ICE1_MOUSE
ID ICE1_MOUSE Reviewed; 2241 AA.
AC E9Q286; Q6ZQ20;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Little elongation complex subunit 1;
DE AltName: Full=Interactor of little elongator complex ELL subunit 1;
GN Name=Ice1; Synonyms=Kiaa0947;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 510-2241.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676; SER-1582 AND THR-1607,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the little elongation complex (LEC), a complex
CC required to regulate small nuclear RNA (snRNA) gene transcription by
CC RNA polymerase II and III. Specifically acts as a scaffold protein that
CC promotes the LEC complex formation and recruitment and RNA polymerase
CC II occupancy at snRNA genes in subnuclear bodies (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the little elongation complex (LEC), at least
CC composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts
CC (via N-terminus domain) with ELL. Interacts (via C-terminus domain)
CC with ICE2 and ZC3H8 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2F5}. Nucleus,
CC Cajal body {ECO:0000250|UniProtKB:Q9Y2F5}. Note=Colocalizes with COIL
CC in subnuclear Cajal and histone locus bodies. Associates to
CC transcriptionally active chromatin at snRNA genes.
CC {ECO:0000250|UniProtKB:Q9Y2F5}.
CC -!- DOMAIN: The N-termimus domain is necessary and sufficient for its
CC targeting to subnuclear cajal and histone locus bodies. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ICE1 family. {ECO:0000305}.
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DR EMBL; AC113508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129244; BAC98054.1; -; mRNA.
DR CCDS; CCDS49309.1; -.
DR RefSeq; NP_659086.2; NM_144837.3.
DR AlphaFoldDB; E9Q286; -.
DR SMR; E9Q286; -.
DR BioGRID; 230020; 9.
DR IntAct; E9Q286; 2.
DR STRING; 10090.ENSMUSP00000036482; -.
DR iPTMnet; E9Q286; -.
DR PhosphoSitePlus; E9Q286; -.
DR EPD; E9Q286; -.
DR jPOST; E9Q286; -.
DR MaxQB; E9Q286; -.
DR PaxDb; E9Q286; -.
DR PeptideAtlas; E9Q286; -.
DR PRIDE; E9Q286; -.
DR ProteomicsDB; 269525; -.
DR Antibodypedia; 64954; 46 antibodies from 10 providers.
DR Ensembl; ENSMUST00000043493; ENSMUSP00000036482; ENSMUSG00000034525.
DR GeneID; 218333; -.
DR KEGG; mmu:218333; -.
DR UCSC; uc007rcx.2; mouse.
DR CTD; 23379; -.
DR MGI; MGI:2385865; Ice1.
DR VEuPathDB; HostDB:ENSMUSG00000034525; -.
DR eggNOG; ENOG502QX8H; Eukaryota.
DR GeneTree; ENSGT00950000183199; -.
DR HOGENOM; CLU_001630_0_0_1; -.
DR InParanoid; E9Q286; -.
DR OMA; DHWTIIN; -.
DR OrthoDB; 265329at2759; -.
DR TreeFam; TF330760; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 218333; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Ice1; mouse.
DR PRO; PR:E9Q286; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; E9Q286; protein.
DR Bgee; ENSMUSG00000034525; Expressed in animal zygote and 251 other tissues.
DR ExpressionAtlas; E9Q286; baseline and differential.
DR Genevisible; E9Q286; MM.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0035363; C:histone locus body; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008023; C:transcription elongation factor complex; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; ISO:MGI.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..2241
FT /note="Little elongation complex subunit 1"
FT /id="PRO_0000430423"
FT REGION 222..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..185
FT /evidence="ECO:0000255"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 803
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1189
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
FT MOD_RES 1820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2F5"
SQ SEQUENCE 2241 AA; 242254 MW; 92C55F104302D8E0 CRC64;
MMPGETHPAA PGPADLARCQ GCASLQQNLN EYVEALIALK QKIINTDNLL TEYQKKCDEL
QFARRENSTL HHQVEQMLQK ISPLQKCQEE LGSLKAELEE KKSSLKLYQD THQEYARVKE
ECLRTDAQKK KLEAKVKKLE EAAVKQTQDF KQLRNEKKIL EKEFKKTQER LDEFSKQKNE
KELRHIGTQI SSDSHGSIDK RKVKVLLKEL WLCVNTAHRL SGEGGRRIPE KPAKGSSAAR
ASEQDELLPV QGGPARAADM RSFFSKLSME MEGDFSSSES AEEELPSGAS PSTEHAFCEE
RHSEVSGQRP DDGNRTNVYD HEHFFDDDLQ AAIDFFKLPP PLLSPVPSPP PMASGSLPSS
LAPESFFGEF TDSSDSDSVP PRDSMESALE DYTAESRAYF DLLEKIKRSD QYVKKPGSLE
ATQAVNSLTP LGFVTGRTAL GEPSAAASLA QGRHWTESSE FVRDRGDSVE EAERMVEARE
VDKSVQVGKG LLKHNRKLWL EMASRGPARK KEAGAGESEI CFSSLGKRTF SELIESEGKT
LSSKALCPSQ SEFSKRTLTD GSASKSPCVT GSGRFQRRER DVRESTPQSG ICAAAAGRGH
SARLPSSSSA TSVPVSVCSN HQTPWPGCVS VGTPAEGTCT EQKSPTRTLN TFLLRSEPTA
CFPKENDPEN SLSTLSPKSK LGTSTFSDWK SRGLESFSTL KSTAKGHSLP QSVFPKPTGG
GQCKGRGPGA TLILPKSDWT SLARSQAGFT RRSSGSADST SWHRSDVLRR GSGGSPRASS
EYQQRTRLQL EKATPASQNS SLTAMHGPSG ESTIPPESNA AAALLPNQVS VITKQARPRR
VLGSSLEPWQ PHGNTLSPAV NGGKETGLMP SVSACVGDGD PIAQVPEQIA DKETPSPEVS
VSWRNPICDS PSDSLLAENF SCSTDRKLPF SSEDNIFQCA MNEHLQQKPT KSPQTTQSGA
SRLEAGELLP SGVTSGVFPA EQVPHGPHHQ ADTEAPVVAR ESHSAPQNAS APPVVPSRGP
LRARVPTVPV CPSSLSRAEE ETQGTSQSSL PGASYCYTGI RERGEEDTEV EDEAVSCSEG
EHEAEAVMGR RQQEQAEDSH RPLGDPEAGV GEAGHPSDVG DLTSALEECN LSTLLYIDKL
STSEVVMVLE SCQLGDYSSR VSASECASKG SLSEEMNTEL RQSEISRKKC GKRLWEEKLL
RASEEWAESE GDDSCGRTSC QHAQCPLEVP SDVLTKTGEE LDTNPVDCGG TDTEHALLES
THHSQAAEDL TEDALPEETS SPMPHTAELP DPSAVDGGGS SPLSSRSDPE HIQSSYEDEP
NSGECLSIGE EGLAEPGELL TLSSDSSTPP RLEQSSDCVA ETAFRYQISA VTSEVISVLI
NKDQDLVIEK GDNWTIISGV AISPGMEQVV LCDTLGDAAS SQDQGGLDDG SMEKSPEASP
SGPLPQEPPC GGDLSGAQED ISSNGQSANF DKSRLRNRPV KPSIWIRSQI YDQTLETEKV
ASDHTYYNWK LEPLGKNKPR SKISNKDQAS KLAKTLVLNR GEVHLNEVPQ PASGEGTNIK
LPRSQAQPIM AGTDRSTPTN CSPDTLSKIR QEVGPPLPPL LPPLIATPPR SSQTLSPLVP
NSGPSSRSSP AGHVSPLCEV PGPPVLSPWP EELQQASPLD PSPSPSTAAA SGRIVSSPLQ
FCAATPKHAL PVPGRLPSCA PGHAAVSGPQ QENSVKILDT MYPELSARAR TLSLLKGNMQ
LSRGSTVDGK VLPGRVSALL GLKAITSTST AFVLTGGSSG ADGSQGKSQD SGVQQDAGGK
RTLAVSMLRS AKRLRLDNKS PEPDTREVTG EGVPEDPQGG SPLAEVVPAE EEQADVPVCS
AASLLRVNPR EMAESYNIAI TRALRKIAES SFDLLPVIRS HVYVGNISKK PVMRDQEKEV
VYEFSTTNKH LGEYLLRSIL SELKIQKTSL DHSYIHALCR VYVGICRQLG DLERARLFCY
SLLKEDFPES EKLTLFIANM WREVFLSQSA ISEAMQLVAR QRARGEVLNC LRAFLSWEKN
APIDVGIVVS KLLLTIQLCP KTEFQSSEEF GEDLSANIWE YIFAIDLLCC HQRWIWTHDN
IISKELWPVM DKWIKYRKGH SNIAYTPDVI VASVLRLIGR LGQLGLKEGF PTAVKNISSV
IGMFIQHAQD EDIPWGVQLA AVYALCDLSP SNPAEISKIL EAWRTQTSNA IPSAIVHCLE
EVGSLSADGS AGCTSKGDSA P
