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Protein

Ribonuclease pancreatic

Gene

RNASE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Binding sitei35SubstrateBy similarity1
Binding sitei38SubstrateBy similarity1
Active sitei40Proton acceptor1
Binding sitei94SubstrateBy similarity1
Binding sitei113SubstrateBy similarity1
Active sitei147Proton donor1

GO - Molecular functioni

  • endonuclease activity Source: GO_Central
  • nucleic acid binding Source: InterPro
  • ribonuclease A activity Source: ProtInc
  • ribonuclease activity Source: UniProtKB

GO - Biological processi

  • RNA phosphodiester bond hydrolysis Source: UniProtKB

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAi3.1.27.5 2681

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000129538.13
HGNCiHGNC:10044 RNASE1
MIMi180440 gene
neXtProtiNX_P07998

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-95, A-116, D-117 and D-119. 1 Publication1
Mutagenesisi95N → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, A-116, D-117 and D-119. 1 Publication1
Mutagenesisi116 – 117NG → RS: No effect on inhibition by RNH1. 1 Publication2
Mutagenesisi116N → A: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, D-117 and D-119. 1 Publication1
Mutagenesisi117G → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-119. 1 Publication1
Mutagenesisi119R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-117. 1 Publication1

Organism-specific databases

DisGeNETi6035
OpenTargetsiENSG00000129538
PharmGKBiPA34412

Chemistry databases

ChEMBLiCHEMBL5425
DrugBankiDB03765 2'-cytidylic acid
DB03448 2'-Deoxyuridine 3'-Monophosphate
DB02363 2'-Monophosphoadenosine-5'-Diphosphate
DB03900 2-Methyl-2-Propanol
DB01842 3'-Phosphate-Adenosine-5'-Diphosphate
DB02714 3'-Uridinemonophosphate
DB08596 5'-deoxy-5'-piperidin-1-ylthymidine
DB02098 Adenosine-2'-5'-Diphosphate
DB01812 Adenosine-3'-5'-Diphosphate
DB04272 Citric Acid
DB02987 Cysteine-S-Acetamide
DB01961 Cytidine-3'-Monophosphate
DB01942 Formic Acid
DB00536 Guanidine
DB02325 Isopropyl Alcohol
DB00128 L-Aspartic Acid
DB04464 N-Formylmethionine
DB04514 Phosphoric Acid-2'-[2'-Deoxy-Uridine]Ester-5'-Guanosine Ester
DB03726 Purine Riboside-5'-Monophosphate
DB03186 U-Pi-a-Pi
DB02805 Uracil arabinose-3'-phosphate
DB03447 Uridylyl-2'-5'-Phospho-Adenosine

Polymorphism and mutation databases

BioMutaiRNASE1
DMDMi1350818

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 286 PublicationsAdd BLAST28
ChainiPRO_000003092129 – 156Ribonuclease pancreaticAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 112
Glycosylationi62N-linked (GlcNAc...) asparagine; partial1 Publication1
Disulfide bondi68 ↔ 123
Disulfide bondi86 ↔ 138
Disulfide bondi93 ↔ 100
Glycosylationi104N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi116N-linked (GlcNAc...) asparagine1 Publication1

Post-translational modificationi

N-linked glycans are of complex type.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP07998
PeptideAtlasiP07998
PRIDEiP07998
ProteomicsDBi52059

PTM databases

iPTMnetiP07998
PhosphoSitePlusiP07998

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

BgeeiENSG00000129538
CleanExiHS_RNASE1
ExpressionAtlasiP07998 baseline and differential
GenevisibleiP07998 HS

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, 5 interactors
IntActiP07998, 7 interactors
MINTiP07998
STRINGi9606.ENSP00000344193

Chemistry databases

BindingDBiP07998

Structurei

Secondary structure

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 40Combined sources9
Turni47 – 50Combined sources4
Helixi53 – 60Combined sources8
Turni61 – 64Combined sources4
Beta strandi65 – 67Combined sources3
Beta strandi70 – 75Combined sources6
Helixi79 – 83Combined sources5
Helixi84 – 87Combined sources4
Beta strandi88 – 92Combined sources5
Beta strandi96 – 102Combined sources7
Beta strandi107 – 114Combined sources8
Beta strandi120 – 122Combined sources3
Beta strandi125 – 139Combined sources15
Turni140 – 143Combined sources4
Beta strandi144 – 152Combined sources9

3D structure databases

ProteinModelPortaliP07998
SMRiP07998
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07998

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 73Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IYEN Eukaryota
ENOG41113F1 LUCA
GeneTreeiENSGT00900000140967
HOVERGENiHBG008396
InParanoidiP07998
KOiK01168
OMAiNCAYRTS
OrthoDBiEOG091G15X3
PhylomeDBiP07998
TreeFamiTF333393

Family and domain databases

Gene3Di3.10.130.10, 1 hit
InterProiView protein in InterPro
IPR001427 RNaseA
IPR036816 RNaseA-like_dom_sf
IPR023411 RNaseA_AS
IPR023412 RNaseA_domain
PANTHERiPTHR11437 PTHR11437, 1 hit
PfamiView protein in Pfam
PF00074 RnaseA, 1 hit
PRINTSiPR00794 RIBONUCLEASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000535 RNaseA, 1 hit
SMARTiView protein in SMART
SM00092 RNAse_Pc, 1 hit
SUPFAMiSSF54076 SSF54076, 1 hit
PROSITEiView protein in PROSITE
PS00127 RNASE_PANCREATIC, 1 hit

Sequencei

Sequence statusi: Complete.

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

P07998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS
60 70 80 90 100
STYCNQMMRR RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC
110 120 130 140 150
YKSNSSMHIT DCRLTNGSRY PNCAYRTSPK ERHIIVACEG SPYVPVHFDA

SVEDST
Length:156
Mass (Da):17,644
Last modified:February 1, 1996 - v4
Checksum:iF63B17B8B55115F9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2A → G in CAA55817 (PubMed:8588814).Curated1
Sequence conflicti4Missing in AAB35096 (PubMed:7649283).Curated1
Sequence conflicti9 – 11RLL → VLP in AAB35096 (PubMed:7649283).Curated3
Sequence conflicti16 – 22ILLVLGW → VLLLVR in AAB35096 (PubMed:7649283).Curated7
Sequence conflicti67R → L in CAG29314 (Ref. 4) Curated1
Sequence conflicti151S → T in CAA55817 (PubMed:8588814).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiRNAS1_HUMAN
AccessioniPrimary (citable) accession number: P07998
Secondary accession number(s): B2R589
, D3DS06, Q16830, Q16869, Q1KHR2, Q6ICS5, Q9UCB4, Q9UCB5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1996
Last modified: June 20, 2018
This is version 187 of the entry and version 4 of the sequence. See 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

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