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Q9HD15 (SRA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
ORF Names:PP7684
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length236 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. Ref.3 Ref.5 Ref.6 Ref.7 Ref.8

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.3 UniProtKB Q80VJ2 UniProtKB Q6QGW5

Subcellular location

Nucleus. Cytoplasm Ref.1.

Tissue specificity

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. Ref.1 Ref.3 Ref.6

Miscellaneous

Appears to be the first example of a new class of functional RNAs also able to encode a protein. Ref.1 Ref.8

Sequence similarities

Belongs to the SRA1 family.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionActivator
Receptor
Ribonucleoprotein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from direct assay Ref.6. Source: UniProtKB

cell proliferation

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Inferred from direct assay Ref.6. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell leading edge

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

intercellular bridge

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Inferred from physical interaction Ref.3. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 16595694PubMed 20398657. Source: IntAct

thyroid hormone receptor activator activity

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HDAC2Q927692EBI-727136,EBI-301821

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Steroid receptor RNA activator 1
PRO_0000234105

Regions

Compositional bias56 – 10449Pro-rich

Amino acid modifications

Modified residue601Phosphoserine Ref.9

Natural variations

Natural variant321Q → E.
Corresponds to variant rs35610885 [ dbSNP | Ensembl ].
VAR_052060

Experimental info

Sequence conflict12 – 132EM → RL in AF092038. Ref.3
Sequence conflict291D → T in AAH40043. Ref.4
Sequence conflict501T → I in AAG02115. Ref.1
Sequence conflict1101V → RL in AAG02116. Ref.1
Sequence conflict1101V → RL in AAL55868. Ref.2

Secondary structure

................ 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HD15 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9B0B60BE30ADD263

FASTA23625,673
        10         20         30         40         50         60 
MTRCPAGQAE VEMAELYVKP GNKERGWNDP PQFSYGLQTQ AGGPRRSLLT KRVAAPQDGS 

        70         80         90        100        110        120 
PRVPASETSP GPPPMGPPPP SSKAPRSPPV GSGPASGVEP TSFPVESEAV MEDVLRPLEQ 

       130        140        150        160        170        180 
ALEDCRGHTR KQVCDDISRR LALLQEQWAG GKLSIPVKKR MALLVQELSS HRWDAADDIH 

       190        200        210        220        230 
RSLMVDHVTE VSQWMVGVKR LIAEKRSLFS EEAANEEKSA ATAEKNHTIP GFQQAS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of new human coding steroid receptor RNA activator isoforms."
Emberley E., Huang G.-J., Hamedani M.K., Czosnek A., Ali D., Grolla A., Lu B., Watson P.H., Murphy L.C., Leygue E.
Biochem. Biophys. Res. Commun. 301:509-515(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Mammary gland.
[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. expand/collapse author list , 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: Lymph.
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34245.1.
RefSeqNP_001030312.2. NM_001035235.3.
UniGeneHs.653135.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MGXNMR-A107-236[»]
4NBOX-ray2.81A/B106-215[»]
ProteinModelPortalQ9HD15.
SMRQ9HD15. Positions 107-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115329. 39 interactions.
IntActQ9HD15. 2 interactions.
MINTMINT-1383311.
STRING9606.ENSP00000337513.

PTM databases

PhosphoSiteQ9HD15.

Polymorphism databases

DMDM74718904.

Proteomic databases

MaxQBQ9HD15.
PaxDbQ9HD15.
PeptideAtlasQ9HD15.
PRIDEQ9HD15.

Protocols and materials databases

DNASU10011.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336283; ENSP00000337513; ENSG00000213523.
GeneID10011.
KEGGhsa:10011.
UCSCuc003lfz.3. human.

Organism-specific databases

CTD10011.
GeneCardsGC05M139911.
HGNCHGNC:11281. SRA1.
HPAHPA044598.
HPA050153.
MIM603819. gene.
neXtProtNX_Q9HD15.
PharmGKBPA36110.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44276.
HOVERGENHBG061820.
InParanoidQ9HD15.
OMAQTQTGGP.
OrthoDBEOG790G2V.
PhylomeDBQ9HD15.
TreeFamTF314789.

Gene expression databases

ArrayExpressQ9HD15.
BgeeQ9HD15.
CleanExHS_SRA1.
GenevestigatorQ9HD15.

Family and domain databases

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

Other

GeneWikiSRA1.
GenomeRNAi10011.
NextBio37823.
PROQ9HD15.
SOURCESearch...

Entry information

Entry nameSRA1_HUMAN
AccessionPrimary (citable) accession number: Q9HD15
Secondary accession number(s): Q6NVU9 expand/collapse secondary AC list , Q8IXM1, Q9HD13, Q9HD14
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM