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}.
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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 Genevisible; O89090; MM.
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.
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
//
