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Steroid receptor RNA activator 1 (Steroid receptor RNA activator protein) (SRAP)

 SRA1_HUMAN              Reviewed;         236 AA.
Q9HD15; Q6NVU9; Q8IXM1; Q9HD13; Q9HD14;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 121.
RecName: Full=Steroid receptor RNA activator 1;
AltName: Full=Steroid receptor RNA activator protein;
Short=SRAP;
Name=SRA1 {ECO:0000312|HGNC:HGNC:11281}; ORFNames=PP7684;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG02114.1}
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Mammary gland {ECO:0000312|EMBL:AAG02114.1};
PubMed=12565891; DOI=10.1016/S0006-291X(02)03070-X;
Emberley E., Huang G.-J., Hamedani M.K., Czosnek A., Ali D.,
Grolla A., Lu B., Watson P.H., Murphy L.C., Leygue E.;
"Identification of new human coding steroid receptor RNA activator
isoforms.";
Biochem. Biophys. Res. Commun. 301:509-515(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15498874; DOI=10.1073/pnas.0404089101;
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.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 12-236, FUNCTION, IDENTIFICATION IN A
RIBONUCLEOPROTEIN COMPLEX WITH NCOA1, AND TISSUE SPECIFICITY.
PubMed=10199399; DOI=10.1016/S0092-8674(00)80711-4;
Lanz R.B., McKenna N.J., Onate S.A., Albrecht U., Wong J., Tsai S.Y.,
Tsai M.-J., O'Malley B.W.;
"A steroid receptor coactivator, SRA, functions as an RNA and is
present in an SRC-1 complex.";
Cell 97:17-27(1999).
[4] {ECO:0000305, ECO:0000312|EMBL:AAH40043.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-236.
TISSUE=Lymph {ECO:0000312|EMBL:AAH40043.2};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305}
FUNCTION.
PubMed=12943696; DOI=10.1016/S0960-0760(03)00225-5;
Deblois G., Giguere V.;
"Ligand-independent coactivation of ERalpha AF-1 by steroid receptor
RNA activator (SRA) via MAPK activation.";
J. Steroid Biochem. Mol. Biol. 85:123-131(2003).
[6] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14517287; DOI=10.1128/MCB.23.20.7163-7176.2003;
Lanz R.B., Chua S.S., Barron N., Soder B.M., DeMayo F., O'Malley B.W.;
"Steroid receptor RNA activator stimulates proliferation as well as
apoptosis in vivo.";
Mol. Cell. Biol. 23:7163-7176(2003).
[7] {ECO:0000305}
FUNCTION.
PubMed=15351741; DOI=10.1016/j.bbrc.2004.08.090;
Coleman K.M., Lam V., Jaber B.M., Lanz R.B., Smith C.L.;
"SRA coactivation of estrogen receptor-alpha is phosphorylation-
independent, and enhances 4-hydroxytamoxifen agonist activity.";
Biochem. Biophys. Res. Commun. 323:332-338(2004).
[8] {ECO:0000305}
FUNCTION.
PubMed=15147866; DOI=10.1016/j.febslet.2004.03.104;
Chooniedass-Kothari S., Emberley E., Hamedani M.K., Troup S., Wang X.,
Czosnek A., Hube F., Mutawe M., Watson P.H., Leygue E.;
"The steroid receptor RNA activator is the first functional RNA
encoding a protein.";
FEBS Lett. 566:43-47(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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.
{ECO:0000269|PubMed:10199399, ECO:0000269|PubMed:12943696,
ECO:0000269|PubMed:14517287, ECO:0000269|PubMed:15147866,
ECO:0000269|PubMed:15351741}.
-!- SUBUNIT: 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. {ECO:0000250|UniProtKB:Q6QGW5,
ECO:0000250|UniProtKB:Q80VJ2, ECO:0000269|PubMed:10199399}.
-!- INTERACTION:
Q92769:HDAC2; NbExp=2; IntAct=EBI-727136, EBI-301821;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12565891}.
Cytoplasm {ECO:0000269|PubMed:12565891}.
-!- 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.
{ECO:0000269|PubMed:10199399, ECO:0000269|PubMed:12565891,
ECO:0000269|PubMed:14517287}.
-!- MISCELLANEOUS: Appears to be the first example of a new class of
functional RNAs also able to encode a protein.
{ECO:0000269|PubMed:12565891, ECO:0000269|PubMed:15147866}.
-!- SIMILARITY: Belongs to the SRA1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH40043.2; Type=Frameshift; Positions=29; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF293024; AAG02114.1; -; mRNA.
EMBL; AF293025; AAG02115.1; -; mRNA.
EMBL; AF293026; AAG02116.1; -; mRNA.
EMBL; AF318361; AAL55868.1; -; mRNA.
EMBL; AF092038; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC040043; AAH40043.2; ALT_FRAME; mRNA.
CCDS; CCDS34245.1; -.
RefSeq; NP_001030312.2; NM_001035235.3.
UniGene; Hs.653135; -.
PDB; 2MGX; NMR; -; A=107-236.
PDB; 4NBO; X-ray; 2.81 A; A/B=106-215.
PDBsum; 2MGX; -.
PDBsum; 4NBO; -.
ProteinModelPortal; Q9HD15; -.
SMR; Q9HD15; -.
BioGrid; 115329; 41.
CORUM; Q9HD15; -.
IntAct; Q9HD15; 11.
MINT; Q9HD15; -.
STRING; 9606.ENSP00000337513; -.
iPTMnet; Q9HD15; -.
PhosphoSitePlus; Q9HD15; -.
BioMuta; SRA1; -.
DMDM; 74718904; -.
EPD; Q9HD15; -.
MaxQB; Q9HD15; -.
PaxDb; Q9HD15; -.
PeptideAtlas; Q9HD15; -.
PRIDE; Q9HD15; -.
DNASU; 10011; -.
Ensembl; ENST00000336283; ENSP00000337513; ENSG00000213523.
GeneID; 10011; -.
KEGG; hsa:10011; -.
UCSC; uc003lga.4; human.
CTD; 10011; -.
DisGeNET; 10011; -.
EuPathDB; HostDB:ENSG00000213523.9; -.
GeneCards; SRA1; -.
HGNC; HGNC:11281; SRA1.
HPA; HPA044598; -.
HPA; HPA050153; -.
MalaCards; SRA1; -.
MIM; 603819; gene.
neXtProt; NX_Q9HD15; -.
OpenTargets; ENSG00000213523; -.
PharmGKB; PA36110; -.
eggNOG; ENOG410IK8X; Eukaryota.
eggNOG; ENOG4112996; LUCA.
GeneTree; ENSGT00390000001803; -.
HOVERGEN; HBG061820; -.
InParanoid; Q9HD15; -.
OMA; YVKPGNQ; -.
OrthoDB; EOG091G0QXX; -.
PhylomeDB; Q9HD15; -.
TreeFam; TF314789; -.
GeneWiki; SRA1; -.
GenomeRNAi; 10011; -.
PRO; PR:Q9HD15; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000213523; -.
CleanEx; HS_SRA1; -.
ExpressionAtlas; Q9HD15; baseline and differential.
Genevisible; Q9HD15; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:2000273; P:positive regulation of signaling receptor activity; IBA:GO_Central.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR009917; SRA1-protein/COPII_Sec31.
Pfam; PF07304; SRA1; 1.
1: Evidence at protein level;
3D-structure; Activator; Apoptosis; Complete proteome; Cytoplasm;
Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Ribonucleoprotein; Transcription; Transcription regulation.
CHAIN 1 236 Steroid receptor RNA activator 1.
/FTId=PRO_0000234105.
COMPBIAS 56 104 Pro-rich. {ECO:0000255}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 32 32 Q -> E (in dbSNP:rs35610885).
/FTId=VAR_052060.
CONFLICT 12 13 EM -> RL (in Ref. 3; AF092038).
{ECO:0000305}.
CONFLICT 29 29 D -> T (in Ref. 4; AAH40043).
{ECO:0000305}.
CONFLICT 50 50 T -> I (in Ref. 1; AAG02115).
{ECO:0000305}.
CONFLICT 110 110 V -> RL (in Ref. 1; AAG02116 and 2;
AAL55868). {ECO:0000305}.
HELIX 111 124 {ECO:0000244|PDB:4NBO}.
TURN 125 128 {ECO:0000244|PDB:4NBO}.
HELIX 131 150 {ECO:0000244|PDB:4NBO}.
HELIX 155 169 {ECO:0000244|PDB:4NBO}.
HELIX 173 191 {ECO:0000244|PDB:4NBO}.
TURN 192 194 {ECO:0000244|PDB:4NBO}.
HELIX 195 209 {ECO:0000244|PDB:4NBO}.
TURN 221 223 {ECO:0000244|PDB:2MGX}.
STRAND 231 234 {ECO:0000244|PDB:2MGX}.
SEQUENCE 236 AA; 25673 MW; 9B0B60BE30ADD263 CRC64;
MTRCPAGQAE VEMAELYVKP GNKERGWNDP PQFSYGLQTQ AGGPRRSLLT KRVAAPQDGS
PRVPASETSP GPPPMGPPPP SSKAPRSPPV GSGPASGVEP TSFPVESEAV MEDVLRPLEQ
ALEDCRGHTR KQVCDDISRR LALLQEQWAG GKLSIPVKKR MALLVQELSS HRWDAADDIH
RSLMVDHVTE VSQWMVGVKR LIAEKRSLFS EEAANEEKSA ATAEKNHTIP GFQQAS


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