Transformer-2 protein homolog beta - Rattus norvegicus (Rat)

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P62997 (TRA2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transformer-2 protein homolog beta
Short name=TRA-2 beta
Short name=TRA2-beta

Alternative name(s):
RA301
Splicing factor, arginine/serine-rich 10
Transformer-2 protein homolog B

Gene names

Name:	Tra2b
Synonyms:	Sfrs10

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA By similarity.
Subunit structure	Found in a pre-mRNA exonic splicing enhancer (ESE) complex with TRA2B/SFRS10, SNRNP70, SNRPA1 and SRRM1. Binds to A3 enhancer proteins SFRS4, SFRS5, SFRS6 and SFRS9. Interacts with CPSF6, RBMY1A1, RNPS1 and phosphorylated SFRS13A By similarity. Interacts with RBMX and SAFB/SAFB1. Ref.3 Ref.5
Subcellular location	Nucleus By similarity.
Induction	Induced by reoxygenation following hypoxia and by exposure to silica. Repressed by interferon gamma, LPS and TPA. Ref.1
Sequence similarities	Belongs to the splicing factor SR family. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of mRNA splicing, via spliceosome Inferred from sequence or structural similarity. Source: UniProtKB regulation of alternative mRNA splicing, via spliceosome Inferred from sequence or structural similarity. Source: UniProtKB response to reactive oxygen species Inferred from expression pattern Ref.1. Source: RGD
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	mRNA binding Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 288

287

Transformer-2 protein homolog beta

PRO_0000081985

Regions

Domain

118 – 196

RRM

Region

193 – 230

Linker

Compositional bias

31 – 113

Arg/Ser-rich (RS1 domain)

Compositional bias

231 – 287

Arg/Ser-rich (RS2 domain)

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

103

Phosphothreonine By similarity

Modified residue

201

Phosphothreonine By similarity

Modified residue

203

Phosphothreonine By similarity

Modified residue

241

Dimethylated arginine By similarity

Modified residue

264

Phosphoserine By similarity

Modified residue

266

Phosphoserine By similarity

Modified residue

280

Phosphoserine Ref.4

Modified residue

282

Phosphoserine Ref.4

Modified residue

284

Phosphoserine Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P62997 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: 60B310C8BA443E28
Show »

FASTA

288

33,666

        10         20         30         40         50         60 
MSDSGEQNYG ERESRSASRS GSAHGSGKSA RHTPARSRSK EDSRRSRSKS RSRSESRSRS 

        70         80         90        100        110        120 
RRSSRRHYTR SRSRSRSHRR SRSRSYSRDY RRRHSHSHSP MSTRRRHVGN RANPDPNCCL 

       130        140        150        160        170        180 
GVFGLSLYTT ERDLREVFSK YGPIADVSIV YDQQSRRSRG FAFVYFENVD DAKEAKERAN 

       190        200        210        220        230        240 
GMELDGRRIR VDFSITKRPH TPTPGIYMGR PTYGSSRRRD YYDRGYDRGY DDRDYYSRSY 

       250        260        270        280 
RGGGGGGGGW RAAQDRDQIY RRRSPSPYYS RGGYRSRSRS RSYSPRRY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a novel RNA binding polypeptide (RA301) induced by hypoxia/reoxygenation." Matsuo N., Ogawa S., Imai Y., Takagi T., Tohyama M., Stern D., Wanaka A. J. Biol. Chem. 270:28216-28222(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: Sprague-Dawley. Tissue: Astrocyte.
[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]. Tissue: Lung.
[3]	"SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements." Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L., Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S. Nucleic Acids Res. 26:3542-3549(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SAFB/SAFB1.
[4]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-282 AND SER-284, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
[5]	"Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA." Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., Stamm S. J. Biol. Chem. 284:14303-14315(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBMX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D49708 mRNA. Translation: BAA08556.1. BC070948 mRNA. Translation: AAH70948.1.
IPI	IPI00202484.
RefSeq	NP_476460.1. NM_057119.1.
UniGene	Rn.8538.
3D structure databases
ProteinModelPortal	P62997.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62997. 1 interaction.
PTM databases
PhosphoSite	P62997.
Proteomic databases
PaxDb	P62997.
PRIDE	P62997.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000002429; ENSRNOP00000002429; ENSRNOG00000001783.
GeneID	117259.
KEGG	rno:117259.
UCSC	RGD:619886. rat.
Organism-specific databases
CTD	6434.
RGD	619886. Tra2b.
Phylogenomic databases
eggNOG	NOG297815.
GeneTree	ENSGT00700000104309.
HOGENOM	HOG000276232.
HOVERGEN	HBG104971.
InParanoid	P62997.
KO	K12897.
OrthoDB	EOG4BVRW2.
Gene expression databases
Genevestigator	P62997.
GermOnline	ENSRNOG00000001783. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	620130.

Entry information

Entry name

TRA2B_RAT

Accession

Primary (citable) accession number: P62997
Secondary accession number(s): O15449, Q15815, Q64283

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents