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P00974

- BPT1_BOVIN

UniProt

P00974 - BPT1_BOVIN

Protein

Pancreatic trypsin inhibitor

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei50 – 512Reactive bond for trypsin

    GO - Molecular functioni

    1. potassium channel inhibitor activity Source: AgBase
    2. protein binding Source: IntAct
    3. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI02.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pancreatic trypsin inhibitor
    Alternative name(s):
    Aprotinin
    Basic protease inhibitor
    Short name:
    BPI
    Short name:
    BPTI
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Pharmaceutical usei

    Available under the name Trasylol (Mile). Used for inhibiting coagulation so as to reduce blood loss during bypass surgery.

    Protein family/group databases

    Allergomei3890. Bos d TI.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 3514PRO_0000016852Add
    BLAST
    Chaini36 – 9358Pancreatic trypsin inhibitorPRO_0000016853Add
    BLAST
    Propeptidei94 – 1007PRO_0000016854

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 90
    Disulfide bondi49 ↔ 731 PublicationPROSITE-ProRule annotation
    Disulfide bondi65 ↔ 861 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP00974.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P007604EBI-1032263,EBI-986385
    Q52V245EBI-1032263,EBI-8755401From a different organism.

    Protein-protein interaction databases

    DIPiDIP-6113N.
    IntActiP00974. 5 interactions.
    MINTiMINT-90698.
    STRINGi9913.ENSBTAP00000023042.

    Structurei

    Secondary structure

    1
    100
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 414
    Beta strandi48 – 503
    Beta strandi53 – 597
    Turni60 – 634
    Beta strandi64 – 707
    Beta strandi72 – 743
    Beta strandi76 – 783
    Beta strandi80 – 823
    Helixi83 – 908

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AALX-ray1.60A/B36-93[»]
    1B0CX-ray2.80A/B/C/D/E36-91[»]
    1BHCX-ray2.70A/B/C/D/E/F/G/H/I/J36-93[»]
    1BPIX-ray1.09A36-93[»]
    1BPTX-ray2.00A36-93[»]
    1BRBX-ray2.10I36-93[»]
    1BTHX-ray2.30P/Q36-93[»]
    1BTIX-ray2.20A36-93[»]
    1BZ5X-ray2.58A/B/C/D/E36-93[»]
    1BZXX-ray2.10I36-93[»]
    1CBWX-ray2.60D/I36-93[»]
    1CO7X-ray1.90I2-100[»]
    1D0DX-ray1.62B36-93[»]
    1EAWX-ray2.93B/D36-93[»]
    1EJMX-ray1.85B/D/F36-93[»]
    1F5RX-ray1.65I36-100[»]
    1F7ZX-ray1.55I36-100[»]
    1FAKX-ray2.10I37-90[»]
    1FANX-ray2.00A36-93[»]
    1FY8X-ray1.70I36-93[»]
    1G6XX-ray0.86A36-93[»]
    1JV8NMR-A36-93[»]
    1JV9NMR-A36-93[»]
    1K09NMR-A/B50-73[»]
    1K6UX-ray1.00A36-93[»]
    1LD5NMR-A36-93[»]
    1LD6NMR-A36-93[»]
    1MTNX-ray2.80D/H36-93[»]
    1NAGX-ray1.90A36-93[»]
    1OA5NMR-536-93[»]
    1OA6NMR-536-93[»]
    1P2IX-ray1.65I36-93[»]
    1P2JX-ray1.35I36-93[»]
    1P2KX-ray1.60I36-93[»]
    1P2MX-ray1.75B/D36-93[»]
    1P2NX-ray1.80B/D36-93[»]
    1P2OX-ray2.00B/D36-93[»]
    1P2QX-ray1.80B/D36-93[»]
    1PITNMR-A36-93[»]
    1QLQX-ray1.42A36-93[»]
    1T7CX-ray1.85B/D36-93[»]
    1T8LX-ray1.75B/D36-93[»]
    1T8MX-ray1.80B/D36-93[»]
    1T8NX-ray1.75B/D36-93[»]
    1T8OX-ray1.70B/D36-93[»]
    1TPAX-ray1.90I36-93[»]
    1UUANMR-A38-93[»]
    1UUBNMR-A38-93[»]
    1YKTX-ray1.70B36-91[»]
    1YLCX-ray1.70B36-91[»]
    1YLDX-ray1.70B36-91[»]
    2FI3X-ray1.58I36-93[»]
    2FI4X-ray1.58I36-93[»]
    2FI5X-ray1.58I36-93[»]
    2FTLX-ray1.62I36-93[»]
    2FTMX-ray1.65B36-93[»]
    2HEXX-ray2.10A/B/C/D/E36-93[»]
    2IJOX-ray2.30I36-93[»]
    2KAIX-ray2.50I36-93[»]
    2PTCX-ray1.90I36-93[»]
    2R9PX-ray1.40E/F/G/I36-93[»]
    2RA3X-ray1.46C/I36-93[»]
    2TGPX-ray1.90I36-93[»]
    2TPIX-ray2.10I36-93[»]
    2ZJXX-ray1.09A/B36-93[»]
    2ZVXX-ray1.09A/B36-93[»]
    3BTDX-ray1.90I36-93[»]
    3BTEX-ray1.85I36-93[»]
    3BTFX-ray1.80I36-93[»]
    3BTGX-ray1.90I36-93[»]
    3BTHX-ray1.75I36-93[»]
    3BTKX-ray1.85I36-93[»]
    3BTMX-ray1.80I36-93[»]
    3BTQX-ray1.90I36-93[»]
    3BTTX-ray1.90I36-93[»]
    3BTWX-ray2.05I36-93[»]
    3FP6X-ray1.49I36-93[»]
    3FP7X-ray1.46I36-50[»]
    J51-93[»]
    3FP8X-ray1.46I36-93[»]
    3GYMX-ray2.80I/J36-93[»]
    3LDIX-ray2.20A/B/C/D/E36-93[»]
    3LDJX-ray1.70A/B/C36-93[»]
    3LDMX-ray2.60A/B/C/D/E36-93[»]
    3OTJOther2.15I36-93[»]
    3P92X-ray1.60E36-93[»]
    3P95X-ray1.30E36-93[»]
    3TGIX-ray1.80I36-100[»]
    3TGJX-ray2.20I36-100[»]
    3TGKX-ray1.70I36-100[»]
    3TPIX-ray1.90I36-93[»]
    3U1JX-ray1.80E36-93[»]
    4BNRX-ray2.00I/J1-100[»]
    4DG4X-ray1.40C/E/F/H36-93[»]
    4PTIX-ray1.50A36-93[»]
    4TPIX-ray2.20I36-93[»]
    5PTIX-ray1.00A36-93[»]
    6PTIX-ray1.70A36-93[»]
    7PTIX-ray1.60A36-93[»]
    8PTIX-ray1.80A36-93[»]
    9PTIX-ray1.22A36-93[»]
    DisProtiDP00729.
    ProteinModelPortaliP00974.
    SMRiP00974. Positions 36-93.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00974.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 9051BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG3540.
    HOGENOMiHOG000007327.
    HOVERGENiHBG006193.
    InParanoidiP00974.

    Family and domain databases

    Gene3Di4.10.410.10. 1 hit.
    InterProiIPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    [Graphical view]
    PfamiPF00014. Kunitz_BPTI. 1 hit.
    [Graphical view]
    PRINTSiPR00759. BASICPTASE.
    SMARTiSM00131. KU. 1 hit.
    [Graphical view]
    SUPFAMiSSF57362. SSF57362. 1 hit.
    PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
    PS50279. BPTI_KUNITZ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00974-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKMSRLCLSV ALLVLLGTLA ASTPGCDTSN QAKAQRPDFC LEPPYTGPCK    50
    ARIIRYFYNA KAGLCQTFVY GGCRAKRNNF KSAEDCMRTC GGAIGPWENL 100
    Length:100
    Mass (Da):10,903
    Last modified:July 1, 1989 - v2
    Checksum:i6A778A4AD763FB19
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20934, M20930, M20932 Genomic DNA. Translation: AAD13685.1.
    X03365 Genomic DNA. Translation: CAA27062.1. Sequence problems.
    X03365 Genomic DNA. Translation: CAA27063.1.
    X05274 mRNA. Translation: CAA28886.1.
    PIRiS00277. TIBO.
    UniGeneiBt.28518.

    Cross-referencesi

    Web resourcesi

    Trasylol

    Clinical information on Trasylol

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20934 , M20930 , M20932 Genomic DNA. Translation: AAD13685.1 .
    X03365 Genomic DNA. Translation: CAA27062.1 . Sequence problems.
    X03365 Genomic DNA. Translation: CAA27063.1 .
    X05274 mRNA. Translation: CAA28886.1 .
    PIRi S00277. TIBO.
    UniGenei Bt.28518.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AAL X-ray 1.60 A/B 36-93 [» ]
    1B0C X-ray 2.80 A/B/C/D/E 36-91 [» ]
    1BHC X-ray 2.70 A/B/C/D/E/F/G/H/I/J 36-93 [» ]
    1BPI X-ray 1.09 A 36-93 [» ]
    1BPT X-ray 2.00 A 36-93 [» ]
    1BRB X-ray 2.10 I 36-93 [» ]
    1BTH X-ray 2.30 P/Q 36-93 [» ]
    1BTI X-ray 2.20 A 36-93 [» ]
    1BZ5 X-ray 2.58 A/B/C/D/E 36-93 [» ]
    1BZX X-ray 2.10 I 36-93 [» ]
    1CBW X-ray 2.60 D/I 36-93 [» ]
    1CO7 X-ray 1.90 I 2-100 [» ]
    1D0D X-ray 1.62 B 36-93 [» ]
    1EAW X-ray 2.93 B/D 36-93 [» ]
    1EJM X-ray 1.85 B/D/F 36-93 [» ]
    1F5R X-ray 1.65 I 36-100 [» ]
    1F7Z X-ray 1.55 I 36-100 [» ]
    1FAK X-ray 2.10 I 37-90 [» ]
    1FAN X-ray 2.00 A 36-93 [» ]
    1FY8 X-ray 1.70 I 36-93 [» ]
    1G6X X-ray 0.86 A 36-93 [» ]
    1JV8 NMR - A 36-93 [» ]
    1JV9 NMR - A 36-93 [» ]
    1K09 NMR - A/B 50-73 [» ]
    1K6U X-ray 1.00 A 36-93 [» ]
    1LD5 NMR - A 36-93 [» ]
    1LD6 NMR - A 36-93 [» ]
    1MTN X-ray 2.80 D/H 36-93 [» ]
    1NAG X-ray 1.90 A 36-93 [» ]
    1OA5 NMR - 5 36-93 [» ]
    1OA6 NMR - 5 36-93 [» ]
    1P2I X-ray 1.65 I 36-93 [» ]
    1P2J X-ray 1.35 I 36-93 [» ]
    1P2K X-ray 1.60 I 36-93 [» ]
    1P2M X-ray 1.75 B/D 36-93 [» ]
    1P2N X-ray 1.80 B/D 36-93 [» ]
    1P2O X-ray 2.00 B/D 36-93 [» ]
    1P2Q X-ray 1.80 B/D 36-93 [» ]
    1PIT NMR - A 36-93 [» ]
    1QLQ X-ray 1.42 A 36-93 [» ]
    1T7C X-ray 1.85 B/D 36-93 [» ]
    1T8L X-ray 1.75 B/D 36-93 [» ]
    1T8M X-ray 1.80 B/D 36-93 [» ]
    1T8N X-ray 1.75 B/D 36-93 [» ]
    1T8O X-ray 1.70 B/D 36-93 [» ]
    1TPA X-ray 1.90 I 36-93 [» ]
    1UUA NMR - A 38-93 [» ]
    1UUB NMR - A 38-93 [» ]
    1YKT X-ray 1.70 B 36-91 [» ]
    1YLC X-ray 1.70 B 36-91 [» ]
    1YLD X-ray 1.70 B 36-91 [» ]
    2FI3 X-ray 1.58 I 36-93 [» ]
    2FI4 X-ray 1.58 I 36-93 [» ]
    2FI5 X-ray 1.58 I 36-93 [» ]
    2FTL X-ray 1.62 I 36-93 [» ]
    2FTM X-ray 1.65 B 36-93 [» ]
    2HEX X-ray 2.10 A/B/C/D/E 36-93 [» ]
    2IJO X-ray 2.30 I 36-93 [» ]
    2KAI X-ray 2.50 I 36-93 [» ]
    2PTC X-ray 1.90 I 36-93 [» ]
    2R9P X-ray 1.40 E/F/G/I 36-93 [» ]
    2RA3 X-ray 1.46 C/I 36-93 [» ]
    2TGP X-ray 1.90 I 36-93 [» ]
    2TPI X-ray 2.10 I 36-93 [» ]
    2ZJX X-ray 1.09 A/B 36-93 [» ]
    2ZVX X-ray 1.09 A/B 36-93 [» ]
    3BTD X-ray 1.90 I 36-93 [» ]
    3BTE X-ray 1.85 I 36-93 [» ]
    3BTF X-ray 1.80 I 36-93 [» ]
    3BTG X-ray 1.90 I 36-93 [» ]
    3BTH X-ray 1.75 I 36-93 [» ]
    3BTK X-ray 1.85 I 36-93 [» ]
    3BTM X-ray 1.80 I 36-93 [» ]
    3BTQ X-ray 1.90 I 36-93 [» ]
    3BTT X-ray 1.90 I 36-93 [» ]
    3BTW X-ray 2.05 I 36-93 [» ]
    3FP6 X-ray 1.49 I 36-93 [» ]
    3FP7 X-ray 1.46 I 36-50 [» ]
    J 51-93 [» ]
    3FP8 X-ray 1.46 I 36-93 [» ]
    3GYM X-ray 2.80 I/J 36-93 [» ]
    3LDI X-ray 2.20 A/B/C/D/E 36-93 [» ]
    3LDJ X-ray 1.70 A/B/C 36-93 [» ]
    3LDM X-ray 2.60 A/B/C/D/E 36-93 [» ]
    3OTJ Other 2.15 I 36-93 [» ]
    3P92 X-ray 1.60 E 36-93 [» ]
    3P95 X-ray 1.30 E 36-93 [» ]
    3TGI X-ray 1.80 I 36-100 [» ]
    3TGJ X-ray 2.20 I 36-100 [» ]
    3TGK X-ray 1.70 I 36-100 [» ]
    3TPI X-ray 1.90 I 36-93 [» ]
    3U1J X-ray 1.80 E 36-93 [» ]
    4BNR X-ray 2.00 I/J 1-100 [» ]
    4DG4 X-ray 1.40 C/E/F/H 36-93 [» ]
    4PTI X-ray 1.50 A 36-93 [» ]
    4TPI X-ray 2.20 I 36-93 [» ]
    5PTI X-ray 1.00 A 36-93 [» ]
    6PTI X-ray 1.70 A 36-93 [» ]
    7PTI X-ray 1.60 A 36-93 [» ]
    8PTI X-ray 1.80 A 36-93 [» ]
    9PTI X-ray 1.22 A 36-93 [» ]
    DisProti DP00729.
    ProteinModelPortali P00974.
    SMRi P00974. Positions 36-93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6113N.
    IntActi P00974. 5 interactions.
    MINTi MINT-90698.
    STRINGi 9913.ENSBTAP00000023042.

    Protein family/group databases

    Allergomei 3890. Bos d TI.
    MEROPSi I02.001.

    Proteomic databases

    PRIDEi P00974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi KOG3540.
    HOGENOMi HOG000007327.
    HOVERGENi HBG006193.
    InParanoidi P00974.

    Miscellaneous databases

    EvolutionaryTracei P00974.

    Family and domain databases

    Gene3Di 4.10.410.10. 1 hit.
    InterProi IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    [Graphical view ]
    Pfami PF00014. Kunitz_BPTI. 1 hit.
    [Graphical view ]
    PRINTSi PR00759. BASICPTASE.
    SMARTi SM00131. KU. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57362. SSF57362. 1 hit.
    PROSITEi PS00280. BPTI_KUNITZ_1. 1 hit.
    PS50279. BPTI_KUNITZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequences of the genes and polypeptide precursors for two bovine protease inhibitors."
      Creighton T.E., Charles I.G.
      J. Mol. Biol. 194:11-22(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Biosynthesis, processing, and evolution of bovine pancreatic trypsin inhibitor."
      Creighton T.E., Charles I.G.
      Cold Spring Harb. Symp. Quant. Biol. 52:511-519(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "Sequences encoding two trypsin inhibitors occur in strikingly similar genomic environments."
      Kingston I.B., Anderson S.
      Biochem. J. 233:443-450(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-97.
    4. "Isolation of a genomic clone for bovine pancreatic trypsin inhibitor by using a unique-sequence synthetic DNA probe."
      Anderson S., Kingston I.B.
      Proc. Natl. Acad. Sci. U.S.A. 80:6838-6842(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-97.
    5. "The basic trypsin inhibitor of bovine pancreas. V. The disulfide linkages."
      Kassell B., Laskowski M.
      Biochem. Biophys. Res. Commun. 20:463-468(1965) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-93, DISULFIDE BONDS.
    6. "The disulfide linkages in kallikrein inactivator of bovine lung."
      Anderer F.A., Hornle S.
      J. Biol. Chem. 241:1568-1572(1966) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-93, DISULFIDE BONDS.
    7. "Covalent structure of a polypeptide inhibitor of trypsin (Kunitz and Northrop inhibitor)."
      Chauvet J., Acher R.
      Bull. Soc. Chim. Biol. 49:985-1000(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-93, DISULFIDE BONDS.
    8. "Sequence of residues 18-20 in pancreatic trypsin inhibitor."
      Dlouha V., Pospisilova D., Meloun B., Sorm F.
      Collect. Czech. Chem. Commun. 33:1363-1365(1968)
      Cited for: PROTEIN SEQUENCE OF 36-93.
    9. "Presence of pancreatic trypsin inhibitor in adrenal medullary chromaffin cells."
      Lewis R.V., Ray P., Coguill R., Kruggel W.
      Biochem. Biophys. Res. Commun. 167:543-547(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-81.
      Tissue: Adrenal chromaffin.
    10. "Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5-A resolution."
      Deisenhofer J., Steigemann W.
      Acta Crystallogr. B 31:238-250(1975)
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
    11. "The basic trypsin inhibitor of bovine pancreas. I. Structure analysis and conformation of the polypeptide chain."
      Huber R., Kukla D., Ruhlmann A., Epp O., Formanek H.
      Naturwissenschaften 57:389-392(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    12. "Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitor."
      Housset D., Kim K.-S., Fuchs J., Woodward C., Wlodawer A.
      J. Mol. Biol. 220:757-770(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLY-70.
    13. "Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures."
      Berndt K.D., Guntert P., Orbons L.P.M., Wuethrich K.
      J. Mol. Biol. 227:757-775(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiBPT1_BOVIN
    AccessioniPrimary (citable) accession number: P00974
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3