ICE2_MOUSE
ID ICE2_MOUSE Reviewed; 988 AA.
AC Q3UZ18; B0V2P1; Q66JS8; Q7TNL8; Q8BQZ1; Q8VEI2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Little elongation complex subunit 2;
DE AltName: Full=Interactor of little elongator complex ELL subunit 2;
DE AltName: Full=NMDA receptor-regulated protein 2;
GN Name=Ice2; Synonyms=Narg2;
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=15606750; DOI=10.1111/j.1432-1033.2004.04414.x;
RA Sugiura N., Dadashev V., Corriveau R.A.;
RT "NARG2 encodes a novel nuclear protein with (S/T)PXX motifs that is
RT expressed during development.";
RL Eur. J. Biochem. 271:4629-4637(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Thymus;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, Head, and Mammary tumor;
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 IDENTIFICATION, INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11297529; DOI=10.1074/jbc.m100011200;
RA Sugiura N., Patel R.G., Corriveau R.A.;
RT "N-methyl-D-aspartate receptors regulate a group of transiently expressed
RT genes in the developing brain.";
RL J. Biol. Chem. 276:14257-14263(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587 AND THR-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587 AND THR-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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. {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 with ICE1 (via C-terminus domain). Interacts with ELL (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15606750}.
CC Note=Colocalizes with COIL in subnuclear Cajal and histone locus
CC bodies. Translocates in the LEC complex to Cajal and histone locus
CC bodies at snRNA genes in a ICE1-dependent manner. Associates to
CC transcriptionally active chromatin at snRNA genes (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UZ18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UZ18-2; Sequence=VSP_027442, VSP_027443;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, liver and testis.
CC {ECO:0000269|PubMed:11297529}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain from 13 dpc to P0, and down-
CC regulated after birth. {ECO:0000269|PubMed:11297529}.
CC -!- INDUCTION: Down-regulated during neuronal differentiation, probably by
CC NMDA receptor. {ECO:0000269|PubMed:11297529,
CC ECO:0000269|PubMed:15606750}.
CC -!- SIMILARITY: Belongs to the ICE2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18458.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH80786.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY244558; AAP56233.1; -; mRNA.
DR EMBL; AK046121; BAC32608.1; -; mRNA.
DR EMBL; AK041772; BAE20602.1; -; mRNA.
DR EMBL; AK134186; BAE22043.1; -; mRNA.
DR EMBL; CT009708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018458; AAH18458.1; ALT_INIT; mRNA.
DR EMBL; BC068183; AAH68183.1; -; mRNA.
DR EMBL; BC080786; AAH80786.1; ALT_FRAME; mRNA.
DR CCDS; CCDS23315.1; -. [Q3UZ18-1]
DR RefSeq; NP_663593.2; NM_145618.3. [Q3UZ18-1]
DR RefSeq; XP_006511636.1; XM_006511573.3. [Q3UZ18-1]
DR AlphaFoldDB; Q3UZ18; -.
DR BioGRID; 220246; 7.
DR STRING; 10090.ENSMUSP00000034761; -.
DR iPTMnet; Q3UZ18; -.
DR PhosphoSitePlus; Q3UZ18; -.
DR EPD; Q3UZ18; -.
DR MaxQB; Q3UZ18; -.
DR PaxDb; Q3UZ18; -.
DR PeptideAtlas; Q3UZ18; -.
DR PRIDE; Q3UZ18; -.
DR ProteomicsDB; 267087; -. [Q3UZ18-1]
DR ProteomicsDB; 267088; -. [Q3UZ18-2]
DR Antibodypedia; 25471; 125 antibodies from 20 providers.
DR DNASU; 93697; -.
DR Ensembl; ENSMUST00000034761; ENSMUSP00000034761; ENSMUSG00000032235. [Q3UZ18-1]
DR Ensembl; ENSMUST00000117246; ENSMUSP00000112700; ENSMUSG00000032235. [Q3UZ18-2]
DR GeneID; 93697; -.
DR KEGG; mmu:93697; -.
DR UCSC; uc009qnd.1; mouse. [Q3UZ18-2]
DR UCSC; uc009qne.1; mouse. [Q3UZ18-1]
DR CTD; 79664; -.
DR MGI; MGI:2135947; Ice2.
DR VEuPathDB; HostDB:ENSMUSG00000032235; -.
DR eggNOG; ENOG502QUWA; Eukaryota.
DR GeneTree; ENSGT00390000006883; -.
DR HOGENOM; CLU_327237_0_0_1; -.
DR InParanoid; Q3UZ18; -.
DR OMA; FHEIPMD; -.
DR OrthoDB; 518363at2759; -.
DR PhylomeDB; Q3UZ18; -.
DR TreeFam; TF106272; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 93697; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ice2; mouse.
DR PRO; PR:Q3UZ18; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UZ18; protein.
DR Bgee; ENSMUSG00000032235; Expressed in animal zygote and 246 other tissues.
DR ExpressionAtlas; Q3UZ18; baseline and differential.
DR Genevisible; Q3UZ18; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0035363; C:histone locus body; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; ISS:UniProtKB.
DR InterPro; IPR019535; ICE2_C.
DR Pfam; PF10505; NARG2_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..988
FT /note="Little elongation complex subunit 2"
FT /id="PRO_0000297965"
FT REGION 402..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q659A1"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 133..141
FT /note="DMKKHVNEE -> VCVYSVHQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027442"
FT VAR_SEQ 142..988
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027443"
FT CONFLICT 66
FT /note="P -> T (in Ref. 2; BAE22043)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="I -> V (in Ref. 4; AAH18458)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="A -> T (in Ref. 4; AAH18458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 109879 MW; 3C0A0999B564D713 CRC64;
MSSSITMSEP RLNWDVTPKN GLKAFFSPEN YKDHSMAPSL KELYILSNRR IGENLSVSAS
SVENEPAVSS ATQAKEKVGM ILLPKPRVPY PRFSRFSQRE QRTYVDLLAK YAKLPSSSKT
VGTNTNEYLQ YLDMKKHVNE EVNEFLKFLQ NSAKKCAQDY NMLSDEARLF TEQLLRACIE
QVKKYPEFYT LHEVTSLMGF FPFKTEMGLK LEKTLLVLGS AKFVKTAFPS MPVKLQLSKE
DMSSIETPQQ KAEVMHCDIS KDPNAEKLVS RYHPQIALTS QALFTLLNNH GPSYKEQWEI
PVCVEMIAVE GSKPVKVIYI NSPLPRKQMT MRERNQIFHE VPLKHIISKN TSVPVSAVFM
DKPEEYTSEV DMPTEAGECR KIETLENLDM DFDGDVTELE TFGVTTTSPP RSPSSESDSS
APLMTDVHAV PKIAAVPLAP ATPVAPTMPV APATPVTPTM PMAPATPEAS ATPNITDDSR
SLCQILMKQL QKEKQLFSGV EGGPEGCKNK DDQGLEPCGE EVPSANAKSL TQDNEVHRTE
GISKESDVGV LCTNDERQGG QGNANNPNNT ATASEAAESE KGIPCGSDTD EDCLIIDTES
RSCDGKTADL GSRPNSSAQA SAGNQATTTV SEESCVLKKP IKRVYKKFDP VGEILKMQDE
LLKPVSRKVP ELPLTNSEES KQPPASEQPS AALDAAPWPK SSWPSAFQKP KGRLPYELQD
YVEDTSEYIA PQEGNFVYKL FSLQDLLLLV RCSIQRVETR PRSKKRKKIR RQFPVYVLPK
VEYQGCYGVE ALTESELCRF WTESLLHSNC SFYVGHIDAF TSKLFMLEEI ASEELKEKLA
ALKISSLFNI LQHILKKLCS LQEGSYLLSH AAEDSSLLIY KTSDGKVTRT AYNLHKAHCD
LPGVPSSLSV PWVPLDPSYL LPYHIHHGRV PCTFPPKPLR PAAQAKVGGT RMPTRNHRNP
VSMETKSSCL PVQQVENEGV ARNKRKIM
