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Protein

Ribonuclease UK114

Gene

HRSP12

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

Functioni

Endoribonuclease responsible for the inhibition of the translation by cleaving mRNA. Inhibits cell-free protein synthesis. Cleaves phosphodiester bonds only in single-stranded RNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease UK114 (EC:3.1.-.-)
Alternative name(s):
14.5 kDa translational inhibitor protein
Short name:
p14.5
Heat-responsive protein 12
UK114 antigen homolog
Gene namesi
Name:HRSP12
Synonyms:PSP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:16897. HRSP12.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Mostly cytoplasmic but, in less differentiated cells occasionally nuclear.

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: ProtInc
  • peroxisome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134890258.

Chemistry

DrugBankiDB03793. Benzoic Acid.

Polymorphism and mutation databases

BioMutaiHRSP12.
DMDMi1717975.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 137136Ribonuclease UK114PRO_0000170308Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei60 – 601N6-succinyllysineBy similarity
Modified residuei67 – 671N6-succinyllysineBy similarity
Modified residuei74 – 741PhosphothreonineCombined sources
Modified residuei136 – 1361PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP52758.
PaxDbiP52758.
PeptideAtlasiP52758.
PRIDEiP52758.
TopDownProteomicsiP52758.

2D gel databases

UCD-2DPAGEP52758.

PTM databases

iPTMnetiP52758.
PhosphoSiteiP52758.

Expressioni

Tissue specificityi

Hepatocytes and renal distal tubular epithelial cells. Only weak expression in other tissues.

Developmental stagei

Up-regulated during cellular differentiation.

Gene expression databases

BgeeiP52758.
CleanExiHS_HRSP12.
ExpressionAtlasiP52758. baseline and differential.
GenevisibleiP52758. HS.

Organism-specific databases

HPAiHPA022856.
HPA023489.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi115541. 25 interactions.
IntActiP52758. 9 interactions.
STRINGi9606.ENSP00000254878.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi22 – 276Combined sources
Beta strandi30 – 367Combined sources
Turni41 – 433Combined sources
Beta strandi48 – 503Combined sources
Helixi51 – 6818Combined sources
Helixi73 – 753Combined sources
Beta strandi76 – 849Combined sources
Helixi86 – 883Combined sources
Helixi89 – 9911Combined sources
Beta strandi106 – 1116Combined sources
Helixi116 – 1183Combined sources
Beta strandi120 – 1289Combined sources
Beta strandi132 – 1354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONIX-ray1.90A/B/C/D/E/F/G/H/I2-137[»]
ProteinModelPortaliP52758.
SMRiP52758. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52758.

Family & Domainsi

Sequence similaritiesi

Belongs to the RutC family.Curated

Phylogenomic databases

eggNOGiKOG2317. Eukaryota.
COG0251. LUCA.
GeneTreeiENSGT00420000029792.
HOGENOMiHOG000267215.
HOVERGENiHBG003597.
InParanoidiP52758.
OrthoDBiEOG75F4G2.
PhylomeDBiP52758.
TreeFamiTF105775.

Family and domain databases

Gene3Di3.30.1330.40. 1 hit.
InterProiIPR013813. Endoribo_LPSP/chorism_mut-like.
IPR006056. RidA.
IPR019897. RidA_CS.
IPR006175. YjgF/YER057c/UK114.
[Graphical view]
PANTHERiPTHR11803. PTHR11803. 1 hit.
PfamiPF01042. Ribonuc_L-PSP. 1 hit.
[Graphical view]
SUPFAMiSSF55298. SSF55298. 1 hit.
TIGRFAMsiTIGR00004. TIGR00004. 1 hit.
PROSITEiPS01094. UPF0076. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P52758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLIRRVIS TAKAPGAIGP YSQAVLVDRT IYISGQIGMD PSSGQLVSGG
60 70 80 90 100
VAEEAKQALK NMGEILKAAG CDFTNVVKTT VLLADINDFN TVNEIYKQYF
110 120 130
KSNFPARAAY QVAALPKGSR IEIEAVAIQG PLTTASL
Length:137
Mass (Da):14,494
Last modified:October 1, 1996 - v1
Checksum:iDD0740621E8BE6AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841A → V in CAG46453 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95384 mRNA. Translation: CAA64670.1.
AY026764 Genomic DNA. Translation: AAK01939.1.
CR456844 mRNA. Translation: CAG33125.1.
CR541652 mRNA. Translation: CAG46453.1.
CH471060 Genomic DNA. Translation: EAW91774.1.
BC010280 mRNA. Translation: AAH10280.1.
BC012592 mRNA. Translation: AAH12592.1.
BC093059 mRNA. Translation: AAH93059.1.
CCDSiCCDS6276.1.
RefSeqiNP_005827.1. NM_005836.2.
UniGeneiHs.18426.

Genome annotation databases

EnsembliENST00000254878; ENSP00000254878; ENSG00000132541.
GeneIDi10247.
KEGGihsa:10247.
UCSCiuc003yii.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95384 mRNA. Translation: CAA64670.1.
AY026764 Genomic DNA. Translation: AAK01939.1.
CR456844 mRNA. Translation: CAG33125.1.
CR541652 mRNA. Translation: CAG46453.1.
CH471060 Genomic DNA. Translation: EAW91774.1.
BC010280 mRNA. Translation: AAH10280.1.
BC012592 mRNA. Translation: AAH12592.1.
BC093059 mRNA. Translation: AAH93059.1.
CCDSiCCDS6276.1.
RefSeqiNP_005827.1. NM_005836.2.
UniGeneiHs.18426.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONIX-ray1.90A/B/C/D/E/F/G/H/I2-137[»]
ProteinModelPortaliP52758.
SMRiP52758. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115541. 25 interactions.
IntActiP52758. 9 interactions.
STRINGi9606.ENSP00000254878.

Chemistry

DrugBankiDB03793. Benzoic Acid.

PTM databases

iPTMnetiP52758.
PhosphoSiteiP52758.

Polymorphism and mutation databases

BioMutaiHRSP12.
DMDMi1717975.

2D gel databases

UCD-2DPAGEP52758.

Proteomic databases

EPDiP52758.
PaxDbiP52758.
PeptideAtlasiP52758.
PRIDEiP52758.
TopDownProteomicsiP52758.

Protocols and materials databases

DNASUi10247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254878; ENSP00000254878; ENSG00000132541.
GeneIDi10247.
KEGGihsa:10247.
UCSCiuc003yii.2. human.

Organism-specific databases

CTDi10247.
GeneCardsiHRSP12.
HGNCiHGNC:16897. HRSP12.
HPAiHPA022856.
HPA023489.
MIMi602487. gene.
neXtProtiNX_P52758.
PharmGKBiPA134890258.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2317. Eukaryota.
COG0251. LUCA.
GeneTreeiENSGT00420000029792.
HOGENOMiHOG000267215.
HOVERGENiHBG003597.
InParanoidiP52758.
OrthoDBiEOG75F4G2.
PhylomeDBiP52758.
TreeFamiTF105775.

Miscellaneous databases

EvolutionaryTraceiP52758.
GeneWikiiHeat-responsive_protein_12.
GenomeRNAii10247.
PROiP52758.
SOURCEiSearch...

Gene expression databases

BgeeiP52758.
CleanExiHS_HRSP12.
ExpressionAtlasiP52758. baseline and differential.
GenevisibleiP52758. HS.

Family and domain databases

Gene3Di3.30.1330.40. 1 hit.
InterProiIPR013813. Endoribo_LPSP/chorism_mut-like.
IPR006056. RidA.
IPR019897. RidA_CS.
IPR006175. YjgF/YER057c/UK114.
[Graphical view]
PANTHERiPTHR11803. PTHR11803. 1 hit.
PfamiPF01042. Ribonuc_L-PSP. 1 hit.
[Graphical view]
SUPFAMiSSF55298. SSF55298. 1 hit.
TIGRFAMsiTIGR00004. TIGR00004. 1 hit.
PROSITEiPS01094. UPF0076. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a 14.5-kDa trichloroacetic-acid-soluble translational inhibitor protein from human monocytes that is upregulated upon cellular differentiation."
    Schmiedeknecht G., Kerkhoff C., Orso E., Stoehr J., Aslanidis C., Nagy G.M., Knuechel R., Schmitz G.
    Eur. J. Biochem. 242:339-351(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-28; 30-43; 68-78 AND 98-113.
    Tissue: Liver.
  2. "Genomic structure of the human translational inhibitor protein p14.5."
    Pozdniakovaite N., Popendikyte V., Naktinis V.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow, Cervix and Skin.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiUK114_HUMAN
AccessioniPrimary (citable) accession number: P52758
Secondary accession number(s): Q6FHU9, Q6IBG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 145 of the entry and version 1 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 8
    Human chromosome 8: 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.