TTP_RAT
ID TTP_RAT Reviewed; 320 AA.
AC P47973; Q54AH1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=mRNA decay activator protein ZFP36 {ECO:0000305};
DE AltName: Full=TPA-induced sequence 11 {ECO:0000250|UniProtKB:P22893};
DE AltName: Full=Tristetraprolin {ECO:0000250|UniProtKB:P26651};
DE AltName: Full=Zinc finger protein 36 {ECO:0000312|RGD:620722};
DE Short=Zfp-36 {ECO:0000250|UniProtKB:P22893};
GN Name=Zfp36 {ECO:0000312|RGD:620722};
GN Synonyms=Tis11 {ECO:0000303|PubMed:1511903},
GN Ttp {ECO:0000250|UniProtKB:P26651};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1511903; DOI=10.1016/0378-1119(92)90202-z;
RA Kaneda N., Oshima M., Chung S.Y., Guroff G.;
RT "Sequence of a rat TIS11 cDNA, an immediate early gene induced by growth
RT factors and phorbol esters.";
RL Gene 118:289-291(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11129950; DOI=10.1023/a:1007172316657;
RA Kaneda N., Murata T., Niimi Y., Minamiyama M.;
RT "Cloning and characterization of the rat TIS11 gene.";
RL Mol. Cell. Biochem. 213:119-126(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-3 AND LEU-10, AND DOMAIN.
RX PubMed=12054509; DOI=10.1016/s0006-291x(02)00363-7;
RA Murata T., Yoshino Y., Morita N., Kaneda N.;
RT "Identification of nuclear import and export signals within the structure
RT of the zinc finger protein TIS11.";
RL Biochem. Biophys. Res. Commun. 293:1242-1247(2002).
RN [5]
RP RNA-BINDING.
RX PubMed=27193233; DOI=10.1007/s00726-016-2261-9;
RA Nowotarski S.L., Origanti S., Sass-Kuhn S., Shantz L.M.;
RT "Destabilization of the ornithine decarboxylase mRNA transcript by the RNA-
RT binding protein tristetraprolin.";
RL Amino Acids 48:2303-2311(2016).
CC -!- FUNCTION: Zinc-finger RNA-binding protein that destabilizes numerous
CC cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by
CC promoting their poly(A) tail removal or deadenylation, and hence
CC provide a mechanism for attenuating protein synthesis
CC (PubMed:27193233). Acts as an 3'-untranslated region (UTR) ARE mRNA-
CC binding adapter protein to communicate signaling events to the mRNA
CC decay machinery. Recruits deadenylase CNOT7 (and probably the CCR4-NOT
CC complex) via association with CNOT1, and hence promotes ARE-mediated
CC mRNA deadenylation. Functions also by recruiting components of the
CC cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs. Self
CC regulates by destabilizing its own mRNA (By similarity). Binds to 3'-
CC UTR ARE of numerous mRNAs (PubMed:27193233). Binds also to ARE of its
CC own mRNA. Plays a role in anti-inflammatory responses; suppresses tumor
CC necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-
CC alpha mRNA decay and several other inflammatory ARE-containing mRNAs in
CC interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages.
CC Also plays a role in the regulation of dendritic cell maturation at the
CC post-transcriptional level, and hence operates as part of a negative
CC feedback loop to limit the inflammatory response. Promotes ARE-mediated
CC mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response
CC of endothelial cells to hypoxia. Positively regulates early
CC adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of
CC immediate early genes (IEGs). Negatively regulates
CC hematopoietic/erythroid cell differentiation by promoting ARE-mediated
CC mRNA decay of the transcription factor STAT5B mRNA. Plays a role in
CC maintaining skeletal muscle satellite cell quiescence by promoting ARE-
CC mediated mRNA decay of the myogenic determination factor MYOD1 mRNA.
CC Associates also with and regulates the expression of non-ARE-containing
CC target mRNAs at the post-transcriptional level, such as MHC class I
CC mRNAs. Participates in association with argonaute RISC catalytic
CC components in the ARE-mediated mRNA decay mechanism; assists microRNA
CC (miRNA) targeting ARE-containing mRNAs. May also play a role in the
CC regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-
CC containing RNAs, in vitro. Involved in the delivery of target ARE-mRNAs
CC to processing bodies (PBs). In addition to its cytosolic mRNA-decay
CC function, affects nuclear pre-mRNA processing. Negatively regulates
CC nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation
CC activity on ARE-containing pre-mRNA during LPS-stimulated macrophages.
CC Also involved in the regulation of stress granule (SG) and P-body (PB)
CC formation and fusion. Plays a role in the regulation of keratinocyte
CC proliferation, differentiation and apoptosis. Plays a role as a tumor
CC suppressor by inhibiting cell proliferation in breast cancer cells (By
CC similarity). {ECO:0000250|UniProtKB:P22893,
CC ECO:0000250|UniProtKB:P26651, ECO:0000269|PubMed:27193233}.
CC -!- SUBUNIT: Associates with cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase
CC complexes to trigger ARE-containing mRNA deadenylation and decay
CC processes. Part of a mRNA decay activation complex at least composed of
CC poly(A)-specific exoribonucleases CNOT6, EXOSC2 and XRN1 and mRNA-
CC decapping enzymes DCP1A and DCP2. Associates with the RNA exosome
CC complex. Interacts (via phosphorylated form) with 14-3-3 proteins;
CC these interactions promote exclusion of ZFP36 from cytoplasmic stress
CC granules in response to arsenite treatment in a MAPKAPK2-dependent
CC manner and does not prevent CCR4-NOT deadenylase complex recruitment or
CC ZFP36-induced ARE-containing mRNA deadenylation and decay processes.
CC Interacts with 14-3-3 proteins; these interactions occur in response to
CC rapamycin in an Akt-dependent manner. Interacts with AGO2 and AGO4.
CC Interacts (via C-terminus) with CNOT1; this interaction occurs in a
CC RNA-independent manner and induces mRNA deadenylation. Interacts (via
CC N-terminus) with CNOT6. Interacts with CNOT6L. Interacts (via C-
CC terminus) with CNOT7; this interaction occurs in a RNA-independent
CC manner, induces mRNA deadenylation and is inhibited in a
CC phosphorylation MAPKAPK2-dependent manner. Interacts (via
CC unphosphorylated form) with CNOT8; this interaction occurs in a RNA-
CC independent manner and is inhibited in a phosphorylation MAPKAPK2-
CC dependent manner. Interacts with DCP1A. Interacts (via N-terminus) with
CC DCP2. Interacts with EDC3. Interacts (via N-terminus) with EXOSC2.
CC Interacts with heat shock 70 kDa proteins. Interacts with KHSRP; this
CC interaction increases upon cytokine-induced treatment. Interacts with
CC MAP3K4; this interaction enhances the association with SH3KBP1/CIN85.
CC Interacts with MAPKAPK2; this interaction occurs upon skeletal muscle
CC satellite cell activation. Interacts with NCL. Interacts with NUP214;
CC this interaction increases upon lipopolysaccharide (LPS) stimulation.
CC Interacts with PABPC1; this interaction occurs in a RNA-dependent
CC manner. Interacts (via hypophosphorylated form) with PABPN1 (via RRM
CC domain and C-terminal arginine-rich region); this interaction occurs in
CC the nucleus in a RNA-independent manner, decreases in presence of
CC single-stranded poly(A) RNA-oligomer and in a p38 MAPK-dependent-manner
CC and inhibits nuclear poly(A) tail synthesis. Interacts with PAN2.
CC Interacts (via C3H1-type zinc finger domains) with PKM. Interacts (via
CC C3H1-type zinc finger domains) with nuclear RNA poly(A) polymerase.
CC Interacts with PPP2CA; this interaction occurs in LPS-stimulated cells
CC and induces ZFP36 dephosphorylation, and hence may promote ARE-
CC containing mRNAs decay. Interacts (via C-terminus) with PRR5L (via C-
CC terminus); this interaction may accelerate ZFP36-mediated mRNA decay
CC during stress. Interacts (via C-terminus) with SFN; this interaction
CC occurs in a phosphorylation-dependent manner. Interacts (via extreme C-
CC terminal region) with SH3KBP1/CIN85 (via SH3 domains); this interaction
CC enhances MAP3K4-induced phosphorylation of ZFP36 at Ser-59 and Ser-86
CC and does not alter neither ZFP36 binding to ARE-containing transcripts
CC nor TNF-alpha mRNA decay. Interacts with XRN1. Interacts (via C-
CC terminus and Ser-179 phosphorylated form) with YWHAB; this interaction
CC occurs in a p38/MAPKAPK2-dependent manner, increases cytoplasmic
CC localization of ZFP36 and protects ZFP36 from Ser-179 dephosphorylation
CC by serine/threonine phosphatase 2A, and hence may be crucial for
CC stabilizing ARE-containing mRNAs. Interacts (via phosphorylated form)
CC with YWHAE. Interacts (via C-terminus) with YWHAG; this interaction
CC occurs in a phosphorylation-dependent manner. Interacts with YWHAH;
CC this interaction occurs in a phosphorylation-dependent manner.
CC Interacts with YWHAQ; this interaction occurs in a phosphorylation-
CC dependent manner. Interacts with (via C-terminus) YWHAZ; this
CC interaction occurs in a phosphorylation-dependent manner. Does not
CC interact with SH3KBP1. Interacts (via P-P-P-P-G repeats) with GIGYF2;
CC the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P22893, ECO:0000250|UniProtKB:P26651}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12054509}. Cytoplasm
CC {ECO:0000269|PubMed:12054509}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P22893}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:P22893}. Note=Shuttles between nucleus and
CC cytoplasm in a CRM1-dependent manner (PubMed:12054509). Localized
CC predominantly in the cytoplasm in a p38 MAPK- and YWHAB-dependent
CC manner. Colocalizes with SH3KBP1 and MAP3K4 in the cytoplasm. Component
CC of cytoplasmic stress granules (SGs). Localizes to cytoplasmic stress
CC granules upon energy starvation. Localizes in processing bodies (PBs).
CC Excluded from stress granules in a phosphorylation MAPKAPK2-dependent
CC manner. Shuttles in and out of both cytoplasmic P-body and SGs (By
CC similarity). {ECO:0000250|UniProtKB:P22893,
CC ECO:0000250|UniProtKB:P26651, ECO:0000269|PubMed:12054509}.
CC -!- DOMAIN: The C3H1-type zinc finger domains are necessary for ARE-binding
CC activity. {ECO:0000250|UniProtKB:P26651}.
CC -!- PTM: Phosphorylated. Phosphorylation at serine and/or threonine
CC residues occurs in a p38 MAPK- and MAPKAPK2-dependent manner.
CC Phosphorylated by MAPKAPK2 at Ser-53 and Ser-179; phosphorylation
CC increases its stability and cytoplasmic localization, promotes binding
CC to 14-3-3 adapter proteins and inhibits the recruitment of cytoplasmic
CC CCR4-NOT and PAN2-PAN3 deadenylase complexes to the mRNA decay
CC machinery, thereby inhibiting ZFP36-induced ARE-containing mRNA
CC deadenylation and decay processes. Phosphorylation by MAPKAPK2 does not
CC impair ARE-containing RNA-binding. Phosphorylated in a MAPKAPK2- and
CC p38 MAPK-dependent manner upon skeletal muscle satellite cell
CC activation; this phosphorylation inhibits ZFP36-mediated mRNA decay
CC activity, and hence stabilizes MYOD1 mRNA. Phosphorylated by MAPK1 upon
CC mitogen stimulation. Phosphorylated at Ser-59 and Ser-86; these
CC phosphorylations increase in a SH3KBP1-dependent manner. Phosphorylated
CC at serine and threonine residues in a pyruvate kinase PKM- and p38
CC MAPK-dependent manner. Phosphorylation at Ser-53 may participate in the
CC PKM-mediated degradation of ZFP36 in a p38 MAPK-dependent manner.
CC Dephosphorylated by serine/threonine phosphatase 2A at Ser-179.
CC {ECO:0000250|UniProtKB:P22893, ECO:0000250|UniProtKB:P26651}.
CC -!- PTM: Ubiquitinated; pyruvate kinase (PKM)-dependent ubiquitination
CC leads to proteasomal degradation through a p38 MAPK signaling pathway.
CC {ECO:0000250|UniProtKB:P26651}.
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DR EMBL; X63369; CAA44970.1; -; mRNA.
DR EMBL; AB025017; BAB12432.1; -; Genomic_DNA.
DR EMBL; BC060308; AAH60308.1; -; mRNA.
DR PIR; JC1255; JC1255.
DR RefSeq; NP_579824.2; NM_133290.3.
DR AlphaFoldDB; P47973; -.
DR SMR; P47973; -.
DR STRING; 10116.ENSRNOP00000026661; -.
DR PhosphoSitePlus; P47973; -.
DR PaxDb; P47973; -.
DR PRIDE; P47973; -.
DR GeneID; 79426; -.
DR KEGG; rno:79426; -.
DR UCSC; RGD:620722; rat.
DR CTD; 7538; -.
DR RGD; 620722; Zfp36.
DR eggNOG; KOG1677; Eukaryota.
DR InParanoid; P47973; -.
DR OrthoDB; 1541140at2759; -.
DR PhylomeDB; P47973; -.
DR Reactome; R-RNO-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR PRO; PR:P47973; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030014; C:CCR4-NOT complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0019957; F:C-C chemokine binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISO:RGD.
DR GO; GO:1904246; P:negative regulation of polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISS:UniProtKB.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:RGD.
DR GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; ISS:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; ISO:RGD.
DR GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
DR GO; GO:1901835; P:positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:1904582; P:positive regulation of intracellular mRNA localization; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:1902172; P:regulation of keratinocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0050779; P:RNA destabilization; ISO:RGD.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; PTHR12547; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; DNA-binding; Exosome; Metal-binding;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Transport; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..320
FT /note="mRNA decay activator protein ZFP36"
FT /id="PRO_0000089165"
FT REPEAT 64..68
FT /note="P-P-P-P-G"
FT REPEAT 191..195
FT /note="P-P-P-P-G"
FT REPEAT 212..216
FT /note="P-P-P-P-G"
FT ZN_FING 96..124
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 134..162
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..167
FT /note="Necessary for localization of ARE-containing mRNAs
FT to processing bodies (PBs)"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 1..93
FT /note="Necessary and sufficient for the association with
FT mRNA decay enzymes and mRNA decay activation"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 1..15
FT /note="Necessary for nuclear export"
FT /evidence="ECO:0000269|PubMed:12054509"
FT REGION 17..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..161
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000269|PubMed:12054509"
FT REGION 90..166
FT /note="Necessary for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 93..320
FT /note="Necessary for localization of ARE-containing mRNAs
FT to processing bodies (PBs)"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 96..187
FT /note="Necessary for interaction with PABPN1"
FT /evidence="ECO:0000250|UniProtKB:P22893"
FT REGION 167..320
FT /note="Necessary for mRNA decay activation"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 180..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..320
FT /note="Interaction with CNOT1"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT COMPBIAS 19..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:P22893"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22893"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 179
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 221
FT /note="Phosphoserine; by MAPK1; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22893"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MUTAGEN 3
FT /note="L->A: Inhibits nucleus export."
FT /evidence="ECO:0000269|PubMed:12054509"
FT MUTAGEN 10
FT /note="L->A: Inhibits nucleus export."
FT /evidence="ECO:0000269|PubMed:12054509"
SQ SEQUENCE 320 AA; 33654 MW; CFC597F3C7E5CA76 CRC64;
MDLSAIYESL MSMSHDLSPD HGGTESSGGL WNINSSDSIP SGVTSRLTGR STSLVEGRSC
SWVPPPPGFA PLAPRPGPEL SPSPTSPTAT PTTSSRYKTE LCRTYSESGR CRYGAKCQFA
HGPGELRQAN RHPKYKTELC HKFYLQGRCP YGSRCHFIHN PTEDLALPGQ PHVLRQSISF
SGLPSGRRTS PPPPGFSGPS LSSCSFSPSS SPPPPGDLPL SPSAFSAAPG TPVSRRDPTP
ACCPSCRRST TPSTIWGPLG GLARSPSAHS LGSDPDDYAS SGSSLGGSDS PVFEAGVFGP
PQPPAPPRRL PIFNRISVSE
