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Reviewed, UniProtKB/Swiss-Prot Q9NPD3 (EXOS4_HUMAN)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Exosome complex exonuclease RRP41
    EC=3.1.13.-
Alternative name(s):
    Ribosomal RNA-processing protein 41
    Exosome component 4
    p12A
Gene names
Name: EXOSC4
Synonyms: RRP41, SKI6
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of the exosome 3'->5' exoribonuclease complex, a complex that degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3'-untranslated regions. Required for the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA. Has a 3'-5' exonuclease activity.

Subunit structure

Component of the exosome multienzyme ribonuclease complex composed of at least 11 proteins: EXOSC1/CSL4, EXOSC2/RRP4, EXOSC3/RRP40, EXOSC4/RRP41, EXOSC5/RRP46, EXOSC6/MTR3, EXOSC7/RRP42, EXOSC8/RRP43, EXOSC9/Scl-75, DIS3/RRP44, and EXOSC10/Scl-100 (only in the nuclear complex). Found in a mRNA decay complex with RENT1, RENT2 and RENT3B. Also associated with the GTPase Ran.

Subcellular location

Cytoplasm. Nucleusnucleolus.

Sequence similarities

Belongs to the RNase PH family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   LigandRNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processrRNA processing Ref.1

Non-traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm Ref.1

Non-traceable author statement. Source: UniProtKB

exosome (RNase complex)

Inferred from electronic annotation. Source: UniProtKB-KW

nucleolus Ref.1

Non-traceable author statement. Source: UniProtKB

   Molecular function3'-5'-exoribonuclease activity Ref.1

Non-traceable author statement. Source: UniProtKB

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 245244Exosome complex exonuclease RRP41
PRO_0000139958

Amino acid modifications

Modified residue21N-acetylalanine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9NPD3-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7A24E97897DAF313

FASTA24526,383
        10         20         30         40         50         60 
MAGLELLSDQ GYRVDGRRAG ELRKIQARMG VFAQADGSAY IEQGNTKALA VVYGPHEIRG 

        70         80         90        100        110        120 
SRARALPDRA LVNCQYSSAT FSTGERKRRP HGDRKSCEMG LQLRQTFEAA ILTQLHPRSQ 

       130        140        150        160        170        180 
IDIYVQVLQA DGGTYAACVN AATLAVLDAG IPMRDFVCAC SAGFVDGTAL ADLSHVEEAA 

       190        200        210        220        230        240 
GGPQLALALL PASGQIALLE MDARLHEDHL ERVLEAAAQA ARDVHTLLDR VVRQHVREAS 


ILLGD 

« Hide

References

« Hide 'large scale' references
[1]"Three novel components of the human exosome."
Brouwer R., Allmang C., Raijmakers R., van Aarssen Y., Egberts W.V., Petfalski E., van Venrooij W.J., Tollervey D., Pruijn G.J.M.
J. Biol. Chem. 276:6177-6184(2001) [PubMed: 11110791] [Abstract]
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. expand/collapse author list , 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].
[3]"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: Skin.
[4]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"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: 10465791] [Abstract]
Cited for: CHARACTERIZATION.
[6]"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: 11719186] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE EXOSOME MULTIENZYME RIBONUCLEASE COMPLEX.
[7]"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.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF281133 mRNA. Translation: AAF82134.1.
AK000598 mRNA. Translation: BAA91279.1.
BC002777 mRNA. Translation: AAH02777.1.
IPIIPI00745613.
RefSeqNP_061910.1.
UniGeneHs.632041

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35B2-244[»]
SMRQ9NPD3. Positions 7-241.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NPD3. 20 interactions.

2-D gel databases

SWISS-2DPAGEQ9NPD3.

Proteomic databases

PRIDEQ9NPD3.

Genome annotation databases

EnsemblENSG00000178896. Homo sapiens. [Contig view]
GeneID54512.
KEGGhsa:54512.
NMPDRfig|9606.3.peg.30882.

Organism-specific databases

GeneCardsGC08P145205.
H-InvDBHIX0020970.
HGNCHGNC:18189. EXOSC4.
MIM606491. gene.
PharmGKBPA134867931.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9NPD3.
OMAQ9NPD3. GDRKSTE.

Gene expression databases

ArrayExpressQ9NPD3.
BgeeQ9NPD3.
CleanExHS_EXOSC4.
GermOnlineENSG00000178896. Homo sapiens.

Family and domain databases

InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
[Graphical view]
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio56896.
SOURCESearch...

Entry information

Entry nameEXOS4_HUMAN
AccessionPrimary (citable) accession number: Q9NPD3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents