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Protein

Non-secretory ribonuclease

Gene

RNASE2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities.2 Publications

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
Active sitei42Proton acceptor1
Active sitei156Proton donor1

GO - Molecular functioni

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

GO - Biological processi

  • chemotaxis Source: UniProtKB
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • RNA catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciZFISH:HS09938-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-secretory ribonuclease (EC:3.1.27.5)
Alternative name(s):
Eosinophil-derived neurotoxin
RNase UpI-2
Ribonuclease 2
Short name:
RNase 2
Ribonuclease US
Gene namesi
Name:RNASE2
Synonyms:EDN, RNS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:10045. RNASE2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: ProtInc
  • lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi6036.
OpenTargetsiENSG00000169385.
PharmGKBiPA34413.

Chemistry databases

ChEMBLiCHEMBL5120.

Polymorphism and mutation databases

BioMutaiRNASE2.
DMDMi133168.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 275 PublicationsAdd BLAST27
ChainiPRO_000003087428 – 161Non-secretory ribonucleaseAdd BLAST134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
GlycosylationiCAR_00000434C-linked (Man)2 Publications1
Glycosylationi44N-linked (GlcNAc...)1
Disulfide bondi50 ↔ 110
Modified residuei60Nitrated tyrosine1 Publication1
Disulfide bondi64 ↔ 123
Disulfide bondi82 ↔ 138
Glycosylationi86N-linked (GlcNAc...)1
Disulfide bondi89 ↔ 98
Glycosylationi92N-linked (GlcNAc...)1
Glycosylationi111N-linked (GlcNAc...)1
Glycosylationi119N-linked (GlcNAc...)1

Post-translational modificationi

A particular signal processing and glycosylation pattern may differentiate the UpI2 RNase, found specifically in pregnant women urine, from other nonsecretory RNases.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

EPDiP10153.
PaxDbiP10153.
PeptideAtlasiP10153.
PRIDEiP10153.

PTM databases

iPTMnetiP10153.
PhosphoSitePlusiP10153.
UniCarbKBiP10153.

Expressioni

Tissue specificityi

Liver, lung, spleen, leukocytes and body fluids.

Gene expression databases

BgeeiENSG00000169385.
CleanExiHS_RNASE2.
ExpressionAtlasiP10153. baseline and differential.
GenevisibleiP10153. HS.

Organism-specific databases

HPAiHPA044983.

Interactioni

Subunit structurei

Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur.3 Publications

Protein-protein interaction databases

BioGridi111965. 2 interactors.
IntActiP10153. 1 interactor.
STRINGi9606.ENSP00000303276.

Chemistry databases

BindingDBiP10153.

Structurei

Secondary structure

1161
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi34 – 42Combined sources9
Beta strandi46 – 49Combined sources4
Helixi50 – 61Combined sources12
Beta strandi66 – 73Combined sources8
Helixi75 – 82Combined sources8
Beta strandi98 – 100Combined sources3
Beta strandi105 – 114Combined sources10
Helixi120 – 122Combined sources3
Beta strandi124 – 140Combined sources17
Turni143 – 145Combined sources3
Beta strandi151 – 161Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GQVX-ray0.98A28-161[»]
1HI2X-ray1.60A28-161[»]
1HI3X-ray1.80A28-161[»]
1HI4X-ray1.80A28-161[»]
1HI5X-ray1.80A28-161[»]
1K2AX-ray1.00A26-160[»]
2BEXX-ray1.99C/D28-161[»]
2BZZX-ray0.98A28-161[»]
2C01X-ray1.24X28-161[»]
2C02X-ray2.00A28-161[»]
2C05X-ray1.86A28-161[»]
5E13X-ray1.34A1-161[»]
ProteinModelPortaliP10153.
SMRiP10153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10153.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni65 – 69Substrate binding5

Domaini

The N-terminal region is necessary for mediating chemotactic activity.

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JDT3. Eukaryota.
ENOG411136R. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiP10153.
KOiK01168.
OMAiMFYIVAC.
OrthoDBiEOG091G0SFK.
PhylomeDBiP10153.
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.

P10153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC
60 70 80 90 100
TNAMQVINNY QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHH
110 120 130 140 150
SGSQVPLIHC NLTTPSPQNI SNCRYAQTPA NMFYIVACDN RDQRRDPPQY
160
PVVPVHLDRI I
Length:161
Mass (Da):18,354
Last modified:January 1, 1990 - v2
Checksum:i9406C4596CA69038
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37W → R AA sequence (PubMed:3926759).Curated1
Sequence conflicti39 – 40ET → QE AA sequence (PubMed:3926759).Curated2
Sequence conflicti46T → V AA sequence (PubMed:3926759).Curated1
Sequence conflicti47S → T AA sequence (PubMed:3182786).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_059820100H → Q.Corresponds to variant rs8012891dbSNPEnsembl.1
Natural variantiVAR_013150156H → N.1 PublicationCorresponds to variant rs146887874dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30510 mRNA. Translation: AAC82505.1.
M28129 mRNA. Translation: AAA50284.1.
M24157 mRNA. Translation: AAA52337.1.
X16546 Genomic DNA. Translation: CAA34546.1.
AF294007 Genomic DNA. Translation: AAG31577.1.
AF294008 Genomic DNA. Translation: AAG31578.1.
AF294009 Genomic DNA. Translation: AAG31579.1.
AF294010 Genomic DNA. Translation: AAG31580.1.
AF294011 Genomic DNA. Translation: AAG31581.1.
AF294012 Genomic DNA. Translation: AAG31582.1.
AF294013 Genomic DNA. Translation: AAG31583.1.
AF294014 Genomic DNA. Translation: AAG31584.1.
AF294015 Genomic DNA. Translation: AAG31585.1.
X55987 Genomic DNA. Translation: CAA39459.1.
X55988 mRNA. Translation: CAA39460.1.
BC093678 mRNA. Translation: AAH93678.1.
BC093680 mRNA. Translation: AAH93680.1.
BC096059 mRNA. Translation: AAH96059.1.
CCDSiCCDS9561.1.
PIRiA35328. A33922.
RefSeqiNP_002925.1. NM_002934.2.
UniGeneiHs.728.

Genome annotation databases

EnsembliENST00000304625; ENSP00000303276; ENSG00000169385.
GeneIDi6036.
KEGGihsa:6036.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30510 mRNA. Translation: AAC82505.1.
M28129 mRNA. Translation: AAA50284.1.
M24157 mRNA. Translation: AAA52337.1.
X16546 Genomic DNA. Translation: CAA34546.1.
AF294007 Genomic DNA. Translation: AAG31577.1.
AF294008 Genomic DNA. Translation: AAG31578.1.
AF294009 Genomic DNA. Translation: AAG31579.1.
AF294010 Genomic DNA. Translation: AAG31580.1.
AF294011 Genomic DNA. Translation: AAG31581.1.
AF294012 Genomic DNA. Translation: AAG31582.1.
AF294013 Genomic DNA. Translation: AAG31583.1.
AF294014 Genomic DNA. Translation: AAG31584.1.
AF294015 Genomic DNA. Translation: AAG31585.1.
X55987 Genomic DNA. Translation: CAA39459.1.
X55988 mRNA. Translation: CAA39460.1.
BC093678 mRNA. Translation: AAH93678.1.
BC093680 mRNA. Translation: AAH93680.1.
BC096059 mRNA. Translation: AAH96059.1.
CCDSiCCDS9561.1.
PIRiA35328. A33922.
RefSeqiNP_002925.1. NM_002934.2.
UniGeneiHs.728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GQVX-ray0.98A28-161[»]
1HI2X-ray1.60A28-161[»]
1HI3X-ray1.80A28-161[»]
1HI4X-ray1.80A28-161[»]
1HI5X-ray1.80A28-161[»]
1K2AX-ray1.00A26-160[»]
2BEXX-ray1.99C/D28-161[»]
2BZZX-ray0.98A28-161[»]
2C01X-ray1.24X28-161[»]
2C02X-ray2.00A28-161[»]
2C05X-ray1.86A28-161[»]
5E13X-ray1.34A1-161[»]
ProteinModelPortaliP10153.
SMRiP10153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111965. 2 interactors.
IntActiP10153. 1 interactor.
STRINGi9606.ENSP00000303276.

Chemistry databases

BindingDBiP10153.
ChEMBLiCHEMBL5120.

PTM databases

iPTMnetiP10153.
PhosphoSitePlusiP10153.
UniCarbKBiP10153.

Polymorphism and mutation databases

BioMutaiRNASE2.
DMDMi133168.

Proteomic databases

EPDiP10153.
PaxDbiP10153.
PeptideAtlasiP10153.
PRIDEiP10153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304625; ENSP00000303276; ENSG00000169385.
GeneIDi6036.
KEGGihsa:6036.

Organism-specific databases

CTDi6036.
DisGeNETi6036.
GeneCardsiRNASE2.
HGNCiHGNC:10045. RNASE2.
HPAiHPA044983.
MIMi131410. gene.
neXtProtiNX_P10153.
OpenTargetsiENSG00000169385.
PharmGKBiPA34413.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JDT3. Eukaryota.
ENOG411136R. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiP10153.
KOiK01168.
OMAiMFYIVAC.
OrthoDBiEOG091G0SFK.
PhylomeDBiP10153.
TreeFamiTF333393.

Enzyme and pathway databases

BioCyciZFISH:HS09938-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiRNASE2. human.
EvolutionaryTraceiP10153.
GeneWikiiEosinophil-derived_neurotoxin.
GenomeRNAii6036.
PROiP10153.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169385.
CleanExiHS_RNASE2.
ExpressionAtlasiP10153. baseline and differential.
GenevisibleiP10153. 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 nameiRNAS2_HUMAN
AccessioniPrimary (citable) accession number: P10153
Secondary accession number(s): Q52M39, Q9H2B7, Q9UCG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 184 of the entry and version 2 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.