ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P22893


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TTP_MOUSE
Primary accession number P22893
Secondary accession number P11520
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on August 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 89)
Name and origin of the protein
Protein name Tristetraproline
Synonyms TTP
Zinc finger protein 36
Zfp-36
Protein TIS11A
TIS11
Growth factor-inducible nuclear protein NUP475
TPA-induced sequence 11
Gene name
Name: Zfp36
Synonyms: Tis11, Tis11a
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2204625 [NCBI, ExPASy, EBI, Israel, Japan]
Lai W.S., Stumpo D.J., Blackshear P.J.;
"Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein.";
J. Biol. Chem. 265:16556-16563(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1699942 [NCBI, ExPASy, EBI, Israel, Japan]
Dubois R.N., McLane M.W., Ryder K., Lau L.F., Nathans D.;
"A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence.";
J. Biol. Chem. 265:19185-19191(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Swiss;
PubMed=2915901 [NCBI, ExPASy, EBI, Israel, Japan]
Varnum B.C., Lim R.W., Sukhatme V.P., Herschman H.R.;
"Nucleotide sequence of a cDNA encoding TIS11, a message induced in Swiss 3T3 cells by the tumor promoter tetradecanoyl phorbol acetate.";
Oncogene 4:119-120(1989).
[4]
SEQUENCE REVISION.
PubMed=1861870 [NCBI, ExPASy, EBI, Israel, Japan]
Ma Q., Herschman H.R.;
"A corrected sequence for the predicted protein from the mitogen-inducible TIS11 primary response gene.";
Oncogene 6:1277-1278(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
PubMed=1996120 [NCBI, ExPASy, EBI, Israel, Japan]
Varnum B.C., Ma Q., Chi T., Fletcher B.S., Herschman H.R.;
"The TIS11 primary response gene is a member of a gene family that encodes proteins with a highly conserved sequence containing an unusual Cys-His repeat.";
Mol. Cell. Biol. 11:1754-1758(1991).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/c;
TISSUE=Liver;
DOI=10.1074/jbc.270.42.25266; PubMed=7559666 [NCBI, ExPASy, EBI, Israel, Japan]
Lai W.S., Thompson M.J., Taylor G.A., Liu Y., Blackshear P.J.;
"Promoter analysis of Zfp-36, the mitogen-inducible gene encoding the zinc finger protein tristetraprolin.";
J. Biol. Chem. 270:25266-25272(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION AT SER-220.
DOI=10.1074/jbc.270.22.13341; PubMed=7768935 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor G.A., Thompson M.J., Lai W.S., Blackshear P.J.;
"Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro.";
J. Biol. Chem. 270:13341-13347(1995).
[9]
PHOSPHORYLATION AT SER-52; SER-80; SER-82; SER-85; SER-178; THR-249 AND SER-316, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M310486200; PubMed=14688255 [NCBI, ExPASy, EBI, Israel, Japan]
Chrestensen C.A., Schroeder M.J., Shabanowitz J., Hunt D.F., Pelo J.W., Worthington M.T., Sturgill T.W.;
"MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding.";
J. Biol. Chem. 279:10176-10184(2004).
Comments
  • FUNCTION: Probable regulatory protein with a novel zinc finger structure involved in regulating the response to growth factors. Has been experimentally shown to be able to bind zinc.
  • SUBCELLULAR LOCATION: Nucleus.
  • TISSUE SPECIFICITY: Especially abundant in intestine, thymus and regenerating liver, and in macrophage cell line stimulated by gamma-interferon.
  • INDUCTION: By growth factors and by extracellular signaling agents.
  • PTM: Phosphorylated upon mitogen stimulation.
  • PTM: Phosphorylated by MAPKAPK2, major sites are Ser-52 and Ser-178.
  • SIMILARITY: Contains 2 C3H1-type zinc fingers.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M57422; AAA40498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M58691; AAA39837.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14678; CAA32807.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M58565; AAA72947.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L42317; AAC37676.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021391; AAH21391.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A36600; A36600.
S04743; S04743.
RefSeq NP_035886.1; -.
UniGene Mm.389856
3D structure databases
PDB
1M9O; NMR; -; A=91-163.[ExPASy / RCSB / EBI]
PDBsum 1M9O; -.
ModBase P22893.
Protein-protein interaction databases
IntAct P22893; -.
PTM databases
PhosphoSite P22893; -.
Organism-specific databases
MGI MGI:99180; Zfp36.
Gene expression databases
ArrayExpress P22893; -.
CleanEx MM_ZFP36; -.
GermOnline ENSMUSG00000044786; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from MGI).
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0017091; Molecular function: AU-rich element binding (inferred from direct assay from MGI).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003729; Molecular function: mRNA binding (inferred from direct assay from MGI).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0050728; Biological process: negative regulation of inflammatory response (inferred from mutant phenotype from MGI).
GO:0045638; Biological process: negative regulation of myeloid cell differentiation (inferred from mutant phenotype from MGI).
GO:0000289; Biological process: nuclear-transcribed mRNA poly(A) tail shortening (inferred from direct assay from MGI).
GO:0007243; Biological process: protein kinase cascade (inferred from direct assay from MGI).
GO:0043488; Biological process: regulation of mRNA stability (inferred from direct assay from MGI).
GO:0050779; Biological process: RNA destabilization (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000571; Znf_CCCH.
Graphical view of domain structure.
Pfam PF00642; zf-CCCH; 2.
Pfam graphical view of domain structure.
SMART SM00356; ZnF_C3H1; 2.
SMART graphical view of domain structure.
PROSITE PS50103; ZF_C3H1; 2.
PROSITE graphical view of domain structure (profiles).
ProtoNet P22893.
Genome annotation databases
Ensembl ENSMUSG00000044786; Mus musculus. [Contig view]
GeneID 22695; -.
KEGG mmu:22695; -.
Phylogenomic databases
HOGENOM P22893; -.
HOVERGEN P22893; -.
Other
NextBio 303151; -.
SOURCE Zfp36; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Repeat; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   319  319     Tristetraproline. PRO_0000089164
REPEAT   63    67  5     P-P-P-P-G. 
REPEAT   190   194  5     P-P-P-P-G. 
REPEAT   211   215  5     P-P-P-P-G. 
ZN_FING   95   123  29     C3H1-type 1. 
ZN_FING   133   161  29     C3H1-type 2. 
MOD_RES   52    52        Phosphoserine. 
MOD_RES   80    80        Phosphoserine. 
MOD_RES   82    82        Phosphoserine. 
MOD_RES   85    85        Phosphoserine. 
MOD_RES   178   178        Phosphoserine. 
MOD_RES   220   220        Phosphoserine; by MAPK; in vitro. 
MOD_RES   250   250        Phosphothreonine. 
MOD_RES   316   316        Phosphoserine. 
HELIX   103   106  4      
TURN   111   115  5      
STRAND   120   122  3      
HELIX   125   127  3      
Sequence information
Length: 319 AA [This is the length of the unprocessed precursor] Molecular weight: 33613 Da [This is the MW of the unprocessed precursor] CRC64: 860DD6DDA80386F8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDLSAIYESL QSMSHDLSSD HGGTESLGGL WNINSDSIPS GVTSRLTGRS TSLVEGRSCG 

        70         80         90        100        110        120 
WVPPPPGFAP LAPRPGPELS PSPTSPTATP TTSSRYKTEL CRTYSESGRC RYGAKCQFAH 

       130        140        150        160        170        180 
GLGELRQANR HPKYKTELCH KFYLQGRCPY GSRCHFIHNP TEDLALPGQP HVLRQSISFS 

       190        200        210        220        230        240 
GLPSGRRSSP PPPGFSGPSL SSCSFSPSSS PPPPGDLPLS PSAFSAAPGT PVTRRDPNQA 

       250        260        270        280        290        300 
CCPSCRRSTT PSTIWGPLGG LARSPSAHSL GSDPDDYASS GSSLGGSDSP VFEAGVFGPP 

       310 
QTPAPPRRLP IFNRISVSE 

P22893 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!