PARN
entrez
5073
canonical
uniprot
O95453
canonical
ensembl
ENSG00000140694
resolver
ensembl
ENSG00000274829
resolver
ensp
ENSP00000345456
resolver
ensp
ENSP00000387911
resolver
ensp
ENSP00000410525
resolver
ensp
ENSP00000498644
resolver
ensp
ENSP00000499078
resolver
ensp
ENSP00000499110
resolver
ensp
ENSP00000703183
resolver
ensp
ENSP00000782720
resolver
enst
ENST00000650960
resolver
enst
ENST00000651049
resolver
enst
ENST00000651634
resolver
genesymbol
PARN
resolver
genesymbol_syn
DAN
resolver
hgnc
HGNC:8609
resolver
uniprot
A0A494C0Q2
resolver
uniprot
A0A494C1K5
resolver
uniprot
A0A494C1N1
resolver
uniprot
B2RCB3
resolver
uniprot
B3KN69
resolver
uniprot
B4DDG8
resolver
uniprot
B4DSB0
resolver
uniprot
B4DWR4
resolver
uniprot
B4E1H6
resolver
uniprot_entry
A0A494C0Q2_HUMAN
resolver
uniprot_entry
A0A494C1K5_HUMAN
resolver
uniprot_entry
A0A494C1N1_HUMAN
resolver
uniprot_entry
B3KN69_HUMAN
resolver
uniprot_entry
PARN_HUMAN
resolver
uniprot_sec
B2RCB3
resolver
uniprot_sec
B4DDG8
resolver
uniprot_sec
B4DSB0
resolver
uniprot_sec
B4DWR4
resolver
uniprot_sec
B4E1H6
resolver
amino_acid_sequence
MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW
uniprot
proteins
disease_involvement
DISEASE: Dyskeratosis congenita, autosomal recessive, 6 (DKCB6) [MIM:616353]: A 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. {ECO:0000269|PubMed:25893599}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pulmonary fibrosis, and/or bone marrow failure syndrome, telomere-related, 4 (PFBMFT4) [MIM:616371]: An autosomal dominant 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. {ECO:0000269|PubMed:25848748}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.13.4
uniprot
proteins
function
FUNCTION: 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 (PubMed:10882133, PubMed:11359775, PubMed:12748283, PubMed:15175153, PubMed:9736620). Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability (PubMed:22442037, PubMed:25049417). {ECO:0000269|PubMed:10882133, ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15175153, ECO:0000269|PubMed:22442037, ECO:0000269|PubMed:25049417, ECO:0000269|PubMed:9736620}.
uniprot
proteins
mass_dalton
73451
uniprot
proteins
mutagenesis
MUTAGEN 28; /note="D->A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15358788"; MUTAGEN 28; /note="D->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+)."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15358788"; MUTAGEN 30; /note="E->A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15358788"; MUTAGEN 30; /note="E->C: Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+)."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15358788"; MUTAGEN 31; /note="F->A: Reduced affinity for poly(A). Loss of activity."; /evidence="ECO:0000269|PubMed:16281054"; MUTAGEN 34; /note="I->A: Reduced affinity for poly(A). Strongly reduced activity."; /evidence="ECO:0000269|PubMed:16281054"; MUTAGEN 113; /note="I->A: Loss of dimerization. Loss of activity."; /evidence="ECO:0000269|PubMed:16281054"; MUTAGEN 115; /note="F->A: Reduced affinity for poly(A). Little effect on activity."; MUTAGEN 123; /note="F->A: Loss of dimerization. Loss of activity."; /evidence="ECO:0000269|PubMed:16281054"; MUTAGEN 292; /note="D->A: Loss of function but does not abolish ability to bind RNA."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:15358788"; MUTAGEN 292; /note="D->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+)."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:15358788"; MUTAGEN 326; /note="K->A: Reduced affinity for poly(A). Little effect on activity."; MUTAGEN 377; /note="H->A: Loss of activity."; /evidence="ECO:0000269|PubMed:16281054"; MUTAGEN 382; /note="D->A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15358788"; MUTAGEN 382; /note="D->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+)."; /evidence="ECO:0000269|PubMed:11742007, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15358788"; MUTAGEN 557; /note="S->A: Strong reduction of phosphorylation by MAPKAPK2.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress. {ECO:0000269|PubMed:20932473}.
uniprot
proteins
protein_family
CAF1 family
uniprot
proteins
pubmed
10640832
uniprot
proteins
pubmed
10801819
uniprot
proteins
pubmed
10882133
uniprot
proteins
pubmed
11359775
uniprot
proteins
pubmed
11742007
uniprot
proteins
pubmed
12429849
uniprot
proteins
pubmed
12748283
uniprot
proteins
pubmed
14527413
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14731398
uniprot
proteins
pubmed
15175153
uniprot
proteins
pubmed
15358788
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16281054
uniprot
proteins
pubmed
16601207
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20932473
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21876179
uniprot
proteins
pubmed
22442037
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25049417
uniprot
proteins
pubmed
25848748
uniprot
proteins
pubmed
25893599
uniprot
proteins
pubmed
9736620
uniprot
proteins
sequence_length
639
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9736620}. Cytoplasm {ECO:0000269|PubMed:9736620}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22442037}. Note=Some nuclear fraction is nucleolar.
uniprot
proteins