GSE1_MOUSE
ID GSE1_MOUSE Reviewed; 1213 AA.
AC Q3U3C9; Q3UWZ5; Q80U67; Q80XR0; Q8CCF2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Genetic suppressor element 1;
GN Name=Gse1; Synonyms=Kiaa0182;
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 MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Egg, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-1213 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 376-434.
RX PubMed=8170981; DOI=10.1073/pnas.91.9.3744;
RA Gudkov A.V., Kazarov A.R., Thimmapaya R., Axenovich S.A., Mazo I.A.,
RA Roninson I.B.;
RT "Cloning mammalian genes by expression selection of genetic suppressor
RT elements: association of kinesin with drug resistance and cell
RT immortalization.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3744-3748(1994).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-95; SER-766 AND
RP SER-1099, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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 -!- SUBUNIT: May be a component of a BHC histone deacetylase complex that
CC contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3U3C9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U3C9-2; Sequence=VSP_021823;
CC Name=3;
CC IsoId=Q3U3C9-3; Sequence=VSP_021822;
CC Name=4;
CC IsoId=Q3U3C9-4; Sequence=VSP_021824;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43094.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC28215.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK033263; BAC28215.1; ALT_FRAME; mRNA.
DR EMBL; AK136004; BAE22769.1; -; mRNA.
DR EMBL; AK154829; BAE32859.1; -; mRNA.
DR EMBL; BC043094; AAH43094.1; ALT_INIT; mRNA.
DR EMBL; AK122216; BAC65498.1; -; mRNA.
DR EMBL; L27155; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS52687.1; -. [Q3U3C9-2]
DR CCDS; CCDS52688.1; -. [Q3U3C9-1]
DR CCDS; CCDS52689.1; -. [Q3U3C9-3]
DR RefSeq; NP_001139368.1; NM_001145896.1. [Q3U3C9-1]
DR RefSeq; NP_001139369.1; NM_001145897.1. [Q3U3C9-3]
DR RefSeq; NP_941073.2; NM_198671.2. [Q3U3C9-2]
DR AlphaFoldDB; Q3U3C9; -.
DR SMR; Q3U3C9; -.
DR BioGRID; 238197; 2.
DR STRING; 10090.ENSMUSP00000034279; -.
DR iPTMnet; Q3U3C9; -.
DR PhosphoSitePlus; Q3U3C9; -.
DR EPD; Q3U3C9; -.
DR jPOST; Q3U3C9; -.
DR MaxQB; Q3U3C9; -.
DR PaxDb; Q3U3C9; -.
DR PeptideAtlas; Q3U3C9; -.
DR PRIDE; Q3U3C9; -.
DR ProteomicsDB; 271469; -. [Q3U3C9-1]
DR ProteomicsDB; 271470; -. [Q3U3C9-2]
DR ProteomicsDB; 271471; -. [Q3U3C9-3]
DR ProteomicsDB; 271472; -. [Q3U3C9-4]
DR Antibodypedia; 30633; 48 antibodies from 19 providers.
DR Ensembl; ENSMUST00000034279; ENSMUSP00000034279; ENSMUSG00000031822. [Q3U3C9-2]
DR Ensembl; ENSMUST00000118136; ENSMUSP00000112981; ENSMUSG00000031822. [Q3U3C9-1]
DR Ensembl; ENSMUST00000120493; ENSMUSP00000113577; ENSMUSG00000031822. [Q3U3C9-3]
DR GeneID; 382034; -.
DR KEGG; mmu:382034; -.
DR UCSC; uc009nqz.2; mouse. [Q3U3C9-2]
DR UCSC; uc009nra.2; mouse. [Q3U3C9-1]
DR UCSC; uc009nrc.2; mouse. [Q3U3C9-4]
DR CTD; 23199; -.
DR MGI; MGI:1098275; Gse1.
DR VEuPathDB; HostDB:ENSMUSG00000031822; -.
DR eggNOG; ENOG502QR0Q; Eukaryota.
DR GeneTree; ENSGT00700000104539; -.
DR HOGENOM; CLU_009387_0_0_1; -.
DR InParanoid; Q3U3C9; -.
DR OMA; CWSPRGC; -.
DR OrthoDB; 207938at2759; -.
DR PhylomeDB; Q3U3C9; -.
DR TreeFam; TF332496; -.
DR BioGRID-ORCS; 382034; 11 hits in 74 CRISPR screens.
DR ChiTaRS; Gse1; mouse.
DR PRO; PR:Q3U3C9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3U3C9; protein.
DR Bgee; ENSMUSG00000031822; Expressed in animal zygote and 218 other tissues.
DR ExpressionAtlas; Q3U3C9; baseline and differential.
DR Genevisible; Q3U3C9; MM.
DR InterPro; IPR022207; GSE-like.
DR InterPro; IPR042337; GSE1.
DR PANTHER; PTHR17608; PTHR17608; 1.
DR Pfam; PF12540; DUF3736; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1213
FT /note="Genetic suppressor element 1"
FT /id="PRO_0000262925"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 319..402
FT /evidence="ECO:0000255"
FT COILED 1093..1197
FT /evidence="ECO:0000255"
FT COMPBIAS 11..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 496
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 739
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 905
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14687"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..3
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021822"
FT VAR_SEQ 1..2
FT /note="MK -> MFGLKPPLYYLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021823"
FT VAR_SEQ 882..917
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_021824"
FT CONFLICT 22
FT /note="T -> A (in Ref. 1; BAE32859)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="Missing (in Ref. 1; BAE32859)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="H -> R (in Ref. 1; BAE32859)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="E -> K (in Ref. 1; BAE32859)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="R -> W (in Ref. 1; BAE32859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1213 AA; 136228 MW; CC844DBE6B2B9BA0 CRC64;
MKGMSHEPKS PSIGMLSTAT RTTATVNPLT PSPLNGALVP TGSPATSSTL SAQAAPSSSF
AAALRKLAKQ AEEPRGSSLS SESSPVSSPA TNHSSPASTP KRVPMGPIIV PPGGHSVPST
PPVVTIAPTK TVNGVWRSES RQDSGSRGSS SGRERLLVEP PLAQEKAAGP AIPSHLLSTP
YPFGLSPGSV VQDSRFQPLN LQRPVHHVVP PSTVTEDYLR SFRPYHTAED LRMSSLPPLG
LDPATAAAYY HPSYLAPHPF PHPAFRMDDS YCLSALRSPF YPIPTPGSLP PLHPSAMHLH
LSGVRYPPEL SHSSLAALHS ERMSSLSAER LQMDEELRRE RERERERERE ADREREKERE
REQREKEREK ELEREREKER ERELERQREQ RAREKELLAA KALEPTTFLP VAELHGLRGH
STEERPKPSE QLTPTRAEKL KDVGLQAPKP VQHPLHPVPA PHHTVPSLIS SHGIFSLPGS
SATTALLIQR TNEEEKWLAR QRRLRQEKED RQSQVSEFRQ QVLEQHLDLG RPLVPTEAEH
RPESTRPGTN RHEQGSREPP QHFGGPPPLI SPKPQQHTVP TALWNPVSLM DNALETRRAE
SHSLHSHPTA FEPSRQAAVP LVKVERVYCS EKAEEPRKRE ATPLDKYQPP PPPPPPREAG
SLEPQTFPHG PGPFLTELEK STQTILGQQR PSLSQATSFG ELSGPLKPGS PYCHPTARGP
DPAYIYDEFL QQRRKLVSKL DLEERRRREA QEKGYYYDLD DSYDESDEEE VRAHLRCVAE
QPPLKLDTSS EKLEFLQLFG LTTQQQKEEL VAQKRRKRRR MLRERSPSPP AVQCKRQTPS
PRLALSTRYS PDEMNNSPNF EEKRKFLTFF NLTHISAEKR KDKERLVEML RAMKQRALSA
ADSVTNSSRD SPPVSLSEPA TQPAPLETDQ PVGVPASLSD VPKTTETGRL EQLRPQELLR
VQEPAPPSGE KARLSEAPGG KKSLSMLHYL RGAAPKDIPV PLSHSINGKS KPWEPFVAEE
FAHQFHESVL QSTQKALQKH KGNSALLSAE QSHKVDTAIH YNIPELQSSS RVPLPQHNGQ
QEPPMGRKGP PMQEADQDSE EDSEEDSEEE AEEAPRRQWQ GIEAIFEAYQ EHIEEQNLER
QVLQTQCRRL EAQNYSLSLT AEQLSHSMAE LRSQKQKMVS ERERLQAELD HLRKCLALPT
MHWPRGYFKG YPR
