O95453 (PARN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(A)-specific ribonuclease PARN
EC=3.1.13.4

Alternative name(s):
Deadenylating nuclease
Deadenylation nuclease
Polyadenylate-specific ribonuclease

Gene names

Name:	PARN
Synonyms:	DAN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.7 Ref.8 Ref.12 Ref.13
Catalytic activity	Exonucleolytic cleavage of poly(A) to 5'-AMP. Ref.1 Ref.6
Cofactor	Divalent metal cations. Mg2+ is the most probable. Ref.8 Ref.14
Subunit structure	Homodimer. Interacts with KHSRP and CELF1/CUGBP1. Found in a mRNA decay complex with RENT1, RENT2 and RENT3B. Ref.6 Ref.13 Ref.17 Ref.22
Subcellular location	Nucleus. Cytoplasm. Nucleus › nucleolus. Note: Some nuclear fraction is nucleolar. Ref.1 Ref.10
Tissue specificity	Ubiquitous. Ref.1 Ref.5
Post-translational modification	Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress.
Sequence similarities	Belongs to the CAF1 family. Contains 1 R3H domain.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA modification Traceable author statement. Source: ProtInc female gamete generation Traceable author statement. Source: ProtInc nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype. Source: UniProtKB nuclear-transcribed mRNA poly(A) tail shortening Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	mRNA 3'-UTR binding Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A)-specific ribonuclease activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 639

639

Poly(A)-specific ribonuclease PARN

PRO_0000212851

Regions

Domain

178 – 245

68

R3H

Sites

Metal binding

28

1

Divalent metal cation; catalytic Probable

Metal binding

30

1

Divalent metal cation; catalytic Probable

Metal binding

292

1

Divalent metal cation; catalytic Probable

Metal binding

382

1

Divalent metal cation; catalytic Probable

Site

326

1

Interaction with poly(A)

Amino acid modifications

Modified residue

163

1

Phosphoserine Ref.16 Ref.19 Ref.20

Modified residue

220

1

N6-acetyllysine Ref.21

Modified residue

499

1

N6-acetyllysine Ref.21

Modified residue

557

1

Phosphoserine; by MAPKAPK2 Ref.16 Ref.18 Ref.20 Ref.23

Modified residue

587

1

Phosphoserine Ref.19

Modified residue

619

1

Phosphoserine Ref.15 Ref.19

Modified residue

623

1

Phosphoserine Ref.19

Modified residue

628

1

Phosphoserine Ref.19

Experimental info

Mutagenesis

28

1

D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. Ref.9 Ref.12 Ref.14

Mutagenesis

28

1

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+). Ref.9 Ref.12 Ref.14

Mutagenesis

30

1

E → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. Ref.9 Ref.12 Ref.14

Mutagenesis

30

1

E → C: Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+). Ref.9 Ref.12 Ref.14

Mutagenesis

31

1

F → A: Reduced affinity for poly(A). Loss of activity. Ref.22

Mutagenesis

34

1

I → A: Reduced affinity for poly(A). Strongly reduced activity. Ref.22

Mutagenesis

113

1

I → A: Loss of dimerization. Loss of activity. Ref.22

Mutagenesis

115

1

F → A: Reduced affinity for poly(A). Little effect on activity.

Mutagenesis

123

1

F → A: Loss of dimerization. Loss of activity. Ref.22

Mutagenesis

292

1

D → A: Loss of function but does not abolish ability to bind RNA. Ref.9 Ref.14

Mutagenesis

292

1

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+). Ref.9 Ref.14

Mutagenesis

326

1

K → A: Reduced affinity for poly(A). Little effect on activity.

Mutagenesis

377

1

H → A: Loss of activity. Ref.22

Mutagenesis

382

1

D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. Ref.9 Ref.12 Ref.14

Mutagenesis

382

1

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+). Ref.9 Ref.12 Ref.14

Mutagenesis

557

1

S → A: Strong reduction of phosphorylation by MAPKAPK2.

Secondary structure

1

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639

Helix Strand Turn

Details...

Helix

5 – 21

17

Beta strand

23 – 32

10

Beta strand

36 – 38

3

Helix

50 – 60

11

Turn

61 – 63

3

Beta strand

66 – 77

12

Turn

78 – 81

4

Beta strand

82 – 92

11

Beta strand

97 – 101

5

Beta strand

105 – 109

5

Helix

110 – 118

9

Helix

123 – 127

5

Helix

136 – 141

6

Helix

260 – 265

6

Helix

271 – 280

10

Beta strand

283 – 288

6

Helix

290 – 300

11

Helix

308 – 318

11

Beta strand

320 – 324

5

Helix

325 – 329

5

Turn

332 – 337

6

Helix

343 – 349

7

Beta strand

360 – 362

3

Helix

379 – 397

19

Helix

398 – 400

3

Beta strand

401 – 403

3

Helix

416 – 418

3

Beta strand

424 – 429

6

Sequences

	Sequence		Length	Mass (Da)
	O95453 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6994BE39384DF7AC	FASTA	639	73,451
	10 20 30 40 50 60 MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP EERYQKLKKH 70 80 90 100 110 120 SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS SPDVKFVCQS SSIDFLASQG 130 140 150 160 170 180 FDFNKVFRNG IPYLNQEEER QLREQYDEKR SQANGAGALS YVSPNTSKCP VTIPEDQKKF 190 200 210 220 230 240 IDQVVEKIED LLQSEENKNL DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV 250 260 270 280 290 300 ISKVDEEERK RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF 310 320 330 340 350 360 YCPLPADLSE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL KETPFNPPKV 370 380 390 400 410 420 ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF LSPPKIHVSA RSKLIEPFFN 430 440 450 460 470 480 KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV TFPKEWKTSD LYQLFSAFGN IQISWIDDTS 490 500 510 520 530 540 AFVSLSQPEQ VKIAVNTSKY AESYRIQTYA EYMGRKQEEK QIKRKWTEDS WKEADSKRLN 550 560 570 580 590 600 PQCIPYTLQN HYYRNNSFTA PSTVGKRNLS PSQEEAGLED GVSGEISDTE LEQTDSCAEP 610 620 630 LSEGRKKAKK LKRMKKELSP AGSISKNSPA TLFEVPDTW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes." Koerner C.G., Wormington M., Muckenthaler M., Schneider S., Dehlin E., Wahle E. EMBO J. 17:5427-5437(1998) [PubMed: 9736620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"The human gene for the poly(A)-specific ribonuclease (PARN) maps to 16p13 and has a truncated copy in the Prader-Willi/Angelman syndrome region on 15q11-->q13." Buiting K., Koerner C., Ulrich B., Wahle E., Horsthemke B. Cytogenet. Cell Genet. 87:125-131(1999) [PubMed: 10640832] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonuclease." Martinez J., Ren Y.-G., Thuresson A.-C., Hellman U., Aastroem J., Virtanen A. J. Biol. Chem. 275:24222-24230(2000) [PubMed: 10801819] [Abstract] Cited for: ENZYME ACTIVITY, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
[7]	"Interaction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitro." Gao M., Fritz D.T., Ford L.P., Wilusz J. Mol. Cell 5:479-488(2000) [PubMed: 10882133] [Abstract] Cited for: FUNCTION.
[8]	"The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation." Martinez J., Ren Y.-G., Nilsson P., Ehrenberg M., Virtanen A. J. Biol. Chem. 276:27923-27929(2001) [PubMed: 11359775] [Abstract] Cited for: FUNCTION, COFACTOR.
[9]	"Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe(2+)-mediated cleavage." Ren Y.-G., Martinez J., Virtanen A. J. Biol. Chem. 277:5982-5987(2002) [PubMed: 11742007] [Abstract] Cited for: MUTAGENESIS OF ASP-28; GLU-30; ASP-292 AND ASP-382.
[10]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed: 12429849] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities." Lejeune F., Li X., Maquat L.E. Mol. Cell 12:675-687(2003) [PubMed: 14527413] [Abstract] Cited for: IDENTIFICATION IN A MRNA DECAY COMPLEX WITH RENT1; RENT2 AND RENT3B.
[12]	"Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease." Lai W.S., Kennington E.A., Blackshear P.J. Mol. Cell. Biol. 23:3798-3812(2003) [PubMed: 12748283] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-28; GLU-30 AND ASP-382.
[13]	"A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery." Gherzi R., Lee K.-Y., Briata P., Wegmueller D., Moroni C., Karin M., Chen C.-Y. Mol. Cell 14:571-583(2004) [PubMed: 15175153] [Abstract] Cited for: FUNCTION, INTERACTION WITH KHSRP.
[14]	"Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease." Ren Y.-G., Kirsebom L.A., Virtanen A. J. Biol. Chem. 279:48702-48706(2004) [PubMed: 15358788] [Abstract] Cited for: COFACTOR, MUTAGENESIS OF ASP-28; GLU-30; ASP-292 AND ASP-382.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-557, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"CUG-BP binds to RNA substrates and recruits PARN deadenylase." Moraes K.C., Wilusz C.J., Wilusz J. RNA 12:1084-1091(2006) [PubMed: 16601207] [Abstract] Cited for: INTERACTION WITH CELF1.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-587; SER-619; SER-623 AND SER-628, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-557, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-499, MASS SPECTROMETRY.
[22]	"Structural insight into poly(A) binding and catalytic mechanism of human PARN." Wu M., Reuter M., Lilie H., Liu Y., Wahle E., Song H. EMBO J. 24:4082-4093(2005) [PubMed: 16281054] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-430 IN COMPLEX WITH DNA, MUTAGENESIS OF PHE-31; ILE-34; ILE-113; PHE-123 AND HIS-377, SUBUNIT.
[23]	"DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization." Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B. Mol. Cell 40:34-49(2010) [PubMed: 20932473] [Abstract] Cited for: PHOSPHORYLATION AT SER-557 BY MAPKAPK2, PHOSPHORYLATION AT SER-557.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ005698 mRNA. Translation: CAA06683.1.
AK315020 mRNA. Translation: BAG37510.1.
CH471112 Genomic DNA. Translation: EAW85110.1.
BC050029 mRNA. Translation: AAH50029.1.

IPI

IPI00294744.

RefSeq

NP_002573.1. NM_002582.3.

UniGene

Hs.253197.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A1R	X-ray	2.60	A/B	1-430	[»]
2A1S	X-ray	2.60	A/B/C/D	1-430	[»]
3CTR	X-ray	2.10	A	445-540	[»]

ProteinModelPortal

O95453.

SMR

O95453. Positions 1-514.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95453. 2 interactions.

STRING

O95453.

PTM databases

PhosphoSite

O95453.

2D gel databases

SWISS-2DPAGE

O95453.

Proteomic databases

PRIDE

O95453.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000437198; ENSP00000387911; ENSG00000140694.

GeneID

5073.

KEGG

hsa:5073.

UCSC

uc002dcl.1. human.

Organism-specific databases

CTD

5073.

GeneCards

GC16M014437.

H-InvDB

HIX0012830.

HGNC

HGNC:8609. PARN.

HPA

CAB011673.
HPA006314.
HPA012010.

MIM

604212. gene.

neXtProt

NX_O95453.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08602.

GeneTree

ENSGT00530000063673.

HOGENOM

HBG445122.

HOVERGEN

HBG053512.

InParanoid

O95453.

OMA

QKLKKHS.

PhylomeDB

O95453.

Enzyme and pathway databases

BRENDA

3.1.13.4. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

O95453.

Bgee

O95453.

CleanEx

HS_PARN.

Genevestigator

O95453.

GermOnline

ENSG00000140694. Homo sapiens.

Family and domain databases

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR014789. PolyA-riboNase_RNA_binding.
IPR001374. R3H_ss-bd.
IPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

KO

K01148.

Pfam

PF04857. CAF1. 1 hit.
PF01424. R3H. 1 hit.
PF08675. RNA_bind. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS51061. R3H. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

19548.

SOURCE

Search...

Entry information

Entry name

PARN_HUMAN

Accession

Primary (citable) accession number: O95453
Secondary accession number(s): B2RCB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.