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Q13868

- EXOS2_HUMAN

UniProt

Q13868 - EXOS2_HUMAN

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Protein

Exosome complex component RRP4

Gene

EXOSC2

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. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7.1 Publication

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: ProtInc
  2. 7S RNA binding Source: ProtInc

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. positive regulation of cell growth Source: UniProtKB
  6. RNA metabolic process Source: Reactome
  7. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  8. rRNA processing Source: ProtInc
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 RRP4
Alternative name(s):
Exosome component 2
Ribosomal RNA-processing protein 4
Gene namesi
Name:EXOSC2
Synonyms:RRP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17097. EXOSC2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. exosome (RNase complex) Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134876020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Exosome complex component RRP4PRO_0000087129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13868.
PaxDbiQ13868.
PRIDEiQ13868.

PTM databases

PhosphoSiteiQ13868.

Expressioni

Gene expression databases

BgeeiQ13868.
CleanExiHS_EXOSC2.
ExpressionAtlasiQ13868. baseline and differential.
GenevestigatoriQ13868.

Organism-specific databases

HPAiHPA021790.

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 GTPBP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DIS3LQ8TF46-12EBI-301735,EBI-3895807
EXOSC3Q9NQT55EBI-301735,EBI-371866
EXOSC4Q9NPD35EBI-301735,EBI-371823
EXOSC7Q150245EBI-301735,EBI-371841
MPHOSPH6Q995473EBI-301735,EBI-373187
ZNF408Q9H9D43EBI-301735,EBI-347633

Protein-protein interaction databases

BioGridi116977. 31 interactions.
IntActiQ13868. 34 interactions.
MINTiMINT-2633872.
STRINGi9606.ENSP00000361433.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 473
Beta strandi49 – 546
Beta strandi56 – 638
Beta strandi66 – 738
Beta strandi80 – 823
Beta strandi86 – 927
Beta strandi95 – 995
Beta strandi101 – 1044
Beta strandi106 – 1116
Helixi129 – 1346
Beta strandi144 – 1496
Turni150 – 1523
Beta strandi153 – 1575
Beta strandi171 – 1733
Beta strandi193 – 1986
Turni199 – 2013
Beta strandi202 – 2065
Helixi220 – 2223
Helixi228 – 24619
Helixi253 – 2619
Turni262 – 2665
Helixi275 – 28915
Turni290 – 2923

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35H1-293[»]
ProteinModelPortaliQ13868.
SMRiQ13868. Positions 25-293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13868.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 15981S1 motifAdd
BLAST

Sequence similaritiesi

Belongs to the RRP4 family.Curated
Contains 1 S1 motif domain.Curated

Phylogenomic databases

eggNOGiCOG1097.
GeneTreeiENSGT00440000033656.
HOGENOMiHOG000193685.
HOVERGENiHBG051517.
InParanoidiQ13868.
KOiK03679.
OMAiSRLRNCV.
OrthoDBiEOG7JX34R.
PhylomeDBiQ13868.
TreeFamiTF105623.

Family and domain databases

InterProiIPR025721. Exosome_cplx_N_dom.
IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
[Graphical view]
PANTHERiPTHR21321. PTHR21321. 1 hit.
PfamiPF14382. ECR1_N. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13868) [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
MAMEMRLPVA RKPLSERLGR DTKKHLVVPG DTITTDTGFM RGHGTYMGEE
60 70 80 90 100
KLIASVAGSV ERVNKLICVK ALKTRYIGEV GDIVVGRITE VQQKRWKVET
110 120 130 140 150
NSRLDSVLLL SSMNLPGGEL RRRSAEDELA MRGFLQEGDL ISAEVQAVFS
160 170 180 190 200
DGAVSLHTRS LKYGKLGQGV LVQVSPSLVK RQKTHFHDLP CGASVILGNN
210 220 230 240 250
GFIWIYPTPE HKEEEAGGFI ANLEPVSLAD REVISRLRNC IISLVTQRMM
260 270 280 290
LYDTSILYCY EASLPHQIKD ILKPEIMEEI VMETRQRLLE QEG
Length:293
Mass (Da):32,789
Last modified:April 27, 2001 - v2
Checksum:i882033F50791643F
GO
Isoform 2 (identifier: Q13868-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-168: Missing.

Note: No experimental confirmation available.

Show »
Length:267
Mass (Da):30,045
Checksum:iFCBD02E381F5FAB9
GO

Sequence cautioni

The sequence AAB60392.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei143 – 16826Missing in isoform 2. 1 PublicationVSP_054921Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07561 Genomic DNA. Translation: AAB60392.1. Sequence problems.
AK001916 mRNA. Translation: BAA91977.1.
AK022460 mRNA. Translation: BAB14043.1.
AK296605 mRNA. Translation: BAG59218.1.
AL359092 Genomic DNA. Translation: CAM45748.1.
CH471090 Genomic DNA. Translation: EAW87944.1.
BC000747 mRNA. Translation: AAH00747.1.
CCDSiCCDS65160.1. [Q13868-2]
CCDS6935.1. [Q13868-1]
RefSeqiNP_001269637.1. NM_001282708.1. [Q13868-2]
NP_055100.2. NM_014285.6. [Q13868-1]
UniGeneiHs.654643.

Genome annotation databases

EnsembliENST00000372358; ENSP00000361433; ENSG00000130713. [Q13868-1]
ENST00000546165; ENSP00000444917; ENSG00000130713. [Q13868-2]
GeneIDi23404.
KEGGihsa:23404.
UCSCiuc004bzu.2. human. [Q13868-1]
uc011mbz.1. human.

Polymorphism databases

DMDMi13878748.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07561 Genomic DNA. Translation: AAB60392.1 . Sequence problems.
AK001916 mRNA. Translation: BAA91977.1 .
AK022460 mRNA. Translation: BAB14043.1 .
AK296605 mRNA. Translation: BAG59218.1 .
AL359092 Genomic DNA. Translation: CAM45748.1 .
CH471090 Genomic DNA. Translation: EAW87944.1 .
BC000747 mRNA. Translation: AAH00747.1 .
CCDSi CCDS65160.1. [Q13868-2 ]
CCDS6935.1. [Q13868-1 ]
RefSeqi NP_001269637.1. NM_001282708.1. [Q13868-2 ]
NP_055100.2. NM_014285.6. [Q13868-1 ]
UniGenei Hs.654643.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NN6 X-ray 3.35 H 1-293 [» ]
ProteinModelPortali Q13868.
SMRi Q13868. Positions 25-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116977. 31 interactions.
IntActi Q13868. 34 interactions.
MINTi MINT-2633872.
STRINGi 9606.ENSP00000361433.

PTM databases

PhosphoSitei Q13868.

Polymorphism databases

DMDMi 13878748.

Proteomic databases

MaxQBi Q13868.
PaxDbi Q13868.
PRIDEi Q13868.

Protocols and materials databases

DNASUi 23404.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372358 ; ENSP00000361433 ; ENSG00000130713 . [Q13868-1 ]
ENST00000546165 ; ENSP00000444917 ; ENSG00000130713 . [Q13868-2 ]
GeneIDi 23404.
KEGGi hsa:23404.
UCSCi uc004bzu.2. human. [Q13868-1 ]
uc011mbz.1. human.

Organism-specific databases

CTDi 23404.
GeneCardsi GC09P133569.
H-InvDB HIX0008473.
HGNCi HGNC:17097. EXOSC2.
HPAi HPA021790.
MIMi 602238. gene.
neXtProti NX_Q13868.
PharmGKBi PA134876020.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1097.
GeneTreei ENSGT00440000033656.
HOGENOMi HOG000193685.
HOVERGENi HBG051517.
InParanoidi Q13868.
KOi K03679.
OMAi SRLRNCV.
OrthoDBi EOG7JX34R.
PhylomeDBi Q13868.
TreeFami TF105623.

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

ChiTaRSi EXOSC2. human.
EvolutionaryTracei Q13868.
GeneWikii Exosome_component_2.
GenomeRNAii 23404.
NextBioi 35472812.
PROi Q13868.
SOURCEi Search...

Gene expression databases

Bgeei Q13868.
CleanExi HS_EXOSC2.
ExpressionAtlasi Q13868. baseline and differential.
Genevestigatori Q13868.

Family and domain databases

InterProi IPR025721. Exosome_cplx_N_dom.
IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR022967. S1_dom.
[Graphical view ]
PANTHERi PTHR21321. PTHR21321. 1 hit.
Pfami PF14382. ECR1_N. 1 hit.
[Graphical view ]
SMARTi SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the human abl and bcr genes."
    Chissoe S.L.
    Thesis (1994), University of Oklahoma, United States
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lung carcinoma.
  2. "The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases."
    Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.
    Cell 91:457-466(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION.
    Tissue: Cervix adenocarcinoma.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Colon, Mammary gland and Placenta.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Tissue: Lung.
  7. "The 3' end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism."
    Mitchell P., Petfalski E., Tollervey D.
    Genes Dev. 10:502-513(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "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.
  9. "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, PROTEIN INTERACTION.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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, SUBCELLULAR LOCATION, INTERACTION WITH DIS3.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
    Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
    FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GTPBP1.
  18. "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), RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
  19. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2007)

Entry informationi

Entry nameiEXOS2_HUMAN
AccessioniPrimary (citable) accession number: Q13868
Secondary accession number(s): A3KFL3, B4DKK6, Q9NUY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: October 29, 2014
This is version 145 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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