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P07998 (RNAS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RNASE1
Synonyms:RIB1, RNS1
OrganismHomo sapiens (Human) [Reference 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. Ref.19

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. Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein. Ref.19

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RNH1P134892EBI-2823523,EBI-1237106

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
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.11
Glycosylation1041N-linked (GlcNAc...) Ref.11
Glycosylation1161N-linked (GlcNAc...) Ref.11
Disulfide bond54 ↔ 112 Ref.18 Ref.19 Ref.20
Disulfide bond68 ↔ 123 Ref.18 Ref.19 Ref.20
Disulfide bond86 ↔ 138 Ref.18 Ref.19 Ref.20
Disulfide bond93 ↔ 100 Ref.18 Ref.19 Ref.20

Experimental info

Mutagenesis671R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-95, A-116, D-117 and D-119. Ref.16 Ref.19
Mutagenesis951N → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, A-116, D-117 and D-119. Ref.16 Ref.19
Mutagenesis116 – 1172NG → RS: No effect on inhibition by RNH1. Ref.16 Ref.19
Mutagenesis1161N → A: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, D-117 and D-119. Ref.16 Ref.19
Mutagenesis1171G → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-119. Ref.16 Ref.19
Mutagenesis1191R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-117. Ref.16 Ref.19
Sequence conflict21A → G in CAA55817. Ref.7
Sequence conflict41Missing in AAB35096. Ref.8
Sequence conflict9 – 113RLL → VLP in AAB35096. Ref.8
Sequence conflict16 – 227ILLVLGW → VLLLVR in AAB35096. Ref.8
Sequence conflict671R → L in CAG29314. Ref.4
Sequence conflict1511S → T in CAA55817. Ref.7

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P07998 [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] [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. 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] [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]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].
[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]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI53530.
NRHU1. S45003.
RefSeqNP_002924.1. NM_002933.4.
NP_937875.1. NM_198232.2.
NP_937877.1. NM_198234.2.
NP_937878.1. NM_198235.2.
UniGeneHs.78224.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
4KXHX-ray2.70A/B/C/D29-156[»]
ProteinModelPortalP07998.
SMRP07998. Positions 36-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111964. 1 interaction.
IntActP07998. 6 interactions.
MINTMINT-4845964.
STRING9606.ENSP00000344193.

Chemistry

BindingDBP07998.
ChEMBLCHEMBL5425.

PTM databases

PhosphoSiteP07998.

Polymorphism databases

DMDM1350818.

Proteomic databases

PaxDbP07998.
PeptideAtlasP07998.
PRIDEP07998.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340900; ENSP00000344193; ENSG00000129538.
ENST00000397967; ENSP00000381057; ENSG00000129538.
ENST00000397970; ENSP00000381060; ENSG00000129538.
ENST00000412779; ENSP00000399493; ENSG00000129538.
GeneID6035.
KEGGhsa:6035.
UCSCuc001vyf.3. human.

Organism-specific databases

CTD6035.
GeneCardsGC14M021269.
HGNCHGNC:10044. RNASE1.
HPAHPA001140.
MIM180440. gene.
neXtProtNX_P07998.
PharmGKBPA34412.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40319.
HOVERGENHBG008396.
InParanoidP07998.
KOK01168.
OMANCAYRTS.
OrthoDBEOG7J1826.
PhylomeDBP07998.
TreeFamTF333393.

Gene expression databases

ArrayExpressP07998.
BgeeP07998.
CleanExHS_RNASE1.
GenevestigatorP07998.

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

ChiTaRSRNASE1. human.
EvolutionaryTraceP07998.
GeneWikiRNASE1.
GenomeRNAi6035.
NextBio23515.
PROP07998.
SOURCESearch...

Entry information

Entry nameRNAS1_HUMAN
AccessionPrimary (citable) accession number: P07998
Secondary accession number(s): B2R589 expand/collapse secondary AC list , D3DS06, Q16830, Q16869, Q1KHR2, Q6ICS5, Q9UCB4, Q9UCB5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 156 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

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