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P61823 (RNAS1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease pancreatic

EC=3.1.27.5
Alternative name(s):
RNase 1
RNase A
Gene names
Name:RNASE1
Synonyms:RNS1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

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.

Subcellular location

Secreted.

Tissue specificity

Pancreas.

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.

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDI1P179672EBI-908364,EBI-13012From a different organism.
RNH1P134893EBI-908364,EBI-1237106From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.4 Ref.5
Chain27 – 150124Ribonuclease pancreatic
PRO_0000030915

Regions

Region67 – 715Substrate binding

Sites

Active site381Proton acceptor Ref.7 Ref.8
Active site1451Proton donor Ref.7 Ref.8
Binding site331Substrate
Binding site361Substrate
Binding site921Substrate
Binding site1111Substrate

Amino acid modifications

Glycosylation271N-linked (Glc) (glycation); in vitro Ref.9
Glycosylation331N-linked (Glc) (glycation); in vitro Ref.9
Glycosylation601N-linked (GlcNAc...); partial Ref.11
CAR_000006
Glycosylation631N-linked (Glc) (glycation); in vitro Ref.9
Glycosylation671N-linked (Glc) (glycation); in vitro Ref.9
Disulfide bond52 ↔ 110 Ref.4
Disulfide bond66 ↔ 121 Ref.4
Disulfide bond84 ↔ 136 Ref.4
Disulfide bond91 ↔ 98 Ref.4

Experimental info

Mutagenesis381H → A: Loss of activity.
Mutagenesis1451H → A: Loss of activity.

Secondary structure

.............................. 150
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61823 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 74E5DC61E679187D

FASTA15016,461
        10         20         30         40         50         60 
MALKSLVLLS LLVLVLLLVR VQPSLGKETA AAKFERQHMD SSTSAASSSN YCNQMMKSRN 

        70         80         90        100        110        120 
LTKDRCKPVN TFVHESLADV QAVCSQKNVA CKNGQTNCYQ SYSTMSITDC RETGSSKYPN 

       130        140        150 
CAYKTTQANK HIIVACEGNP YVPVHFDASV 

« Hide

References

« Hide 'large scale' references
[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]"The structure of ribonuclease at 2.5-A resolution."
Carlisle C.H., Palmer R.A., Mazumdar S.K., Gorinsky B.A., Yeates D.G.R.
J. Mol. Biol. 85:1-18(1974) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRNRBO. S00897.
RefSeqNP_001014408.2. NM_001014386.4.
XP_005211519.1. XM_005211462.1.
UniGeneBt.4630.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray2.25B50-150[»]
1D5EX-ray2.25B50-150[»]
1D5HX-ray2.25B50-150[»]
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-ray2.10A84-99[»]
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-ray1.68A27-150[»]
3MWRX-ray1.85A27-150[»]
3MX8X-ray2.10A27-150[»]
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[»]
B140-150[»]
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[»]
4K7MX-ray1.80A27-150[»]
4L55X-ray1.65A/B27-150[»]
4MXFX-ray2.25A/B27-150[»]
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[»]
ProteinModelPortalP61823.
SMRP61823. Positions 27-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid159601. 1 interaction.
IntActP61823. 6 interactions.
MINTMINT-1510416.
STRING9913.ENSBTAP00000011586.

Chemistry

BindingDBP61823.
ChEMBLCHEMBL6091.
DrugBankDB00536. Guanidine.
DB00128. L-Aspartic Acid.

Proteomic databases

PaxDbP61823.
PRIDEP61823.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000011586; ENSBTAP00000011586; ENSBTAG00000008793.
GeneID282340.
KEGGbta:282340.

Organism-specific databases

CTD6035.

Phylogenomic databases

eggNOGNOG40319.
GeneTreeENSGT00390000007840.
HOGENOMHOG000276883.
HOVERGENHBG008396.
InParanoidP61823.
KOK01168.
OMADITACRL.
OrthoDBEOG7J1826.
TreeFamTF333393.

Enzyme and pathway databases

BRENDA3.1.27.5. 908.
SABIO-RKP61823.

Family and domain databases

Gene3D3.10.130.10. 1 hit.
InterProIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERPTHR11437. PTHR11437. 1 hit.
PfamPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSPR00794. RIBONUCLEASE.
ProDomPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMSSF54076. SSF54076. 1 hit.
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61823.
NextBio20806135.
PMAP-CutDBP61823.

Entry information

Entry nameRNAS1_BOVIN
AccessionPrimary (citable) accession number: P61823
Secondary accession number(s): A6QPW8, P00656, Q9TSF2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references