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P07998

- RNAS1_HUMAN

UniProt

P07998 - RNAS1_HUMAN

Protein

Ribonuclease pancreatic

Gene

RNASE1

Organism
Homo sapiens (Human)
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 sitei35 – 351SubstrateBy similarity
    Binding sitei38 – 381SubstrateBy similarity
    Active sitei40 – 401Proton acceptor
    Binding sitei94 – 941SubstrateBy similarity
    Binding sitei113 – 1131SubstrateBy similarity
    Active sitei147 – 1471Proton donor

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. pancreatic ribonuclease activity Source: ProtInc
    3. protein binding Source: IntAct

    GO - Biological processi

    1. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease pancreatic (EC:3.1.27.5)
    Alternative name(s):
    HP-RNase
    RIB-1
    RNase UpI-1
    Ribonuclease 1
    Short name:
    RNase 1
    Ribonuclease A
    Short name:
    RNase A
    Gene namesi
    Name:RNASE1
    Synonyms:RIB1, RNS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:10044. RNASE1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-95, A-116, D-117 and D-119. 2 Publications
    Mutagenesisi95 – 951N → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, A-116, D-117 and D-119. 2 Publications
    Mutagenesisi116 – 1172NG → RS: No effect on inhibition by RNH1. 2 Publications
    Mutagenesisi116 – 1161N → A: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, D-117 and D-119. 2 Publications
    Mutagenesisi117 – 1171G → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-119. 2 Publications
    Mutagenesisi119 – 1191R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-117. 2 Publications

    Organism-specific databases

    PharmGKBiPA34412.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28286 PublicationsAdd
    BLAST
    Chaini29 – 156128Ribonuclease pancreaticPRO_0000030921Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 112
    Glycosylationi62 – 621N-linked (GlcNAc...); partial1 Publication
    Disulfide bondi68 ↔ 123
    Disulfide bondi86 ↔ 138
    Disulfide bondi93 ↔ 100
    Glycosylationi104 – 1041N-linked (GlcNAc...)1 Publication
    Glycosylationi116 – 1161N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    N-linked glycans are of complex type.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP07998.
    PeptideAtlasiP07998.
    PRIDEiP07998.

    PTM databases

    PhosphoSiteiP07998.

    Expressioni

    Tissue specificityi

    Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion).

    Gene expression databases

    ArrayExpressiP07998.
    BgeeiP07998.
    CleanExiHS_RNASE1.
    GenevestigatoriP07998.

    Organism-specific databases

    HPAiHPA001140.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RNH1P134892EBI-2823523,EBI-1237106

    Protein-protein interaction databases

    BioGridi111964. 1 interaction.
    IntActiP07998. 6 interactions.
    MINTiMINT-4845964.
    STRINGi9606.ENSP00000344193.

    Structurei

    Secondary structure

    1
    156
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 409
    Turni47 – 504
    Helixi53 – 608
    Turni61 – 644
    Beta strandi65 – 673
    Beta strandi70 – 756
    Helixi79 – 835
    Helixi84 – 874
    Beta strandi88 – 925
    Beta strandi96 – 1027
    Beta strandi107 – 1148
    Beta strandi120 – 1223
    Beta strandi125 – 13915
    Turni140 – 1434
    Beta strandi144 – 1529

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DZAX-ray1.65A/B28-156[»]
    1E21X-ray1.90A29-156[»]
    1H8XX-ray2.00A/B29-156[»]
    1Z7XX-ray1.95X/Z29-156[»]
    2E0JX-ray1.60A/B29-156[»]
    2E0LX-ray1.60A/B29-156[»]
    2E0MX-ray1.70A/B29-156[»]
    2E0OX-ray2.00A/B29-156[»]
    2K11NMR-A29-155[»]
    2Q4GX-ray1.95X/Z29-156[»]
    3F8GX-ray2.60A/B29-153[»]
    4KXHX-ray2.70A/B/C/D29-156[»]
    ProteinModelPortaliP07998.
    SMRiP07998. Positions 36-153.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07998.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni69 – 735Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the pancreatic ribonuclease family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40319.
    HOVERGENiHBG008396.
    InParanoidiP07998.
    KOiK01168.
    OMAiNCAYRTS.
    OrthoDBiEOG7J1826.
    PhylomeDBiP07998.
    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.

    P07998-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS    50
    STYCNQMMRR RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC 100
    YKSNSSMHIT DCRLTNGSRY PNCAYRTSPK ERHIIVACEG SPYVPVHFDA 150
    SVEDST 156
    Length:156
    Mass (Da):17,644
    Last modified:February 1, 1996 - v4
    Checksum:iF63B17B8B55115F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → G in CAA55817. (PubMed:8588814)Curated
    Sequence conflicti4 – 41Missing in AAB35096. (PubMed:7649283)Curated
    Sequence conflicti9 – 113RLL → VLP in AAB35096. (PubMed:7649283)Curated
    Sequence conflicti16 – 227ILLVLGW → VLLLVR in AAB35096. (PubMed:7649283)Curated
    Sequence conflicti67 – 671R → L in CAG29314. 1 PublicationCurated
    Sequence conflicti151 – 1511S → T in CAA55817. (PubMed:8588814)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26129 mRNA. Translation: BAA05124.1.
    DQ494867 Genomic DNA. Translation: ABF00144.1.
    AK312100 mRNA. Translation: BAG35036.1.
    CR450318 mRNA. Translation: CAG29314.1.
    CH471078 Genomic DNA. Translation: EAW66437.1.
    CH471078 Genomic DNA. Translation: EAW66438.1.
    BC005324 mRNA. Translation: AAH05324.1.
    BC022882 mRNA. Translation: AAH22882.1.
    X79235 Genomic DNA. Translation: CAA55817.1.
    S79281 mRNA. Translation: AAB35096.1.
    X62946 Genomic DNA. Translation: CAA44718.1.
    CCDSiCCDS9559.1.
    PIRiI53530.
    S45003. NRHU1.
    RefSeqiNP_002924.1. NM_002933.4.
    NP_937875.1. NM_198232.2.
    NP_937877.1. NM_198234.2.
    NP_937878.1. NM_198235.2.
    UniGeneiHs.78224.

    Genome annotation databases

    EnsembliENST00000340900; ENSP00000344193; ENSG00000129538.
    ENST00000397967; ENSP00000381057; ENSG00000129538.
    ENST00000397970; ENSP00000381060; ENSG00000129538.
    ENST00000412779; ENSP00000399493; ENSG00000129538.
    GeneIDi6035.
    KEGGihsa:6035.
    UCSCiuc001vyf.3. human.

    Polymorphism databases

    DMDMi1350818.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26129 mRNA. Translation: BAA05124.1 .
    DQ494867 Genomic DNA. Translation: ABF00144.1 .
    AK312100 mRNA. Translation: BAG35036.1 .
    CR450318 mRNA. Translation: CAG29314.1 .
    CH471078 Genomic DNA. Translation: EAW66437.1 .
    CH471078 Genomic DNA. Translation: EAW66438.1 .
    BC005324 mRNA. Translation: AAH05324.1 .
    BC022882 mRNA. Translation: AAH22882.1 .
    X79235 Genomic DNA. Translation: CAA55817.1 .
    S79281 mRNA. Translation: AAB35096.1 .
    X62946 Genomic DNA. Translation: CAA44718.1 .
    CCDSi CCDS9559.1.
    PIRi I53530.
    S45003. NRHU1.
    RefSeqi NP_002924.1. NM_002933.4.
    NP_937875.1. NM_198232.2.
    NP_937877.1. NM_198234.2.
    NP_937878.1. NM_198235.2.
    UniGenei Hs.78224.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DZA X-ray 1.65 A/B 28-156 [» ]
    1E21 X-ray 1.90 A 29-156 [» ]
    1H8X X-ray 2.00 A/B 29-156 [» ]
    1Z7X X-ray 1.95 X/Z 29-156 [» ]
    2E0J X-ray 1.60 A/B 29-156 [» ]
    2E0L X-ray 1.60 A/B 29-156 [» ]
    2E0M X-ray 1.70 A/B 29-156 [» ]
    2E0O X-ray 2.00 A/B 29-156 [» ]
    2K11 NMR - A 29-155 [» ]
    2Q4G X-ray 1.95 X/Z 29-156 [» ]
    3F8G X-ray 2.60 A/B 29-153 [» ]
    4KXH X-ray 2.70 A/B/C/D 29-156 [» ]
    ProteinModelPortali P07998.
    SMRi P07998. Positions 36-153.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111964. 1 interaction.
    IntActi P07998. 6 interactions.
    MINTi MINT-4845964.
    STRINGi 9606.ENSP00000344193.

    Chemistry

    BindingDBi P07998.
    ChEMBLi CHEMBL5425.

    PTM databases

    PhosphoSitei P07998.

    Polymorphism databases

    DMDMi 1350818.

    Proteomic databases

    PaxDbi P07998.
    PeptideAtlasi P07998.
    PRIDEi P07998.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340900 ; ENSP00000344193 ; ENSG00000129538 .
    ENST00000397967 ; ENSP00000381057 ; ENSG00000129538 .
    ENST00000397970 ; ENSP00000381060 ; ENSG00000129538 .
    ENST00000412779 ; ENSP00000399493 ; ENSG00000129538 .
    GeneIDi 6035.
    KEGGi hsa:6035.
    UCSCi uc001vyf.3. human.

    Organism-specific databases

    CTDi 6035.
    GeneCardsi GC14M021269.
    HGNCi HGNC:10044. RNASE1.
    HPAi HPA001140.
    MIMi 180440. gene.
    neXtProti NX_P07998.
    PharmGKBi PA34412.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40319.
    HOVERGENi HBG008396.
    InParanoidi P07998.
    KOi K01168.
    OMAi NCAYRTS.
    OrthoDBi EOG7J1826.
    PhylomeDBi P07998.
    TreeFami TF333393.

    Miscellaneous databases

    ChiTaRSi RNASE1. human.
    EvolutionaryTracei P07998.
    GeneWikii RNASE1.
    GenomeRNAii 6035.
    NextBioi 23515.
    PROi P07998.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07998.
    Bgeei P07998.
    CleanExi HS_RNASE1.
    Genevestigatori P07998.

    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. "Nucleotide sequence encoding human pancreatic ribonuclease."
      Seno M., Fatami J.I., Kosaka M., Seno S., Yamada H.
      Biochim. Biophys. Acta 1218:466-468(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pancreas.
    2. "Duplication and divergence of two distinct pancreatic ribonuclease genes in leaf-eating African and Asian colobine monkeys."
      Schienman J.E., Holt R.A., Auerbach M.R., Stewart C.B.
      Mol. Biol. Evol. 23:1465-1479(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
      Tissue: Testis.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pancreas and Prostate.
    7. "Primary structure of the coding part of the gene for human pancreatic ribonuclease and its chromosomal location."
      Kochetov A.V., Lukasheva V.V., Filipenko M.L., Mertvetsov N.P., Rivkin M.I.
      Bioorg. Khim. 21:691-694(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
      Tissue: Placenta.
    8. "Expression in mammalian cells, purification and characterization of recombinant human pancreatic ribonuclease."
      Russo N., de Nigris M., Ciardiello A., Di Donato A., D'Alessio G.
      FEBS Lett. 369:352-352(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-155.
    9. "The DNA sequences of the human and hamster secretory ribonucleases determined with the polymerase chain reaction (PCR)."
      Haugg M., Schein C.H.
      Nucleic Acids Res. 20:612-612(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-149.
      Tissue: Placenta.
    10. "The amino acid sequence of human pancreatic ribonuclease."
      Beintema J.J., Wietzes P., Weickmann J.L., Glitz D.G.
      Anal. Biochem. 136:48-64(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-156.
      Tissue: Pancreas.
    11. "Differences in glycosylation pattern of human secretory ribonucleases."
      Beintema J.J., Blank A., Schieven G.L., Dekker C.A., Sorrentino S., Libonati M.
      Biochem. J. 255:501-505(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-156, GLYCOSYLATION AT ASN-62; ASN-104 AND ASN-116.
    12. "Purification and characterization of three ribonucleases from human kidney: comparison with urine ribonucleases."
      Mizuta K., Awazu S., Yasuda T., Kishi K.
      Arch. Biochem. Biophys. 281:144-151(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-47.
    13. "A putative mouse oocyte maturation inhibitory protein from urine of pregnant women: N-terminal sequence homology with human nonsecretory ribonuclease."
      Sakakibara R., Hashida K., Tominaga N., Sakai K., Ishiguro M., Imamura S., Ohmatsu F., Sato E.
      Chem. Pharm. Bull. 39:146-149(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-43.
    14. "Characterization of a unique nonsecretory ribonuclease from urine of pregnant women."
      Sakakibara R., Hashida K., Kitahara T., Ishiguro M.
      J. Biochem. 111:325-330(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-48.
      Tissue: Urine.
    15. "Two distinct secretory ribonucleases from human cerebrum: purification, characterization and relationships to other ribonucleases."
      Yasuda T., Nadano D., Takeshita H., Kishi K.
      Biochem. J. 296:617-625(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-49.
    16. "Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases."
      Pous J., Canals A., Terzyan S.S., Guasch A., Benito A., Ribo M., Vilanova M., Coll M.
      J. Mol. Biol. 303:49-60(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 29-156, MUTAGENESIS OF 116-ASN-GLY-117.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-156.
    18. "The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization."
      Canals A., Pous J., Guasch A., Benito A., Ribo M., Vilanova M., Coll M.
      Structure 9:967-976(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-156, DISULFIDE BONDS.
    19. "Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein."
      Johnson R.J., McCoy J.G., Bingman C.A., Phillips G.N. Jr., Raines R.T.
      J. Mol. Biol. 368:434-449(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-156 IN COMPLEX WITH RNH1, FUNCTION, SUBUNIT, INTERACTION WITH RNH1, DISULFIDE BONDS, MUTAGENESIS OF ARG-67; ASN-95; ASN-116; GLY-117 AND ARG-119.
    20. "'Crystal lattice engineering,' an approach to engineer protein crystal contacts by creating intermolecular symmetry: crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines."
      Yamada H., Tamada T., Kosaka M., Miyata K., Fujiki S., Tano M., Moriya M., Yamanishi M., Honjo E., Tada H., Ino T., Yamaguchi H., Futami J., Seno M., Nomoto T., Hirata T., Yoshimura M., Kuroki R.
      Protein Sci. 16:1389-1397(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-156, DISULFIDE BONDS.

    Entry informationi

    Entry nameiRNAS1_HUMAN
    AccessioniPrimary (citable) accession number: P07998
    Secondary accession number(s): B2R589
    , D3DS06, Q16830, Q16869, Q1KHR2, Q6ICS5, Q9UCB4, Q9UCB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 160 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3