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Protein

Ribonuclease pancreatic

Gene

RNASE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • nucleic acid binding Source: InterPro
  • ribonuclease A activity Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BioCyciZFISH:HS05292-MONOMER.
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

HGNCiHGNC:10044. RNASE1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

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.
DrugBankiDB00536. Guanidine.
DB02325. Isopropyl Alcohol.
DB00128. L-Aspartic Acid.

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...); partial1 Publication1
Disulfide bondi68 ↔ 123
Disulfide bondi86 ↔ 138
Disulfide bondi93 ↔ 100
Glycosylationi104N-linked (GlcNAc...)1 Publication1
Glycosylationi116N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

N-linked glycans are of complex type.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP07998.
PeptideAtlasiP07998.
PRIDEiP07998.

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.
MINTiMINT-4845964.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
GeneTreeiENSGT00840000129759.
HOVERGENiHBG008396.
InParanoidiP07998.
KOiK01168.
OMAiNCAYRTS.
OrthoDBiEOG091G15X3.
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

        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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111964. 5 interactors.
IntActiP07998. 7 interactors.
MINTiMINT-4845964.
STRINGi9606.ENSP00000344193.

Chemistry databases

BindingDBiP07998.
ChEMBLiCHEMBL5425.
DrugBankiDB00536. Guanidine.
DB02325. Isopropyl Alcohol.
DB00128. L-Aspartic Acid.

PTM databases

iPTMnetiP07998.
PhosphoSitePlusiP07998.

Polymorphism and mutation databases

BioMutaiRNASE1.
DMDMi1350818.

Proteomic databases

PaxDbiP07998.
PeptideAtlasiP07998.
PRIDEiP07998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6035.
DisGeNETi6035.
GeneCardsiRNASE1.
HGNCiHGNC:10044. RNASE1.
HPAiHPA001140.
MIMi180440. gene.
neXtProtiNX_P07998.
OpenTargetsiENSG00000129538.
PharmGKBiPA34412.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IYEN. Eukaryota.
ENOG41113F1. LUCA.
GeneTreeiENSGT00840000129759.
HOVERGENiHBG008396.
InParanoidiP07998.
KOiK01168.
OMAiNCAYRTS.
OrthoDBiEOG091G15X3.
PhylomeDBiP07998.
TreeFamiTF333393.

Enzyme and pathway databases

BioCyciZFISH:HS05292-MONOMER.
BRENDAi3.1.27.5. 2681.

Miscellaneous databases

ChiTaRSiRNASE1. human.
EvolutionaryTraceiP07998.
GeneWikiiRNASE1.
GenomeRNAii6035.
PROiP07998.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000129538.
CleanExiHS_RNASE1.
ExpressionAtlasiP07998. baseline and differential.
GenevisibleiP07998. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 179 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.