CREM_MOUSE
ID CREM_MOUSE Reviewed; 357 AA.
AC P27699; P27698; Q5XTP8; Q5XTP9; Q5XTQ0; Q5XTQ1; Q5XTQ2; Q5XTQ3; Q99JF1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=cAMP-responsive element modulator;
DE AltName: Full=Inducible cAMP early repressor;
DE Short=ICER;
GN Name=Crem;
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 11), ALTERNATIVE PROMOTER USAGE,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=8252624; DOI=10.1016/0092-8674(93)90532-u;
RA Molina C.A., Foulkes N.S., Lalli E., Sassone-Corsi P.;
RT "Inducibility and negative autoregulation of CREM: an alternative promoter
RT directs the expression of ICER, an early response repressor.";
RL Cell 75:875-886(1993).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-357 (ISOFORMS 2; 3 AND 4).
RX PubMed=1847666; DOI=10.1016/0092-8674(91)90503-q;
RA Foulkes N.S., Borrelli E., Sassone-Corsi P.;
RT "CREM gene: use of alternative DNA-binding domains generates multiple
RT antagonists of cAMP-induced transcription.";
RL Cell 64:739-749(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-357 (ISOFORMS 5; 6; 7; 8; 9 AND 10).
RC TISSUE=Osteoblast;
RX PubMed=16059773; DOI=10.1007/s00223-005-0003-1;
RA Liu F., Huang Y.-F., Kream B.E.;
RT "Identification of novel cAMP responsive element modulator (CREM) isoforms
RT expressed by osteoblasts.";
RL Calcif. Tissue Int. 77:91-95(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-357 (ISOFORM 1).
RX PubMed=1370576; DOI=10.1038/355080a0;
RA Foulkes N.S., Mellstroem B., Benusiglio E., Sassone-Corsi P.;
RT "Developmental switch of CREM function during spermatogenesis: from
RT antagonist to activator.";
RL Nature 355:80-84(1992).
RN [6]
RP INTERACTION WITH FHL5.
RX PubMed=10086359; DOI=10.1038/18237;
RA Fimia G.M., De Cesare D., Sassone-Corsi P.;
RT "CBP-independent activation of CREM and CREB by the LIM-only protein ACT.";
RL Nature 398:165-169(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH CREB3L4.
RX PubMed=16595651; DOI=10.1074/jbc.m602051200;
RA Nagamori I., Yomogida K., Adams P.D., Sassone-Corsi P., Nojima H.;
RT "Transcription factors, cAMP-responsive element modulator (CREM) and
RT Tisp40, act in concert in postmeiotic transcriptional regulation.";
RL J. Biol. Chem. 281:15073-15081(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-287 AND SER-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [9]
RP FUNCTION (ISOFORM 11), ALTERNATIVE PROMOTER USAGE, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RX PubMed=23443664; DOI=10.1074/jbc.m112.445692;
RA Zmrzljak U.P., Korencic A., Kosir R., Golicnik M., Sassone-Corsi P.,
RA Rozman D.;
RT "Inducible cAMP early repressor regulates the Period 1 gene of the hepatic
RT and adrenal clocks.";
RL J. Biol. Chem. 288:10318-10327(2013).
RN [10]
RP INTERACTION WITH TSSK4, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-116, AND
RP MUTAGENESIS OF SER-116.
RX PubMed=26940607; DOI=10.1080/09168451.2016.1146067;
RA Fu G., Wei Y., Wang X., Yu L.;
RT "Phosphorylated testis-specific serine/threonine kinase 4 may phosphorylate
RT Crem at Ser-117.";
RL Biosci. Biotechnol. Biochem. 80:1088-1094(2016).
CC -!- FUNCTION: Transcriptional regulator that binds the cAMP response
CC element (CRE), a sequence present in many viral and cellular promoters.
CC Isoforms are either transcriptional activators or repressors. Isoform
CC 2, isoform 3 and isoform 4 are repressors, while isoform 1 is an
CC activator. Plays a role in spermatogenesis and is involved in spermatid
CC maturation. Binding of isoform 1 (activator) to CRE is increased by
CC CREB3L4. The CREM isoform 1-CREB3L4 heterodimer functions through CRE
CC and may recruit HIRA to CRE to regulate histone exchange
CC (PubMed:16595651). {ECO:0000269|PubMed:16595651}.
CC -!- FUNCTION: [Isoform 11]: Plays a role in the regulation of the circadian
CC clock: acts as a transcriptional repressor of the core circadian
CC component PER1 by directly binding to cAMP response elements in its
CC promoter. {ECO:0000269|PubMed:16595651, ECO:0000269|PubMed:23443664}.
CC -!- SUBUNIT: Binds DNA as a dimer (By similarity). Interacts with CDC34 (By
CC similarity). Interacts with FHL5 (PubMed:10086359). May interact with
CC TSSK4 (PubMed:26940607). Isoform 1 forms a heterodimer with CREB3L4
CC (PubMed:16595651). {ECO:0000250|UniProtKB:Q03060,
CC ECO:0000269|PubMed:10086359, ECO:0000269|PubMed:16595651,
CC ECO:0000269|PubMed:26940607}.
CC -!- INTERACTION:
CC P27699; O09106: Hdac1; NbExp=3; IntAct=EBI-8744406, EBI-301912;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23443664,
CC ECO:0000269|PubMed:8252624}.
CC -!- SUBCELLULAR LOCATION: [Isoform 11]: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=11;
CC Name=1; Synonyms=CREM-BCEFGgammaHIbeta, Tau;
CC IsoId=P27699-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=P27699-2; Sequence=VSP_000602, VSP_000603, VSP_000604,
CC VSP_000607;
CC Name=3; Synonyms=Beta;
CC IsoId=P27699-3; Sequence=VSP_000602, VSP_000603, VSP_000604;
CC Name=4; Synonyms=Gamma;
CC IsoId=P27699-4; Sequence=VSP_000602, VSP_000605, VSP_000606;
CC Name=5; Synonyms=Tau Alpha Gamma;
CC IsoId=P27699-5; Sequence=VSP_038016, VSP_000607;
CC Name=6; Synonyms=Tau 2 Alpha;
CC IsoId=P27699-6; Sequence=VSP_000602, VSP_000607;
CC Name=7; Synonyms=Tau 1 Alpha;
CC IsoId=P27699-7; Sequence=VSP_000603, VSP_000604, VSP_000607;
CC Name=8; Synonyms=Tau 1 Alpha Gamma;
CC IsoId=P27699-8; Sequence=VSP_000605, VSP_000606, VSP_000607;
CC Name=9; Synonyms=Tau 1 Gamma;
CC IsoId=P27699-9; Sequence=VSP_000605, VSP_000606;
CC Name=10; Synonyms=Alpha Gamma;
CC IsoId=P27699-10; Sequence=VSP_000602, VSP_000605, VSP_000606,
CC VSP_000607;
CC Name=11; Synonyms=Icer Gamma;
CC IsoId=P27699-11; Sequence=VSP_055987, VSP_000607;
CC -!- TISSUE SPECIFICITY: Expressed in the testis.
CC {ECO:0000269|PubMed:26940607}.
CC -!- DEVELOPMENTAL STAGE: In premeiotic germ cells, expressed at low amounts
CC in the antagonist form. Subsequently, during spermatogenesis, isoform 1
CC (activator) is generated exclusively and in extremely high amounts.
CC -!- INDUCTION: Isoform 11 is expressed in a circadian manner in the adrenal
CC gland with an expression peak at ZT20 (at protein level). It is induced
CC by cAMP in an immediate-early fashion and can repress its own
CC production via a negative autoregulatory mechanism.
CC {ECO:0000269|PubMed:23443664, ECO:0000269|PubMed:8252624}.
CC -!- PTM: Stimulated by phosphorylation (By similarity). Phosphorylated on
CC Ser-116 by TSSK4 in vitro. {ECO:0000250|UniProtKB:Q01147,
CC ECO:0000269|PubMed:26940607}.
CC -!- PTM: Ubiquitinated by CDC34 and RAD6B in order to be degraded by the
CC proteasome. {ECO:0000250}.
CC -!- MISCELLANEOUS: CREM-null deficient mice display male infertility: while
CC spermatogonia differentiate normally into round spermatids, all the
CC elongating spermatids are eliminated by apoptosis during
CC spermiogenesis.
CC -!- MISCELLANEOUS: [Isoform 11]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA17496.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA17497.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV28551.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV28552.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV28553.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV28554.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV28555.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV28556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ311667; CAC34846.1; -; mRNA.
DR EMBL; AC117589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M60285; AAA17495.1; ALT_INIT; mRNA.
DR EMBL; M60285; AAA17496.1; ALT_INIT; mRNA.
DR EMBL; M60285; AAA17497.1; ALT_INIT; mRNA.
DR EMBL; AY738715; AAV28551.1; ALT_INIT; mRNA.
DR EMBL; AY738716; AAV28552.1; ALT_INIT; mRNA.
DR EMBL; AY738717; AAV28553.1; ALT_INIT; mRNA.
DR EMBL; AY738718; AAV28554.1; ALT_INIT; mRNA.
DR EMBL; AY738719; AAV28555.1; ALT_INIT; mRNA.
DR EMBL; AY738721; AAV28556.1; ALT_INIT; mRNA.
DR CCDS; CCDS29031.2; -. [P27699-2]
DR CCDS; CCDS50214.1; -. [P27699-7]
DR CCDS; CCDS50215.1; -. [P27699-1]
DR CCDS; CCDS70862.1; -. [P27699-6]
DR CCDS; CCDS70863.1; -. [P27699-8]
DR CCDS; CCDS70864.1; -. [P27699-5]
DR PIR; A37944; A37944.
DR PIR; B37944; B37944.
DR PIR; C37944; C37944.
DR PIR; S20827; S20827.
DR RefSeq; NP_001104320.1; NM_001110850.2. [P27699-10]
DR RefSeq; NP_001104324.2; NM_001110854.1.
DR RefSeq; NP_001104325.2; NM_001110855.1.
DR RefSeq; NP_001104326.1; NM_001110856.2. [P27699-7]
DR RefSeq; NP_001104327.1; NM_001110857.2. [P27699-3]
DR RefSeq; NP_001104328.1; NM_001110858.2. [P27699-4]
DR RefSeq; NP_001104329.1; NM_001110859.2. [P27699-1]
DR RefSeq; NP_001258432.1; NM_001271503.1. [P27699-9]
DR RefSeq; NP_001258433.1; NM_001271504.1. [P27699-8]
DR RefSeq; NP_001258434.1; NM_001271505.1. [P27699-6]
DR RefSeq; NP_001258435.1; NM_001271506.1. [P27699-5]
DR RefSeq; NP_038526.2; NM_013498.3. [P27699-2]
DR RefSeq; XP_006525618.1; XM_006525555.3. [P27699-1]
DR RefSeq; XP_006525619.1; XM_006525556.3. [P27699-5]
DR RefSeq; XP_006525624.1; XM_006525561.3. [P27699-6]
DR RefSeq; XP_006525628.1; XM_006525565.3. [P27699-7]
DR RefSeq; XP_006525630.1; XM_006525567.3. [P27699-8]
DR RefSeq; XP_006525631.1; XM_006525568.3. [P27699-9]
DR RefSeq; XP_006525636.1; XM_006525573.3. [P27699-2]
DR RefSeq; XP_006525637.1; XM_006525574.3. [P27699-3]
DR RefSeq; XP_006525638.1; XM_006525575.3. [P27699-10]
DR RefSeq; XP_006525639.1; XM_006525576.3. [P27699-4]
DR AlphaFoldDB; P27699; -.
DR SMR; P27699; -.
DR BioGRID; 198877; 6.
DR IntAct; P27699; 3.
DR MINT; P27699; -.
DR STRING; 10090.ENSMUSP00000121233; -.
DR iPTMnet; P27699; -.
DR PhosphoSitePlus; P27699; -.
DR MaxQB; P27699; -.
DR PaxDb; P27699; -.
DR PRIDE; P27699; -.
DR ProteomicsDB; 284124; -. [P27699-1]
DR ProteomicsDB; 284125; -. [P27699-2]
DR ProteomicsDB; 284126; -. [P27699-3]
DR ProteomicsDB; 284127; -. [P27699-4]
DR ProteomicsDB; 284128; -. [P27699-5]
DR ProteomicsDB; 284129; -. [P27699-6]
DR ProteomicsDB; 284130; -. [P27699-7]
DR ProteomicsDB; 284131; -. [P27699-8]
DR ProteomicsDB; 284132; -. [P27699-9]
DR ProteomicsDB; 284133; -. [P27699-10]
DR ProteomicsDB; 284134; -. [P27699-11]
DR Antibodypedia; 4333; 434 antibodies from 36 providers.
DR DNASU; 12916; -.
DR Ensembl; ENSMUST00000025069; ENSMUSP00000025069; ENSMUSG00000063889. [P27699-5]
DR Ensembl; ENSMUST00000082141; ENSMUSP00000080780; ENSMUSG00000063889. [P27699-6]
DR Ensembl; ENSMUST00000150235; ENSMUSP00000121233; ENSMUSG00000063889. [P27699-1]
DR Ensembl; ENSMUST00000154135; ENSMUSP00000122051; ENSMUSG00000063889. [P27699-2]
DR Ensembl; ENSMUST00000154470; ENSMUSP00000118128; ENSMUSG00000063889. [P27699-8]
DR Ensembl; ENSMUST00000165086; ENSMUSP00000127353; ENSMUSG00000063889. [P27699-7]
DR GeneID; 12916; -.
DR KEGG; mmu:12916; -.
DR UCSC; uc008dxp.2; mouse. [P27699-8]
DR UCSC; uc008dxq.2; mouse. [P27699-9]
DR UCSC; uc008dxr.2; mouse. [P27699-5]
DR UCSC; uc008dxs.2; mouse. [P27699-6]
DR UCSC; uc033hfn.1; mouse. [P27699-1]
DR UCSC; uc033hfo.1; mouse. [P27699-4]
DR UCSC; uc033hfp.1; mouse. [P27699-7]
DR UCSC; uc033hfq.1; mouse. [P27699-2]
DR UCSC; uc033hfr.1; mouse. [P27699-3]
DR UCSC; uc033hfs.1; mouse. [P27699-10]
DR CTD; 1390; -.
DR MGI; MGI:88495; Crem.
DR VEuPathDB; HostDB:ENSMUSG00000063889; -.
DR eggNOG; KOG3584; Eukaryota.
DR GeneTree; ENSGT00940000156952; -.
DR InParanoid; P27699; -.
DR OrthoDB; 957343at2759; -.
DR PhylomeDB; P27699; -.
DR TreeFam; TF106464; -.
DR BioGRID-ORCS; 12916; 1 hit in 69 CRISPR screens.
DR ChiTaRS; Crem; mouse.
DR PRO; PR:P27699; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P27699; protein.
DR Bgee; ENSMUSG00000063889; Expressed in spermatid and 229 other tissues.
DR ExpressionAtlas; P27699; baseline and differential.
DR Genevisible; P27699; MM.
DR GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051591; P:response to cAMP; IDA:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR003102; Coactivator_CBP_pKID.
DR InterPro; IPR001630; Leuzip_CREB.
DR PANTHER; PTHR45879; PTHR45879; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF02173; pKID; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS50953; KID; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative promoter usage; Alternative splicing;
KW Biological rhythms; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..357
FT /note="cAMP-responsive element modulator"
FT /id="PRO_0000076608"
FT DOMAIN 101..160
FT /note="KID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00312"
FT DOMAIN 299..357
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..325
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 327..348
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26940607"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03060"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..245
FT /note="MSKCGRKKYMRTNVRQMTMETVESQQDRSVTRSVAEHSSAHMQTGQISVPTL
FT AQVSVAGSGTGRGSPAVTLVQLPSGQTVQVQGVIQTPHPSVIQSPQIQTVQVATIAETD
FT DSADSEVIDSHKRREILSRRPSYRKILNELSSDVPGIPKIEEEKSEEEGTPPNIATMAV
FT PTSIYQTSTGQYIAIAQGGTIQISNPGSDGVQGLQALTMTNSGAPPPGATIVQYAAQSA
FT DGTQQFFVPGSQVVVQ -> MAVTGDET (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:8252624"
FT /id="VSP_055987"
FT VAR_SEQ 55..103
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 6 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:16059773,
FT ECO:0000303|PubMed:1847666"
FT /id="VSP_000602"
FT VAR_SEQ 183..257
FT /note="Missing (in isoform 4, isoform 8, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:16059773,
FT ECO:0000303|PubMed:1847666"
FT /id="VSP_000605"
FT VAR_SEQ 183..245
FT /note="Missing (in isoform 2, isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16059773,
FT ECO:0000303|PubMed:1847666"
FT /id="VSP_000603"
FT VAR_SEQ 246..257
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16059773"
FT /id="VSP_038016"
FT VAR_SEQ 246
FT /note="D -> N (in isoform 2, isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16059773,
FT ECO:0000303|PubMed:1847666"
FT /id="VSP_000604"
FT VAR_SEQ 258
FT /note="A -> T (in isoform 4, isoform 8, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:16059773,
FT ECO:0000303|PubMed:1847666"
FT /id="VSP_000606"
FT VAR_SEQ 314..357
FT /note="KECRRRKKEYVKCLESRVAVLEVQNKKLIEELETLKDICSPKTD -> RECR
FT RKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKAE (in isoform 2,
FT isoform 5, isoform 6, isoform 7, isoform 8, isoform 10 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:16059773,
FT ECO:0000303|PubMed:1847666, ECO:0000303|PubMed:8252624"
FT /id="VSP_000607"
FT MUTAGEN 116
FT /note="S->M: Loss of in vitro phosphorylation by TSSK4."
FT /evidence="ECO:0000269|PubMed:26940607"
SQ SEQUENCE 357 AA; 38516 MW; 0B387B7247113088 CRC64;
MSKCGRKKYM RTNVRQMTME TVESQQDRSV TRSVAEHSSA HMQTGQISVP TLAQVSVAGS
GTGRGSPAVT LVQLPSGQTV QVQGVIQTPH PSVIQSPQIQ TVQVATIAET DDSADSEVID
SHKRREILSR RPSYRKILNE LSSDVPGIPK IEEEKSEEEG TPPNIATMAV PTSIYQTSTG
QYIAIAQGGT IQISNPGSDG VQGLQALTMT NSGAPPPGAT IVQYAAQSAD GTQQFFVPGS
QVVVQDEETD LAPSHMAAAT GDMPTYQIRA PTTALPQGVV MAASPGSLHS PQQLAEEATR
KRELRLMKNR EAAKECRRRK KEYVKCLESR VAVLEVQNKK LIEELETLKD ICSPKTD
