SAS10_MOUSE
ID SAS10_MOUSE Reviewed; 469 AA.
AC Q9JI13; Q3UL95; Q8R5C6; Q9JJ12;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Something about silencing protein 10;
DE AltName: Full=Charged amino acid-rich leucine zipper 1;
DE Short=Crl-1;
DE AltName: Full=Disrupter of silencing SAS10;
DE AltName: Full=UTP3 homolog;
GN Name=Utp3; Synonyms=Crl1, Crlz1, Sas10 {ECO:0000312|EMBL:AAF91409.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF80256.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CBFB,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain {ECO:0000312|EMBL:AAF80256.2};
RX PubMed=11404095; DOI=10.1016/s0925-4773(01)00366-5;
RA Sakuma T., Li Q.-L., Jin Y., Choi L.-W., Kim E.-G., Ito K., Ito Y.,
RA Nomura S., Bae S.-C.;
RT "Cloning and expression pattern of a novel PEBP2 beta-binding protein
RT (charged amino acid rich leucine zipper-1[Crl-1]) in the mouse.";
RL Mech. Dev. 104:151-154(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF91409.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAF91409.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:AAF91409.1};
RA Frye R.A.;
RT "Human and mouse homologs of yeast SAS10 disrupter of silencing gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH22994.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH22994.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH22994.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-140, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [7]
RP CITRULLINATION AT ARG-375.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: Essential for gene silencing: has a role in the structure of
CC silenced chromatin. Plays a role in the developing brain.
CC {ECO:0000250|UniProtKB:Q12136, ECO:0000269|PubMed:11404095}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11404095}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11404095};
CC IsoId=Q9JI13-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:15489334};
CC IsoId=Q9JI13-2; Sequence=VSP_051655, VSP_051656;
CC -!- TISSUE SPECIFICITY: Detected mainly in subsets of neuronal cells of the
CC brain. In the 17.5 dpc embryo, mainly expressed in the olfactory bulb
CC and cerebral cortex. Postnatally, additionally expressed in the
CC cerebellar cortex, most strongly in the hippocampus.
CC {ECO:0000269|PubMed:11404095}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:11404095}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the SAS10 family. {ECO:0000305}.
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DR EMBL; AF155362; AAF80256.2; -; mRNA.
DR EMBL; AF271213; AAF91409.1; -; mRNA.
DR EMBL; AK010316; BAB26848.1; -; mRNA.
DR EMBL; AK145637; BAE26555.1; -; mRNA.
DR EMBL; BC022994; AAH22994.1; -; mRNA.
DR CCDS; CCDS19402.1; -. [Q9JI13-1]
DR RefSeq; NP_075541.1; NM_023054.1. [Q9JI13-1]
DR AlphaFoldDB; Q9JI13; -.
DR SMR; Q9JI13; -.
DR BioGRID; 211158; 10.
DR IntAct; Q9JI13; 2.
DR STRING; 10090.ENSMUSP00000087896; -.
DR iPTMnet; Q9JI13; -.
DR PhosphoSitePlus; Q9JI13; -.
DR EPD; Q9JI13; -.
DR MaxQB; Q9JI13; -.
DR PaxDb; Q9JI13; -.
DR PeptideAtlas; Q9JI13; -.
DR PRIDE; Q9JI13; -.
DR ProteomicsDB; 256918; -. [Q9JI13-1]
DR ProteomicsDB; 256919; -. [Q9JI13-2]
DR Antibodypedia; 24355; 127 antibodies from 23 providers.
DR DNASU; 65961; -.
DR Ensembl; ENSMUST00000090413; ENSMUSP00000087896; ENSMUSG00000070697. [Q9JI13-1]
DR GeneID; 65961; -.
DR KEGG; mmu:65961; -.
DR UCSC; uc008xzv.1; mouse. [Q9JI13-1]
DR CTD; 57050; -.
DR MGI; MGI:1919230; Utp3.
DR VEuPathDB; HostDB:ENSMUSG00000070697; -.
DR eggNOG; KOG3118; Eukaryota.
DR GeneTree; ENSGT00500000044947; -.
DR HOGENOM; CLU_025161_1_0_1; -.
DR InParanoid; Q9JI13; -.
DR OMA; EEYIRPQ; -.
DR OrthoDB; 1451774at2759; -.
DR PhylomeDB; Q9JI13; -.
DR TreeFam; TF315177; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 65961; 19 hits in 56 CRISPR screens.
DR ChiTaRS; Il27ra; mouse.
DR PRO; PR:Q9JI13; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JI13; protein.
DR Bgee; ENSMUSG00000070697; Expressed in embryonic post-anal tail and 270 other tissues.
DR Genevisible; Q9JI13; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IPI:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR InterPro; IPR018972; Sas10_C_dom.
DR PANTHER; PTHR13237; PTHR13237; 2.
DR Pfam; PF09368; Sas10; 1.
DR Pfam; PF04000; Sas10_Utp3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Citrullination;
KW Developmental protein; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..469
FT /note="Something about silencing protein 10"
FT /id="PRO_0000114327"
FT REGION 17..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..439
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQZ2"
FT MOD_RES 140
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQZ2"
FT MOD_RES 375
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQZ2"
FT VAR_SEQ 412
FT /note="T -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051655"
FT VAR_SEQ 414..469
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051656"
FT CONFLICT 10
FT /note="A -> R (in Ref. 1; AAF80256)"
FT /evidence="ECO:0000305"
FT CONFLICT 14..15
FT /note="AA -> RP (in Ref. 1; AAF80256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 53399 MW; D469094FF0AB9632 CRC64;
MVKKSRRRGA AQWAAVRAQA GLTATDENED DLGLPPSPGD SSYYQDQVDE FHEARSRAVL
AKGWNEVESG EEDGDEEEEV LPLDIDDGDD EDGESSEEEE VGEDDDGGSS VQSEAEASVD
PSLSWGQRKK LYYDTDYGSK SRGRQSQQEV EEEEREEEEE AQIIQRRLAQ ALQEDDFGVA
WVEAFAKPVP QVDEAETRVV KDLAKVSVKE KLKMLKKESP ELLELIEDLQ AKLTEVKDEL
EPLLQLVEKG VIPTGRGSEY LKTKYNLYLN YCANISFYLI LKARRVPAHG HPVIERLVTY
RNLINKLSVV DQKLSSEIRH LLTAKDGAVK KEMTPKAKLT KTKPKSVKQA AAVALTDEPD
FDGAALKYYK EMEDRQELKR KKEENSAEEQ ALEEQNAKRA ITYQIAKNRG LTPRRKKIDR
NPRVKHREKF RKAKIRRRGQ VREVRREEQR YSGELSGIRA GVKKSIKLK
