ID SP1_MOUSE Reviewed; 784 AA. AC O89090; O89087; Q62251; Q64167; DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 24-JAN-2024, entry version 197. DE RecName: Full=Transcription factor Sp1; DE AltName: Full=Specificity protein 1 {ECO:0000303|PubMed:27918959}; GN Name=Sp1; 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). RC TISSUE=Neuroblastoma; RX PubMed=9628590; DOI=10.1089/dna.1998.17.471; RA Yajima S., Lee S.H., Minowa T., Mouradian M.M.; RT "Sp family transcription factors regulate expression of rat D2 dopamine RT receptor gene."; RL DNA Cell Biol. 17:471-479(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=7568082; DOI=10.1073/pnas.92.20.9107; RA Persengiev S.P., Saffer J.D., Kilpatrick D.L.; RT "An alternatively spliced form of the transcription factor Sp1 containing RT only a single glutamine-rich transactivation domain."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9107-9111(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Thymus; RA Park E.J., Kim J.H., Kim C.G., Park S.D., Hong S.S.; RT "Isolation of cDNA encoding transcription factor sp1 containing two RT glutamine-rich transactivation domain."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-784. RX PubMed=1633330; DOI=10.3109/10425179209030966; RA Chestier A., Charnay P.; RT "Difference in the genomic organizations of the related transcription RT factors Sp1 and Krox-20; possible evolutionary significance."; RL DNA Seq. 2:325-327(1992). RN [5] RP INTERACTION WITH MURINE MINUTE VIRUS NS1. RX PubMed=7799962; DOI=10.1128/mcb.15.1.524; RA Krady J.K., Ward D.C.; RT "Transcriptional activation by the parvoviral nonstructural protein NS-1 is RT mediated via a direct interaction with Sp1."; RL Mol. Cell. Biol. 15:524-533(1995). RN [6] RP INTERACTION WITH MURINE MINUTE VIRUS NS1. RX PubMed=9454706; DOI=10.1006/viro.1997.8940; RA Lorson C., Pearson J., Burger L., Pintel D.J.; RT "An Sp1-binding site and TATA element are sufficient to support full RT transactivation by proximally bound NS1 protein of minute virus of mice."; RL Virology 240:326-337(1998). RN [7] RP INTERACTION WITH MSX1 AND MSX3. RX PubMed=10215616; DOI=10.1042/bj3390751; RA Shetty S., Takahashi T., Matsui H., Ayengar R., Raghow R.; RT "Transcriptional autorepression of Msx1 gene is mediated by interactions of RT Msx1 protein with a multi-protein transcriptional complex containing TATA- RT binding protein, Sp1 and cAMP-response-element-binding protein-binding RT protein (CBP/p300)."; RL Biochem. J. 339:751-758(1999). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Heart, Kidney, Liver, Lung, 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). RN [10] RP FUNCTION. RX PubMed=24030830; DOI=10.1074/jbc.m113.507038; RA Xiao J., Zhou Y., Lai H., Lei S., Chi L.H., Mo X.; RT "Transcription factor NF-Y is a functional regulator of the transcription RT of core clock gene Bmal1."; RL J. Biol. Chem. 288:31930-31936(2013). RN [11] RP FUNCTION, INTERACTION WITH RNF112, INDUCTION, AND SUBCELLULAR LOCATION. RX PubMed=27918959; DOI=10.1016/j.redox.2016.11.012; RA Chuang J.Y., Kao T.J., Lin S.H., Wu A.C., Lee P.T., Su T.P., Yeh S.H., RA Lee Y.C., Wu C.C., Chang W.C.; RT "Specificity protein 1-zinc finger protein 179 pathway is involved in the RT attenuation of oxidative stress following brain injury."; RL Redox Biol. 11:135-143(2017). CC -!- FUNCTION: Transcription factor that can activate or repress CC transcription in response to physiological and pathological stimuli. CC Binds with high affinity to GC-rich motifs and regulates the expression CC of a large number of genes involved in a variety of processes such as CC cell growth, apoptosis, differentiation and immune responses. Highly CC regulated by post-translational modifications (phosphorylations, CC sumoylation, proteolytic cleavage, glycosylation and acetylation). CC Binds also the PDGFR-alpha G-box promoter. May have a role in CC modulating the cellular response to DNA damage. Implicated in chromatin CC remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c- CC FOS promoter Plays an essential role in the regulation of FE65 gene CC expression (By similarity). Positively regulates the transcription of CC the core clock component BMAL1 (PubMed:24030830). Plays a role in CC protecting cells against oxidative stress following brain injury by CC regulating the expression of RNF112 (PubMed:27918959). CC {ECO:0000250|UniProtKB:P08047, ECO:0000250|UniProtKB:Q01714, CC ECO:0000269|PubMed:24030830, ECO:0000269|PubMed:27918959}. CC -!- SUBUNIT: Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and CC PHC2. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major CC capsid protein VP1; this interaction leads to a cooperativity between CC the 2 proteins in DNA binding. Interacts with HLTF; the interaction may CC be required for basal transcriptional activity of HLTF. Interacts CC (deacetylated form) with EP300; the interaction enhances gene CC expression. Interacts with HDAC1 and JUN. Interacts with ELF1; the CC interaction is inhibited by glycosylation of SP1. Interaction with CC NFYA; the interaction is inhibited by glycosylation of SP1. Interacts CC with SMARCA4/BRG1. Interacts with ATF7IP and TBP. Interacts with MEIS2 CC isoform 4 and PBX1 isoform PBX1a. Interacts with EGR1 (By similarity). CC Interacts with RNF112 in an oxidative stress-regulated manner CC (PubMed:27918959). Interacts with ZBTB7A; ZBTB7A prevents the binding CC to GC-rich motifs in promoters and represses the transcriptional CC activity of SP1 (By similarity). Interacts with DDX3X; this interaction CC potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription (By similarity). CC Interacts with MSX1; the interaction may inhibit MSX1 autoinactivation CC (PubMed:10215616). Interacts with MSX3 (PubMed:10215616). CC {ECO:0000250|UniProtKB:P08047, ECO:0000250|UniProtKB:Q01714, CC ECO:0000269|PubMed:10215616, ECO:0000269|PubMed:27918959}. CC -!- SUBUNIT: (Microbial infection) Interacts with murine minute virus NS1; CC this interaction allows high levels of viral P38 promoter CC transactivation by NS1. {ECO:0000269|PubMed:7799962, CC ECO:0000269|PubMed:9454706}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27918959}. Cytoplasm CC {ECO:0000250}. Note=Nuclear location is governed by CC glycosylated/phosphorylated states. Insulin promotes nuclear location, CC while glucagon favors cytoplasmic location (By similarity). CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O89090-1; Sequence=Displayed; CC Name=2; Synonyms=Sp1-S; CC IsoId=O89090-2; Sequence=VSP_007376; CC -!- INDUCTION: Up-regulated by traumatic brain injury and hydrogen peroxide CC (at protein level)(PubMed:27918959). {ECO:0000269|PubMed:27918959}. CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large CC number of yeast and animal transcription factors. CC {ECO:0000250|UniProtKB:P08047}. CC -!- PTM: Phosphorylated on multiple serine and threonine residues. CC Phosphorylation is coupled to ubiquitination, sumoylation and CC proteolytic processing. Phosphorylation on Ser-61 enhances proteolytic CC cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein CC degradation. Hyperphosphorylation on Ser-103 in response to DNA damage CC has no effect on transcriptional activity. MAPK1/MAPK3-mediated CC phosphorylation on Thr-455 and Thr-738 enhances VEGF transcription but, CC represses FGF2-triggered PDGFR-alpha transcription. Also implicated in CC the repression of RECK by ERBB2. Hyperphosphorylated on Thr-280 and CC Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the CC ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain CC by calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by PKCzeta CC is critical for TSA-activated LHR gene expression through release of CC its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 is CC stimulated by angiotensin II via the AT1 receptor inducing increased CC binding to the PDGF-D promoter. This phosphorylation is increased in CC injured artey wall. Ser-61 and Thr-682 can both be dephosphorylated by CC PP2A during cell-cycle interphase. Dephosphorylation on Ser-61 leads to CC increased chromatin association during interphase and increases the CC transcriptional activity. On insulin stimulation, sequentially CC glycosylated and phosphorylated on several C-terminal serine and CC threonine residues (By similarity). {ECO:0000250}. CC -!- PTM: Acetylated. Acetylation/deacetylation events affect CC transcriptional activity. Deacetylation leads to an increase in the CC expression the 12(s)-lipooxygenase gene though recruitment of p300 to CC the promoter (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal CC proteolytically-cleaved peptide and is triggered by phosphorylation (By CC similarity). {ECO:0000250}. CC -!- PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage CC of the N-terminal repressor domain. Sumoylation levels are attenuated CC during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By CC similarity). {ECO:0000250}. CC -!- PTM: Proteolytic cleavage in the N-terminal repressor domain is CC prevented by sumoylation. The C-terminal cleaved product is susceptible CC to degradation (By similarity). {ECO:0000250}. CC -!- PTM: O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels CC are controlled by insulin and the SP1 phosphorylation states. Insulin- CC mediated O-glycosylation locates SP1 to the nucleus, where it is CC sequentially deglycosylated and phosphorylated. O-glycosylation affects CC transcriptional activity through disrupting the interaction with a CC number of transcription factors including ELF1 and NFYA. Inhibited by CC peroxisomome proliferator receptor gamma (PPARgamma) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF062566; AAC16484.1; -; mRNA. DR EMBL; S79832; AAB35321.1; -; mRNA. DR EMBL; AF022363; AAC08527.1; -; mRNA. DR EMBL; X60136; CAA42721.1; -; Genomic_DNA. DR PIR; S30493; S30493. DR RefSeq; NP_038700.2; NM_013672.2. DR AlphaFoldDB; O89090; -. DR SMR; O89090; -. DR BioGRID; 203414; 29. DR CORUM; O89090; -. DR DIP; DIP-35276N; -. DR IntAct; O89090; 11. DR MINT; O89090; -. DR STRING; 10090.ENSMUSP00000001326; -. DR GlyCosmos; O89090; 6 sites, No reported glycans. DR GlyGen; O89090; 7 sites, 1 O-linked glycan (6 sites). DR iPTMnet; O89090; -. DR PhosphoSitePlus; O89090; -. DR EPD; O89090; -. DR MaxQB; O89090; -. DR PaxDb; 10090-ENSMUSP00000001326; -. DR PeptideAtlas; O89090; -. DR ProteomicsDB; 261485; -. [O89090-1] DR ProteomicsDB; 261486; -. [O89090-2] DR Pumba; O89090; -. DR Antibodypedia; 892; 1267 antibodies from 47 providers. DR DNASU; 20683; -. DR Ensembl; ENSMUST00000163709.8; ENSMUSP00000130747.2; ENSMUSG00000001280.14. [O89090-2] DR GeneID; 20683; -. DR KEGG; mmu:20683; -. DR UCSC; uc012aab.1; mouse. [O89090-2] DR AGR; MGI:98372; -. DR CTD; 6667; -. DR MGI; MGI:98372; Sp1. DR VEuPathDB; HostDB:ENSMUSG00000001280; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000157804; -. DR HOGENOM; CLU_019688_1_0_1; -. DR InParanoid; O89090; -. DR OrthoDB; 5396935at2759; -. DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression. DR Reactome; R-MMU-9762293; Regulation of CDH11 gene transcription. DR BioGRID-ORCS; 20683; 24 hits in 84 CRISPR screens. DR ChiTaRS; Sp1; mouse. DR PRO; PR:O89090; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; O89090; Protein. DR Bgee; ENSMUSG00000001280; Expressed in rostral migratory stream and 271 other cell types or tissues. DR ExpressionAtlas; O89090; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000791; C:euchromatin; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI. DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI. DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI. DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI. DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; 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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI. DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI. DR GO; GO:0060216; P:definitive hemopoiesis; IGI:MGI. DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IGI:MGI. DR GO; GO:0001892; P:embryonic placenta development; IGI:MGI. DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IGI:MGI. DR GO; GO:0048706; P:embryonic skeletal system development; IGI:MGI. DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IGI:MGI. DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI. DR GO; GO:0001889; P:liver development; IGI:MGI. DR GO; GO:0030324; P:lung development; IGI:MGI. DR GO; GO:0030219; P:megakaryocyte differentiation; IGI:MGI. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IGI:MGI. DR GO; GO:0001503; P:ossification; IGI:MGI. DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI. DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI. DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:1904828; P:positive regulation of hydrogen sulfide biosynthetic process; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0033194; P:response to hydroperoxide; IDA:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0001829; P:trophectodermal cell differentiation; IGI:MGI. DR CDD; cd22539; SP1_N; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR23235:SF16; TRANSCRIPTION FACTOR SP1; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00355; ZnF_C2H2; 3. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. DR Genevisible; O89090; MM. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Biological rhythms; KW Cytoplasm; DNA-binding; Glycoprotein; Host-virus interaction; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:17242355" FT CHAIN 2..784 FT /note="Transcription factor Sp1" FT /id="PRO_0000047138" FT ZN_FING 627..656 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 657..686 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 687..714 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..84 FT /note="Repressor domain" FT /evidence="ECO:0000250" FT REGION 111..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 148..253 FT /note="Transactivation domain A (Gln-rich)" FT /evidence="ECO:0000250" FT REGION 263..497 FT /note="Transactivation domain B (Gln-rich)" FT /evidence="ECO:0000250" FT REGION 282..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 333..398 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 498..611 FT /note="Transactivation domain C (highly charged)" FT /evidence="ECO:0000250" FT REGION 566..598 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 620..784 FT /note="VZV IE62-binding" FT /evidence="ECO:0000250" FT REGION 709..784 FT /note="Domain D" FT /evidence="ECO:0000250" FT MOTIF 464..472 FT /note="9aaTAD" FT /evidence="ECO:0000250|UniProtKB:P08047" FT COMPBIAS 1..16 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 30..65 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..95 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 65..66 FT /note="Cleavage" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 103 FT /note="Phosphoserine; by ATM" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 280 FT /note="Phosphothreonine; by MAPK8" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 455 FT /note="Phosphothreonine; by MAPK1 and MAPK3" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 613 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 641 FT /note="Phosphothreonine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 642 FT /note="Phosphoserine; by PKC/PRKCZ; alternate" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 652 FT /note="Phosphothreonine; by PKC/PRKCZ" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 669 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 671 FT /note="Phosphoserine; by PKC/PRKCZ" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 682 FT /note="Phosphothreonine; by PKC/PRKCZ" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 699 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 703 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 704 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P08047" FT MOD_RES 738 FT /note="Phosphothreonine; by MAPK1, MAPK3 and MAPK8" FT /evidence="ECO:0000250|UniProtKB:P08047" FT CARBOHYD 493 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 613 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CARBOHYD 641 FT /note="O-linked (GlcNAc) threonine; alternate" FT /evidence="ECO:0000250" FT CARBOHYD 642 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CARBOHYD 699 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CARBOHYD 703 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CROSSLNK 16 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 16 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08047" FT VAR_SEQ 56..372 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7568082" FT /id="VSP_007376" FT CONFLICT 100 FT /note="T -> A (in Ref. 1; AAC16484)" FT /evidence="ECO:0000305" FT CONFLICT 131..133 FT /note="Missing (in Ref. 1; AAC16484)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="R -> E (in Ref. 3; AAC08527)" FT /evidence="ECO:0000305" FT CONFLICT 462 FT /note="G -> V (in Ref. 1; AAC16484)" FT /evidence="ECO:0000305" SQ SEQUENCE 784 AA; 80732 MW; B6B989F0A252CEE5 CRC64; MSDQDHSMDE VTAVVKIEKD VGGNNGGSGN GGGAAFSQTR SSSTGSSSSS GGGGGQESQP SPLALLAATC SRIESPNENS NNSQGPSQSG GTGELDLTAT QLSQGANGWQ IISSSSGATP TSKEQSGNST NGSNGSESSK NRTVSGGQYV VAATPNLQNQ QVLTGLPGVM PNIQYQVIPQ FQTVDGQQLQ FAATGAQVQQ DGSGQIQIIP GANQQIIPNR GSGGNIIAAM PNLLQQAVPL QGLANNVLSG QTQYVTNVPV ALNGNITLLP VNSVSAATLT PSSQAGTISS SGSQESSSQP VTSGTAISSA SLVSSQASSS SFFTNANSYS TTTTTSNMGI MNFTSSGSSG TSSQGQTPQR VGGLQGSDSL NIQQNQTSGG SLQGSQQKEG EQSQQTQQQQ ILIQPQLVQG GQALQALQAA PLSGQTFTTQ AISQETLQNL QLQAVQNSGP IIIRTPTVGP NGQVSWQTLQ LQNLQVQNPQ AQTITLAPMQ GVSLGQTSSS NTTLTPIASA ASIPAGTVTV NAAQLSSMPG LQTINLSALG TSGIQVHQLP GLPLAIANTP GDHGTQLGLH GSGGDGIHDE TAGGEGENSS DLQPQAGRRT RREACTCPYC KDSEGRASGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW HTGERPFMCN WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD HLSKHIKTHQ NKKGGPGVAL SVGTLPLDSG AGSEGTATPS ALITTNMVAM EAICPEGIAR LANSGINVMQ VTELQSINIS GNGF //