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Q9HD15

- SRA1_HUMAN

UniProt

Q9HD15 - SRA1_HUMAN

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Protein

Steroid receptor RNA activator 1

Gene

SRA1

Organism
Homo sapiens (Human)
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.5 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB
  3. cell proliferation Source: UniProtKB
  4. positive regulation of receptor activity Source: RefGenome
  5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. regulation of apoptotic process Source: UniProtKB
  7. 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:SRA1Imported
ORF Names:PP7684
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:11281. SRA1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cell leading edge Source: Ensembl
  2. cytoplasm Source: HPA
  3. intercellular bridge Source: HPA
  4. microtubule cytoskeleton Source: HPA
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: HPA
  7. ribonucleoprotein complex Source: UniProtKB
  8. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36110.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Steroid receptor RNA activator 1PRO_0000234105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HD15.
PaxDbiQ9HD15.
PeptideAtlasiQ9HD15.
PRIDEiQ9HD15.

PTM databases

PhosphoSiteiQ9HD15.

Expressioni

Tissue specificityi

Highly expressed in liver and skeletal muscle and to a lesser extent in brain. Also expressed in both normal and tumorigenic breast epithelial cell lines. Significantly up-regulated in human tumors of the breast, ovary, and uterus.3 Publications

Gene expression databases

BgeeiQ9HD15.
CleanExiHS_SRA1.
GenevestigatoriQ9HD15.

Organism-specific databases

HPAiHPA044598.
HPA050153.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC2Q927692EBI-727136,EBI-301821

Protein-protein interaction databases

BioGridi115329. 39 interactions.
IntActiQ9HD15. 2 interactions.
MINTiMINT-1383311.
STRINGi9606.ENSP00000337513.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi111 – 12414Combined sources
Turni125 – 1284Combined sources
Helixi131 – 15020Combined sources
Helixi155 – 16915Combined sources
Helixi173 – 19119Combined sources
Turni192 – 1943Combined sources
Helixi195 – 20915Combined sources
Turni221 – 2233Combined sources
Beta strandi231 – 2344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MGXNMR-A107-236[»]
4NBOX-ray2.81A/B106-215[»]
ProteinModelPortaliQ9HD15.
SMRiQ9HD15. Positions 107-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi56 – 10449Pro-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SRA1 family.Curated

Phylogenomic databases

eggNOGiNOG44276.
GeneTreeiENSGT00390000001803.
HOVERGENiHBG061820.
InParanoidiQ9HD15.
OMAiQTQTGGP.
OrthoDBiEOG790G2V.
PhylomeDBiQ9HD15.
TreeFamiTF314789.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9HD15-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRCPAGQAE VEMAELYVKP GNKERGWNDP PQFSYGLQTQ AGGPRRSLLT
60 70 80 90 100
KRVAAPQDGS PRVPASETSP GPPPMGPPPP SSKAPRSPPV GSGPASGVEP
110 120 130 140 150
TSFPVESEAV MEDVLRPLEQ ALEDCRGHTR KQVCDDISRR LALLQEQWAG
160 170 180 190 200
GKLSIPVKKR MALLVQELSS HRWDAADDIH RSLMVDHVTE VSQWMVGVKR
210 220 230
LIAEKRSLFS EEAANEEKSA ATAEKNHTIP GFQQAS
Length:236
Mass (Da):25,673
Last modified:March 1, 2001 - v1
Checksum:i9B0B60BE30ADD263
GO

Sequence cautioni

The sequence AAH40043.2 differs from that shown. Reason: Frameshift at position 29. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 132EM → RL in AF092038. (PubMed:10199399)Curated
Sequence conflicti29 – 291D → T in AAH40043. (PubMed:15489334)Curated
Sequence conflicti50 – 501T → I in AAG02115. (PubMed:12565891)Curated
Sequence conflicti110 – 1101V → RL in AAG02116. (PubMed:12565891)Curated
Sequence conflicti110 – 1101V → RL in AAL55868. (PubMed:15498874)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321Q → E.
Corresponds to variant rs35610885 [ dbSNP | Ensembl ].
VAR_052060

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293024 mRNA. Translation: AAG02114.1.
AF293025 mRNA. Translation: AAG02115.1.
AF293026 mRNA. Translation: AAG02116.1.
AF318361 mRNA. Translation: AAL55868.1.
AF092038 mRNA. No translation available.
BC040043 mRNA. Translation: AAH40043.2. Frameshift.
CCDSiCCDS34245.1.
RefSeqiNP_001030312.2. NM_001035235.3.
UniGeneiHs.653135.

Genome annotation databases

EnsembliENST00000336283; ENSP00000337513; ENSG00000213523.
GeneIDi10011.
KEGGihsa:10011.
UCSCiuc003lfz.3. human.

Polymorphism databases

DMDMi74718904.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293024 mRNA. Translation: AAG02114.1 .
AF293025 mRNA. Translation: AAG02115.1 .
AF293026 mRNA. Translation: AAG02116.1 .
AF318361 mRNA. Translation: AAL55868.1 .
AF092038 mRNA. No translation available.
BC040043 mRNA. Translation: AAH40043.2 . Frameshift.
CCDSi CCDS34245.1.
RefSeqi NP_001030312.2. NM_001035235.3.
UniGenei Hs.653135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MGX NMR - A 107-236 [» ]
4NBO X-ray 2.81 A/B 106-215 [» ]
ProteinModelPortali Q9HD15.
SMRi Q9HD15. Positions 107-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115329. 39 interactions.
IntActi Q9HD15. 2 interactions.
MINTi MINT-1383311.
STRINGi 9606.ENSP00000337513.

PTM databases

PhosphoSitei Q9HD15.

Polymorphism databases

DMDMi 74718904.

Proteomic databases

MaxQBi Q9HD15.
PaxDbi Q9HD15.
PeptideAtlasi Q9HD15.
PRIDEi Q9HD15.

Protocols and materials databases

DNASUi 10011.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336283 ; ENSP00000337513 ; ENSG00000213523 .
GeneIDi 10011.
KEGGi hsa:10011.
UCSCi uc003lfz.3. human.

Organism-specific databases

CTDi 10011.
GeneCardsi GC05M139911.
HGNCi HGNC:11281. SRA1.
HPAi HPA044598.
HPA050153.
MIMi 603819. gene.
neXtProti NX_Q9HD15.
PharmGKBi PA36110.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG44276.
GeneTreei ENSGT00390000001803.
HOVERGENi HBG061820.
InParanoidi Q9HD15.
OMAi QTQTGGP.
OrthoDBi EOG790G2V.
PhylomeDBi Q9HD15.
TreeFami TF314789.

Miscellaneous databases

GeneWikii SRA1.
GenomeRNAii 10011.
NextBioi 37823.
PROi Q9HD15.
SOURCEi Search...

Gene expression databases

Bgeei Q9HD15.
CleanExi HS_SRA1.
Genevestigatori Q9HD15.

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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Mammary glandImported.
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex."
    Lanz R.B., McKenna N.J., Onate S.A., Albrecht U., Wong J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
    Cell 97:17-27(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-236, FUNCTION, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH NCOA1, TISSUE SPECIFICITY.
  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] OF 22-236.
    Tissue: LymphImported.
  5. "Ligand-independent coactivation of ERalpha AF-1 by steroid receptor RNA activator (SRA) via MAPK activation."
    Deblois G., Giguere V.
    J. Steroid Biochem. Mol. Biol. 85:123-131(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Steroid receptor RNA activator stimulates proliferation as well as apoptosis in vivo."
    Lanz R.B., Chua S.S., Barron N., Soder B.M., DeMayo F., O'Malley B.W.
    Mol. Cell. Biol. 23:7163-7176(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "SRA coactivation of estrogen receptor-alpha is phosphorylation-independent, and enhances 4-hydroxytamoxifen agonist activity."
    Coleman K.M., Lam V., Jaber B.M., Lanz R.B., Smith C.L.
    Biochem. Biophys. Res. Commun. 323:332-338(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The steroid receptor RNA activator is the first functional RNA encoding a protein."
    Chooniedass-Kothari S., Emberley E., Hamedani M.K., Troup S., Wang X., Czosnek A., Hube F., Mutawe M., Watson P.H., Leygue E.
    FEBS Lett. 566:43-47(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRA1_HUMAN
AccessioniPrimary (citable) accession number: Q9HD15
Secondary accession number(s): Q6NVU9
, Q8IXM1, Q9HD13, Q9HD14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Appears to be the first example of a new class of functional RNAs also able to encode a protein.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3