STIL_MOUSE
ID STIL_MOUSE Reviewed; 1262 AA.
AC Q60988; Q80VK7; Q8C7U6; Q8CEL7; Q99KL4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=SCL-interrupting locus protein homolog;
GN Name=Stil; Synonyms=Sil;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=8825637; DOI=10.1006/geno.1995.1271;
RA Collazo-Garcia N., Scherer P., Aplan P.D.;
RT "Cloning and characterization of a murine SIL gene.";
RL Genomics 30:506-513(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11156618; DOI=10.1101/gr.153001;
RA Goettgens B., Gilbert J.G.R., Barton L.M., Grafham D., Rogers J.,
RA Bentley D.R., Green A.R.;
RT "Long-range comparison of human and mouse SCL loci: localized regions of
RT sensitivity to restriction endonucleases correspond precisely with peaks of
RT conserved noncoding sequences.";
RL Genome Res. 11:87-97(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1094 AND 449-1262.
RC STRAIN=C57BL/6J; TISSUE=Skin;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-957 AND 1056-1262.
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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 TISSUE SPECIFICITY.
RX PubMed=1922059; DOI=10.1128/mcb.11.11.5462-5469.1991;
RA Aplan P.D., Lombardi D.P., Kirsch I.R.;
RT "Structural characterization of SIL, a gene frequently disrupted in T-cell
RT acute lymphoblastic leukemia.";
RL Mol. Cell. Biol. 11:5462-5469(1991).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10385121; DOI=10.1038/21429;
RA Izraeli S., Lowe L.A., Bertness V.L., Good D.J., Dorward D.W., Kirsch I.R.,
RA Kuehn M.R.;
RT "The SIL gene is required for mouse embryonic axial development and left-
RT right specification.";
RL Nature 399:691-694(1999).
RN [7]
RP FUNCTION.
RX PubMed=11668681; DOI=10.1002/gene.10004;
RA Izraeli S., Lowe L.A., Bertness V.L., Campaner S., Hahn H., Kirsch I.R.,
RA Kuehn M.R.;
RT "Genetic evidence that Sil is required for the Sonic Hedgehog response
RT pathway.";
RL Genesis 31:72-77(2001).
RN [8]
RP INTERACTION WITH PIN1, REGION, MUTAGENESIS OF THR-574; SER-643; SER-656;
RP SER-664; THR-686; SER-699 AND SER-760, AND PHOSPHORYLATION.
RX PubMed=16024801; DOI=10.1128/mcb.25.15.6660-6672.2005;
RA Campaner S., Kaldis P., Izraeli S., Kirsch I.R.;
RT "Sil phosphorylation in a Pin1 binding domain affects the duration of the
RT spindle checkpoint.";
RL Mol. Cell. Biol. 25:6660-6672(2005).
CC -!- FUNCTION: Immediate-early gene. Plays an important role in embryonic
CC development as well as in cellular growth and proliferation; its long-
CC term silencing affects cell survival and cell cycle distribution as
CC well as decreases CDK1 activity correlated with reduced phosphorylation
CC of CDK1. Plays a role as a positive regulator of the sonic hedgehog
CC pathway, acting downstream of PTCH1. Plays an important role in the
CC regulation of centriole duplication. Required for the onset of
CC procentriole formation and proper mitotic progression. During
CC procentriole formation, is essential for the correct loading of SASS6
CC and CENPJ to the base of the procentriole to initiate procentriole
CC assembly (By similarity). {ECO:0000250|UniProtKB:Q15468,
CC ECO:0000269|PubMed:10385121, ECO:0000269|PubMed:11668681,
CC ECO:0000269|PubMed:8825637}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PIN1 via its WW
CC domain. This interaction is dependent on Stil mitotic phosphorylation
CC (PubMed:16024801). Interacts with CENPJ. Interacts with RBM14 and this
CC interaction interferes with the interaction of STIL with CENPJ. Forms a
CC complex with CENPJ and SASS6 (By similarity).
CC {ECO:0000250|UniProtKB:Q15468, ECO:0000269|PubMed:16024801}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q15468}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult and fetal tissues.
CC Highly expressed in hematopoietic tissues such as thymus, bone marrow
CC and spleen. {ECO:0000269|PubMed:1922059, ECO:0000269|PubMed:8825637}.
CC -!- INDUCTION: Down-regulated during cell terminal differentiation.
CC Accumulates during G2 phase and falls at completion of the cell cycle.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q15468}.
CC -!- PTM: Phosphorylated following the activation of the mitotic checkpoint.
CC {ECO:0000305|PubMed:16024801}.
CC -!- DISRUPTION PHENOTYPE: Death during embryonic development between days
CC 8.5 and 10.5. Embryos are reduced in size and display delayed
CC development. They have axial midline defects, and randomized cardiac
CC looping. The midline sonic hedgehog signaling is blocked in these mice.
CC {ECO:0000269|PubMed:10385121}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25593.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U36778; AAC52386.1; -; mRNA.
DR EMBL; AJ297131; CAC14001.1; -; Genomic_DNA.
DR EMBL; AK019471; BAC25593.1; ALT_FRAME; mRNA.
DR EMBL; AK049223; BAC33619.1; -; mRNA.
DR EMBL; BC004585; AAH04585.1; -; mRNA.
DR EMBL; BC049865; AAH49865.1; ALT_SEQ; mRNA.
DR CCDS; CCDS18485.1; -.
DR RefSeq; NP_033211.2; NM_009185.3.
DR AlphaFoldDB; Q60988; -.
DR SMR; Q60988; -.
DR BioGRID; 203250; 2.
DR ComplexPortal; CPX-1297; CPAP-STIL complex.
DR IntAct; Q60988; 1.
DR MINT; Q60988; -.
DR STRING; 10090.ENSMUSP00000030490; -.
DR iPTMnet; Q60988; -.
DR PhosphoSitePlus; Q60988; -.
DR EPD; Q60988; -.
DR MaxQB; Q60988; -.
DR PaxDb; Q60988; -.
DR PRIDE; Q60988; -.
DR ProteomicsDB; 254760; -.
DR DNASU; 20460; -.
DR GeneID; 20460; -.
DR KEGG; mmu:20460; -.
DR CTD; 6491; -.
DR MGI; MGI:107477; Stil.
DR eggNOG; ENOG502QVJ5; Eukaryota.
DR InParanoid; Q60988; -.
DR OrthoDB; 342602at2759; -.
DR PhylomeDB; Q60988; -.
DR BioGRID-ORCS; 20460; 20 hits in 77 CRISPR screens.
DR ChiTaRS; Stil; mouse.
DR PRO; PR:Q60988; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60988; protein.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0120099; C:procentriole replication complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0051298; P:centrosome duplication; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0000578; P:embryonic axis specification; IMP:MGI.
DR GO; GO:0033504; P:floor plate development; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0030903; P:notochord development; IMP:MGI.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISO:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IC:ComplexPortal.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IC:ComplexPortal.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR InterPro; IPR026123; Sil.
DR PANTHER; PTHR15128; PTHR15128; 1.
DR Pfam; PF15253; STIL_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Developmental protein; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1262
FT /note="SCL-interrupting locus protein homolog"
FT /id="PRO_0000271333"
FT REGION 1..992
FT /note="Interaction with RBM14"
FT /evidence="ECO:0000250|UniProtKB:Q15468"
FT REGION 220..762
FT /note="Interaction with CENPJ"
FT /evidence="ECO:0000250|UniProtKB:Q15468"
FT REGION 368..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..760
FT /note="PIN1-binding"
FT REGION 650..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15468"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15468"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15468"
FT MUTAGEN 574
FT /note="T->A: Abolishes mitotic phosphorylation and
FT decreases mitotic index as well as CDK1 activity; when
FT associated with A-643; A-656; A-664; A-686; A-699 and A-
FT 760."
FT /evidence="ECO:0000269|PubMed:16024801"
FT MUTAGEN 643
FT /note="S->A: Abolishes mitotic phosphorylation and
FT decreases mitotic index as well as CDK1 activity; when
FT associated with A-574; A-656; A-664; A-686; A-699 and A-
FT 760."
FT /evidence="ECO:0000269|PubMed:16024801"
FT MUTAGEN 656
FT /note="S->A: Abolishes mitotic phosphorylation and
FT decreases mitotic index as well as CDK1 activity; when
FT associated with A-574; A-643; A-664; A-686; A-699 and A-
FT 760."
FT /evidence="ECO:0000269|PubMed:16024801"
FT MUTAGEN 664
FT /note="S->A: Abolishes mitotic phosphorylation and
FT decreases mitotic index as well as CDK1 activity; when
FT associated with A-574; A-643; A-656; A-686; A-699 and A-
FT 760."
FT /evidence="ECO:0000269|PubMed:16024801"
FT MUTAGEN 686
FT /note="T->A: Abolishes mitotic phosphorylation and
FT decreases mitotic index as well as CDK1 activity; when
FT associated with A-574; A-643; A-656; A-664; A-699 and A-
FT 760."
FT /evidence="ECO:0000269|PubMed:16024801"
FT MUTAGEN 699
FT /note="S->A: Abolishes mitotic phosphorylation and
FT decreases mitotic index as well as CDK1 activity; when
FT associated with A-574; A-643; A-656; A-664; A-686 and A-
FT 760."
FT /evidence="ECO:0000269|PubMed:16024801"
FT MUTAGEN 760
FT /note="S->A: Abolishes mitotic phosphorylation and
FT decreases mitotic index as well as CDK1 activity; when
FT associated with A-574; A-643; A-656; A-664; A-686 and A-
FT 699."
FT /evidence="ECO:0000269|PubMed:16024801"
FT CONFLICT 374
FT /note="V -> L (in Ref. 3; BAC33619)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="T -> M (in Ref. 3; BAC25593/BAC33619)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="M -> V (in Ref. 3; BAC25593/BAC33619)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="R -> K (in Ref. 3; BAC25593/BAC33619)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="H -> R (in Ref. 3; BAC25593/BAC33619)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="K -> N (in Ref. 4; AAH04585)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="V -> A (in Ref. 4; AAH04585)"
FT /evidence="ECO:0000305"
FT CONFLICT 1164
FT /note="R -> C (in Ref. 4; AAH04585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1262 AA; 138757 MW; EF2678A1445F9743 CRC64;
MNTRFPSSKM VPFHFPPSKL ALWNPMPIGE CIYLHLSYYR KPKLMVTEKA IRLAYRHAKQ
NKKNVPCFLL GSLTVDEDEE GVTLTIDRFD PGREIPECLE RTPTASLPGD FLIPCRVHIQ
GLGSRDVIVH NADDFSSALK ALQYHVCSKD FLDCGKLLCL RAQITPRESL DGVDFNLQWT
AVTLANSFKC VPVKPIPIIP TALARNLSSN LNISQVQGTY KHGYITMDET RKLLLLLQSD
PKVSSLPLVG IWLAGIIHVY SPQVWACCLR YMFSSSIQER VFSESGNFII VLYSLTHKEP
EFYECLPCES RTPDLQFQLL TNKETLHLFN NVEPSGKNPI HFELSAESQD AEAEAEVLSK
ISKTLPVKRS SQKVSPGKIP INKHDTDLED EDFSPRPIPS PHPVSQKISK VQPSVPELSL
VLDNNFTESS NQSNPLEMMT VENPLLIKPS QPELCDAKHS SEATTGEPFR RGPTNQLSQD
TALRQSRGKQ SSTCKKESLQ FRNTNAKPSL SVPSPDVAEK LQAVSAGSMQ KEDYPVRPST
LDSRQPSLAP QAQPHNLVFS THNSTRPMEL QVPTPSLPSY YPTNVCSCCQ HHGHIQYSTI
NSWQGNTVGS IQDLRSESLP KHAFFHSSGC PSLCPNAIYS SSSPVSMKQG GMGAYSPHSN
GEPSPVAGPS HVDSCVPHPC AMCMHTPNTA PDNGMMGLSP DAYRFVTEQD RQLRLLQAQI
QRLLEAQSLD PGSHKTVATM EDTVKAARQM ELVSMEAQSS PGLHMRKSVS IAVSTGASLF
WNAAGDDQEP DSQPKQDDTK ISSEDMNFSV DINNEATSLP GSASSLKAVD IPSFEESNLA
VEEVNQPLPE SNSSSEQSKE PGVPVFFPNA LLAESVSMCL QTAPTEGASN STELPQGTKD
EPYRPSDNQK IYQDLLGQVN HLLSNASQET EEPPTKAVVT NHECAKTQNT HHARKKRHNS
GLVDKDCVLS ATIKQLRSLG VKIDSPTKVK KNEQKVDHAS VLACISPEAV ISGLNYMSFG
NVGMSSLSPT GVDLSMEANA IALKYLSENQ LSQLSLARSK QNNGDSSVGL LHINSDRSTV
GLSLVSPSNM SFATKKYMKR YGLLQSSDNS EDEEEPPSHA DSESDHVLNR NPACRPVQCG
HEKEPSWNAC EIAQCSDCGS ADTRTDVPVL RNITNQAVQP RATEHLNEDS AISLRNLKPN
PAMNLRTGKA EFTHHPEKEN ERDIAVFPGT LPSPETLKQM NSMDSVGTFL DVKRLRQLPK
LF
