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Reviewed, UniProtKB/Swiss-Prot P07998 (RNAS1_HUMAN)

Last modified November 3, 2009. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ribonuclease pancreatic
    EC=3.1.27.5
Alternative name(s):
    RNase 1
    RNase A
    RNase UpI-1
    RIB-1
    HP-RNase
Gene names
Name: RNASE1
Synonyms: RIB1, RNS1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length156 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.

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

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

Post-translational modification

N-linked glycans are of complex type.

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

pancreatic ribonuclease activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Chain29 – 156128Ribonuclease pancreatic
PRO_0000030921

Regions

Region69 – 735Substrate binding By similarity

Sites

Active site401Proton acceptor
Active site1471Proton donor
Binding site351Substrate By similarity
Binding site381Substrate By similarity
Binding site941Substrate By similarity
Binding site1131Substrate By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...); partial Ref.10
Glycosylation1041N-linked (GlcNAc...) Ref.10
Glycosylation1161N-linked (GlcNAc...) Ref.10
Disulfide bond54 ↔ 112
Disulfide bond68 ↔ 123
Disulfide bond86 ↔ 138
Disulfide bond93 ↔ 100

Experimental info

Mutagenesis116 – 1172NG → RS: No effect on inhibition by RNase inhibitor 1. Ref.15
Sequence conflict21A → G in CAA55817. Ref.6
Sequence conflict41Missing in AAB35096. Ref.7
Sequence conflict9 – 113RLL → VLP in AAB35096. Ref.7
Sequence conflict16 – 227ILLVLGW → VLLLVR in AAB35096. Ref.7
Sequence conflict1511S → T in CAA55817. Ref.6

Secondary structure

..................... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07998-1 [UniParc].

Last modified February 1, 1996. Version 4.
Checksum: F63B17B8B55115F9

FASTA15617,644
        10         20         30         40         50         60 
MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS STYCNQMMRR 

        70         80         90        100        110        120 
RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC YKSNSSMHIT DCRLTNGSRY 

       130        140        150 
PNCAYRTSPK ERHIIVACEG SPYVPVHFDA SVEDST 

« Hide

References

« Hide 'large scale' references
[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: 8049276] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"Duplication and divergence of two distinct pancreatic ribnuclease 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: 16751256] [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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas and Prostate.
[6]"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: 8588814] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
Tissue: Placenta.
[7]"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: 7649283] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-155.
[8]"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: 1741299] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-149.
Tissue: Placenta.
[9]"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: 6201087] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-156.
Tissue: Pancreas.
[10]"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: 3202829] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-156, GLYCOSYLATION AT ASN-62; ASN-104 AND ASN-116.
[11]"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: 2383019] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-47.
[12]"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: 2049798] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-43.
[13]"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: 1587793] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-48.
Tissue: Urine.
[14]"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: 8280059] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-49.
[15]"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: 11021969] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-156, MUTAGENESIS OF 116-ASN-GLY-117.
[16]"Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution."
Pous J., Mallorqui-Fernandez G., Peracaula R., Terzyan S.S., Futami J., Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X., Coll M.
Acta Crystallogr. D 57:498-505(2001) [PubMed: 11264578] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 35-153.
+Additional computationally mapped references.

Cross-references

Sequence databases

D26129 mRNA. Translation: BAA05124.1.
DQ494867 Genomic DNA. Translation: ABF00144.1.
AK312100 mRNA. Translation: BAG35036.1.
CH471078 Genomic DNA. Translation: EAW66437.1.
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.
IPIIPI00014048.
PIRI53530.
NRHU1. S45003.
RefSeqNP_002924.1.
NP_937875.1.
NP_937877.1.
NP_937878.1.
UniGeneHs.78224

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DZAX-ray1.65A/B29-156[»]
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[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP07998.

Proteomic databases

PeptideAtlasP07998.
PRIDEP07998.

Genome annotation databases

EnsemblENST00000340900; ENSP00000344193; ENSG00000129538; Homo sapiens. [Genome view]
ENST00000397967; ENSP00000381057; ENSG00000129538; Homo sapiens. [Genome view]
ENST00000397970; ENSP00000381060; ENSG00000129538; Homo sapiens. [Genome view]
ENST00000412779; ENSP00000399493; ENSG00000129538; Homo sapiens. [Genome view]
GeneID6035.
KEGGhsa:6035.
UCSCuc001vyf.1. human.

Organism-specific databases

CTD6035.
GeneCardsGC14M020339.
H-InvDBHIX0011495.
HGNCHGNC:10044. RNASE1.
HPAHPA001140.
MIM180440. gene.
PharmGKBPA34412.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP07998.
HOVERGENP07998.
OMANCAYRTS.

Enzyme and pathway databases

BRENDA3.1.27.5. 247.

Gene expression databases

ArrayExpressP07998.
BgeeP07998.
CleanExHS_RNASE1.
GenevestigatorP07998.
GermOnlineENSG00000129538. Homo sapiens.

Family and domain databases

InterProIPR001427. RNaseA.
[Graphical view]
Gene3DG3DSA:3.10.130.10. RNaseA. 1 hit.
PANTHERPTHR11437. RNaseA. 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]
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio23515.
SOURCESearch...

Entry information

Entry nameRNAS1_HUMAN
AccessionPrimary (citable) accession number: P07998
Secondary accession number(s): B2R589 expand/collapse secondary AC list , Q16830, Q16869, Q1KHR2, Q9UCB4, Q9UCB5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1996
Last modified: November 3, 2009
This is version 118 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents