ID   TTP_HUMAN               Reviewed;         326 AA.
AC   P26651;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 83.
DE   RecName: Full=Tristetraproline;
DE            Short=TTP;
DE   AltName: Full=Zinc finger protein 36 homolog;
DE            Short=Zfp-36;
DE   AltName: Full=Protein TIS11A;
DE            Short=TIS11;
DE   AltName: Full=Growth factor-inducible nuclear protein NUP475;
DE   AltName: Full=G0/G1 switch regulatory protein 24;
GN   Name=ZFP36; Synonyms=G0S24, RNF162A, TIS11A, TTP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=91288233; PubMed=2062660; DOI=10.1093/nar/19.12.3454;
RA   Taylor G.A., Lai W.S., Oakey R.J., Seldin M.F., Shows T.B.,
RA   Eddy R.L. Jr., Blackshear P.J.;
RT   "The human TTP protein: sequence, alignment with related proteins, and
RT   chromosomal localization of the mouse and human genes.";
RL   Nucleic Acids Res. 19:3454-3454(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-37; PHE-259 AND
RP   PHE-324.
RA   Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N.,
RA   Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Schackwitz W.S.,
RA   Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
RT   "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT   of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable regulatory protein with a novel zinc finger
CC       structure involved in regulating the response to growth factors.
CC       Has been experimentally shown to be able to bind zinc.
CC   -!- INTERACTION:
CC       Q9NPI6:DCP1A; NbExp=1; IntAct=EBI-374248, EBI-374238;
CC       Q8IU60-1:DCP2; NbExp=1; IntAct=EBI-374248, EBI-521586;
CC       Q96F86:EDC3; NbExp=1; IntAct=EBI-374248, EBI-997311;
CC       Q96B26:EXOSC8; NbExp=1; IntAct=EBI-374248, EBI-371922;
CC       Q9HAU5:UPF2; NbExp=1; IntAct=EBI-374248, EBI-372073;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: By stimulation with various mitogens.
CC   -!- SIMILARITY: Contains 2 C3H1-type zinc fingers.
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DR   EMBL; M92843; AAA58489.1; -; mRNA.
DR   EMBL; M92844; AAC37600.1; -; Genomic_DNA.
DR   EMBL; M63625; AAA61240.1; -; mRNA.
DR   EMBL; AY771351; AAV28731.1; -; Genomic_DNA.
DR   EMBL; BC009693; AAH09693.1; -; mRNA.
DR   PIR; S34427; S34427.
DR   RefSeq; NP_003398.1; -.
DR   UniGene; Hs.534052; -.
DR   UniGene; Hs.704733; -.
DR   HSSP; P22893; 1M9O.
DR   SMR; P26651; 102-170.
DR   IntAct; P26651; -.
DR   PhosphoSite; P26651; -.
DR   Ensembl; ENSG00000128016; Homo sapiens.
DR   GeneID; 7538; -.
DR   KEGG; hsa:7538; -.
DR   HGNC; HGNC:12862; ZFP36.
DR   HPA; HPA006009; -.
DR   MIM; 190700; gene.
DR   PharmGKB; PA37451; -.
DR   HOGENOM; P26651; -.
DR   HOVERGEN; P26651; -.
DR   NextBio; 29497; -.
DR   ArrayExpress; P26651; -.
DR   CleanEx; HS_ZFP36; -.
DR   GermOnline; ENSG00000128016; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003727; F:single-stranded RNA binding; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    326       Tristetraproline.
FT                                /FTId=PRO_0000089163.
FT   REPEAT       71     75       P-P-P-P-G.
FT   REPEAT      198    202       P-P-P-P-G.
FT   REPEAT      219    223       P-P-P-P-G.
FT   ZN_FING     103    131       C3H1-type 1.
FT   ZN_FING     141    169       C3H1-type 2.
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES      93     93       Phosphoserine (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   MOD_RES     257    257       Phosphothreonine (By similarity).
FT   MOD_RES     323    323       Phosphoserine (By similarity).
FT   VARIANT      37     37       P -> S.
FT                                /FTId=VAR_021064.
FT   VARIANT     259    259       I -> F.
FT                                /FTId=VAR_021065.
FT   VARIANT     324    324       V -> F.
FT                                /FTId=VAR_021066.
SQ   SEQUENCE   326 AA;  34003 MW;  DDD9AD950AF7AF98 CRC64;
     MDLTAIYESL LSLSPDVPVP SDHGGTESSP GWGSSGPWSL SPSDSSPSGV TSRLPGRSTS
     LVEGRSCGWV PPPPGFAPLA PRLGPELSPS PTSPTATSTT PSRYKTELCR TFSESGRCRY
     GAKCQFAHGL GELRQANRHP KYKTELCHKF YLQGRCPYGS RCHFIHNPSE DLAAPGHPPV
     LRQSISFSGL PSGRRTSPPP PGLAGPSLSS SSFSPSSSPP PPGDLPLSPS AFSAAPGTPL
     ARRDPTPVCC PSCRRATPIS VWGPLGGLVR TPSVQSLGSD PDEYASSGSS LGGSDSPVFE
     AGVFAPPQPV AAPRRLPIFN RISVSE
//