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Q5SZQ8 (CELF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CUGBP Elav-like family member 3

Short name=CELF-3
Alternative name(s):
Bruno-like protein 1
CAG repeat protein 4
CUG-BP- and ETR-3-like factor 3
ELAV-type RNA-binding protein 1
Short name=ETR-1
Expanded repeat domain protein CAG/CTG 4
RNA-binding protein BRUNOL-1
Trinucleotide repeat-containing gene 4 protein
Gene names
Name:CELF3
Synonyms:BRUNOL1, CAGH4, ERDA4, TNRC4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein involved in the regulation of pre-mRNA alternative splicing. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Activates the splicing of MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Ref.1 Ref.8

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Tissue specificity

Expressed in brain. Ref.1

Polymorphism

The poly-Gln tract in AAK07474 may be polymorphic.

Sequence similarities

Belongs to the CELF/BRUNOL family.

Contains 3 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAB91444.1 differs from that shown. Reason: Frameshift at position 136.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5SZQ8-1)

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.
Isoform 2 (identifier: Q5SZQ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     330-330: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5SZQ8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     93-93: Missing.
Isoform 4 (identifier: Q5SZQ8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     258-307: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465CUGBP Elav-like family member 3
PRO_0000295198

Regions

Domain7 – 8882RRM 1
Domain95 – 17581RRM 2
Domain380 – 45879RRM 3
Compositional bias352 – 37322Gln-rich

Natural variations

Alternative sequence931Missing in isoform 3.
VSP_026824
Alternative sequence258 – 30750Missing in isoform 4.
VSP_046642
Alternative sequence3301Missing in isoform 2.
VSP_026825

Experimental info

Sequence conflict1491Q → K in AAH52491. Ref.5
Sequence conflict1981A → T in AAH52491. Ref.5
Sequence conflict2841P → Q in AAH52491. Ref.5
Sequence conflict3121A → V in AAK07474. Ref.1
Sequence conflict3121A → V in AAN73884. Ref.2

Secondary structure

............... 465
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 59B74F120090C15F

FASTA46550,548
        10         20         30         40         50         60 
MKEPDAIKLF VGQIPRHLEE KDLKPIFEQF GRIFELTVIK DKYTGLHKGC AFLTYCARDS 

        70         80         90        100        110        120 
ALKAQSALHE QKTLPGMNRP IQVKPADSES RGEDRKLFVG MLGKQQTDED VRKMFEPFGT 

       130        140        150        160        170        180 
IDECTVLRGP DGTSKGCAFV KFQTHAEAQA AINTLHSSRT LPGASSSLVV KFADTEKERG 

       190        200        210        220        230        240 
LRRMQQVATQ LGMFSPIALQ FGAYSAYTQA LMQQQAALVA AHSAYLSPMA TMAAVQMQHM 

       250        260        270        280        290        300 
AAINANGLIA TPITPSSGTS TPPAIAATPV SAIPAALGVN GYSPVPTQPT GQPAPDALYP 

       310        320        330        340        350        360 
NGVHPYPAQS PAAPVDPLQQ AYAGMQHYTA AYPAAYSLVA PAFPQPPALV AQQPPPPPQQ 

       370        380        390        400        410        420 
QQQQQQQQQQ QQQREGPDGC NIFIYHLPQE FTDSEILQMF VPFGHVISAK VFVDRATNQS 

       430        440        450        460 
KCFGFVSFDN PASAQAAIQA MNGFQIGMKR LKVQLKRPKD ANRPY 

« Hide

Isoform 2 [UniParc].

Checksum: E02FE9050D638FA3
Show »

FASTA46450,477
Isoform 3 [UniParc].

Checksum: D1C98752B8DD9F70
Show »

FASTA46450,419
Isoform 4 [UniParc].

Checksum: DA0C7D67794166E0
Show »

FASTA41545,686

References

« Hide 'large scale' references
[1]"The CELF family of RNA binding proteins is implicated in cell-specific and developmentally regulated alternative splicing."
Ladd A.N., Charlet-B N., Cooper T.A.
Mol. Cell. Biol. 21:1285-1296(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, RNA-BINDING, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"The RNA binding protein CELF3 associates to the DMPK mRNA and is a negative regulator of mRNA stability involved in neuronal differentiation."
d'Apolito M., Savino M., Grifa A., Quattrone A.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 1; 2 AND 3).
Tissue: Brain and Retinoblastoma.
[6]"cDNAs with long CAG trinucleotide repeats from human brain."
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.
Hum. Genet. 100:114-122(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-465 (ISOFORM 1).
Tissue: Fetal brain.
[7]"A family of human RNA-binding proteins related to the Drosophila Bruno translational regulator."
Good P.J., Chen Q., Warner S.J., Herring D.C.
J. Biol. Chem. 275:28583-28592(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 326-465.
[8]"Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors."
Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.
J. Neurochem. 88:1078-1090(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Solution structure of RNA binding domain in trinucleotide repeat containing 4 variant."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 90-178.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF329264 mRNA. Translation: AAK07474.1.
AY165003 mRNA. Translation: AAN73884.1.
AL589765 Genomic DNA. Translation: CAI17166.1.
CH471121 Genomic DNA. Translation: EAW53422.1.
BC052491 mRNA. Translation: AAH52491.1.
BC068008 mRNA. Translation: AAH68008.1.
BC104758 mRNA. Translation: AAI04759.1.
BC143226 mRNA. Translation: AAI43227.1.
U80746 mRNA. Translation: AAB91444.1. Frameshift.
AF284423 mRNA. Translation: AAG14457.1.
CCDSCCDS1002.1. [Q5SZQ8-1]
CCDS53367.1. [Q5SZQ8-4]
RefSeqNP_001166120.1. NM_001172649.3. [Q5SZQ8-4]
NP_001278035.1. NM_001291106.1. [Q5SZQ8-2]
NP_001278036.1. NM_001291107.1. [Q5SZQ8-3]
NP_009116.3. NM_007185.6. [Q5SZQ8-1]
UniGeneHs.26047.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNONMR-A90-178[»]
ProteinModelPortalQ5SZQ8.
SMRQ5SZQ8. Positions 1-180, 364-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116359. 7 interactions.
IntActQ5SZQ8. 5 interactions.
MINTMINT-4866187.

PTM databases

PhosphoSiteQ5SZQ8.

Polymorphism databases

DMDM74756184.

Proteomic databases

PaxDbQ5SZQ8.
PRIDEQ5SZQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290583; ENSP00000290583; ENSG00000159409. [Q5SZQ8-1]
ENST00000290585; ENSP00000290585; ENSG00000159409. [Q5SZQ8-4]
GeneID11189.
KEGGhsa:11189.
UCSCuc001eyr.3. human. [Q5SZQ8-3]
uc001eys.2. human. [Q5SZQ8-1]
uc009wmx.2. human. [Q5SZQ8-2]

Organism-specific databases

CTD11189.
GeneCardsGC01M151674.
HGNCHGNC:11967. CELF3.
HPAHPA006292.
MIM612678. gene.
neXtProtNX_Q5SZQ8.
PharmGKBPA36654.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251494.
HOVERGENHBG107646.
KOK13207.
OrthoDBEOG7DVDBR.
PhylomeDBQ5SZQ8.
TreeFamTF314924.

Gene expression databases

ArrayExpressQ5SZQ8.
BgeeQ5SZQ8.
CleanExHS_TNRC4.
GenevestigatorQ5SZQ8.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5SZQ8.
GenomeRNAi11189.
NextBio42591.
PROQ5SZQ8.
SOURCESearch...

Entry information

Entry nameCELF3_HUMAN
AccessionPrimary (citable) accession number: Q5SZQ8
Secondary accession number(s): B7ZKK6 expand/collapse secondary AC list , O15414, Q499Y6, Q5SZQ7, Q6NVK0, Q8IZ98, Q9BZC2, Q9HB30
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM