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Q80VJ2 (SRA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Steroid receptor RNA activator 1
Alternative name(s):
Steroid receptor RNA activator protein
Short name=SRAP
Gene names
Name:Sra1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of steroid receptors ligand-dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis By similarity. UniProtKB Q9HD15

Subunit structure

SRA1 RNA exists in a ribonucleoprotein complex containing NCOA1. The RNA also forms a complex with PUS1 and RARG in the nucleus. Interacts with AR. Ref.4 UniProtKB Q9HD15 UniProtKB Q6QGW5

Subcellular location

Nucleus. Cytoplasm By similarity UniProtKB Q9HD15.

Miscellaneous

Appears to be the first example of a new class of functional RNAs also able to encode a protein By similarity. UniProtKB Q9HD15

Sequence similarities

Belongs to the SRA1 family.

Sequence caution

The sequence AAH26480.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH26480.1 differs from that shown. Reason: Contaminating sequence.

The sequence AAH48362.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB24943.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB26893.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE32451.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Molecular functionActivator
Receptor
Ribonucleoprotein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

execution phase of apoptosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor activity

Inferred from direct assay PubMed 15180993. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.4. Source: MGI

regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from sequence orthology PubMed 10199399. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell leading edge

Inferred from direct assay PubMed 16831833. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

steroid hormone aporeceptor complex

Inferred from sequence orthology PubMed 10199399. Source: MGI

transcription factor complex

Inferred from direct assay Ref.4. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15343387. Source: MGI

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay Ref.4. Source: MGI

thyroid hormone receptor activator activity

Inferred from direct assay PubMed 15180993. Source: MGI

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription cofactor activity

Inferred from sequence orthology PubMed 10199399. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Steroid receptor RNA activator 1
PRO_0000234106

Regions

Compositional bias56 – 10146Pro-rich

Amino acid modifications

Modified residue601Phosphoserine By similarity

Experimental info

Sequence conflict51P → A in BAB24943. Ref.2
Sequence conflict101E → G in BAB24943. Ref.2
Sequence conflict271W → G in BAB24943. Ref.2
Sequence conflict1401A → V in AAH48362. Ref.3
Sequence conflict1851H → Y in AAH48362. Ref.3
Sequence conflict2041K → R in AAH48362. Ref.3

Secondary structure

............. 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q80VJ2 [UniParc].

Last modified June 28, 2011. Version 3.
Checksum: 0838CA544C75A678

FASTA23225,557
        10         20         30         40         50         60 
MMRCPAGGAE VEMAELYVKP GNKERGWNDP PQFSYGLQTQ TGGPKRTPLT KRVAAPQDGS 

        70         80         90        100        110        120 
PRAPETSGPP PVDHPPPSSK ASRPPPMGSC PATGVEPPSS PVIESETLIE DVLRPLEQAL 

       130        140        150        160        170        180 
EDCHGHTKKQ VCDDISRRLA LLREQWAGGK LSIPVKKRMA LLVQELLHHQ WDAADDIHRS 

       190        200        210        220        230 
LMVDHVTEVS QWMVGVKRLI AEKKSLSSEE TKEEKFTVEP ENQTIPGFQQ PS 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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. expand/collapse author list , 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] OF 5-232.
Strain: C57BL/6J and NOD.
Tissue: Embryonic stem cell and Testis.
[3]"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] OF 10-232.
Strain: Czech II.
Tissue: Eye, Mammary gland and Testis.
[4]"Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator."
Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.
Mol. Cell 15:549-558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PUS1 AND RARG.
[5]"Solution structure of mouse steroid receptor RNA activator 1 (SRA1) protein."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 99-207.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC115631 Genomic DNA. No translation available.
AK007302 mRNA. Translation: BAB24943.1. Different initiation.
AK010375 mRNA. Translation: BAB26893.1. Different initiation.
AK154232 mRNA. Translation: BAE32451.1. Different initiation.
BC026480 mRNA. Translation: AAH26480.1. Sequence problems.
BC048362 mRNA. Translation: AAH48362.1. Different initiation.
CN836515 mRNA. No translation available.
CCDSCCDS29156.2.
RefSeqNP_001157878.1. NM_001164406.1.
NP_079567.2. NM_025291.3.
UniGeneMm.29058.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRUNMR-A102-206[»]
ProteinModelPortalQ80VJ2.
SMRQ80VJ2. Positions 99-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204880. 2 interactions.
IntActQ80VJ2. 2 interactions.
MINTMINT-4125677.

PTM databases

PhosphoSiteQ80VJ2.

2D gel databases

REPRODUCTION-2DPAGEIPI00317966.

Proteomic databases

MaxQBQ80VJ2.
PaxDbQ80VJ2.
PRIDEQ80VJ2.

Protocols and materials databases

DNASU24068.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000173875; ENSMUSP00000133360; ENSMUSG00000006050.
GeneID24068.
KEGGmmu:24068.
UCSCuc008eny.2. mouse.

Organism-specific databases

CTD10011.
MGIMGI:1344414. Sra1.

Phylogenomic databases

eggNOGNOG44276.
GeneTreeENSGT00390000001803.
HOGENOMHOG000127508.
HOVERGENHBG061820.
InParanoidQ80VJ2.
OMAQTQTGGP.
OrthoDBEOG790G2V.
TreeFamTF314789.

Gene expression databases

BgeeQ80VJ2.
CleanExMM_SRA1.
GenevestigatorQ80VJ2.

Family and domain databases

InterProIPR009917. SRA1-protein/COPII_Sec31.
[Graphical view]
PfamPF07304. SRA1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ80VJ2.
NextBio304045.
PROQ80VJ2.
SOURCESearch...

Entry information

Entry nameSRA1_MOUSE
AccessionPrimary (citable) accession number: Q80VJ2
Secondary accession number(s): E9QM44 expand/collapse secondary AC list , Q8R0S3, Q9CWU7, Q9D973
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot