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Protein

Non-secretory ribonuclease

Gene

RNASE2

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

GO - Biological processi

  • chemotaxis Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • neutrophil degranulation Source: Reactome
  • RNA catabolic process Source: ProtInc
  • RNA phosphodiester bond hydrolysis Source: UniProtKB

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processChemotaxis

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000169385.2
HGNCiHGNC:10045 RNASE2
MIMi131410 gene
neXtProtiNX_P10153

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

Lysosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi6036
OpenTargetsiENSG00000169385
PharmGKBiPA34413

Chemistry databases

ChEMBLiCHEMBL5120
DrugBankiDB02098 Adenosine-2'-5'-Diphosphate
DB01812 Adenosine-3'-5'-Diphosphate

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) tryptophan2 Publications1
Glycosylationi44N-linked (GlcNAc...) asparagine1
Disulfide bondi50 ↔ 110
Modified residuei60Nitrated tyrosine1 Publication1
Disulfide bondi64 ↔ 123
Disulfide bondi82 ↔ 138
Glycosylationi86N-linked (GlcNAc...) asparagine1
Disulfide bondi89 ↔ 98
Glycosylationi92N-linked (GlcNAc...) asparagine1
Glycosylationi111N-linked (GlcNAc...) asparagine1
Glycosylationi119N-linked (GlcNAc...) asparagine1

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
ProteomicsDBi52573

PTM databases

GlyConnecti436
437
539
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
ELMiP10153
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

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
GeneTreeiENSGT00900000140993
HOGENOMiHOG000276882
HOVERGENiHBG008396
InParanoidiP10153
KOiK01168
OMAiMFYIVAC
OrthoDBiEOG091G0SFK
PhylomeDBiP10153
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.

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 dbSNP:rs8012891Ensembl.1
Natural variantiVAR_013150156H → N1 PublicationCorresponds to variant dbSNP:rs146887874Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiRNAS2_HUMAN
AccessioniPrimary (citable) accession number: P10153
Secondary accession number(s): Q52M39, Q9H2B7, Q9UCG7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: June 20, 2018
This is version 195 of the entry and version 2 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. 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

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