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Q80VJ2

- SRA1_MOUSE

UniProt

Q80VJ2 - SRA1_MOUSE

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Protein
Steroid receptor RNA activator 1
Gene
Sra1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. ligand-dependent nuclear receptor transcription coactivator activity Source: MGI
  3. thyroid hormone receptor activator activity Source: MGI
  4. transcription coactivator activity Source: UniProtKB
  5. transcription cofactor activity Source: MGI

GO - Biological processi

  1. cell differentiation Source: UniProtKB
  2. cell proliferation Source: UniProtKB
  3. execution phase of apoptosis Source: Ensembl
  4. positive regulation of receptor activity Source: GOC
  5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  6. regulation of apoptotic process Source: UniProtKB
  7. regulation of transcription from RNA polymerase II promoter Source: MGI
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor, Ribonucleoprotein

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Steroid receptor RNA activator 1
Alternative name(s):
Steroid receptor RNA activator protein
Short name:
SRAP
Gene namesi
Name:Sra1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1344414. Sra1.

Subcellular locationi

Nucleus. Cytoplasm By similarity By similarity

GO - Cellular componenti

  1. cell leading edge Source: MGI
  2. nucleus Source: UniProtKB
  3. ribonucleoprotein complex Source: UniProtKB
  4. steroid hormone aporeceptor complex Source: MGI
  5. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 232232Steroid receptor RNA activator 1
PRO_0000234106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ80VJ2.
PaxDbiQ80VJ2.
PRIDEiQ80VJ2.

2D gel databases

REPRODUCTION-2DPAGEIPI00317966.

PTM databases

PhosphoSiteiQ80VJ2.

Expressioni

Gene expression databases

BgeeiQ80VJ2.
CleanExiMM_SRA1.
GenevestigatoriQ80VJ2.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi204880. 2 interactions.
IntActiQ80VJ2. 2 interactions.
MINTiMINT-4125677.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi109 – 12416
Helixi129 – 14820
Helixi153 – 16816
Helixi171 – 18313
Helixi186 – 1894
Turni190 – 1923
Helixi193 – 20614

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRUNMR-A102-206[»]
ProteinModelPortaliQ80VJ2.
SMRiQ80VJ2. Positions 99-207.

Miscellaneous databases

EvolutionaryTraceiQ80VJ2.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi56 – 10146Pro-rich
Add
BLAST

Sequence similaritiesi

Belongs to the SRA1 family.

Phylogenomic databases

eggNOGiNOG44276.
GeneTreeiENSGT00390000001803.
HOGENOMiHOG000127508.
HOVERGENiHBG061820.
InParanoidiQ80VJ2.
OMAiQTQTGGP.
OrthoDBiEOG790G2V.
TreeFamiTF314789.

Family and domain databases

InterProiIPR009917. SRA1-protein/COPII_Sec31.
[Graphical view]
PfamiPF07304. SRA1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80VJ2-1 [UniParc]FASTAAdd to Basket

« Hide

MMRCPAGGAE VEMAELYVKP GNKERGWNDP PQFSYGLQTQ TGGPKRTPLT    50
KRVAAPQDGS PRAPETSGPP PVDHPPPSSK ASRPPPMGSC PATGVEPPSS 100
PVIESETLIE DVLRPLEQAL EDCHGHTKKQ VCDDISRRLA LLREQWAGGK 150
LSIPVKKRMA LLVQELLHHQ WDAADDIHRS LMVDHVTEVS QWMVGVKRLI 200
AEKKSLSSEE TKEEKFTVEP ENQTIPGFQQ PS 232
Length:232
Mass (Da):25,557
Last modified:June 28, 2011 - v3
Checksum:i0838CA544C75A678
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51P → A in BAB24943. 1 Publication
Sequence conflicti10 – 101E → G in BAB24943. 1 Publication
Sequence conflicti27 – 271W → G in BAB24943. 1 Publication
Sequence conflicti140 – 1401A → V in AAH48362. 1 Publication
Sequence conflicti185 – 1851H → Y in AAH48362. 1 Publication
Sequence conflicti204 – 2041K → R in AAH48362. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS29156.2.
RefSeqiNP_001157878.1. NM_001164406.1.
NP_079567.2. NM_025291.3.
UniGeneiMm.29058.

Genome annotation databases

EnsembliENSMUST00000173875; ENSMUSP00000133360; ENSMUSG00000006050.
GeneIDi24068.
KEGGimmu:24068.
UCSCiuc008eny.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS29156.2.
RefSeqi NP_001157878.1. NM_001164406.1.
NP_079567.2. NM_025291.3.
UniGenei Mm.29058.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YRU NMR - A 102-206 [» ]
ProteinModelPortali Q80VJ2.
SMRi Q80VJ2. Positions 99-207.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204880. 2 interactions.
IntActi Q80VJ2. 2 interactions.
MINTi MINT-4125677.

PTM databases

PhosphoSitei Q80VJ2.

2D gel databases

REPRODUCTION-2DPAGE IPI00317966.

Proteomic databases

MaxQBi Q80VJ2.
PaxDbi Q80VJ2.
PRIDEi Q80VJ2.

Protocols and materials databases

DNASUi 24068.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000173875 ; ENSMUSP00000133360 ; ENSMUSG00000006050 .
GeneIDi 24068.
KEGGi mmu:24068.
UCSCi uc008eny.2. mouse.

Organism-specific databases

CTDi 10011.
MGIi MGI:1344414. Sra1.

Phylogenomic databases

eggNOGi NOG44276.
GeneTreei ENSGT00390000001803.
HOGENOMi HOG000127508.
HOVERGENi HBG061820.
InParanoidi Q80VJ2.
OMAi QTQTGGP.
OrthoDBi EOG790G2V.
TreeFami TF314789.

Miscellaneous databases

EvolutionaryTracei Q80VJ2.
NextBioi 304045.
PROi Q80VJ2.
SOURCEi Search...

Gene expression databases

Bgeei Q80VJ2.
CleanExi MM_SRA1.
Genevestigatori Q80VJ2.

Family and domain databases

InterProi IPR009917. SRA1-protein/COPII_Sec31.
[Graphical view ]
Pfami PF07304. SRA1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiSRA1_MOUSE
AccessioniPrimary (citable) accession number: Q80VJ2
Secondary accession number(s): E9QM44
, Q8R0S3, Q9CWU7, Q9D973
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi