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Protein

Exosome complex component CSL4

Gene

Exosc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_288807. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.
REACT_307913. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component CSL4
Alternative name(s):
Exosome component 1
Gene namesi
Name:Exosc1
Synonyms:Csl4
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1913833. Exosc1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Exosome complex component CSL4PRO_0000087128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9DAA6.
PaxDbiQ9DAA6.
PRIDEiQ9DAA6.

PTM databases

PhosphoSiteiQ9DAA6.

Expressioni

Gene expression databases

BgeeiQ9DAA6.
CleanExiMM_EXOSC1.
GenevisibleiQ9DAA6. MM.

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 EXOSC5, EXOSC7 and EXOSC10 (By similarity). Interacts with DDX60 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211569. 2 interactions.
STRINGi10090.ENSMUSP00000074756.

Structurei

3D structure databases

ProteinModelPortaliQ9DAA6.
SMRiQ9DAA6. Positions 6-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 14782S1 motifAdd
BLAST

Sequence similaritiesi

Belongs to the CSL4 family.Curated
Contains 1 S1 motif domain.Curated

Phylogenomic databases

eggNOGiCOG1096.
GeneTreeiENSGT00390000015287.
HOGENOMiHOG000177330.
HOVERGENiHBG051516.
InParanoidiQ9DAA6.
KOiK07573.
OMAiARVQPEY.
OrthoDBiEOG7V4B0J.
PhylomeDBiQ9DAA6.
TreeFamiTF316607.

Family and domain databases

InterProiIPR019495. EXOSC1.
IPR025721. Exosome_cplx_N_dom.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
[Graphical view]
PfamiPF14382. ECR1_N. 1 hit.
PF10447. EXOSC1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DAA6-1) [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
MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKTSENGAV
60 70 80 90 100
PVVSVMRETE SQLLPDVGAV VTCKVSSINS RFAKVHILYV GSTPLKNAFR
110 120 130 140 150
GTIRKEDIRA TEKDKVEIYK SFRPGDIVLA KVISLGDAQS NYLLTTAENE
160 170 180 190
LGVVVAHSES GVQMVPISWC EMQCPKTHTK EFRKVARVQP EFLQT
Length:195
Mass (Da):21,424
Last modified:June 1, 2001 - v1
Checksum:i2F8D214B2B6A2953
GO
Isoform 2 (identifier: Q9DAA6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-116: Missing.

Note: No experimental confirmation available.
Show »
Length:154
Mass (Da):16,794
Checksum:i7FA6B8509060F16C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei76 – 11641Missing in isoform 2. 1 PublicationVSP_004176Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002930 mRNA. Translation: BAB22465.1.
AK006018 mRNA. Translation: BAB24368.1.
BC024423 mRNA. Translation: AAH24423.1.
CCDSiCCDS29816.1. [Q9DAA6-1]
CCDS50436.1. [Q9DAA6-2]
RefSeqiNP_001158033.1. NM_001164561.1. [Q9DAA6-2]
NP_079920.1. NM_025644.4. [Q9DAA6-1]
UniGeneiMm.289086.

Genome annotation databases

EnsembliENSMUST00000075280; ENSMUSP00000074756; ENSMUSG00000034321. [Q9DAA6-1]
ENSMUST00000112123; ENSMUSP00000107751; ENSMUSG00000034321. [Q9DAA6-2]
GeneIDi66583.
KEGGimmu:66583.
UCSCiuc008hmm.2. mouse. [Q9DAA6-1]
uc008hmn.2. mouse. [Q9DAA6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002930 mRNA. Translation: BAB22465.1.
AK006018 mRNA. Translation: BAB24368.1.
BC024423 mRNA. Translation: AAH24423.1.
CCDSiCCDS29816.1. [Q9DAA6-1]
CCDS50436.1. [Q9DAA6-2]
RefSeqiNP_001158033.1. NM_001164561.1. [Q9DAA6-2]
NP_079920.1. NM_025644.4. [Q9DAA6-1]
UniGeneiMm.289086.

3D structure databases

ProteinModelPortaliQ9DAA6.
SMRiQ9DAA6. Positions 6-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211569. 2 interactions.
STRINGi10090.ENSMUSP00000074756.

PTM databases

PhosphoSiteiQ9DAA6.

Proteomic databases

MaxQBiQ9DAA6.
PaxDbiQ9DAA6.
PRIDEiQ9DAA6.

Protocols and materials databases

DNASUi66583.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075280; ENSMUSP00000074756; ENSMUSG00000034321. [Q9DAA6-1]
ENSMUST00000112123; ENSMUSP00000107751; ENSMUSG00000034321. [Q9DAA6-2]
GeneIDi66583.
KEGGimmu:66583.
UCSCiuc008hmm.2. mouse. [Q9DAA6-1]
uc008hmn.2. mouse. [Q9DAA6-2]

Organism-specific databases

CTDi51013.
MGIiMGI:1913833. Exosc1.

Phylogenomic databases

eggNOGiCOG1096.
GeneTreeiENSGT00390000015287.
HOGENOMiHOG000177330.
HOVERGENiHBG051516.
InParanoidiQ9DAA6.
KOiK07573.
OMAiARVQPEY.
OrthoDBiEOG7V4B0J.
PhylomeDBiQ9DAA6.
TreeFamiTF316607.

Enzyme and pathway databases

ReactomeiREACT_288807. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.
REACT_307913. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

ChiTaRSiExosc1. mouse.
NextBioi322064.
PROiQ9DAA6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAA6.
CleanExiMM_EXOSC1.
GenevisibleiQ9DAA6. MM.

Family and domain databases

InterProiIPR019495. EXOSC1.
IPR025721. Exosome_cplx_N_dom.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
[Graphical view]
PfamiPF14382. ECR1_N. 1 hit.
PF10447. EXOSC1. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "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] (ISOFORM 1).

Entry informationi

Entry nameiEXOS1_MOUSE
AccessioniPrimary (citable) accession number: Q9DAA6
Secondary accession number(s): Q9DCB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.