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Protein

Poly(A)-specific ribonuclease PARN

Gene

PARN

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

Functioni

3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization.5 Publications

Catalytic activityi

Exonucleolytic cleavage of poly(A) to 5'-AMP.2 Publications

Cofactori

Mg2+2 PublicationsNote: Divalent metal cations. Mg2+ is the most probable.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi28Divalent metal cation; catalyticCurated1
Metal bindingi30Divalent metal cation; catalyticCurated1
Metal bindingi292Divalent metal cation; catalyticCurated1
Metal bindingi382Divalent metal cation; catalyticCurated1

GO - Molecular functioni

  • cation binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR binding Source: ProtInc
  • nuclease activity Source: ProtInc
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • poly(A)-specific ribonuclease activity Source: Reactome
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • female gamete generation Source: ProtInc
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  • nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  • regulation of mRNA stability Source: Reactome
  • RNA modification Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Nonsense-mediated mRNA decay

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:HS06752-MONOMER.
ReactomeiR-HSA-380994. ATF4 activates genes.
R-HSA-429947. Deadenylation of mRNA.
R-HSA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
SIGNORiO95453.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(A)-specific ribonuclease PARN (EC:3.1.13.4)
Alternative name(s):
Deadenylating nuclease
Deadenylation nuclease
Polyadenylate-specific ribonuclease
Gene namesi
Name:PARN
Synonyms:DAN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:8609. PARN.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • nucleolus Source: UniProtKB-SubCell
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Dyskeratosis congenita, autosomal recessive, 6 (DKCB6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dyskeratosis congenita, a rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
See also OMIM:616353
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073782383A → V in DKCB6. 1 PublicationCorresponds to variant rs786200999dbSNPEnsembl.1
Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 4 (PFBMFT4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length.
See also OMIM:616371
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073783421K → R in PFBMFT4. 1 PublicationCorresponds to variant rs777090017dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi28D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications1
Mutagenesisi28D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). 3 Publications1
Mutagenesisi30E → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications1
Mutagenesisi30E → C: Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+). 3 Publications1
Mutagenesisi31F → A: Reduced affinity for poly(A). Loss of activity. 1 Publication1
Mutagenesisi34I → A: Reduced affinity for poly(A). Strongly reduced activity. 1 Publication1
Mutagenesisi113I → A: Loss of dimerization. Loss of activity. 1 Publication1
Mutagenesisi115F → A: Reduced affinity for poly(A). Little effect on activity. 1
Mutagenesisi123F → A: Loss of dimerization. Loss of activity. 1 Publication1
Mutagenesisi292D → A: Loss of function but does not abolish ability to bind RNA. 2 Publications1
Mutagenesisi292D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). 2 Publications1
Mutagenesisi326K → A: Reduced affinity for poly(A). Little effect on activity. 1
Mutagenesisi377H → A: Loss of activity. 1 Publication1
Mutagenesisi382D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications1
Mutagenesisi382D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). 3 Publications1
Mutagenesisi557S → A: Strong reduction of phosphorylation by MAPKAPK2. 1

Keywords - Diseasei

Disease mutation, Dyskeratosis congenita

Organism-specific databases

DisGeNETi5073.
MIMi616353. phenotype.
616371. phenotype.
OpenTargetsiENSG00000140694.
ENSG00000274829.
PharmGKBiPA29072.
PA32949.

Chemistry databases

ChEMBLiCHEMBL3616362.

Polymorphism and mutation databases

BioMutaiPARN.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002128511 – 639Poly(A)-specific ribonuclease PARNAdd BLAST639

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei163PhosphoserineCombined sources1
Modified residuei167PhosphoserineCombined sources1
Modified residuei220N6-acetyllysineCombined sources1
Modified residuei499N6-acetyllysineCombined sources1
Modified residuei530PhosphoserineCombined sources1
Modified residuei557Phosphoserine; by MAPKAPK2Combined sources1 Publication1
Modified residuei583PhosphoserineBy similarity1
Modified residuei587PhosphoserineBy similarity1
Modified residuei619PhosphoserineCombined sources1
Modified residuei623PhosphoserineCombined sources1
Modified residuei628PhosphoserineCombined sources1
Modified residuei631PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO95453.
MaxQBiO95453.
PaxDbiO95453.
PeptideAtlasiO95453.
PRIDEiO95453.

2D gel databases

SWISS-2DPAGEO95453.

PTM databases

iPTMnetiO95453.
PhosphoSitePlusiO95453.
SwissPalmiO95453.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

BgeeiENSG00000140694.
CleanExiHS_PARN.
ExpressionAtlasiO95453. baseline and differential.
GenevisibleiO95453. HS.

Organism-specific databases

HPAiCAB011673.
HPA006314.
HPA012010.

Interactioni

Subunit structurei

Homodimer. Interacts with KHSRP and CELF1/CUGBP1. Found in a mRNA decay complex with RENT1, RENT2 and RENT3B. Interacts with ZC3HAV1 in an RNA-independent manner.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei326Interaction with poly(A)1 Publication1

Binary interactionsi

WithEntry#Exp.IntActNotes
BARD1Q997284EBI-372832,EBI-473181
CSTF2P332405EBI-372832,EBI-711360
NCBP1Q091612EBI-372832,EBI-464743

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111107. 20 interactors.
DIPiDIP-31124N.
IntActiO95453. 6 interactors.
MINTiMINT-3002980.
STRINGi9606.ENSP00000387911.

Chemistry databases

BindingDBiO95453.

Structurei

Secondary structure

1639
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 21Combined sources17
Beta strandi23 – 32Combined sources10
Beta strandi36 – 38Combined sources3
Helixi50 – 60Combined sources11
Turni61 – 63Combined sources3
Beta strandi66 – 77Combined sources12
Turni78 – 81Combined sources4
Beta strandi82 – 92Combined sources11
Beta strandi97 – 101Combined sources5
Beta strandi105 – 109Combined sources5
Helixi110 – 118Combined sources9
Helixi123 – 127Combined sources5
Helixi136 – 141Combined sources6
Helixi175 – 177Combined sources3
Helixi178 – 192Combined sources15
Helixi207 – 217Combined sources11
Turni222 – 224Combined sources3
Beta strandi228 – 231Combined sources4
Beta strandi237 – 240Combined sources4
Beta strandi245 – 248Combined sources4
Turni249 – 252Combined sources4
Helixi260 – 265Combined sources6
Helixi271 – 280Combined sources10
Beta strandi283 – 288Combined sources6
Helixi290 – 300Combined sources11
Helixi308 – 318Combined sources11
Beta strandi320 – 324Combined sources5
Helixi325 – 329Combined sources5
Turni332 – 337Combined sources6
Helixi343 – 349Combined sources7
Beta strandi360 – 362Combined sources3
Helixi379 – 397Combined sources19
Helixi398 – 400Combined sources3
Beta strandi401 – 403Combined sources3
Turni413 – 415Combined sources3
Helixi416 – 418Combined sources3
Beta strandi419 – 429Combined sources11
Beta strandi445 – 451Combined sources7
Helixi458 – 464Combined sources7
Turni465 – 467Combined sources3
Beta strandi468 – 477Combined sources10
Beta strandi480 – 488Combined sources9
Helixi490 – 498Combined sources9
Helixi509 – 513Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A1RX-ray2.60A/B1-430[»]
2A1SX-ray2.60A/B/C/D1-430[»]
3CTRX-ray2.10A445-540[»]
ProteinModelPortaliO95453.
SMRiO95453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini178 – 245R3HPROSITE-ProRule annotationAdd BLAST68

Sequence similaritiesi

Belongs to the CAF1 family.Curated
Contains 1 R3H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1990. Eukaryota.
ENOG410XS9D. LUCA.
GeneTreeiENSGT00530000063673.
HOGENOMiHOG000007285.
HOVERGENiHBG053512.
InParanoidiO95453.
KOiK01148.
OMAiEDGWKEA.
OrthoDBiEOG091G04CM.
PhylomeDBiO95453.
TreeFamiTF314502.

Family and domain databases

Gene3Di3.30.1370.50. 1 hit.
3.30.420.10. 2 hits.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR014789. PolyA-riboNase_RNA_binding.
IPR001374. R3H_dom.
IPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF04857. CAF1. 1 hit.
PF01424. R3H. 1 hit.
PF08675. RNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.
SSF54928. SSF54928. 1 hit.
SSF82708. SSF82708. 1 hit.
PROSITEiPS51061. R3H. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95453-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP
60 70 80 90 100
EERYQKLKKH SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS
110 120 130 140 150
SPDVKFVCQS SSIDFLASQG FDFNKVFRNG IPYLNQEEER QLREQYDEKR
160 170 180 190 200
SQANGAGALS YVSPNTSKCP VTIPEDQKKF IDQVVEKIED LLQSEENKNL
210 220 230 240 250
DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV ISKVDEEERK
260 270 280 290 300
RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF
310 320 330 340 350
YCPLPADLSE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL
360 370 380 390 400
KETPFNPPKV ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF
410 420 430 440 450
LSPPKIHVSA RSKLIEPFFN KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV
460 470 480 490 500
TFPKEWKTSD LYQLFSAFGN IQISWIDDTS AFVSLSQPEQ VKIAVNTSKY
510 520 530 540 550
AESYRIQTYA EYMGRKQEEK QIKRKWTEDS WKEADSKRLN PQCIPYTLQN
560 570 580 590 600
HYYRNNSFTA PSTVGKRNLS PSQEEAGLED GVSGEISDTE LEQTDSCAEP
610 620 630
LSEGRKKAKK LKRMKKELSP AGSISKNSPA TLFEVPDTW
Length:639
Mass (Da):73,451
Last modified:May 1, 1999 - v1
Checksum:i6994BE39384DF7AC
GO
Isoform 2 (identifier: O95453-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.

Note: No experimental confirmation available. Non canonical splice junctions.
Show »
Length:578
Mass (Da):66,574
Checksum:i5E62F237DB650802
GO
Isoform 3 (identifier: O95453-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-98: Missing.

Show »
Length:593
Mass (Da):67,722
Checksum:i2908EEB765F91D80
GO
Isoform 4 (identifier: O95453-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-233: Missing.

Note: No experimental confirmation available.
Show »
Length:464
Mass (Da):52,989
Checksum:i6C4163C9604DFC5C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073782383A → V in DKCB6. 1 PublicationCorresponds to variant rs786200999dbSNPEnsembl.1
Natural variantiVAR_073783421K → R in PFBMFT4. 1 PublicationCorresponds to variant rs777090017dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0428461 – 61Missing in isoform 2. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_04284753 – 98Missing in isoform 3. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_05726959 – 233Missing in isoform 4. 1 PublicationAdd BLAST175

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005698 mRNA. Translation: CAA06683.1.
AK293189 mRNA. Translation: BAG56729.1.
AK299653 mRNA. Translation: BAG61572.1.
AK301648 mRNA. Translation: BAG63126.1.
AK315020 mRNA. Translation: BAG37510.1.
AC009167 Genomic DNA. No translation available.
AC092291 Genomic DNA. No translation available.
KF456163 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85110.1.
BC050029 mRNA. Translation: AAH50029.1.
CCDSiCCDS45419.1. [O95453-1]
CCDS45420.1. [O95453-2]
CCDS58425.1. [O95453-3]
RefSeqiNP_001127949.1. NM_001134477.2. [O95453-2]
NP_001229921.1. NM_001242992.1. [O95453-3]
NP_002573.1. NM_002582.3. [O95453-1]
UniGeneiHs.253197.

Genome annotation databases

EnsembliENST00000341484; ENSP00000345456; ENSG00000140694. [O95453-2]
ENST00000420015; ENSP00000410525; ENSG00000140694. [O95453-3]
ENST00000437198; ENSP00000387911; ENSG00000140694. [O95453-1]
ENST00000539279; ENSP00000444381; ENSG00000140694. [O95453-4]
ENST00000615183; ENSP00000478668; ENSG00000274829. [O95453-1]
ENST00000618929; ENSP00000484279; ENSG00000274829. [O95453-3]
ENST00000631868; ENSP00000488554; ENSG00000274829. [O95453-4]
ENST00000634004; ENSP00000487634; ENSG00000274829. [O95453-2]
GeneIDi5073.
KEGGihsa:5073.
UCSCiuc010uzc.3. human. [O95453-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005698 mRNA. Translation: CAA06683.1.
AK293189 mRNA. Translation: BAG56729.1.
AK299653 mRNA. Translation: BAG61572.1.
AK301648 mRNA. Translation: BAG63126.1.
AK315020 mRNA. Translation: BAG37510.1.
AC009167 Genomic DNA. No translation available.
AC092291 Genomic DNA. No translation available.
KF456163 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85110.1.
BC050029 mRNA. Translation: AAH50029.1.
CCDSiCCDS45419.1. [O95453-1]
CCDS45420.1. [O95453-2]
CCDS58425.1. [O95453-3]
RefSeqiNP_001127949.1. NM_001134477.2. [O95453-2]
NP_001229921.1. NM_001242992.1. [O95453-3]
NP_002573.1. NM_002582.3. [O95453-1]
UniGeneiHs.253197.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A1RX-ray2.60A/B1-430[»]
2A1SX-ray2.60A/B/C/D1-430[»]
3CTRX-ray2.10A445-540[»]
ProteinModelPortaliO95453.
SMRiO95453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111107. 20 interactors.
DIPiDIP-31124N.
IntActiO95453. 6 interactors.
MINTiMINT-3002980.
STRINGi9606.ENSP00000387911.

Chemistry databases

BindingDBiO95453.
ChEMBLiCHEMBL3616362.

PTM databases

iPTMnetiO95453.
PhosphoSitePlusiO95453.
SwissPalmiO95453.

Polymorphism and mutation databases

BioMutaiPARN.

2D gel databases

SWISS-2DPAGEO95453.

Proteomic databases

EPDiO95453.
MaxQBiO95453.
PaxDbiO95453.
PeptideAtlasiO95453.
PRIDEiO95453.

Protocols and materials databases

DNASUi2987.
5073.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341484; ENSP00000345456; ENSG00000140694. [O95453-2]
ENST00000420015; ENSP00000410525; ENSG00000140694. [O95453-3]
ENST00000437198; ENSP00000387911; ENSG00000140694. [O95453-1]
ENST00000539279; ENSP00000444381; ENSG00000140694. [O95453-4]
ENST00000615183; ENSP00000478668; ENSG00000274829. [O95453-1]
ENST00000618929; ENSP00000484279; ENSG00000274829. [O95453-3]
ENST00000631868; ENSP00000488554; ENSG00000274829. [O95453-4]
ENST00000634004; ENSP00000487634; ENSG00000274829. [O95453-2]
GeneIDi5073.
KEGGihsa:5073.
UCSCiuc010uzc.3. human. [O95453-1]

Organism-specific databases

CTDi5073.
DisGeNETi5073.
GeneCardsiPARN.
HGNCiHGNC:8609. PARN.
HPAiCAB011673.
HPA006314.
HPA012010.
MIMi604212. gene.
616353. phenotype.
616371. phenotype.
neXtProtiNX_O95453.
OpenTargetsiENSG00000140694.
ENSG00000274829.
PharmGKBiPA29072.
PA32949.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1990. Eukaryota.
ENOG410XS9D. LUCA.
GeneTreeiENSGT00530000063673.
HOGENOMiHOG000007285.
HOVERGENiHBG053512.
InParanoidiO95453.
KOiK01148.
OMAiEDGWKEA.
OrthoDBiEOG091G04CM.
PhylomeDBiO95453.
TreeFamiTF314502.

Enzyme and pathway databases

BioCyciZFISH:HS06752-MONOMER.
ReactomeiR-HSA-380994. ATF4 activates genes.
R-HSA-429947. Deadenylation of mRNA.
R-HSA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
SIGNORiO95453.

Miscellaneous databases

ChiTaRSiPARN. human.
EvolutionaryTraceiO95453.
GeneWikiiPARN.
Poly(A)-specific_ribonuclease.
GenomeRNAii5073.
PROiO95453.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140694.
CleanExiHS_PARN.
ExpressionAtlasiO95453. baseline and differential.
GenevisibleiO95453. HS.

Family and domain databases

Gene3Di3.30.1370.50. 1 hit.
3.30.420.10. 2 hits.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR014789. PolyA-riboNase_RNA_binding.
IPR001374. R3H_dom.
IPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF04857. CAF1. 1 hit.
PF01424. R3H. 1 hit.
PF08675. RNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.
SSF54928. SSF54928. 1 hit.
SSF82708. SSF82708. 1 hit.
PROSITEiPS51061. R3H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARN_HUMAN
AccessioniPrimary (citable) accession number: O95453
Secondary accession number(s): B2RCB3
, B4DDG8, B4DSB0, B4DWR4, B4E1H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 148 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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.