P62996 (TRA2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Silica-induced gene 41 protein
Short name=SIG-41
Splicing factor, arginine/serine-rich 10
Transformer-2 protein homolog B

Gene names

Name:	Tra2b
Synonyms:	Sfrs10, Silg41

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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, SAFB/SAFB1, RBMX and phosphorylated SFRS13A By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Widely expressed. Highly expressed in uterus and brain. Ref.2
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
Coding sequence diversity	Alternative splicing
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
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P62996-1)

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: P62996-2)

The sequence of this isoform differs from the canonical sequence as follows:
     23-38: AHGSGKSARHTPARSR → RHLTSFINEYLKLRNK
     39-288: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 288	287	Transformer-2 protein homolog beta		PRO_0000081984
Regions
	Domain	118 – 196	79	RRM
	Region	193 – 230	38	Linker
	Compositional bias	31 – 113	83	Arg/Ser-rich (RS1 domain)
	Compositional bias	231 – 287	57	Arg/Ser-rich (RS2 domain)
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	2	1	Phosphoserine Ref.7
	Modified residue	4	1	Phosphoserine Ref.7
	Modified residue	14	1	Phosphoserine Ref.7
	Modified residue	50	1	Phosphoserine Ref.7
	Modified residue	52	1	Phosphoserine Ref.7
	Modified residue	54	1	Phosphoserine Ref.7
	Modified residue	56	1	Phosphoserine Ref.7
	Modified residue	83	1	Phosphoserine Ref.7
	Modified residue	85	1	Phosphoserine Ref.7
	Modified residue	95	1	Phosphoserine By similarity
	Modified residue	97	1	Phosphoserine By similarity
	Modified residue	99	1	Phosphoserine By similarity
	Modified residue	103	1	Phosphothreonine By similarity
	Modified residue	201	1	Phosphothreonine Ref.6
	Modified residue	203	1	Phosphothreonine By similarity
	Modified residue	241	1	Dimethylated arginine By similarity
	Modified residue	264	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
	Modified residue	266	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
	Modified residue	280	1	Phosphoserine By similarity
	Modified residue	282	1	Phosphoserine By similarity
	Modified residue	284	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	23 – 38	16	AHGSG…PARSR → RHLTSFINEYLKLRNK in isoform 2.		VSP_011509
	Alternative sequence	39 – 288	250	Missing in isoform 2.		VSP_011510

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 31, 2004. Version 1. Checksum: 60B310C8BA443E28	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
	Isoform 2 [UniParc]. Checksum: E499E3AFDD3D7BCA	FASTA	38	4,392
	10 20 30 MSDSGEQNYG ERESRSASRS GSRHLTSFIN EYLKLRNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of nine gene sequences induced by silica in murine macrophages." Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S. J. Immunol. 154:2384-2392(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION. Tissue: Macrophage.
[2]	"Molecular cloning of a mouse homologue for the Drosophila splicing regulator Tra2." Segade F., Hurle B., Claudio E., Ramos S., Lazo P.S. FEBS Lett. 387:152-156(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]	"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: Thymus.
[4]	"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: Brain.
[5]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-266, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; SER-264 AND SER-266, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; SER-14; SER-50; SER-52; SER-54; SER-56; SER-83; SER-85; SER-264; SER-266 AND SER-284, MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-266, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80232 mRNA. Translation: CAA56518.1. AK049573 mRNA. Translation: BAC33819.1. AK077418 mRNA. Translation: BAC36791.1. AK080378 mRNA. Translation: BAC37898.1. BC061177 mRNA. Translation: AAH61177.1.
IPI	IPI00139259. IPI00457594.
PIR	S68798.
RefSeq	NP_033212.1. NM_009186.4.
UniGene	Mm.210352. Mm.389440. Mm.442193.
3D structure databases
ProteinModelPortal	P62996.
ModBase	Search...
PTM databases
PhosphoSite	P62996.
Proteomic databases
PaxDb	P62996.
PRIDE	P62996.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000161286; ENSMUSP00000124846; ENSMUSG00000022858. ENSMUST00000162413; ENSMUSP00000123782; ENSMUSG00000022858.
GeneID	20462.
KEGG	mmu:20462.
UCSC	uc007ysc.1. mouse.
Organism-specific databases
CTD	6434.
MGI	MGI:106016. Tra2b.
Phylogenomic databases
eggNOG	NOG297815.
GeneTree	ENSGT00700000104309.
HOGENOM	HOG000276232.
HOVERGEN	HBG104971.
InParanoid	P62996.
KO	K12897.
OMA	YDDREYY.
OrthoDB	EOG4BVRW2.
Gene expression databases
ArrayExpress	P62996.
Bgee	P62996.
Genevestigator	P62996.
GermOnline	ENSMUSG00000022858. Mus musculus.
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	24991.
SOURCE	Search...

Entry information

Entry name

TRA2B_MOUSE

Accession

Primary (citable) accession number: P62996
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 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program