STIL_HUMAN
ID STIL_HUMAN Reviewed; 1287 AA.
AC Q15468; Q5T0C5; Q68CN9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=SCL-interrupting locus protein;
DE AltName: Full=TAL-1-interrupting locus protein;
GN Name=STIL; Synonyms=SIL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL REARRANGEMENT, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), AND
RP VARIANTS VAL-86 AND ARG-1012.
RX PubMed=12438740; DOI=10.1159/000064057;
RA Karkera J.D., Izraeli S., Roessler E., Dutra A., Kirsch I.R., Muenke M.;
RT "The genomic structure, chromosomal localization, and analysis of SIL as a
RT candidate gene for holoprosencephaly.";
RL Cytogenet. Genome Res. 97:62-67(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS VAL-86 AND
RP ARG-984.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=2209547; DOI=10.1002/j.1460-2075.1990.tb07535.x;
RA Brown L., Cheng J.-T., Chen Q., Siciliano M.J., Crist W., Buchanan G.,
RA Baer R.;
RT "Site-specific recombination of the tal-1 gene is a common occurrence in
RT human T cell leukemia.";
RL EMBO J. 9:3343-3351(1990).
RN [7]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=2255914; DOI=10.1126/science.2255914;
RA Aplan P.D., Lombardi D.P., Ginsberg A.M., Cossman J., Bertness V.L.,
RA Kirsch I.R.;
RT "Disruption of the human SCL locus by 'illegitimate' V-(D)-J recombinase
RT activity.";
RL Science 250:1426-1429(1990).
RN [8]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=1311214;
RA Aplan P.D., Lombardi D.P., Reaman G.H., Sather H.N., Hammond G.D.,
RA Kirsch I.R.;
RT "Involvement of the putative hematopoietic transcription factor SCL in T-
RT cell acute lymphoblastic leukemia.";
RL Blood 79:1327-1333(1992).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=9372240;
RA Izraeli S., Colaizzo-Anas T., Bertness V.L., Mani K., Aplan P.D.,
RA Kirsch I.R.;
RT "Expression of the SIL gene is correlated with growth induction and
RT cellular proliferation.";
RL Cell Growth Differ. 8:1171-1179(1997).
RN [10]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=11390401; DOI=10.1074/jbc.m103797200;
RA Raghavan S.C., Kirsch I.R., Lieber M.R.;
RT "Analysis of the V(D)J recombination efficiency at lymphoid chromosomal
RT translocation breakpoints.";
RL J. Biol. Chem. 276:29126-29133(2001).
RN [11]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=12681356; DOI=10.1016/s0145-2126(02)00260-6;
RA Curry J.D., Smith M.T.;
RT "Measurement of SIL-TAL1 fusion gene transcripts associated with human T-
RT cell lymphocytic leukemia by real-time reverse transcriptase-PCR.";
RL Leuk. Res. 27:575-582(2003).
RN [12]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=14504110; DOI=10.1182/blood-2003-05-1495;
RA Cave H., Suciu S., Preudhomme C., Poppe B., Robert A., Uyttebroeck A.,
RA Malet M., Boutard P., Benoit Y., Mauvieux L., Lutz P., Mechinaud F.,
RA Grardel N., Mazingue F., Dupont M., Margueritte G., Pages M.-P.,
RA Bertrand Y., Plouvier E., Brunie G., Bastard C., Plantaz D.,
RA Vande Velde I., Hagemeijer A., Speleman F., Lessard M., Otten J.,
RA Vilmer E., Dastugue N.;
RT "Clinical significance of HOX11L2 expression linked to t(5;14)(q35;q32), of
RT HOX11 expression, and of SIL-TAL fusion in childhood T-cell malignancies:
RT results of EORTC studies 58881 and 58951.";
RL Blood 103:442-450(2004).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=15107824; DOI=10.1038/sj.onc.1207685;
RA Erez A., Perelman M., Hewitt S.M., Cojacaru G., Goldberg I., Shahar I.,
RA Yaron P., Muler I., Campaner S., Amariglio N., Rechavi G., Kirsch I.R.,
RA Krupsky M., Kaminski N., Izraeli S.;
RT "Sil overexpression in lung cancer characterizes tumors with increased
RT mitotic activity.";
RL Oncogene 23:5371-5377(2004).
RN [14]
RP FUNCTION, 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).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-753, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP INVOLVEMENT IN MCPH7.
RX PubMed=19215732; DOI=10.1016/j.ajhg.2009.01.017;
RA Kumar A., Girimaji S.C., Duvvari M.R., Blanton S.H.;
RT "Mutations in STIL, encoding a pericentriolar and centrosomal protein,
RT cause primary microcephaly.";
RL Am. J. Hum. Genet. 84:286-290(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH CENPJ, FORMATION
RP OF A COMPLEX WITH CENPJ AND SASS6, AND UBIQUITINATION.
RX PubMed=22020124; DOI=10.1038/emboj.2011.378;
RA Tang C.J., Lin S.Y., Hsu W.B., Lin Y.N., Wu C.T., Lin Y.C., Chang C.W.,
RA Wu K.S., Tang T.K.;
RT "The human microcephaly protein STIL interacts with CPAP and is required
RT for procentriole formation.";
RL EMBO J. 30:4790-4804(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-779 AND SER-1135,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RBM14 AND CENPJ.
RX PubMed=25385835; DOI=10.15252/embj.201488979;
RA Shiratsuchi G., Takaoka K., Ashikawa T., Hamada H., Kitagawa D.;
RT "RBM14 prevents assembly of centriolar protein complexes and maintains
RT mitotic spindle integrity.";
RL EMBO J. 34:97-114(2015).
RN [22]
RP VARIANT MCPH7 TRP-798.
RX PubMed=22989186; DOI=10.1111/j.1399-0004.2012.01949.x;
RA Papari E., Bastami M., Farhadi A., Abedini S.S., Hosseini M., Bahman I.,
RA Mohseni M., Garshasbi M., Moheb L.A., Behjati F., Kahrizi K., Ropers H.H.,
RA Najmabadi H.;
RT "Investigation of primary microcephaly in Bushehr province of Iran: novel
RT STIL and ASPM mutations.";
RL Clin. Genet. 83:488-490(2013).
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 (PubMed:16024801, PubMed:9372240).
CC Plays an important role in the regulation of centriole duplication.
CC Required for the onset of procentriole formation and proper mitotic
CC progression. During procentriole formation, is essential for the
CC correct loading of SASS6 and CENPJ to the base of the procentriole to
CC initiate procentriole assembly (PubMed:22020124).
CC {ECO:0000269|PubMed:16024801, ECO:0000269|PubMed:22020124,
CC ECO:0000269|PubMed:9372240}.
CC -!- SUBUNIT: Homodimer (PubMed:22020124). Interacts with PIN1 via its WW
CC domain. This interaction is dependent on STIL mitotic phosphorylation
CC (By similarity). Interacts with CENPJ (PubMed:22020124,
CC PubMed:25385835). Interacts with RBM14 and this interaction interferes
CC with the interaction of STIL with CENPJ (PubMed:25385835). Forms a
CC complex with CENPJ and SASS6 (PubMed:22020124).
CC {ECO:0000250|UniProtKB:Q60988, ECO:0000269|PubMed:22020124,
CC ECO:0000269|PubMed:25385835}.
CC -!- INTERACTION:
CC Q15468; Q9HC77: CENPJ; NbExp=15; IntAct=EBI-7488405, EBI-946194;
CC Q15468; O00444: PLK4; NbExp=11; IntAct=EBI-7488405, EBI-746202;
CC Q15468; Q6UVJ0: SASS6; NbExp=4; IntAct=EBI-7488405, EBI-1570153;
CC Q15468; Q15468: STIL; NbExp=4; IntAct=EBI-7488405, EBI-7488405;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q60988}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:22020124,
CC ECO:0000269|PubMed:25385835}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15468-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15468-2; Sequence=VSP_022301;
CC -!- TISSUE SPECIFICITY: Expressed in all hematopoietic tissues and cell
CC lines. Highly expressed in a variety of tumors characterized by
CC increased mitotic activity with highest expression in lung cancer.
CC {ECO:0000269|PubMed:15107824, ECO:0000269|PubMed:1922059}.
CC -!- INDUCTION: Down-regulated when cell proliferation ceased. Accumulates
CC during G2 phase and falls at completion of the cell cycle.
CC {ECO:0000269|PubMed:9372240}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:22020124}.
CC -!- PTM: Phosphorylated following the activation of the mitotic checkpoint.
CC {ECO:0000269|PubMed:16024801}.
CC -!- DISEASE: Note=A chromosomal aberration involving STIL may be a cause of
CC some T-cell acute lymphoblastic leukemias (T-ALL). A deletion at 1p32
CC between STIL and TAL1 genes leads to STIL/TAL1 fusion mRNA with STIL
CC exon 1 splicing to TAL1 exon 3. As both STIL exon 1 and TAL1 exon 3 are
CC 5'-untranslated exons, STIL/TAL1 fusion mRNA predicts a full-length
CC TAL1 protein under the control of the STIL promoter, leading to
CC inappropriate TAL1 expression. In childhood T-cell malignancies (T-
CC ALL), a type of defect such as STIL/TAL1 fusion is associated with a
CC good prognosis. In cultured lymphocytes from healthy adults, STIL/TAL1
CC fusion mRNA may be detected after 7 days of culture.
CC {ECO:0000269|PubMed:11390401, ECO:0000269|PubMed:12681356,
CC ECO:0000269|PubMed:1311214, ECO:0000269|PubMed:14504110,
CC ECO:0000269|PubMed:1922059, ECO:0000269|PubMed:2209547,
CC ECO:0000269|PubMed:2255914}.
CC -!- DISEASE: Microcephaly 7, primary, autosomal recessive (MCPH7)
CC [MIM:612703]: A disease defined as a head circumference more than 3
CC standard deviations below the age-related mean. Brain weight is
CC markedly reduced and the cerebral cortex is disproportionately small.
CC Despite this marked reduction in size, the gyral pattern is relatively
CC well preserved, with no major abnormality in cortical architecture.
CC Affected individuals are mentally retarded. Primary microcephaly is
CC further defined by the absence of other syndromic features or
CC significant neurological deficits due to degenerative brain disorder.
CC {ECO:0000269|PubMed:19215732, ECO:0000269|PubMed:22989186}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SILID524ch1p32.html";
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DR EMBL; M74558; AAA60550.1; -; mRNA.
DR EMBL; AF349657; AAK51418.1; -; Genomic_DNA.
DR EMBL; AF349642; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349643; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349645; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349647; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349649; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349651; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349653; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349656; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349655; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349654; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349652; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349650; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349648; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349646; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; AF349644; AAK51418.1; JOINED; Genomic_DNA.
DR EMBL; CR749851; CAH18699.1; -; mRNA.
DR EMBL; AL513322; CAI13468.1; -; Genomic_DNA.
DR EMBL; AL135960; CAI13468.1; JOINED; Genomic_DNA.
DR EMBL; AL135960; CAI19733.1; -; Genomic_DNA.
DR EMBL; AL513322; CAI19733.1; JOINED; Genomic_DNA.
DR EMBL; BC126223; AAI26224.1; -; mRNA.
DR CCDS; CCDS41329.1; -. [Q15468-2]
DR CCDS; CCDS548.1; -. [Q15468-1]
DR PIR; A41685; A41685.
DR RefSeq; NP_001041631.1; NM_001048166.1. [Q15468-2]
DR RefSeq; NP_001269865.1; NM_001282936.1. [Q15468-1]
DR RefSeq; NP_001269866.1; NM_001282937.1.
DR RefSeq; NP_001269867.1; NM_001282938.1.
DR RefSeq; NP_001269868.1; NM_001282939.1.
DR RefSeq; NP_003026.2; NM_003035.2. [Q15468-1]
DR RefSeq; XP_006710897.1; XM_006710834.3. [Q15468-2]
DR RefSeq; XP_011540293.1; XM_011541991.2. [Q15468-2]
DR RefSeq; XP_011540294.1; XM_011541992.2. [Q15468-2]
DR PDB; 4YYP; X-ray; 2.60 A; B=720-751.
DR PDB; 5LHW; X-ray; 0.91 A; A=726-750.
DR PDB; 5LHZ; X-ray; 2.51 A; D/E/F=726-750.
DR PDBsum; 4YYP; -.
DR PDBsum; 5LHW; -.
DR PDBsum; 5LHZ; -.
DR AlphaFoldDB; Q15468; -.
DR SMR; Q15468; -.
DR BioGRID; 112382; 183.
DR ComplexPortal; CPX-1159; CPAP-STIL complex.
DR DIP; DIP-60580N; -.
DR IntAct; Q15468; 86.
DR MINT; Q15468; -.
DR STRING; 9606.ENSP00000360944; -.
DR iPTMnet; Q15468; -.
DR PhosphoSitePlus; Q15468; -.
DR BioMuta; STIL; -.
DR DMDM; 122070597; -.
DR EPD; Q15468; -.
DR jPOST; Q15468; -.
DR MassIVE; Q15468; -.
DR MaxQB; Q15468; -.
DR PaxDb; Q15468; -.
DR PeptideAtlas; Q15468; -.
DR PRIDE; Q15468; -.
DR ProteomicsDB; 60604; -. [Q15468-1]
DR ProteomicsDB; 60605; -. [Q15468-2]
DR Antibodypedia; 53510; 111 antibodies from 18 providers.
DR DNASU; 6491; -.
DR Ensembl; ENST00000360380.7; ENSP00000353544.3; ENSG00000123473.17. [Q15468-1]
DR Ensembl; ENST00000371877.8; ENSP00000360944.3; ENSG00000123473.17. [Q15468-2]
DR GeneID; 6491; -.
DR KEGG; hsa:6491; -.
DR MANE-Select; ENST00000371877.8; ENSP00000360944.3; NM_001048166.1; NP_001041631.1. [Q15468-2]
DR UCSC; uc001crd.2; human. [Q15468-1]
DR CTD; 6491; -.
DR DisGeNET; 6491; -.
DR GeneCards; STIL; -.
DR HGNC; HGNC:10879; STIL.
DR HPA; ENSG00000123473; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; STIL; -.
DR MIM; 181590; gene.
DR MIM; 612703; phenotype.
DR neXtProt; NX_Q15468; -.
DR OpenTargets; ENSG00000123473; -.
DR Orphanet; 93925; Alobar holoprosencephaly.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR Orphanet; 93924; Lobar holoprosencephaly.
DR Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR Orphanet; 220386; Semilobar holoprosencephaly.
DR Orphanet; 280195; Septopreoptic holoprosencephaly.
DR PharmGKB; PA35780; -.
DR VEuPathDB; HostDB:ENSG00000123473; -.
DR eggNOG; ENOG502QVJ5; Eukaryota.
DR GeneTree; ENSGT00390000007310; -.
DR InParanoid; Q15468; -.
DR OMA; CTVNAWG; -.
DR OrthoDB; 342602at2759; -.
DR PhylomeDB; Q15468; -.
DR TreeFam; TF331178; -.
DR PathwayCommons; Q15468; -.
DR SignaLink; Q15468; -.
DR SIGNOR; Q15468; -.
DR BioGRID-ORCS; 6491; 454 hits in 1078 CRISPR screens.
DR ChiTaRS; STIL; human.
DR GeneWiki; STIL; -.
DR GenomeRNAi; 6491; -.
DR Pharos; Q15468; Tbio.
DR PRO; PR:Q15468; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15468; protein.
DR Bgee; ENSG00000123473; Expressed in secondary oocyte and 159 other tissues.
DR ExpressionAtlas; Q15468; baseline and differential.
DR Genevisible; Q15468; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0120099; C:procentriole replication complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051298; P:centrosome duplication; IDA:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL.
DR GO; GO:0000578; P:embryonic axis specification; ISS:BHF-UCL.
DR GO; GO:0033504; P:floor plate development; ISS:BHF-UCL.
DR GO; GO:0030900; P:forebrain development; ISS:BHF-UCL.
DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; ISS:BHF-UCL.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; ISS:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
DR GO; GO:0021915; P:neural tube development; ISS:BHF-UCL.
DR GO; GO:0030903; P:notochord development; ISS:BHF-UCL.
DR GO; GO:0046601; P:positive regulation of centriole replication; IDA:ComplexPortal.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IC:ComplexPortal.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0046599; P:regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IC:ComplexPortal.
DR GO; GO:0007224; P:smoothened signaling pathway; ISS:BHF-UCL.
DR InterPro; IPR026123; Sil.
DR PANTHER; PTHR15128; PTHR15128; 1.
DR Pfam; PF15253; STIL_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Cytoplasm; Cytoskeleton; Developmental protein; Disease variant;
KW Intellectual disability; Phosphoprotein; Primary microcephaly;
KW Proto-oncogene; Reference proteome; Ubl conjugation.
FT CHAIN 1..1287
FT /note="SCL-interrupting locus protein"
FT /id="PRO_0000271332"
FT REGION 1..1018
FT /note="Interaction with RBM14"
FT /evidence="ECO:0000269|PubMed:25385835"
FT REGION 231..781
FT /note="Interaction with CENPJ"
FT /evidence="ECO:0000269|PubMed:22020124,
FT ECO:0000269|PubMed:25385835"
FT REGION 378..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..779
FT /note="PIN1-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 387..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 872
FT /note="N -> NS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_022301"
FT VARIANT 86
FT /note="A -> V (in dbSNP:rs3125630)"
FT /evidence="ECO:0000269|PubMed:12438740,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_029870"
FT VARIANT 798
FT /note="L -> W (in MCPH7; dbSNP:rs398122976)"
FT /evidence="ECO:0000269|PubMed:22989186"
FT /id="VAR_072404"
FT VARIANT 984
FT /note="H -> R (in dbSNP:rs13376679)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_029871"
FT VARIANT 1012
FT /note="P -> R"
FT /evidence="ECO:0000269|PubMed:12438740"
FT /id="VAR_029872"
FT VARIANT 1145
FT /note="A -> V (in dbSNP:rs3766317)"
FT /id="VAR_051386"
FT CONFLICT 70..71
FT /note="KQ -> NE (in Ref. 1; AAA60550 and 2; AAK51418)"
FT /evidence="ECO:0000305"
FT HELIX 726..746
FT /evidence="ECO:0007829|PDB:5LHW"
SQ SEQUENCE 1287 AA; 142955 MW; 7F15BEDA8717659C CRC64;
MEPIYPFARP QMNTRFPSSR MVPFHFPPSK CALWNPTPTG DFIYLHLSYY RNPKLVVTEK
TIRLAYRHAK QNKKNSSCFL LGSLTADEDE EGVTLTVDRF DPGREVPECL EITPTASLPG
DFLIPCKVHT QELCSREMIV HSVDDFSSAL KALQCHICSK DSLDCGKLLS LRVHITSRES
LDSVEFDLHW AAVTLANNFK CTPVKPIPII PTALARNLSS NLNISQVQGT YKYGYLTMDE
TRKLLLLLES DPKVYSLPLV GIWLSGITHI YSPQVWACCL RYIFNSSVQE RVFSESGNFI
IVLYSMTHKE PEFYECFPCD GKIPDFRFQL LTSKETLHLF KNVEPPDKNP IRCELSAESQ
NAETEFFSKA SKNFSIKRSS QKLSSGKMPI HDHDSGVEDE DFSPRPIPSP HPVSQKISKI
QPSVPELSLV LDGNFIESNP LPTPLEMVNN ENPPLINHLE HLKPLQPQLY DEKHSPEVEA
GEPSLRGIPN QLNQDKPALL RHCKVRQPPA YKKGNPHTRN SIKPSSHNGP SHDIFEKLQT
VSAGNVQNEE YPIRPSTLNS RQSSLAPQSQ PHDFVFSPHN SGRPMELQIP TPPLPSYCST
NVCRCCQHHS HIQYSPLNSW QGANTVGSIQ DVQSEALQKH SLFHPSGCPA LYCNAFCSSS
SPIALRPQGD MGSCSPHSNI EPSPVARPPS HMDLCNPQPC TVCMHTPKTE SDNGMMGLSP
DAYRFLTEQD RQLRLLQAQI QRLLEAQSLM PCSPKTTAVE DTVQAGRQME LVSVEAQSSP
GLHMRKGVSI AVSTGASLFW NAAGEDQEPD SQMKQDDTKI SSEDMNFSVD INNEVTSLPG
SASSLKAVDI PSFEESNIAV EEEFNQPLSV SNSSLVVRKE PDVPVFFPSG QLAESVSMCL
QTGPTGGASN NSETSEEPKI EHVMQPLLHQ PSDNQKIYQD LLGQVNHLLN SSSKETEQPS
TKAVIISHEC TRTQNVYHTK KKTHHSRLVD KDCVLNATLK QLRSLGVKID SPTKVKKNAH
NVDHASVLAC ISPEAVISGL NCMSFANVGM SGLSPNGVDL SMEANAIALK YLNENQLSQL
SVTRSNQNNC DPFSLLHINT DRSTVGLSLI SPNNMSFATK KYMKRYGLLQ SSDNSEDEEE
PPDNADSKSE YLLNQNLRSI PEQLGGQKEP SKNDHEIINC SNCESVGTNA DTPVLRNITN
EVLQTKAKQQ LTEKPAFLVK NLKPSPAVNL RTGKAEFTQH PEKENEGDIT IFPESLQPSE
TLKQMNSMNS VGTFLDVKRL RQLPKLF
