA41204.
    RefSeqiNP_001265470.1. NM_001278541.1.
    NP_001863.3. NM_001872.4. [Q96IY4-1]
    UniGeneiHs.512937.

    Genome annotation databases

    EnsembliENST00000181383; ENSP00000181383; ENSG00000080618. [Q96IY4-1]
    GeneIDi1361.
    KEGGihsa:1361.
    UCSCiuc001vaw.3. human. [Q96IY4-1]

    Polymorphism databases

    DMDMi317373332.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75106 mRNA. Translation: AAA60042.1 .
    AB011969 mRNA. Translation: BAA90475.1 .
    BT006936 mRNA. Translation: AAP35582.1 .
    AK290829 mRNA. Translation: BAF83518.1 .
    AY714780 Genomic DNA. Translation: AAT97987.1 .
    AL157758 , AL137141 Genomic DNA. Translation: CAI10904.1 .
    AL157758 , AL137141 Genomic DNA. Translation: CAI10905.1 .
    AL137141 , AL157758 Genomic DNA. Translation: CAI12170.1 .
    AL137141 , AL157758 Genomic DNA. Translation: CAI12171.1 .
    BC007057 mRNA. Translation: AAH07057.1 .
    CCDSi CCDS9401.1. [Q96IY4-1 ]
    PIRi A41204.
    RefSeqi NP_001265470.1. NM_001278541.1.
    NP_001863.3. NM_001872.4. [Q96IY4-1 ]
    UniGenei Hs.512937.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3D66 X-ray 3.10 A/B/C 24-423 [» ]
    3D67 X-ray 3.40 A/B/C 24-423 [» ]
    3D68 X-ray 2.80 A/B/C 24-423 [» ]
    3LMS X-ray 2.50 A 115-423 [» ]
    ProteinModelPortali Q96IY4.
    SMRi Q96IY4. Positions 24-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107753. 7 interactions.
    IntActi Q96IY4. 1 interaction.
    STRINGi 9606.ENSP00000181383.

    Chemistry

    BindingDBi Q96IY4.
    ChEMBLi CHEMBL3419.

    Protein family/group databases

    MEROPSi M14.009.

    PTM databases

    PhosphoSitei Q96IY4.

    Polymorphism databases

    DMDMi 317373332.

    Proteomic databases

    MaxQBi Q96IY4.
    PaxDbi Q96IY4.
    PRIDEi Q96IY4.

    Protocols and materials databases

    DNASUi 1361.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000181383 ; ENSP00000181383 ; ENSG00000080618 . [Q96IY4-1 ]
    GeneIDi 1361.
    KEGGi hsa:1361.
    UCSCi uc001vaw.3. human. [Q96IY4-1 ]

    Organism-specific databases

    CTDi 1361.
    GeneCardsi GC13M046627.
    HGNCi HGNC:2300. CPB2.
    HPAi HPA004146.
    MIMi 603101. gene.
    neXtProti NX_Q96IY4.
    PharmGKBi PA26822.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2866.
    HOGENOMi HOG000252968.
    HOVERGENi HBG050815.
    InParanoidi Q96IY4.
    KOi K01300.
    OMAi EIYSWIE.
    OrthoDBi EOG7RZ5Q9.
    PhylomeDBi Q96IY4.
    TreeFami TF317197.

    Enzyme and pathway databases

    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    EvolutionaryTracei Q96IY4.
    GeneWikii Carboxypeptidase_B2.
    GenomeRNAii 1361.
    NextBioi 5513.
    PMAP-CutDB A8K464.
    PROi Q96IY4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96IY4.
    CleanExi HS_CPB2.
    Genevestigatori Q96IY4.

    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.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma."
      Eaton D.L., Malloy B.E., Tsai S.P., Henzel W., Drayna D.
      J. Biol. Chem. 266:21833-21838(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, INTERACTION WITH PLASMINOGEN, VARIANTS THR-169 AND THR-347.
      Tissue: Liver.
    2. "Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma."
      Matsumoto A.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-347.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS THR-169 AND THR-347.
      Tissue: Liver.
    5. SeattleSNPs variation discovery resource
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-347.
    6. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1), VARIANT THR-347.
      Tissue: Skeletal muscle.
    8. "Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans."
      Mao S.S., Cooper C.M., Wood T., Shafer J.A., Gardell S.J.
      J. Biol. Chem. 274:35046-35052(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    9. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44; ASN-73 AND ASN-108.
      Tissue: Plasma.
    10. "Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-44; ASN-73; ASN-85; ASN-108 AND ASN-241, DISULFIDE BONDS.
    11. "Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108.
      Tissue: Liver.
    12. "Human urinary glycoproteomics; attachment site specific analysis of N-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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-108, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Crystal structures of TAFI elucidate the inactivation mechanism of activated 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-423 ALONE AND IN COMPLEX WITH INHIBITOR, GLYCOSYLATION AT ASN-44; ASN-73; ASN-85 AND ASN-108, ACTIVE SITE, ZINC-BINDING SITES, ENZYME REGULATION, DISULFIDE BONDS.
    14. "Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor."
      Sanglas L., Arolas J.L., Valnickova Z., Aviles F.X., Enghild J.J., Gomis-Ruth F.X.
      J. Thromb. Haemost. 8:1056-1065(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 115-423 IN COMPLEX WITH INHIBITOR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCBPB2_HUMAN
    AccessioniPrimary (citable) accession number: Q96IY4
    Secondary accession number(s): A8K464
    , Q15114, Q5T9K1, Q5T9K2, Q9P2Y6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 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 13
      Human chromosome 13: 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