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Q9NPD3

- EXOS4_HUMAN

UniProt

Q9NPD3 - EXOS4_HUMAN

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Protein

Exosome complex component RRP41

Gene

EXOSC4

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

Functioni

Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC4 binds to ARE-containing RNAs.5 Publications

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: UniProtKB
  2. AU-rich element binding Source: UniProtKB

GO - Biological processi

  1. defense response to virus Source: MGI
  2. DNA deamination Source: UniProtKB
  3. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  4. gene expression Source: Reactome
  5. histone mRNA catabolic process Source: UniProtKB
  6. maturation of 5.8S rRNA Source: UniProtKB
  7. mRNA metabolic process Source: Reactome
  8. nuclear mRNA surveillance Source: UniProtKB
  9. nuclear-transcribed mRNA catabolic process Source: UniProtKB
  10. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  11. positive regulation of cell growth Source: UniProtKB
  12. RNA metabolic process Source: Reactome
  13. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  14. rRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP41
Alternative name(s):
Exosome component 4
Ribosomal RNA-processing protein 41
p12A
Gene namesi
Name:EXOSC4
Synonyms:RRP41, SKI6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:18189. EXOSC4.

Subcellular locationi

Cytoplasm 1 Publication. Nucleusnucleolus 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. exosome (RNase complex) Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134867931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 245244Exosome complex component RRP41PRO_0000139958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NPD3.
PaxDbiQ9NPD3.
PRIDEiQ9NPD3.

2D gel databases

SWISS-2DPAGEQ9NPD3.

PTM databases

PhosphoSiteiQ9NPD3.

Expressioni

Gene expression databases

BgeeiQ9NPD3.
CleanExiHS_EXOSC4.
ExpressionAtlasiQ9NPD3. baseline and differential.
GenevestigatoriQ9NPD3.

Organism-specific databases

HPAiHPA024792.

Interactioni

Subunit structurei

Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with DDX60.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EXOSC1Q9Y3B24EBI-371823,EBI-371892
EXOSC10Q017803EBI-371823,EBI-358236
EXOSC2Q138685EBI-371823,EBI-301735
EXOSC3Q9NQT54EBI-371823,EBI-371866
EXOSC9Q062653EBI-371823,EBI-347966

Protein-protein interaction databases

BioGridi120007. 40 interactions.
DIPiDIP-31165N.
IntActiQ9NPD3. 29 interactions.
MINTiMINT-2818708.
STRINGi9606.ENSP00000315476.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 174Combined sources
Beta strandi25 – 306Combined sources
Beta strandi32 – 4514Combined sources
Beta strandi47 – 5711Combined sources
Beta strandi60 – 623Combined sources
Beta strandi72 – 787Combined sources
Turni80 – 823Combined sources
Beta strandi83 – 853Combined sources
Turni89 – 913Combined sources
Helixi94 – 10916Combined sources
Helixi113 – 1153Combined sources
Beta strandi119 – 12911Combined sources
Helixi134 – 14815Combined sources
Beta strandi158 – 1658Combined sources
Beta strandi168 – 1725Combined sources
Helixi175 – 1784Combined sources
Beta strandi185 – 1895Combined sources
Turni191 – 1933Combined sources
Beta strandi198 – 2014Combined sources
Helixi210 – 23930Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35B2-245[»]
ProteinModelPortaliQ9NPD3.
SMRiQ9NPD3. Positions 7-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPD3.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG0689.
GeneTreeiENSGT00550000074804.
HOGENOMiHOG000229515.
HOVERGENiHBG051519.
InParanoidiQ9NPD3.
KOiK11600.
OMAiDYVCACT.
PhylomeDBiQ9NPD3.
TreeFamiTF313915.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9NPD3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGLELLSDQ GYRVDGRRAG ELRKIQARMG VFAQADGSAY IEQGNTKALA
60 70 80 90 100
VVYGPHEIRG SRARALPDRA LVNCQYSSAT FSTGERKRRP HGDRKSCEMG
110 120 130 140 150
LQLRQTFEAA ILTQLHPRSQ IDIYVQVLQA DGGTYAACVN AATLAVLDAG
160 170 180 190 200
IPMRDFVCAC SAGFVDGTAL ADLSHVEEAA GGPQLALALL PASGQIALLE
210 220 230 240
MDARLHEDHL ERVLEAAAQA ARDVHTLLDR VVRQHVREAS ILLGD
Length:245
Mass (Da):26,383
Last modified:January 23, 2007 - v3
Checksum:i7A24E97897DAF313
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF281133 mRNA. Translation: AAF82134.1.
AK000598 mRNA. Translation: BAA91279.1.
AC109322 Genomic DNA. No translation available.
BC002777 mRNA. Translation: AAH02777.1.
CCDSiCCDS6414.1.
RefSeqiNP_061910.1. NM_019037.2.
UniGeneiHs.632041.

Genome annotation databases

EnsembliENST00000316052; ENSP00000315476; ENSG00000178896.
GeneIDi54512.
KEGGihsa:54512.
UCSCiuc003zau.3. human.

Polymorphism databases

DMDMi14285756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF281133 mRNA. Translation: AAF82134.1 .
AK000598 mRNA. Translation: BAA91279.1 .
AC109322 Genomic DNA. No translation available.
BC002777 mRNA. Translation: AAH02777.1 .
CCDSi CCDS6414.1.
RefSeqi NP_061910.1. NM_019037.2.
UniGenei Hs.632041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NN6 X-ray 3.35 B 2-245 [» ]
ProteinModelPortali Q9NPD3.
SMRi Q9NPD3. Positions 7-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120007. 40 interactions.
DIPi DIP-31165N.
IntActi Q9NPD3. 29 interactions.
MINTi MINT-2818708.
STRINGi 9606.ENSP00000315476.

PTM databases

PhosphoSitei Q9NPD3.

Polymorphism databases

DMDMi 14285756.

2D gel databases

SWISS-2DPAGE Q9NPD3.

Proteomic databases

MaxQBi Q9NPD3.
PaxDbi Q9NPD3.
PRIDEi Q9NPD3.

Protocols and materials databases

DNASUi 54512.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316052 ; ENSP00000315476 ; ENSG00000178896 .
GeneIDi 54512.
KEGGi hsa:54512.
UCSCi uc003zau.3. human.

Organism-specific databases

CTDi 54512.
GeneCardsi GC08P145133.
HGNCi HGNC:18189. EXOSC4.
HPAi HPA024792.
MIMi 606491. gene.
neXtProti NX_Q9NPD3.
PharmGKBi PA134867931.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0689.
GeneTreei ENSGT00550000074804.
HOGENOMi HOG000229515.
HOVERGENi HBG051519.
InParanoidi Q9NPD3.
KOi K11600.
OMAi DYVCACT.
PhylomeDBi Q9NPD3.
TreeFami TF313915.

Enzyme and pathway databases

Reactomei REACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

EvolutionaryTracei Q9NPD3.
GeneWikii Exosome_component_4.
GenomeRNAii 54512.
NextBioi 56896.
PROi Q9NPD3.
SOURCEi Search...

Gene expression databases

Bgeei Q9NPD3.
CleanExi HS_EXOSC4.
ExpressionAtlasi Q9NPD3. baseline and differential.
Genevestigatori Q9NPD3.

Family and domain databases

Gene3Di 3.30.230.70. 1 hit.
InterProi IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
Pfami PF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  5. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  6. "The yeast exosome and human PM-Scl are related complexes of 3'-->5' exonucleases."
    Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P.
    Genes Dev. 13:2148-2158(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
    Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
    Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
  8. "Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome."
    Anderson J.R., Mukherjee D., Muthukumaraswamy K., Moraes K.C., Wilusz C.J., Wilusz J.
    RNA 12:1810-1816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ARE-CONTAINING MRNA-BINDING.
  9. "Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways."
    van Dijk E.L., Schilders G., Pruijn G.J.
    RNA 13:1027-1035(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION.
  10. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
    Mullen T.E., Marzluff W.F.
    Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
  11. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Dis3-like 1: a novel exoribonuclease associated with the human exosome."
    Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
    EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Addition of poly(A) and poly(A)-rich tails during RNA degradation in the cytoplasm of human cells."
    Slomovic S., Fremder E., Staals R.H., Pruijn G.J., Schuster G.
    Proc. Natl. Acad. Sci. U.S.A. 107:7407-7412(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RRNA MATURATION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates."
    Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J., Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K., Gregory R.I., Deng H., Lima C.D., Alt F.W.
    Cell 144:353-363(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE.
  16. "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling."
    Miyashita M., Oshiumi H., Matsumoto M., Seya T.
    Mol. Cell. Biol. 31:3802-3819(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX60.
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
    Liu Q., Greimann J.C., Lima C.D.
    Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
  20. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2007)

Entry informationi

Entry nameiEXOS4_HUMAN
AccessioniPrimary (citable) accession number: Q9NPD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 136 of the entry and version 3 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

Caution

The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active.Curated

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

External Data

Dasty 3