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P61823

- RNAS1_BOVIN

UniProt

P61823 - RNAS1_BOVIN

Protein

Ribonuclease pancreatic

Gene

RNASE1

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

    Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.1 Publication

    Catalytic activityi

    Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331Substrate
    Binding sitei36 – 361Substrate
    Active sitei38 – 381Proton acceptor
    Binding sitei92 – 921Substrate
    Binding sitei111 – 1111Substrate
    Active sitei145 – 1451Proton donor

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. pancreatic ribonuclease activity Source: UniProtKB-EC
    3. protein binding Source: IntAct

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Enzyme and pathway databases

    BRENDAi3.1.27.5. 908.
    SABIO-RKP61823.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease pancreatic (EC:3.1.27.5)
    Alternative name(s):
    RNase 1
    RNase A
    Gene namesi
    Name:RNASE1
    Synonyms:RNS1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 10

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381H → A: Loss of activity.
    Mutagenesisi145 – 1451H → A: Loss of activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26262 PublicationsAdd
    BLAST
    Chaini27 – 150124Ribonuclease pancreaticPRO_0000030915Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi27 – 271N-linked (Glc) (glycation); in vitro
    Glycosylationi33 – 331N-linked (Glc) (glycation); in vitro
    Disulfide bondi52 ↔ 1101 Publication
    Glycosylationi60 – 601N-linked (GlcNAc...); partial1 PublicationCAR_000006
    Glycosylationi63 – 631N-linked (Glc) (glycation); in vitro
    Disulfide bondi66 ↔ 1211 Publication
    Glycosylationi67 – 671N-linked (Glc) (glycation); in vitro
    Disulfide bondi84 ↔ 1361 Publication
    Disulfide bondi91 ↔ 981 Publication

    Keywords - PTMi

    Disulfide bond, Glycation, Glycoprotein

    Proteomic databases

    PaxDbiP61823.
    PRIDEiP61823.

    Miscellaneous databases

    PMAP-CutDBP61823.

    Expressioni

    Tissue specificityi

    Pancreas.

    Interactioni

    Subunit structurei

    Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein By similarity. Monomer.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDI1P179672EBI-908364,EBI-13012From a different organism.
    RNH1P134893EBI-908364,EBI-1237106From a different organism.

    Protein-protein interaction databases

    BioGridi159601. 1 interaction.
    DIPiDIP-36384N.
    IntActiP61823. 6 interactions.
    MINTiMINT-1510416.
    STRINGi9913.ENSBTAP00000011586.

    Structurei

    Secondary structure

    1
    150
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 389
    Beta strandi43 – 453
    Helixi48 – 503
    Helixi51 – 588
    Beta strandi61 – 655
    Beta strandi68 – 736
    Helixi77 – 826
    Helixi83 – 853
    Beta strandi86 – 894
    Beta strandi92 – 943
    Beta strandi98 – 1003
    Beta strandi102 – 11211
    Beta strandi113 – 1153
    Beta strandi118 – 1203
    Beta strandi123 – 1308
    Beta strandi132 – 1376
    Turni138 – 1414
    Beta strandi142 – 1498

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A2WX-ray2.10A/B27-150[»]
    1A5PX-ray1.60A27-150[»]
    1A5QX-ray2.30A27-150[»]
    1AFKX-ray1.70A/B27-150[»]
    1AFLX-ray1.70A/B27-150[»]
    1AFUX-ray2.00A/B27-150[»]
    1AQPX-ray2.00A27-150[»]
    1B6VX-ray2.00A/B27-150[»]
    1BELX-ray1.60A27-150[»]
    1BZQX-ray2.80A/B/C/D27-150[»]
    1C0BX-ray1.90A23-150[»]
    1C0CX-ray2.00A23-150[»]
    1C8WX-ray1.80A27-150[»]
    1C9VX-ray1.70A27-150[»]
    1C9XX-ray1.80A27-150[»]
    1CJQX-ray3.00A27-41[»]
    B50-150[»]
    1CJRX-ray2.30A27-41[»]
    B50-150[»]
    1D5DX-ray2.25A27-41[»]
    B50-150[»]
    1D5EX-ray2.25A27-41[»]
    B50-150[»]
    1D5HX-ray2.25A27-41[»]
    B50-150[»]
    1DFJX-ray2.50E27-150[»]
    1DY5X-ray0.87A/B27-150[»]
    1EICX-ray1.40A27-150[»]
    1EIDX-ray1.40A27-150[»]
    1EIEX-ray1.40A27-150[»]
    1EOSX-ray2.00A/B27-150[»]
    1EOWX-ray2.00A27-150[»]
    1F0VX-ray1.70A/B/C/D27-150[»]
    1FEVX-ray2.25A27-41[»]
    B50-150[»]
    1FS3X-ray1.40A27-150[»]
    1GV7X-ray2.10A84-111[»]
    1IZPX-ray1.50A27-150[»]
    1IZQX-ray1.80A27-150[»]
    1IZRX-ray1.50A27-150[»]
    1J7ZX-ray2.25A27-41[»]
    B47-150[»]
    1J80X-ray2.10A27-41[»]
    B47-150[»]
    1J81X-ray2.20A27-41[»]
    B47-150[»]
    1J82X-ray2.30A27-41[»]
    B47-150[»]
    1JN4X-ray1.80A/B27-150[»]
    1JS0X-ray2.20A/B/C27-150[»]
    1JVTX-ray2.05A/B27-150[»]
    1JVUX-ray1.78A/B27-150[»]
    1JVVX-ray2.20A/B27-150[»]
    1KF2X-ray1.10A27-150[»]
    1KF3X-ray1.05A27-150[»]
    1KF4X-ray1.10A27-150[»]
    1KF5X-ray1.15A27-150[»]
    1KF7X-ray1.15A27-150[»]
    1KF8X-ray1.15A27-150[»]
    1KH8X-ray2.00A27-150[»]
    1LSQX-ray1.90A/B27-150[»]
    1O0FX-ray1.50A/B27-150[»]
    1O0HX-ray1.20A/B27-150[»]
    1O0MX-ray1.50A/B27-150[»]
    1O0NX-ray1.50A/B27-150[»]
    1O0OX-ray1.20A/B27-150[»]
    1QHCX-ray1.70A/B27-150[»]
    1RARX-ray1.90A28-150[»]
    1RASX-ray1.70A28-150[»]
    1RATX-ray1.50A27-150[»]
    1RBBX-ray2.50A/B27-150[»]
    1RBCX-ray2.00A47-150[»]
    S27-41[»]
    1RBDX-ray1.70A47-150[»]
    S27-41[»]
    1RBEX-ray1.75A47-150[»]
    S27-41[»]
    1RBFX-ray1.80A47-150[»]
    S27-41[»]
    1RBGX-ray1.80A47-150[»]
    S27-41[»]
    1RBHX-ray1.70A47-150[»]
    S27-41[»]
    1RBIX-ray1.80A47-150[»]
    S27-41[»]
    1RBJX-ray2.70A27-150[»]
    1RBNX-ray2.10A27-150[»]
    1RBWX-ray1.69A27-150[»]
    1RBXX-ray1.69A27-150[»]
    1RCAX-ray1.90A27-150[»]
    1RCNX-ray2.32E27-150[»]
    1RHAX-ray1.80A27-150[»]
    1RHBX-ray1.50A27-150[»]
    1RNCX-ray1.50A27-150[»]
    1RNDX-ray1.50A27-150[»]
    1RNMX-ray2.00E27-150[»]
    1RNNX-ray1.80E27-150[»]
    1RNOX-ray1.90A27-150[»]
    1RNQX-ray2.00A27-150[»]
    1RNUX-ray1.60A27-150[»]
    1RNVX-ray1.60A27-150[»]
    1RNWX-ray1.80A27-150[»]
    1RNXX-ray1.90A27-150[»]
    1RNYX-ray2.00A27-150[»]
    1RNZX-ray1.90A27-150[»]
    1ROBX-ray1.60A27-150[»]
    1RPFX-ray2.20A27-150[»]
    1RPGX-ray1.40A27-150[»]
    1RPHX-ray2.20A27-150[»]
    1RSMX-ray2.00A27-150[»]
    1RTAX-ray2.50E27-150[»]
    1RTBX-ray2.50A27-150[»]
    1RUVX-ray1.25A27-150[»]
    1SRNX-ray1.80A27-144[»]
    B137-150[»]
    1SSAX-ray2.00A27-144[»]
    B137-150[»]
    1SSBX-ray2.00A27-144[»]
    B137-150[»]
    1SSCX-ray2.00A27-138[»]
    B140-150[»]
    1U1BX-ray2.00A/B27-150[»]
    1UN5X-ray2.60A-[»]
    1W4OX-ray1.60A/B27-150[»]
    1W4PX-ray1.69A/B27-150[»]
    1W4QX-ray1.68A/B27-150[»]
    1WBUX-ray1.90A/B27-150[»]
    1XPSX-ray1.80A/B27-150[»]
    1XPTX-ray1.90A/B27-150[»]
    1YMNX-ray1.45A27-150[»]
    1YMRX-ray1.50A27-150[»]
    1YMWX-ray1.50A27-150[»]
    1Z3LX-ray1.80E47-150[»]
    S27-41[»]
    1Z3MX-ray2.00E47-150[»]
    S27-41[»]
    1Z3PX-ray2.00E47-150[»]
    S27-41[»]
    1Z6DX-ray1.54A/B27-150[»]
    1Z6SX-ray1.50A/B27-150[»]
    2AASNMR-A27-150[»]
    2APQX-ray1.80A27-150[»]
    2APUmodel-0/1/2/3/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z27-150[»]
    2BLPX-ray1.40A27-150[»]
    2BLZX-ray1.40A27-150[»]
    2E33X-ray2.70B27-150[»]
    2E3WX-ray1.05A27-150[»]
    2G4WX-ray1.84A/B27-150[»]
    2G4XX-ray1.95A27-150[»]
    2G8QX-ray1.50A/B27-150[»]
    2G8RX-ray1.70A/B27-150[»]
    2NUIX-ray1.10A27-150[»]
    2OP2X-ray1.60A27-150[»]
    2OQFX-ray2.30A/B/C/D27-150[»]
    2P42X-ray1.80A/C27-150[»]
    2P43X-ray1.65A27-150[»]
    2P44X-ray1.80A27-150[»]
    2P45X-ray1.10A27-150[»]
    2P46X-ray2.50A/C27-150[»]
    2P47X-ray2.50A27-150[»]
    2P48X-ray2.30A27-150[»]
    2P49X-ray1.38A27-150[»]
    2P4AX-ray1.90A/C27-150[»]
    2QCAX-ray1.33A27-150[»]
    2RATX-ray1.50A27-150[»]
    2RLNX-ray1.85E42-150[»]
    S27-41[»]
    2RNSX-ray1.60A27-150[»]
    2W5GX-ray1.70A/B27-150[»]
    2W5IX-ray2.40A/B27-150[»]
    2W5KX-ray1.70A/B27-150[»]
    2W5LX-ray1.70A/B27-150[»]
    2W5MX-ray1.80A/B27-150[»]
    2XOGX-ray1.72A/B27-150[»]
    2XOIX-ray1.72A/B27-150[»]
    3A1Rneutron diffraction1.70A27-150[»]
    3D6OX-ray1.58A/B27-150[»]
    3D6PX-ray1.60A/B27-150[»]
    3D6QX-ray1.60A/B27-150[»]
    3D7BX-ray1.60A/B27-150[»]
    3D8YX-ray1.72A/B27-150[»]
    3D8ZX-ray1.98A/B27-150[»]
    3DH5X-ray1.60A27-150[»]
    3DH6X-ray1.60A27-150[»]
    3DI7X-ray1.60A27-150[»]
    3DI8X-ray1.60A27-150[»]
    3DI9X-ray2.00A27-150[»]
    3DIBX-ray1.40A27-150[»]
    3DICX-ray1.60A27-150[»]
    3DXGX-ray1.39A/B27-150[»]
    3DXHX-ray1.40A/B27-150[»]
    3EUXX-ray1.65A/B27-150[»]
    3EUYX-ray1.95A/B27-150[»]
    3EUZX-ray1.84A/B27-150[»]
    3EV0X-ray1.76A/B27-150[»]
    3EV1X-ray2.00A/B27-150[»]
    3EV2X-ray2.02A/B27-150[»]
    3EV3X-ray1.68A/B27-150[»]
    3EV4X-ray1.93A/B27-150[»]
    3EV5X-ray1.68A/B27-150[»]
    3EV6X-ray1.76A/B27-150[»]
    3FKZX-ray1.99A/B27-150[»]
    3FL0X-ray1.94A/B27-150[»]
    3FL1X-ray1.90A/B27-150[»]
    3FL3X-ray1.60A/B27-150[»]
    3I67X-ray1.30A27-150[»]
    3I6FX-ray1.30A27-150[»]
    3I6HX-ray1.30A27-150[»]
    3I6JX-ray1.30A27-150[»]
    3I7WX-ray2.35A27-150[»]
    3I7XX-ray2.60A27-150[»]
    3I7YX-ray2.40A27-150[»]
    3JW1X-ray1.60A/B27-150[»]
    3LXOX-ray1.55A27-150[»]
    3MWQX-ray1.68A26-150[»]
    3MWRX-ray1.85A27-150[»]
    3MX8X-ray2.10A26-150[»]
    3MZQX-ray1.50A23-150[»]
    3MZRX-ray1.50A23-150[»]
    3OQYX-ray1.49A/B47-150[»]
    a/b27-41[»]
    3OQZX-ray2.50A/B47-150[»]
    a/b27-41[»]
    3OR0X-ray2.30A/B47-150[»]
    a/b27-41[»]
    3QL1X-ray1.29A27-150[»]
    3QL2X-ray1.49A/B27-150[»]
    3QSKX-ray1.75A27-150[»]
    3RATX-ray1.50A27-150[»]
    3RH1X-ray2.10A27-150[»]
    3RIDX-ray2.18A/B/C/D27-150[»]
    3RN3X-ray1.45A27-150[»]
    3RSDX-ray1.60A27-150[»]
    3RSKX-ray2.00A27-150[»]
    3RSPX-ray1.70A27-150[»]
    3SRNX-ray2.00A27-139[»]
    B140-146[»]
    4AO1X-ray1.58A27-150[»]
    4G8VX-ray1.70A/B27-150[»]
    4G8YX-ray1.80A/B27-150[»]
    4G90X-ray1.90A/B27-150[»]
    4J5ZX-ray1.80A27-150[»]
    4J60X-ray1.69A27-150[»]
    4J61X-ray1.69A27-150[»]
    4J62X-ray2.04A27-150[»]
    4J63X-ray2.04A27-150[»]
    4J64X-ray1.78A27-150[»]
    4J65X-ray1.96A27-150[»]
    4J66X-ray2.04A27-150[»]
    4J67X-ray1.86A27-150[»]
    4J68X-ray1.78A27-150[»]
    4J69X-ray1.89A27-150[»]
    4J6AX-ray2.04A27-150[»]
    4K7LX-ray1.38A27-41[»]
    B47-150[»]
    4K7MX-ray1.80A27-150[»]
    4L55X-ray1.65A/B27-150[»]
    4MXFX-ray2.25A/B27-150[»]
    4O36X-ray1.22A27-41[»]
    B47-150[»]
    4O37X-ray1.40A27-41[»]
    B47-150[»]
    4RATX-ray1.50A27-150[»]
    4RSDX-ray1.60A27-150[»]
    4RSKX-ray2.10A27-150[»]
    4SRNX-ray2.00A27-139[»]
    B140-150[»]
    5RATX-ray1.50A27-150[»]
    5RSAX-ray2.00A27-150[»]
    6RATX-ray1.50A27-150[»]
    6RSAX-ray2.00A27-150[»]
    7RATX-ray1.50A27-150[»]
    7RSAX-ray1.26A27-150[»]
    8RATX-ray1.50A27-150[»]
    8RSAX-ray1.80A/B27-150[»]
    9RATX-ray1.50A27-150[»]
    9RSAX-ray1.80A/B27-150[»]
    ProteinModelPortaliP61823.
    SMRiP61823. Positions 27-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61823.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni67 – 715Substrate binding

    Sequence similaritiesi

    Belongs to the pancreatic ribonuclease family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40319.
    GeneTreeiENSGT00390000007840.
    HOGENOMiHOG000276883.
    HOVERGENiHBG008396.
    InParanoidiP61823.
    KOiK01168.
    OMAiANKHIIV.
    OrthoDBiEOG7J1826.
    TreeFamiTF333393.

    Family and domain databases

    Gene3Di3.10.130.10. 1 hit.
    InterProiIPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view]
    PANTHERiPTHR11437. PTHR11437. 1 hit.
    PfamiPF00074. RnaseA. 1 hit.
    [Graphical view]
    PRINTSiPR00794. RIBONUCLEASE.
    ProDomiPD000535. RNaseA. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00092. RNAse_Pc. 1 hit.
    [Graphical view]
    SUPFAMiSSF54076. SSF54076. 1 hit.
    PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P61823-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALKSLVLLS LLVLVLLLVR VQPSLGKETA AAKFERQHMD SSTSAASSSN    50
    YCNQMMKSRN LTKDRCKPVN TFVHESLADV QAVCSQKNVA CKNGQTNCYQ 100
    SYSTMSITDC RETGSSKYPN CAYKTTQANK HIIVACEGNP YVPVHFDASV 150
    Length:150
    Mass (Da):16,461
    Last modified:June 7, 2004 - v1
    Checksum:i74E5DC61E679187D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07283 Genomic DNA. Translation: CAA30263.1.
    BC149529 mRNA. Translation: AAI49530.1.
    BC149636 mRNA. Translation: AAI49637.1.
    S80747 mRNA. Translation: AAB35594.1.
    S81740 Genomic DNA. Translation: AAB36134.1.
    PIRiS00897. NRBO.
    RefSeqiNP_001014408.2. NM_001014386.4.
    XP_005211519.1. XM_005211462.1.
    UniGeneiBt.4630.

    Genome annotation databases

    EnsembliENSBTAT00000011586; ENSBTAP00000011586; ENSBTAG00000008793.
    GeneIDi282340.
    KEGGibta:282340.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual
    Functional Glycomics Gateway - Glycan Binding

    RNase A

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07283 Genomic DNA. Translation: CAA30263.1 .
    BC149529 mRNA. Translation: AAI49530.1 .
    BC149636 mRNA. Translation: AAI49637.1 .
    S80747 mRNA. Translation: AAB35594.1 .
    S81740 Genomic DNA. Translation: AAB36134.1 .
    PIRi S00897. NRBO.
    RefSeqi NP_001014408.2. NM_001014386.4.
    XP_005211519.1. XM_005211462.1.
    UniGenei Bt.4630.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A2W X-ray 2.10 A/B 27-150 [» ]
    1A5P X-ray 1.60 A 27-150 [» ]
    1A5Q X-ray 2.30 A 27-150 [» ]
    1AFK X-ray 1.70 A/B 27-150 [» ]
    1AFL X-ray 1.70 A/B 27-150 [» ]
    1AFU X-ray 2.00 A/B 27-150 [» ]
    1AQP X-ray 2.00 A 27-150 [» ]
    1B6V X-ray 2.00 A/B 27-150 [» ]
    1BEL X-ray 1.60 A 27-150 [» ]
    1BZQ X-ray 2.80 A/B/C/D 27-150 [» ]
    1C0B X-ray 1.90 A 23-150 [» ]
    1C0C X-ray 2.00 A 23-150 [» ]
    1C8W X-ray 1.80 A 27-150 [» ]
    1C9V X-ray 1.70 A 27-150 [» ]
    1C9X X-ray 1.80 A 27-150 [» ]
    1CJQ X-ray 3.00 A 27-41 [» ]
    B 50-150 [» ]
    1CJR X-ray 2.30 A 27-41 [» ]
    B 50-150 [» ]
    1D5D X-ray 2.25 A 27-41 [» ]
    B 50-150 [» ]
    1D5E X-ray 2.25 A 27-41 [» ]
    B 50-150 [» ]
    1D5H X-ray 2.25 A 27-41 [» ]
    B 50-150 [» ]
    1DFJ X-ray 2.50 E 27-150 [» ]
    1DY5 X-ray 0.87 A/B 27-150 [» ]
    1EIC X-ray 1.40 A 27-150 [» ]
    1EID X-ray 1.40 A 27-150 [» ]
    1EIE X-ray 1.40 A 27-150 [» ]
    1EOS X-ray 2.00 A/B 27-150 [» ]
    1EOW X-ray 2.00 A 27-150 [» ]
    1F0V X-ray 1.70 A/B/C/D 27-150 [» ]
    1FEV X-ray 2.25 A 27-41 [» ]
    B 50-150 [» ]
    1FS3 X-ray 1.40 A 27-150 [» ]
    1GV7 X-ray 2.10 A 84-111 [» ]
    1IZP X-ray 1.50 A 27-150 [» ]
    1IZQ X-ray 1.80 A 27-150 [» ]
    1IZR X-ray 1.50 A 27-150 [» ]
    1J7Z X-ray 2.25 A 27-41 [» ]
    B 47-150 [» ]
    1J80 X-ray 2.10 A 27-41 [» ]
    B 47-150 [» ]
    1J81 X-ray 2.20 A 27-41 [» ]
    B 47-150 [» ]
    1J82 X-ray 2.30 A 27-41 [» ]
    B 47-150 [» ]
    1JN4 X-ray 1.80 A/B 27-150 [» ]
    1JS0 X-ray 2.20 A/B/C 27-150 [» ]
    1JVT X-ray 2.05 A/B 27-150 [» ]
    1JVU X-ray 1.78 A/B 27-150 [» ]
    1JVV X-ray 2.20 A/B 27-150 [» ]
    1KF2 X-ray 1.10 A 27-150 [» ]
    1KF3 X-ray 1.05 A 27-150 [» ]
    1KF4 X-ray 1.10 A 27-150 [» ]
    1KF5 X-ray 1.15 A 27-150 [» ]
    1KF7 X-ray 1.15 A 27-150 [» ]
    1KF8 X-ray 1.15 A 27-150 [» ]
    1KH8 X-ray 2.00 A 27-150 [» ]
    1LSQ X-ray 1.90 A/B 27-150 [» ]
    1O0F X-ray 1.50 A/B 27-150 [» ]
    1O0H X-ray 1.20 A/B 27-150 [» ]
    1O0M X-ray 1.50 A/B 27-150 [» ]
    1O0N X-ray 1.50 A/B 27-150 [» ]
    1O0O X-ray 1.20 A/B 27-150 [» ]
    1QHC X-ray 1.70 A/B 27-150 [» ]
    1RAR X-ray 1.90 A 28-150 [» ]
    1RAS X-ray 1.70 A 28-150 [» ]
    1RAT X-ray 1.50 A 27-150 [» ]
    1RBB X-ray 2.50 A/B 27-150 [» ]
    1RBC X-ray 2.00 A 47-150 [» ]
    S 27-41 [» ]
    1RBD X-ray 1.70 A 47-150 [» ]
    S 27-41 [» ]
    1RBE X-ray 1.75 A 47-150 [» ]
    S 27-41 [» ]
    1RBF X-ray 1.80 A 47-150 [» ]
    S 27-41 [» ]
    1RBG X-ray 1.80 A 47-150 [» ]
    S 27-41 [» ]
    1RBH X-ray 1.70 A 47-150 [» ]
    S 27-41 [» ]
    1RBI X-ray 1.80 A 47-150 [» ]
    S 27-41 [» ]
    1RBJ X-ray 2.70 A 27-150 [» ]
    1RBN X-ray 2.10 A 27-150 [» ]
    1RBW X-ray 1.69 A 27-150 [» ]
    1RBX X-ray 1.69 A 27-150 [» ]
    1RCA X-ray 1.90 A 27-150 [» ]
    1RCN X-ray 2.32 E 27-150 [» ]
    1RHA X-ray 1.80 A 27-150 [» ]
    1RHB X-ray 1.50 A 27-150 [» ]
    1RNC X-ray 1.50 A 27-150 [» ]
    1RND X-ray 1.50 A 27-150 [» ]
    1RNM X-ray 2.00 E 27-150 [» ]
    1RNN X-ray 1.80 E 27-150 [» ]
    1RNO X-ray 1.90 A 27-150 [» ]
    1RNQ X-ray 2.00 A 27-150 [» ]
    1RNU X-ray 1.60 A 27-150 [» ]
    1RNV X-ray 1.60 A 27-150 [» ]
    1RNW X-ray 1.80 A 27-150 [» ]
    1RNX X-ray 1.90 A 27-150 [» ]
    1RNY X-ray 2.00 A 27-150 [» ]
    1RNZ X-ray 1.90 A 27-150 [» ]
    1ROB X-ray 1.60 A 27-150 [» ]
    1RPF X-ray 2.20 A 27-150 [» ]
    1RPG X-ray 1.40 A 27-150 [» ]
    1RPH X-ray 2.20 A 27-150 [» ]
    1RSM X-ray 2.00 A 27-150 [» ]
    1RTA X-ray 2.50 E 27-150 [» ]
    1RTB X-ray 2.50 A 27-150 [» ]
    1RUV X-ray 1.25 A 27-150 [» ]
    1SRN X-ray 1.80 A 27-144 [» ]
    B 137-150 [» ]
    1SSA X-ray 2.00 A 27-144 [» ]
    B 137-150 [» ]
    1SSB X-ray 2.00 A 27-144 [» ]
    B 137-150 [» ]
    1SSC X-ray 2.00 A 27-138 [» ]
    B 140-150 [» ]
    1U1B X-ray 2.00 A/B 27-150 [» ]
    1UN5 X-ray 2.60 A - [» ]
    1W4O X-ray 1.60 A/B 27-150 [» ]
    1W4P X-ray 1.69 A/B 27-150 [» ]
    1W4Q X-ray 1.68 A/B 27-150 [» ]
    1WBU X-ray 1.90 A/B 27-150 [» ]
    1XPS X-ray 1.80 A/B 27-150 [» ]
    1XPT X-ray 1.90 A/B 27-150 [» ]
    1YMN X-ray 1.45 A 27-150 [» ]
    1YMR X-ray 1.50 A 27-150 [» ]
    1YMW X-ray 1.50 A 27-150 [» ]
    1Z3L X-ray 1.80 E 47-150 [» ]
    S 27-41 [» ]
    1Z3M X-ray 2.00 E 47-150 [» ]
    S 27-41 [» ]
    1Z3P X-ray 2.00 E 47-150 [» ]
    S 27-41 [» ]
    1Z6D X-ray 1.54 A/B 27-150 [» ]
    1Z6S X-ray 1.50 A/B 27-150 [» ]
    2AAS NMR - A 27-150 [» ]
    2APQ X-ray 1.80 A 27-150 [» ]
    2APU model - 0/1/2/3/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z 27-150 [» ]
    2BLP X-ray 1.40 A 27-150 [» ]
    2BLZ X-ray 1.40 A 27-150 [» ]
    2E33 X-ray 2.70 B 27-150 [» ]
    2E3W X-ray 1.05 A 27-150 [» ]
    2G4W X-ray 1.84 A/B 27-150 [» ]
    2G4X X-ray 1.95 A 27-150 [» ]
    2G8Q X-ray 1.50 A/B 27-150 [» ]
    2G8R X-ray 1.70 A/B 27-150 [» ]
    2NUI X-ray 1.10 A 27-150 [» ]
    2OP2 X-ray 1.60 A 27-150 [» ]
    2OQF X-ray 2.30 A/B/C/D 27-150 [» ]
    2P42 X-ray 1.80 A/C 27-150 [» ]
    2P43 X-ray 1.65 A 27-150 [» ]
    2P44 X-ray 1.80 A 27-150 [» ]
    2P45 X-ray 1.10 A 27-150 [» ]
    2P46 X-ray 2.50 A/C 27-150 [» ]
    2P47 X-ray 2.50 A 27-150 [» ]
    2P48 X-ray 2.30 A 27-150 [» ]
    2P49 X-ray 1.38 A 27-150 [» ]
    2P4A X-ray 1.90 A/C 27-150 [» ]
    2QCA X-ray 1.33 A 27-150 [» ]
    2RAT X-ray 1.50 A 27-150 [» ]
    2RLN X-ray 1.85 E 42-150 [» ]
    S 27-41 [» ]
    2RNS X-ray 1.60 A 27-150 [» ]
    2W5G X-ray 1.70 A/B 27-150 [» ]
    2W5I X-ray 2.40 A/B 27-150 [» ]
    2W5K X-ray 1.70 A/B 27-150 [» ]
    2W5L X-ray 1.70 A/B 27-150 [» ]
    2W5M X-ray 1.80 A/B 27-150 [» ]
    2XOG X-ray 1.72 A/B 27-150 [» ]
    2XOI X-ray 1.72 A/B 27-150 [» ]
    3A1R neutron diffraction 1.70 A 27-150 [» ]
    3D6O X-ray 1.58 A/B 27-150 [» ]
    3D6P X-ray 1.60 A/B 27-150 [» ]
    3D6Q X-ray 1.60 A/B 27-150 [» ]
    3D7B X-ray 1.60 A/B 27-150 [» ]
    3D8Y X-ray 1.72 A/B 27-150 [» ]
    3D8Z X-ray 1.98 A/B 27-150 [» ]
    3DH5 X-ray 1.60 A 27-150 [» ]
    3DH6 X-ray 1.60 A 27-150 [» ]
    3DI7 X-ray 1.60 A 27-150 [» ]
    3DI8 X-ray 1.60 A 27-150 [» ]
    3DI9 X-ray 2.00 A 27-150 [» ]
    3DIB X-ray 1.40 A 27-150 [» ]
    3DIC X-ray 1.60 A 27-150 [» ]
    3DXG X-ray 1.39 A/B 27-150 [» ]
    3DXH X-ray 1.40 A/B 27-150 [» ]
    3EUX X-ray 1.65 A/B 27-150 [» ]
    3EUY X-ray 1.95 A/B 27-150 [» ]
    3EUZ X-ray 1.84 A/B 27-150 [» ]
    3EV0 X-ray 1.76 A/B 27-150 [» ]
    3EV1 X-ray 2.00 A/B 27-150 [» ]
    3EV2 X-ray 2.02 A/B 27-150 [» ]
    3EV3 X-ray 1.68 A/B 27-150 [» ]
    3EV4 X-ray 1.93 A/B 27-150 [» ]
    3EV5 X-ray 1.68 A/B 27-150 [» ]
    3EV6 X-ray 1.76 A/B 27-150 [» ]
    3FKZ X-ray 1.99 A/B 27-150 [» ]
    3FL0 X-ray 1.94 A/B 27-150 [» ]
    3FL1 X-ray 1.90 A/B 27-150 [» ]
    3FL3 X-ray 1.60 A/B 27-150 [» ]
    3I67 X-ray 1.30 A 27-150 [» ]
    3I6F X-ray 1.30 A 27-150 [» ]
    3I6H X-ray 1.30 A 27-150 [» ]
    3I6J X-ray 1.30 A 27-150 [» ]
    3I7W X-ray 2.35 A 27-150 [» ]
    3I7X X-ray 2.60 A 27-150 [» ]
    3I7Y X-ray 2.40 A 27-150 [» ]
    3JW1 X-ray 1.60 A/B 27-150 [» ]
    3LXO X-ray 1.55 A 27-150 [» ]
    3MWQ X-ray 1.68 A 26-150 [» ]
    3MWR X-ray 1.85 A 27-150 [» ]
    3MX8 X-ray 2.10 A 26-150 [» ]
    3MZQ X-ray 1.50 A 23-150 [» ]
    3MZR X-ray 1.50 A 23-150 [» ]
    3OQY X-ray 1.49 A/B 47-150 [» ]
    a/b 27-41 [» ]
    3OQZ X-ray 2.50 A/B 47-150 [» ]
    a/b 27-41 [» ]
    3OR0 X-ray 2.30 A/B 47-150 [» ]
    a/b 27-41 [» ]
    3QL1 X-ray 1.29 A 27-150 [» ]
    3QL2 X-ray 1.49 A/B 27-150 [» ]
    3QSK X-ray 1.75 A 27-150 [» ]
    3RAT X-ray 1.50 A 27-150 [» ]
    3RH1 X-ray 2.10 A 27-150 [» ]
    3RID X-ray 2.18 A/B/C/D 27-150 [» ]
    3RN3 X-ray 1.45 A 27-150 [» ]
    3RSD X-ray 1.60 A 27-150 [» ]
    3RSK X-ray 2.00 A 27-150 [» ]
    3RSP X-ray 1.70 A 27-150 [» ]
    3SRN X-ray 2.00 A 27-139 [» ]
    B 140-146 [» ]
    4AO1 X-ray 1.58 A 27-150 [» ]
    4G8V X-ray 1.70 A/B 27-150 [» ]
    4G8Y X-ray 1.80 A/B 27-150 [» ]
    4G90 X-ray 1.90 A/B 27-150 [» ]
    4J5Z X-ray 1.80 A 27-150 [» ]
    4J60 X-ray 1.69 A 27-150 [» ]
    4J61 X-ray 1.69 A 27-150 [» ]
    4J62 X-ray 2.04 A 27-150 [» ]
    4J63 X-ray 2.04 A 27-150 [» ]
    4J64 X-ray 1.78 A 27-150 [» ]
    4J65 X-ray 1.96 A 27-150 [» ]
    4J66 X-ray 2.04 A 27-150 [» ]
    4J67 X-ray 1.86 A 27-150 [» ]
    4J68 X-ray 1.78 A 27-150 [» ]
    4J69 X-ray 1.89 A 27-150 [» ]
    4J6A X-ray 2.04 A 27-150 [» ]
    4K7L X-ray 1.38 A 27-41 [» ]
    B 47-150 [» ]
    4K7M X-ray 1.80 A 27-150 [» ]
    4L55 X-ray 1.65 A/B 27-150 [» ]
    4MXF X-ray 2.25 A/B 27-150 [» ]
    4O36 X-ray 1.22 A 27-41 [» ]
    B 47-150 [» ]
    4O37 X-ray 1.40 A 27-41 [» ]
    B 47-150 [» ]
    4RAT X-ray 1.50 A 27-150 [» ]
    4RSD X-ray 1.60 A 27-150 [» ]
    4RSK X-ray 2.10 A 27-150 [» ]
    4SRN X-ray 2.00 A 27-139 [» ]
    B 140-150 [» ]
    5RAT X-ray 1.50 A 27-150 [» ]
    5RSA X-ray 2.00 A 27-150 [» ]
    6RAT X-ray 1.50 A 27-150 [» ]
    6RSA X-ray 2.00 A 27-150 [» ]
    7RAT X-ray 1.50 A 27-150 [» ]
    7RSA X-ray 1.26 A 27-150 [» ]
    8RAT X-ray 1.50 A 27-150 [» ]
    8RSA X-ray 1.80 A/B 27-150 [» ]
    9RAT X-ray 1.50 A 27-150 [» ]
    9RSA X-ray 1.80 A/B 27-150 [» ]
    ProteinModelPortali P61823.
    SMRi P61823. Positions 27-150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 159601. 1 interaction.
    DIPi DIP-36384N.
    IntActi P61823. 6 interactions.
    MINTi MINT-1510416.
    STRINGi 9913.ENSBTAP00000011586.

    Chemistry

    BindingDBi P61823.
    ChEMBLi CHEMBL6091.
    DrugBanki DB00536. Guanidine.
    DB00128. L-Aspartic Acid.

    Proteomic databases

    PaxDbi P61823.
    PRIDEi P61823.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000011586 ; ENSBTAP00000011586 ; ENSBTAG00000008793 .
    GeneIDi 282340.
    KEGGi bta:282340.

    Organism-specific databases

    CTDi 6035.

    Phylogenomic databases

    eggNOGi NOG40319.
    GeneTreei ENSGT00390000007840.
    HOGENOMi HOG000276883.
    HOVERGENi HBG008396.
    InParanoidi P61823.
    KOi K01168.
    OMAi ANKHIIV.
    OrthoDBi EOG7J1826.
    TreeFami TF333393.

    Enzyme and pathway databases

    BRENDAi 3.1.27.5. 908.
    SABIO-RK P61823.

    Miscellaneous databases

    EvolutionaryTracei P61823.
    NextBioi 20806135.
    PMAP-CutDB P61823.

    Family and domain databases

    Gene3Di 3.10.130.10. 1 hit.
    InterProi IPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view ]
    PANTHERi PTHR11437. PTHR11437. 1 hit.
    Pfami PF00074. RnaseA. 1 hit.
    [Graphical view ]
    PRINTSi PR00794. RIBONUCLEASE.
    ProDomi PD000535. RNaseA. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00092. RNAse_Pc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54076. SSF54076. 1 hit.
    PROSITEi PS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the bovine pancreatic ribonuclease gene: the unique intervening sequence in the 5' untranslated region contains a promoter-like element."
      Carsana A., Confalone E., Palmieri M., Libonati M., Furia A.
      Nucleic Acids Res. 16:5491-5502(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Fetal pancreas.
    3. "Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11."
      Delcardayre S.B., Ribo M., Yokel E.M., Quirk D.J., Rutter W.J., Raines R.T.
      Protein Eng. 8:261-273(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-150, FUNCTION.
    4. "The sequence of amino acid residues in bovine pancreatic ribonuclease: revisions and confirmations."
      Smyth D.G., Stein W.H., Moore S.
      J. Biol. Chem. 238:227-234(1963) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-150, DISULFIDE BONDS.
      Tissue: Pancreas.
    5. "On the structure of bovine pancreatic ribonuclease B. Isolation of a glycopeptide."
      Plummer T.H. Jr., Hirs C.H.W.
      J. Biol. Chem. 239:2530-2538(1964) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-150.
      Tissue: Pancreas.
    6. "Molecular evolution of genes encoding ribonucleases in ruminant species."
      Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M., Vento M.T., Furia A.
      J. Mol. Evol. 41:850-858(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-150.
    7. "The reactivities of the histidine residues at the active site of ribonuclease toward halo acids of different structures."
      Heinrikson R.L., Stein W.H., Crestfield A.M., Moore S.
      J. Biol. Chem. 240:2921-2934(1965) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    8. "Heavy atom-labelled derivatives of bovine pancreatic ribonuclease. I. Specific reactions of ribonuclease with N-acetylhomocysteine thiolactone and silver ion."
      Shall S., Barnard E.A.
      J. Mol. Biol. 41:237-251(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    9. "Glycation of amino groups in protein. Studies on the specificity of modification of RNase by glucose."
      Watkins N.G., Thorpe S.R., Baynes J.W.
      J. Biol. Chem. 260:10629-10636(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCATION AT LYS-27; LYS-33; LYS-63 AND LYS-67.
    10. "The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease."
      McPherson A., Brayer G., Cascio D., Williams R.
      Science 232:765-768(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    11. "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities."
      Thaysen-Andersen M., Mysling S., Hojrup P.
      Anal. Chem. 81:3933-3943(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-60.
    12. "The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A."
      Wyckoff H.W., Tsernoglou D., Hanson A.W., Knox J.R., Lee B., Richards F.M.
      J. Biol. Chem. 245:305-328(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    14. "The refined crystal structure of ribonuclease A at 2.0-A resolution."
      Wlodawer A., Bott R., Sjoelin L.
      J. Biol. Chem. 257:1325-1332(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    15. "Structure of phosphate-free ribonuclease A refined at 1.26 A."
      Wlodawer A., Svensson L.A., Sjoelin L., Gilliland G.L.
      Biochemistry 27:2705-2717(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS).
    16. "Crystal structures of ribonuclease A complexes with 5'-diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7-A resolution."
      Leonidas D.D., Shapiro R., Irons L.I., Russo N., Acharya K.R.
      Biochemistry 36:5578-5588(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    17. "Excavating an active site: the nucleobase specificity of ribonuclease A."
      Kelemen B.R., Schultz L.W., Sweeney R.Y., Raines R.T.
      Biochemistry 39:14487-14494(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-125 OF MUTANT GLY-67.
    18. "Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding."
      Park C., Schultz L.W., Raines R.T.
      Biochemistry 40:4949-4956(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ALA-38 AND ALA-145.
    19. "Cleavage of 3',5'-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin."
      Jardine A.M., Leonidas D.D., Jenkins J.L., Park C., Raines R.T., Acharya K.R., Shapiro R.
      Biochemistry 40:10262-10272(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
    20. "Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 A resolution."
      Chatani E., Hayashi R., Moriyama H., Ueki T.
      Protein Sci. 11:72-81(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF MUTANTS ALA-120; PHE-120 AND TRP-120.
    21. "Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution."
      Robertson A.D., Purisima E.O., Eastman M.A., Scheraga H.A.
      Biochemistry 28:5930-5938(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    22. "Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A."
      Rico M., Bruix M., Santoro J., Gonzalez C., Neira J.L., Nieto J.L., Herranz J.
      Eur. J. Biochem. 183:623-638(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    23. "3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations."
      Rico M., Santoro J., Gonzalez C., Bruix M., Neira J.L., Nieto J.L., Herranz J.
      J. Biomol. NMR 1:283-298(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiRNAS1_BOVIN
    AccessioniPrimary (citable) accession number: P61823
    Secondary accession number(s): A6QPW8, P00656, Q9TSF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Ribonuclease can destabilize or unwind the DNA helix by complexing with single-stranded DNA; this complex arises by an extended multisite cation-anion interaction between the lysine and arginine residues of the enzyme and the phosphate groups of the nucleotides.

    Keywords - Technical termi

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