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Serrate RNA effector molecule homolog (Arsenite-resistance protein 2)

 SRRT_MOUSE              Reviewed;         875 AA.
Q99MR6; Q3UD04; Q5D042; Q8VEE6; Q99MR4; Q99MR5; Q99MR7;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Serrate RNA effector molecule homolog;
AltName: Full=Arsenite-resistance protein 2;
Name=Srrt; Synonyms=Ars2, Asr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
A; B; C AND D).
STRAIN=129/Sv;
PubMed=11239002; DOI=10.1093/nar/29.6.1352;
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
Miller W., Koop B.F.;
"Comparative analysis of the gene-dense ACHE/TFR2 region on human
chromosome 7q22 with the orthologous region on mouse chromosome 5.";
Nucleic Acids Res. 29:1352-1365(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney, and Mammary tumor;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 477-875 (ISOFORM C).
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=18086880; DOI=10.1128/MCB.01565-07;
Wilson M.D., Wang D., Wagner R., Breyssens H., Gertsenstein M.,
Lobe C., Lu X., Nagy A., Burke R.D., Koop B.F., Howard P.L.;
"ARS2 is a conserved eukaryotic gene essential for early mammalian
development.";
Mol. Cell. Biol. 28:1503-1514(2008).
[6]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
INTERACTION WITH NCBP1 AND DROSHA, AND DISRUPTION PHENOTYPE.
PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
Dreyfuss G., Thompson C.B.;
"Ars2 links the nuclear cap-binding complex to RNA interference and
cell proliferation.";
Cell 138:328-339(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22198669; DOI=10.1038/nature10712;
Andreu-Agullo C., Maurin T., Thompson C.B., Lai E.C.;
"Ars2 maintains neural stem-cell identity through direct
transcriptional activation of Sox2.";
Nature 481:195-198(2012).
-!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC)
and the primary microRNAs (miRNAs) processing machinery during
cell proliferation. Contributes to the stability and delivery of
capped primary miRNA transcripts to the primary miRNA processing
complex containing DGCR8 and DROSHA, thereby playing a role in
RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs
(m7GpppG-capped RNA); however interaction is probably mediated via
its interaction with NCBP1/CBP80 component of the CBC complex.
Involved in cell cycle progression at S phase. Does not directly
confer arsenite resistance but rather modulates arsenic
sensitivity. Independently of its activity on miRNAs, necessary
and sufficient to promote neural stem cell self-renewal. Does so
by directly binding SOX2 promoter and positively regulating its
transcription. {ECO:0000269|PubMed:19632182,
ECO:0000269|PubMed:22198669}.
-!- SUBUNIT: Interacts with CASP8AP2 and ERBB4 (By similarity).
Interacts with NCBP1/CBP80 and DROSHA (PubMed:19632182). Interacts
with LUZP4 (By similarity). Interacts with NCBP2/CBP20 and NCBP3
(By similarity). {ECO:0000250|UniProtKB:Q9BXP5,
ECO:0000269|PubMed:19632182}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm.
Note=Predominantly nuclear. Shuttles between the nucleus and the
cytoplasm in a CRM1-dependent way.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=A;
IsoId=Q99MR6-1; Sequence=Displayed;
Name=B;
IsoId=Q99MR6-2; Sequence=VSP_000325;
Name=C;
IsoId=Q99MR6-3; Sequence=VSP_000325, VSP_000326;
Name=D;
IsoId=Q99MR6-4; Sequence=VSP_000326;
-!- TISSUE SPECIFICITY: Widely expressed, with a preference for
proliferating cells. Highly expressed in hematopoietic tissues and
reduced or absent expression in parenchymal organs like liver and
kidney. In the brain, expressed in the subventricular zone by
niche astrocytes, ependymal cells and neural stem cells. In this
cerebral context, expressed in slowly dividing cells.
{ECO:0000269|PubMed:18086880, ECO:0000269|PubMed:19632182,
ECO:0000269|PubMed:22198669}.
-!- INDUCTION: Upon cell proliferation. {ECO:0000269|PubMed:19632182}.
-!- DISRUPTION PHENOTYPE: Death around the time of implantation.
Deletion in adults leads to proliferative arrest and bone marrow
hypoplasia whereas parenchymal organs composed of nonproliferating
cells are unaffected. {ECO:0000269|PubMed:18086880,
ECO:0000269|PubMed:19632182}.
-!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH19117.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE29458.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF312033; AAK28817.1; -; Genomic_DNA.
EMBL; AF312033; AAK28818.1; -; Genomic_DNA.
EMBL; AF312033; AAK28819.1; -; Genomic_DNA.
EMBL; AF312033; AAK28820.1; -; Genomic_DNA.
EMBL; BC019117; AAH19117.1; ALT_INIT; mRNA.
EMBL; BC066831; AAH66831.1; -; mRNA.
EMBL; AK150310; BAE29458.1; ALT_INIT; mRNA.
CCDS; CCDS39331.1; -. [Q99MR6-1]
CCDS; CCDS80439.1; -. [Q99MR6-3]
CCDS; CCDS80440.1; -. [Q99MR6-4]
RefSeq; NP_001103379.1; NM_001109909.1. [Q99MR6-4]
RefSeq; NP_001103380.1; NM_001109910.1. [Q99MR6-3]
RefSeq; NP_113582.1; NM_031405.2. [Q99MR6-1]
RefSeq; XP_006504692.1; XM_006504629.1. [Q99MR6-2]
UniGene; Mm.387734; -.
ProteinModelPortal; Q99MR6; -.
SMR; Q99MR6; -.
BioGrid; 219965; 2.
IntAct; Q99MR6; 2.
MINT; MINT-1853620; -.
STRING; 10090.ENSMUSP00000043123; -.
iPTMnet; Q99MR6; -.
PhosphoSitePlus; Q99MR6; -.
SwissPalm; Q99MR6; -.
PaxDb; Q99MR6; -.
PeptideAtlas; Q99MR6; -.
PRIDE; Q99MR6; -.
Ensembl; ENSMUST00000040873; ENSMUSP00000043123; ENSMUSG00000037364. [Q99MR6-1]
Ensembl; ENSMUST00000197466; ENSMUSP00000142564; ENSMUSG00000037364. [Q99MR6-3]
Ensembl; ENSMUST00000199243; ENSMUSP00000143232; ENSMUSG00000037364. [Q99MR6-4]
GeneID; 83701; -.
KEGG; mmu:83701; -.
UCSC; uc009acb.2; mouse. [Q99MR6-1]
UCSC; uc009acc.2; mouse. [Q99MR6-3]
UCSC; uc012eew.1; mouse. [Q99MR6-4]
CTD; 51593; -.
MGI; MGI:1933527; Srrt.
eggNOG; KOG2295; Eukaryota.
eggNOG; ENOG410XR8S; LUCA.
GeneTree; ENSGT00390000005492; -.
InParanoid; Q99MR6; -.
OMA; WFAEWWR; -.
OrthoDB; EOG091G06J6; -.
PhylomeDB; Q99MR6; -.
TreeFam; TF317609; -.
Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
ChiTaRS; Srrt; mouse.
PRO; PR:Q99MR6; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000037364; -.
CleanEx; MM_ARS2; -.
ExpressionAtlas; Q99MR6; baseline and differential.
Genevisible; Q99MR6; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; IMP:CACAO.
GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR007042; Arsenite-R_2.
InterPro; IPR021933; DUF3546.
InterPro; IPR035979; RBD_domain_sf.
Pfam; PF04959; ARS2; 1.
Pfam; PF12066; DUF3546; 1.
SUPFAM; SSF54928; SSF54928; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; RNA-mediated gene silencing; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9BXP5}.
CHAIN 2 875 Serrate RNA effector molecule homolog.
/FTId=PRO_0000220966.
COMPBIAS 10 82 Arg-rich.
COMPBIAS 258 401 Glu-rich.
COMPBIAS 759 827 Pro-rich.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 8 8 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 539 539 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 543 543 Phosphothreonine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 670 670 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 678 678 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 832 832 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 839 839 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9BXP5}.
MOD_RES 849 849 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9BXP5}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9BXP5}.
VAR_SEQ 775 779 ILPPG -> S (in isoform B and isoform C).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_000325.
VAR_SEQ 809 815 Missing (in isoform C and isoform D).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_000326.
CONFLICT 567 567 E -> G (in Ref. 3; BAE29458).
{ECO:0000305}.
SEQUENCE 875 AA; 100452 MW; 9571445674452886 CRC64;
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR
NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYDMPY AGGGGGPTYG PPQPWGHPDV
HIMQHHVLPI QARLGSIAEI DLGVPPPIMK SFKEFLLSLD DSVDETEAVK RYNDYKLDFR
RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LKVFLSLMES GWFDNLLLDI
DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKT GEASKKEEAR AGPALGEGER
KANDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKEE AEKEAKKSKK RNRKQSGDDS
FDEGSVSESE SESEGGQAEE EKEEAEEALK EKEKPKEEEK EKPKDAAGLE CKPRPLHKTC
SLFMRNIAPN ISRAEIISLC KRYPGFMRVA LSEPQPERRF FRRGWVTFDR SVNIKEICWN
LQNIRLRECE LSPGVNRDLT RRVRNINGIT QHKQIVRNDI KLAAKLIHTL DDRTQLWASE
PGTPPVPTSL PSQNPILKNI TDYLIEEVSA EEEELLGSSG GPPPEEPPKE GNPAEINVER
DEKLIKVLDK LLLYLRIVHS LDYYNTCEYP NEDEMPNRCG IIHVRGPMPP NRISHGEVLE
WQKTFEEKLT PLLSVRESLS EEEAQKMGRK DPEQEVEKFV TSNTQELGKD KWLCPLSGKK
FKGPEFVRKH IFNKHAEKIE EVKKEVAFFN NFLTDAKRPA LPEIKPAQPP GPAQILPPGL
TPGLPYPHQT PQGLMPYGQP RPPILGYGAG AVRPAVPTGG PPYPHAPYGA GRGNYDAFRG
QGGYPGKPRN RMVRGDPRAI VEYRDLDAPD DVDFF


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