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Protein

Protein CASC3

Gene

CASC3

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

Functioni

Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homopolymer.2 Publications

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: MGI
  • poly(A) RNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, Stress response, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein CASC3
Alternative name(s):
Cancer susceptibility candidate gene 3 protein
Metastatic lymph node gene 51 protein
Short name:
MLN 51
Protein barentsz
Short name:
Btz
Gene namesi
Name:CASC3
Synonyms:MLN51
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:17040. CASC3.

Subcellular locationi

  • Cytoplasmperinuclear region
  • Nucleus
  • Nucleus speckle

  • Note: Predominantly found in the perinuclear region (By similarity). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Shuttles between the cytoplasm and the stress granules. More specifically found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing. Colocalizes in nuclear speckles with MAGOH. Under stress condition, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules, which contain stored mRNAs whose translation is stopped in response to stress.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi181 – 1811Y → A: Does not affect EJC formation. 1 Publication
Mutagenesisi184 – 1852RK → AA: Does not affect EJC formation. 1 Publication
Mutagenesisi188 – 1881F → A: Does not affect EJC formation. 1 Publication
Mutagenesisi218 – 2181W → A: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles. 1 Publication
Mutagenesisi220 – 2212HD → AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles. 1 Publication
Mutagenesisi240 – 2412YG → AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles. 1 Publication

Organism-specific databases

PharmGKBiPA134948596.

Polymorphism and mutation databases

BioMutaiCASC3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 703703Protein CASC3PRO_0000089324Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei117 – 1171PhosphoserineCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources
Modified residuei357 – 3571PhosphothreonineCombined sources
Modified residuei363 – 3631PhosphoserineCombined sources
Modified residuei373 – 3731PhosphoserineCombined sources
Modified residuei477 – 4771PhosphoserineCombined sources

Post-translational modificationi

ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.1 Publication
Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation.1 Publication

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO15234.
MaxQBiO15234.
PaxDbiO15234.
PeptideAtlasiO15234.
PRIDEiO15234.
TopDownProteomicsiO15234.

PTM databases

iPTMnetiO15234.
PhosphoSiteiO15234.

Miscellaneous databases

PMAP-CutDBO15234.

Expressioni

Tissue specificityi

Widely expressed. Overexpressed in breast cancers and metastasis, as well as in gastric cancers.1 Publication

Gene expression databases

BgeeiO15234.
CleanExiHS_CASC3.
ExpressionAtlasiO15234. baseline and differential.
GenevisibleiO15234. HS.

Organism-specific databases

HPAiHPA024592.
HPA050262.

Interactioni

Subunit structurei

Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Forms homooligomers. Interacts with STAU in an RNA-dependent manner. Interacts with EIF4A3, MAGOH, NXF1 and RBM8A.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4A3P389197EBI-299118,EBI-299104
MAGOHP613265EBI-299118,EBI-299134

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • identical protein binding Source: MGI
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116475. 47 interactions.
DIPiDIP-33288N.
IntActiO15234. 29 interactions.
STRINGi9606.ENSP00000264645.

Structurei

Secondary structure

1
703
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi172 – 1743Combined sources
Helixi226 – 2283Combined sources
Helixi233 – 2408Combined sources
Turni244 – 2463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HYIX-ray2.30D/J170-246[»]
2J0QX-ray3.20I/T137-286[»]
2J0SX-ray2.21T137-286[»]
2J0UX-ray3.00T137-250[»]
2XB2X-ray3.40S/T137-286[»]
3EX7X-ray2.30D/I138-283[»]
ProteinModelPortaliO15234.
SMRiO15234. Positions 168-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15234.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 283147Necessary for RNA-binding, interaction with MAGOH and localization in nucleus specklesAdd
BLAST
Regioni137 – 283147Sufficient to form the EJCAdd
BLAST
Regioni377 – 703327Necessary for localization in cytoplasmic stress granulesAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili95 – 13137Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi204 – 2107Nuclear localization signal 1Sequence analysis
Motifi254 – 2629Nuclear localization signal 2Sequence analysis
Motifi462 – 4665Nuclear export signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 466Poly-Gly
Compositional biasi392 – 3954Poly-Pro
Compositional biasi425 – 4284Poly-Pro
Compositional biasi643 – 6486Poly-Pro
Compositional biasi692 – 6954Poly-Pro

Domaini

The coiled coil domain may be involved in oligomerization.

Sequence similaritiesi

Belongs to the CASC3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4264. Eukaryota.
ENOG410ZW5Y. LUCA.
GeneTreeiENSGT00390000006930.
HOGENOMiHOG000069997.
HOVERGENiHBG050799.
InParanoidiO15234.
KOiK14323.
OMAiNLTEQNW.
OrthoDBiEOG7R2BM0.
PhylomeDBiO15234.
TreeFamiTF329663.

Family and domain databases

InterProiIPR018545. Btz_dom.
IPR028544. CASC3.
[Graphical view]
PANTHERiPTHR13434. PTHR13434. 1 hit.
PfamiPF09405. Btz. 1 hit.
[Graphical view]
SMARTiSM01044. Btz. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15234-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADRRRQRAS QDTEDEESGA SGSDSGGSPL RGGGSCSGSA GGGGSGSLPS
60 70 80 90 100
QRGGRTGALH LRRVESGGAK SAEESECESE DGIEGDAVLS DYESAEDSEG
110 120 130 140 150
EEGEYSEEEN SKVELKSEAN DAVNSSTKEE KGEEKPDTKS TVTGERQSGD
160 170 180 190 200
GQESTEPVEN KVGKKGPKHL DDDEDRKNPA YIPRKGLFFE HDLRGQTQEE
210 220 230 240 250
EVRPKGRQRK LWKDEGRWEH DKFREDEQAP KSRQELIALY GYDIRSAHNP
260 270 280 290 300
DDIKPRRIRK PRYGSPPQRD PNWNGERLNK SHRHQGLGGT LPPRTFINRN
310 320 330 340 350
AAGTGRMSAP RNYSRSGGFK EGRAGFRPVE AGGQHGGRSG ETVKHEISYR
360 370 380 390 400
SRRLEQTSVR DPSPEADAPV LGSPEKEEAA SEPPAAAPDA APPPPDRPIE
410 420 430 440 450
KKSYSRARRT RTKVGDAVKL AEEVPPPPEG LIPAPPVPET TPTPPTKTGT
460 470 480 490 500
WEAPVDSSTS GLEQDVAQLN IAEQNWSPGQ PSFLQPRELR GMPNHIHMGA
510 520 530 540 550
GPPPQFNRME EMGVQGGRAK RYSSQRQRPV PEPPAPPVHI SIMEGHYYDP
560 570 580 590 600
LQFQGPIYTH GDSPAPLPPQ GMLVQPGMNL PHPGLHPHQT PAPLPNPGLY
610 620 630 640 650
PPPVSMSPGQ PPPQQLLAPT YFSAPGVMNF GNPSYPYAPG ALPPPPPPHL
660 670 680 690 700
YPNTQAPSQV YGGVTYYNPA QQQVQPKPSP PRRTPQPVTI KPPPPEVVSR

GSS
Length:703
Mass (Da):76,278
Last modified:August 14, 2001 - v2
Checksum:i642A4C01C8DD3BE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80199 mRNA. Translation: CAC27699.1.
AK292425 mRNA. Translation: BAF85114.1.
AC068669 Genomic DNA. No translation available.
BC044656 mRNA. Translation: AAH44656.1.
BC050526 mRNA. Translation: AAH50526.1.
CCDSiCCDS11362.1.
RefSeqiNP_031385.2. NM_007359.4.
XP_005257220.1. XM_005257163.1.
UniGeneiHs.743287.

Genome annotation databases

EnsembliENST00000264645; ENSP00000264645; ENSG00000108349.
GeneIDi22794.
KEGGihsa:22794.
UCSCiuc002hue.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80199 mRNA. Translation: CAC27699.1.
AK292425 mRNA. Translation: BAF85114.1.
AC068669 Genomic DNA. No translation available.
BC044656 mRNA. Translation: AAH44656.1.
BC050526 mRNA. Translation: AAH50526.1.
CCDSiCCDS11362.1.
RefSeqiNP_031385.2. NM_007359.4.
XP_005257220.1. XM_005257163.1.
UniGeneiHs.743287.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HYIX-ray2.30D/J170-246[»]
2J0QX-ray3.20I/T137-286[»]
2J0SX-ray2.21T137-286[»]
2J0UX-ray3.00T137-250[»]
2XB2X-ray3.40S/T137-286[»]
3EX7X-ray2.30D/I138-283[»]
ProteinModelPortaliO15234.
SMRiO15234. Positions 168-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116475. 47 interactions.
DIPiDIP-33288N.
IntActiO15234. 29 interactions.
STRINGi9606.ENSP00000264645.

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

iPTMnetiO15234.
PhosphoSiteiO15234.

Polymorphism and mutation databases

BioMutaiCASC3.

Proteomic databases

EPDiO15234.
MaxQBiO15234.
PaxDbiO15234.
PeptideAtlasiO15234.
PRIDEiO15234.
TopDownProteomicsiO15234.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264645; ENSP00000264645; ENSG00000108349.
GeneIDi22794.
KEGGihsa:22794.
UCSCiuc002hue.4. human.

Organism-specific databases

CTDi22794.
GeneCardsiCASC3.
HGNCiHGNC:17040. CASC3.
HPAiHPA024592.
HPA050262.
MIMi606504. gene.
neXtProtiNX_O15234.
PharmGKBiPA134948596.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4264. Eukaryota.
ENOG410ZW5Y. LUCA.
GeneTreeiENSGT00390000006930.
HOGENOMiHOG000069997.
HOVERGENiHBG050799.
InParanoidiO15234.
KOiK14323.
OMAiNLTEQNW.
OrthoDBiEOG7R2BM0.
PhylomeDBiO15234.
TreeFamiTF329663.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiCASC3. human.
EvolutionaryTraceiO15234.
GeneWikiiCASC3.
GenomeRNAii22794.
PMAP-CutDBO15234.
PROiO15234.
SOURCEiSearch...

Gene expression databases

BgeeiO15234.
CleanExiHS_CASC3.
ExpressionAtlasiO15234. baseline and differential.
GenevisibleiO15234. HS.

Family and domain databases

InterProiIPR018545. Btz_dom.
IPR028544. CASC3.
[Graphical view]
PANTHERiPTHR13434. PTHR13434. 1 hit.
PfamiPF09405. Btz. 1 hit.
[Graphical view]
SMARTiSM01044. Btz. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17."
    Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P., Lidereau R., Basset P., Rio M.-C.
    Genomics 28:367-376(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary carcinoma.
  2. "Metastatic lymph node 51, a novel nucleo-cytoplasmic protein overexpressed in breast cancer."
    Degot S.F., Regnier C.H., Wendling C., Chenard M.-P., Rio M.-C., Tomasetto C.L.
    Oncogene 21:4422-4434(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    Tissue: Mammary carcinoma.
  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].
    Tissue: Testis.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Duodenum and Skin.
  6. "Targets of gene amplification and overexpression at 17q in gastric cancer."
    Varis A., Wolf M., Monni O., Vakkari M.-L., Kokkola A., Moskaluk C., Frierson H.F. Jr., Powell S.M., Knuutila S., Kallioniemi A., El-Rifai W.
    Cancer Res. 62:2625-2629(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: OVEREXPRESSION IN GASTRIC CANCERS.
  7. "Association of the breast cancer protein MLN51 with the exon junction complex via its speckle localizer and RNA binding module."
    Degot S., Le Hir H., Alpy F., Kedinger V., Stoll I., Wendling C., Seraphin B., Rio M.-C., Tomasetto C.
    J. Biol. Chem. 279:33702-33715(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGOH; NXF1 AND RBM8A, RNA-BINDING, SUBCELLULAR LOCATION.
  8. "The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity."
    Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.
    Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, INTERACTION WITH EIF4A3, MUTAGENESIS OF TYR-181; 184-ARG-LYS-185; PHE-188; TRP-218; 220-HIS-ASP-221 AND 240-TYR-GLY-241, SUBCELLULAR LOCATION, RNA-BINDING.
  9. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
    Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
    RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "The exon-junction-complex-component metastatic lymph node 51 functions in stress-granule assembly."
    Baguet A., Degot S., Cougot N., Bertrand E., Chenard M.P., Wendling C., Kessler P., Le Hir H., Rio M.C., Tomasetto C.
    J. Cell Sci. 120:2774-2784(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN STRESS RESPONSE, SUBCELLULAR LOCATION.
  12. "MLN51 stimulates the RNA-helicase activity of eIF4AIII."
    Noble C.G., Song H.
    PLoS ONE 2:E303-E303(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EIF4A3 ATPASE AND RNA-HELICASE ACTIVITY.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling."
    Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., Huang S.M., Cong F.
    Nat. Cell Biol. 13:623-629(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION, UBIQUITINATION.
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-148; SER-265; SER-363 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-148; SER-265 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-148 AND THR-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA."
    Bono F., Ebert J., Lorentzen E., Conti E.
    Cell 126:713-725(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 137-286 IN THE EJC COMPLEX WITH EIF4A3; MAGOH; RBM8A AND AMP-PNP.
  23. "Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA."
    Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.
    Science 313:1968-1972(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 170-246 IN THE EJC COMPLEX WITH EIF4A3; MAGOH; RBM8A AND ADP-NP.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 138-283 IN THE EJC COMPLEX WITH EIF4A3; MAGOH; RBM8A AND TRANSITION STATE ANALOG ADP-ALF3.

Entry informationi

Entry nameiCASC3_HUMAN
AccessioniPrimary (citable) accession number: O15234
Secondary accession number(s): A8K8R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 14, 2001
Last modified: July 6, 2016
This is version 157 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 17
    Human chromosome 17: 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

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 one 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.