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SP1_MOUSE
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   03-AUG-2022, entry version 189.
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   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   [8]
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   [9]
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   [10]
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 ARNTL/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       {ECO:0000250|UniProtKB:P08047, ECO:0000250|UniProtKB:Q01714,
CC       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   GlyGen; O89090; 6 sites.
DR   iPTMnet; O89090; -.
DR   PhosphoSitePlus; O89090; -.
DR   EPD; O89090; -.
DR   MaxQB; O89090; -.
DR   PaxDb; O89090; -.
DR   PeptideAtlas; O89090; -.
DR   PRIDE; O89090; -.
DR   ProteomicsDB; 261485; -. [O89090-1]
DR   ProteomicsDB; 261486; -. [O89090-2]
DR   Antibodypedia; 892; 1089 antibodies from 47 providers.
DR   DNASU; 20683; -.
DR   Ensembl; ENSMUST00000163709; ENSMUSP00000130747; ENSMUSG00000001280. [O89090-2]
DR   GeneID; 20683; -.
DR   KEGG; mmu:20683; -.
DR   UCSC; uc012aab.1; mouse. [O89090-2]
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; 1085860at2759; -.
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   BioGRID-ORCS; 20683; 24 hits in 78 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 267 other 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:0140297; F:DNA-binding transcription factor binding; ISO: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:0071837; F:HMG box domain 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:0008022; F:protein C-terminus binding; 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: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
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   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 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
 
 
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