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UniProtKB - P07998 (RNAS1_HUMAN)
Protein
Ribonuclease pancreatic
Gene
RNASE1
Organism
Homo sapiens (Human)
Status
Functioni
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
1 PublicationCatalytic activityi
- An (RNA) containing cytidine + H(2)O = an (RNA)-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA). EC:4.6.1.18
- An (RNA) containing uridine + H(2)O = an (RNA)-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA). EC:4.6.1.18
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 35 | SubstrateBy similarity | 1 | |
Binding sitei | 38 | SubstrateBy similarity | 1 | |
Active sitei | 40 | Proton acceptor | 1 | |
Binding sitei | 94 | SubstrateBy similarity | 1 | |
Binding sitei | 113 | SubstrateBy similarity | 1 | |
Active sitei | 147 | Proton donor | 1 |
GO - Molecular functioni
- lyase activity Source: UniProtKB-KW
- 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 function | Endonuclease, Hydrolase, Lyase, Nuclease |
Enzyme and pathway databases
BRENDAi | 4.6.1.18, 2681 |
PathwayCommonsi | P07998 |
Reactomei | R-HSA-9613829, Chaperone Mediated Autophagy R-HSA-9615710, Late endosomal microautophagy |
SignaLinki | P07998 |
Names & Taxonomyi
Protein namesi | Recommended name: Ribonuclease pancreatic (EC:4.6.1.18)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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:10044, RNASE1 |
MIMi | 180440, gene |
neXtProti | NX_P07998 |
VEuPathDBi | HostDB:ENSG00000129538 |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Keywords - Cellular componenti
SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 67 | R → 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 Publication | 1 | |
Mutagenesisi | 95 | N → 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 Publication | 1 | |
Mutagenesisi | 116 – 117 | NG → RS: No effect on inhibition by RNH1. 1 Publication | 2 | |
Mutagenesisi | 116 | N → 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 Publication | 1 | |
Mutagenesisi | 117 | G → 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 Publication | 1 | |
Mutagenesisi | 119 | R → 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 Publication | 1 |
Organism-specific databases
DisGeNETi | 6035 |
OpenTargetsi | ENSG00000129538 |
PharmGKBi | PA34412 |
Miscellaneous databases
Pharosi | P07998, Tchem |
Chemistry databases
ChEMBLi | CHEMBL5425 |
DrugBanki | DB08661, 1-(2,5-dideoxy-5-pyrrolidin-1-yl-beta-L-erythro-pentofuranosyl)-5-methylpyrimidine-2,4(1H,3H)-dione DB03765, 2'-cytidylic acid DB02573, 2'-deoxycytidine-2'-deoxyadenosine-3',5'-monophosphate DB03448, 2'-Deoxyuridine 3'-Monophosphate DB03155, 2'-fluoro-2'-deoxyuridine 3'-monophosphate DB02363, 2'-Monophosphoadenosine-5'-Diphosphate DB01842, 3'-Phosphate-Adenosine-5'-Diphosphate DB02714, 3'-Uridinemonophosphate DB08596, 5'-deoxy-5'-piperidin-1-ylthymidine DB03792, 5-Aminouracil DB01812, Adenosine 3',5'-diphosphate DB02098, Adenosine-2'-5'-Diphosphate DB03186, Adenylate-3'-phosphate-[[2'-deoxy-uridine-5'-phosphate]-3'-phosphate] DB02805, Arabinouridine 3'-phosphate DB00128, Aspartic acid DB04272, Citric acid DB02987, Cysteine-S-acetamide DB01961, Cytidine 3'-monophosphate DB03326, Deoxycytidylyl-3',5'-guanosine DB01942, Formic acid DB00536, Guanidine DB04464, N-Formylmethionine DB03726, Purine Riboside-5'-Monophosphate DB03900, tert-butanol DB03512, Uridine-2',3'-vanadate DB03447, Uridylyl-2'-5'-phospho-adenosine DB04514, Uridylyl-2'-5'-phospho-guanosine |
Genetic variation databases
BioMutai | RNASE1 |
DMDMi | 1350818 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 28 | 6 PublicationsAdd BLAST | 28 | |
ChainiPRO_0000030921 | 29 – 156 | Ribonuclease pancreaticAdd BLAST | 128 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 54 ↔ 112 | |||
Glycosylationi | 62 | N-linked (GlcNAc...) asparagine; partial1 Publication | 1 | |
Disulfide bondi | 68 ↔ 123 | |||
Disulfide bondi | 86 ↔ 138 | |||
Disulfide bondi | 93 ↔ 100 | |||
Glycosylationi | 104 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 116 | N-linked (GlcNAc...) asparagine1 Publication | 1 |
Post-translational modificationi
N-linked glycans are of complex type.1 Publication
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
jPOSTi | P07998 |
MassIVEi | P07998 |
PaxDbi | P07998 |
PeptideAtlasi | P07998 |
PRIDEi | P07998 |
ProteomicsDBi | 52059 |
PTM databases
GlyConnecti | 1973, 3 N-Linked glycans (2 sites) |
GlyGeni | P07998, 3 sites, 3 N-linked glycans (2 sites) |
iPTMneti | P07998 |
PhosphoSitePlusi | P07998 |
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
Bgeei | ENSG00000129538, Expressed in right testis and 239 other tissues |
ExpressionAtlasi | P07998, baseline and differential |
Genevisiblei | P07998, HS |
Organism-specific databases
HPAi | ENSG00000129538, Tissue enriched (pancreas) |
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 PublicationBinary interactionsi
Protein-protein interaction databases
BioGRIDi | 111964, 11 interactors |
IntActi | P07998, 10 interactors |
MINTi | P07998 |
STRINGi | 9606.ENSP00000381057 |
Chemistry databases
BindingDBi | P07998 |
Miscellaneous databases
RNActi | P07998, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P07998 |
BMRBi | P07998 |
SMRi | P07998 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07998 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 33 – 53 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 69 – 73 | Substrate bindingBy similarity | 5 |
Sequence similaritiesi
Belongs to the pancreatic ribonuclease family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG502SQ4K, Eukaryota |
GeneTreei | ENSGT00940000160869 |
HOGENOMi | CLU_117006_0_0_1 |
InParanoidi | P07998 |
OMAi | SNSTYCN |
OrthoDBi | 1549558at2759 |
PhylomeDBi | P07998 |
TreeFami | TF333393 |
Family and domain databases
Gene3Di | 3.10.130.10, 1 hit |
InterProi | View protein in InterPro IPR001427, RNaseA IPR036816, RNaseA-like_dom_sf IPR023411, RNaseA_AS IPR023412, RNaseA_domain |
PANTHERi | PTHR11437, PTHR11437, 1 hit |
Pfami | View protein in Pfam PF00074, RnaseA, 1 hit |
PRINTSi | PR00794, RIBONUCLEASE |
SMARTi | View protein in SMART SM00092, RNAse_Pc, 1 hit |
SUPFAMi | SSF54076, SSF54076, 1 hit |
PROSITEi | View protein in PROSITE PS00127, RNASE_PANCREATIC, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P07998-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketG3V357 | G3V357_HUMAN | Ribonuclease pancreatic | RNASE1 | 116 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2 | A → G in CAA55817 (PubMed:8588814).Curated | 1 | |
Sequence conflicti | 4 | Missing in AAB35096 (PubMed:7649283).Curated | 1 | |
Sequence conflicti | 9 – 11 | RLL → VLP in AAB35096 (PubMed:7649283).Curated | 3 | |
Sequence conflicti | 16 – 22 | ILLVLGW → VLLLVR in AAB35096 (PubMed:7649283).Curated | 7 | |
Sequence conflicti | 67 | R → L in CAG29314 (Ref. 4) Curated | 1 | |
Sequence conflicti | 151 | S → T in CAA55817 (PubMed:8588814).Curated | 1 |
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 |
CCDSi | CCDS9559.1 |
PIRi | I53530 S45003, NRHU1 |
RefSeqi | NP_002924.1, NM_002933.4 NP_937875.1, NM_198232.2 NP_937877.1, NM_198234.2 NP_937878.1, NM_198235.2 |
Genome annotation databases
Similar proteinsi
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 |
CCDSi | CCDS9559.1 |
PIRi | I53530 S45003, NRHU1 |
RefSeqi | NP_002924.1, NM_002933.4 NP_937875.1, NM_198232.2 NP_937877.1, NM_198234.2 NP_937878.1, NM_198235.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1DZA | X-ray | 1.65 | A/B | 28-156 | [»] | |
1E21 | X-ray | 1.90 | A | 29-156 | [»] | |
1H8X | X-ray | 2.00 | A/B | 29-156 | [»] | |
1Z7X | X-ray | 1.95 | X/Z | 29-156 | [»] | |
2E0J | X-ray | 1.60 | A/B | 29-156 | [»] | |
2E0L | X-ray | 1.60 | A/B | 29-156 | [»] | |
2E0M | X-ray | 1.70 | A/B | 29-156 | [»] | |
2E0O | X-ray | 2.00 | A/B | 29-156 | [»] | |
2K11 | NMR | - | A | 29-155 | [»] | |
2Q4G | X-ray | 1.95 | X/Z | 29-156 | [»] | |
3F8G | X-ray | 2.60 | A/B | 29-153 | [»] | |
4KXH | X-ray | 2.70 | A/B/C/D | 29-156 | [»] | |
AlphaFoldDBi | P07998 | |||||
BMRBi | P07998 | |||||
SMRi | P07998 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111964, 11 interactors |
IntActi | P07998, 10 interactors |
MINTi | P07998 |
STRINGi | 9606.ENSP00000381057 |
Chemistry databases
BindingDBi | P07998 |
ChEMBLi | CHEMBL5425 |
DrugBanki | DB08661, 1-(2,5-dideoxy-5-pyrrolidin-1-yl-beta-L-erythro-pentofuranosyl)-5-methylpyrimidine-2,4(1H,3H)-dione DB03765, 2'-cytidylic acid DB02573, 2'-deoxycytidine-2'-deoxyadenosine-3',5'-monophosphate DB03448, 2'-Deoxyuridine 3'-Monophosphate DB03155, 2'-fluoro-2'-deoxyuridine 3'-monophosphate DB02363, 2'-Monophosphoadenosine-5'-Diphosphate DB01842, 3'-Phosphate-Adenosine-5'-Diphosphate DB02714, 3'-Uridinemonophosphate DB08596, 5'-deoxy-5'-piperidin-1-ylthymidine DB03792, 5-Aminouracil DB01812, Adenosine 3',5'-diphosphate DB02098, Adenosine-2'-5'-Diphosphate DB03186, Adenylate-3'-phosphate-[[2'-deoxy-uridine-5'-phosphate]-3'-phosphate] DB02805, Arabinouridine 3'-phosphate DB00128, Aspartic acid DB04272, Citric acid DB02987, Cysteine-S-acetamide DB01961, Cytidine 3'-monophosphate DB03326, Deoxycytidylyl-3',5'-guanosine DB01942, Formic acid DB00536, Guanidine DB04464, N-Formylmethionine DB03726, Purine Riboside-5'-Monophosphate DB03900, tert-butanol DB03512, Uridine-2',3'-vanadate DB03447, Uridylyl-2'-5'-phospho-adenosine DB04514, Uridylyl-2'-5'-phospho-guanosine |
PTM databases
GlyConnecti | 1973, 3 N-Linked glycans (2 sites) |
GlyGeni | P07998, 3 sites, 3 N-linked glycans (2 sites) |
iPTMneti | P07998 |
PhosphoSitePlusi | P07998 |
Genetic variation databases
BioMutai | RNASE1 |
DMDMi | 1350818 |
Proteomic databases
jPOSTi | P07998 |
MassIVEi | P07998 |
PaxDbi | P07998 |
PeptideAtlasi | P07998 |
PRIDEi | P07998 |
ProteomicsDBi | 52059 |
Protocols and materials databases
Antibodypediai | 18, 285 antibodies from 24 providers |
DNASUi | 6035 |
Genome annotation databases
Organism-specific databases
CTDi | 6035 |
DisGeNETi | 6035 |
GeneCardsi | RNASE1 |
HGNCi | HGNC:10044, RNASE1 |
HPAi | ENSG00000129538, Tissue enriched (pancreas) |
MIMi | 180440, gene |
neXtProti | NX_P07998 |
OpenTargetsi | ENSG00000129538 |
PharmGKBi | PA34412 |
VEuPathDBi | HostDB:ENSG00000129538 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502SQ4K, Eukaryota |
GeneTreei | ENSGT00940000160869 |
HOGENOMi | CLU_117006_0_0_1 |
InParanoidi | P07998 |
OMAi | SNSTYCN |
OrthoDBi | 1549558at2759 |
PhylomeDBi | P07998 |
TreeFami | TF333393 |
Enzyme and pathway databases
BRENDAi | 4.6.1.18, 2681 |
PathwayCommonsi | P07998 |
Reactomei | R-HSA-9613829, Chaperone Mediated Autophagy R-HSA-9615710, Late endosomal microautophagy |
SignaLinki | P07998 |
Miscellaneous databases
BioGRID-ORCSi | 6035, 17 hits in 1074 CRISPR screens |
ChiTaRSi | RNASE1, human |
EvolutionaryTracei | P07998 |
GeneWikii | RNASE1 |
GenomeRNAii | 6035 |
Pharosi | P07998, Tchem |
PROi | PR:P07998 |
RNActi | P07998, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000129538, Expressed in right testis and 239 other tissues |
ExpressionAtlasi | P07998, baseline and differential |
Genevisiblei | P07998, HS |
Family and domain databases
Gene3Di | 3.10.130.10, 1 hit |
InterProi | View protein in InterPro IPR001427, RNaseA IPR036816, RNaseA-like_dom_sf IPR023411, RNaseA_AS IPR023412, RNaseA_domain |
PANTHERi | PTHR11437, PTHR11437, 1 hit |
Pfami | View protein in Pfam PF00074, RnaseA, 1 hit |
PRINTSi | PR00794, RIBONUCLEASE |
SMARTi | View protein in SMART SM00092, RNAse_Pc, 1 hit |
SUPFAMi | SSF54076, SSF54076, 1 hit |
PROSITEi | View protein in PROSITE PS00127, RNASE_PANCREATIC, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RNAS1_HUMAN | |
Accessioni | P07998Primary (citable) accession number: P07998 Secondary accession number(s): B2R589 Q9UCB5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | February 1, 1996 | |
Last modified: | May 25, 2022 | |
This is version 210 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families