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Protein

Transformer-2 protein homolog beta

Gene

Tra2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. mRNA binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. cerebral cortex regionalization Source: MGI
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
  4. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Tra2b
Synonyms:Sfrs10, Silg41
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:106016. Tra2b.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 288287Transformer-2 protein homolog betaPRO_0000081984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei95 – 951PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei99 – 991PhosphoserineBy similarity
Modified residuei103 – 1031PhosphothreonineBy similarity
Modified residuei201 – 2011PhosphothreonineBy similarity
Modified residuei203 – 2031PhosphothreonineBy similarity
Modified residuei241 – 2411Dimethylated arginineBy similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP62996.
PaxDbiP62996.
PRIDEiP62996.

PTM databases

PhosphoSiteiP62996.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in uterus and brain.1 Publication

Inductioni

Induced by reoxygenation following hypoxia and by exposure to silica. Repressed by interferon gamma, LPS and TPA.1 Publication

Gene expression databases

BgeeiP62996.
ExpressionAtlasiP62996. baseline and differential.
GenevestigatoriP62996.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi203252. 1 interaction.
IntActiP62996. 2 interactions.
MINTiMINT-4138402.

Structurei

3D structure databases

ProteinModelPortaliP62996.
SMRiP62996. Positions 106-229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini118 – 19679RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 23038LinkerAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 11383Arg/Ser-rich (RS1 domain)Add
BLAST
Compositional biasi231 – 28757Arg/Ser-rich (RS2 domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG297815.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG104971.
InParanoidiP62996.
KOiK12897.
OMAiYSRDTDH.
OrthoDBiEOG7SFHZZ.
TreeFamiTF106265.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P62996-1) [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
MSDSGEQNYG ERESRSASRS GSAHGSGKSA RHTPARSRSK EDSRRSRSKS
60 70 80 90 100
RSRSESRSRS RRSSRRHYTR SRSRSRSHRR SRSRSYSRDY RRRHSHSHSP
110 120 130 140 150
MSTRRRHVGN RANPDPNCCL GVFGLSLYTT ERDLREVFSK YGPIADVSIV
160 170 180 190 200
YDQQSRRSRG FAFVYFENVD DAKEAKERAN GMELDGRRIR VDFSITKRPH
210 220 230 240 250
TPTPGIYMGR PTYGSSRRRD YYDRGYDRGY DDRDYYSRSY RGGGGGGGGW
260 270 280
RAAQDRDQIY RRRSPSPYYS RGGYRSRSRS RSYSPRRY
Length:288
Mass (Da):33,666
Last modified:August 31, 2004 - v1
Checksum:i60B310C8BA443E28
GO
Isoform 2 (identifier: P62996-2) [UniParc]FASTAAdd to basket

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

Show »
Length:38
Mass (Da):4,392
Checksum:iE499E3AFDD3D7BCA
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei23 – 3816AHGSG…PARSR → RHLTSFINEYLKLRNK in isoform 2. 1 PublicationVSP_011509Add
BLAST
Alternative sequencei39 – 288250Missing in isoform 2. 1 PublicationVSP_011510Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37297.1. [P62996-1]
PIRiS68798.
RefSeqiNP_033212.1. NM_009186.4. [P62996-1]
UniGeneiMm.210352.
Mm.389440.
Mm.442193.

Genome annotation databases

EnsembliENSMUST00000161286; ENSMUSP00000124846; ENSMUSG00000022858. [P62996-1]
GeneIDi20462.
KEGGimmu:20462.
UCSCiuc007ysc.1. mouse. [P62996-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37297.1. [P62996-1]
PIRiS68798.
RefSeqiNP_033212.1. NM_009186.4. [P62996-1]
UniGeneiMm.210352.
Mm.389440.
Mm.442193.

3D structure databases

ProteinModelPortaliP62996.
SMRiP62996. Positions 106-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203252. 1 interaction.
IntActiP62996. 2 interactions.
MINTiMINT-4138402.

PTM databases

PhosphoSiteiP62996.

Proteomic databases

MaxQBiP62996.
PaxDbiP62996.
PRIDEiP62996.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000161286; ENSMUSP00000124846; ENSMUSG00000022858. [P62996-1]
GeneIDi20462.
KEGGimmu:20462.
UCSCiuc007ysc.1. mouse. [P62996-1]

Organism-specific databases

CTDi6434.
MGIiMGI:106016. Tra2b.

Phylogenomic databases

eggNOGiNOG297815.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG104971.
InParanoidiP62996.
KOiK12897.
OMAiYSRDTDH.
OrthoDBiEOG7SFHZZ.
TreeFamiTF106265.

Miscellaneous databases

NextBioi24991.
PROiP62996.
SOURCEiSearch...

Gene expression databases

BgeeiP62996.
ExpressionAtlasiP62996. baseline and differential.
GenevestigatoriP62996.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [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(1995) [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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.

Entry informationi

Entry nameiTRA2B_MOUSE
AccessioniPrimary (citable) accession number: P62996
Secondary accession number(s): O15449, Q15815, Q64283
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 1, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.