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PTBP3_MOUSE
ID   PTBP3_MOUSE             Reviewed;         523 AA.
AC   Q8BHD7; A2ANH0; A2ANH1; Q923C3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Polypyrimidine tract-binding protein 3;
DE   AltName: Full=Regulator of differentiation 1;
DE            Short=Rod1;
GN   Name=Ptbp3; Synonyms=Rod1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Liver, Lung, Pancreas, and Spleen;
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).
CC   -!- FUNCTION: RNA-binding protein that mediates pre-mRNA alternative
CC       splicing regulation. Plays a role in the regulation of cell
CC       proliferation, differentiation and migration. Positive regulator of
CC       EPO-dependent erythropoiesis. Participates in cell differentiation
CC       regulation by repressing tissue-specific exons. Promotes Fas exon 6
CC       skipping. Binds RNA, preferentially to both poly(G) and poly(U) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with THBS4 (via the acidic amphipathic C-terminus).
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BHD7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BHD7-2; Sequence=VSP_010869;
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DR   EMBL; AK033732; BAC28453.1; -; mRNA.
DR   EMBL; AK088560; BAC40425.1; -; mRNA.
DR   EMBL; AL824704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006638; AAH06638.1; -; mRNA.
DR   EMBL; BC057641; AAH57641.1; -; mRNA.
DR   CCDS; CCDS18221.1; -. [Q8BHD7-1]
DR   RefSeq; NP_659153.2; NM_144904.2.
DR   RefSeq; NP_835458.1; NM_178164.3. [Q8BHD7-1]
DR   RefSeq; XP_006537917.1; XM_006537854.3. [Q8BHD7-2]
DR   AlphaFoldDB; Q8BHD7; -.
DR   SMR; Q8BHD7; -.
DR   BioGRID; 230952; 4.
DR   STRING; 10090.ENSMUSP00000099947; -.
DR   iPTMnet; Q8BHD7; -.
DR   PhosphoSitePlus; Q8BHD7; -.
DR   EPD; Q8BHD7; -.
DR   jPOST; Q8BHD7; -.
DR   MaxQB; Q8BHD7; -.
DR   PaxDb; Q8BHD7; -.
DR   PeptideAtlas; Q8BHD7; -.
DR   PRIDE; Q8BHD7; -.
DR   ProteomicsDB; 291613; -. [Q8BHD7-1]
DR   ProteomicsDB; 291614; -. [Q8BHD7-2]
DR   TopDownProteomics; Q8BHD7-1; -. [Q8BHD7-1]
DR   Antibodypedia; 29656; 165 antibodies from 22 providers.
DR   DNASU; 230257; -.
DR   Ensembl; ENSMUST00000030076; ENSMUSP00000030076; ENSMUSG00000028382. [Q8BHD7-1]
DR   Ensembl; ENSMUST00000148331; ENSMUSP00000122840; ENSMUSG00000028382. [Q8BHD7-2]
DR   Ensembl; ENSMUST00000172768; ENSMUSP00000134102; ENSMUSG00000028382. [Q8BHD7-2]
DR   GeneID; 230257; -.
DR   KEGG; mmu:230257; -.
DR   UCSC; uc008szx.2; mouse. [Q8BHD7-1]
DR   CTD; 9991; -.
DR   MGI; MGI:1923334; Ptbp3.
DR   VEuPathDB; HostDB:ENSMUSG00000028382; -.
DR   eggNOG; KOG1190; Eukaryota.
DR   GeneTree; ENSGT01050000244924; -.
DR   InParanoid; Q8BHD7; -.
DR   OrthoDB; 1545178at2759; -.
DR   PhylomeDB; Q8BHD7; -.
DR   BioGRID-ORCS; 230257; 3 hits in 106 CRISPR screens.
DR   ChiTaRS; Ptbp3; mouse.
DR   PRO; PR:Q8BHD7; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8BHD7; protein.
DR   Bgee; ENSMUSG00000028382; Expressed in undifferentiated genital tubercle and 256 other tissues.
DR   ExpressionAtlas; Q8BHD7; baseline and differential.
DR   Genevisible; Q8BHD7; MM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR   GO; GO:0033119; P:negative regulation of RNA splicing; ISO:MGI.
DR   GO; GO:0045595; P:regulation of cell differentiation; ISO:MGI.
DR   GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd12779; RRM1_ROD1; 1.
DR   CDD; cd12693; RRM2_PTBP1_like; 1.
DR   CDD; cd12703; RRM4_ROD1; 1.
DR   Gene3D; 3.30.70.330; -; 4.
DR   InterPro; IPR006536; HnRNP-L/PTB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR021790; PTBP1-like_RRM2.
DR   InterPro; IPR034798; PTBP1/2/3_RRM2.
DR   InterPro; IPR033110; PTBP3_RRM4.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR034326; ROD1_RRM1.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF11835; RRM_8; 1.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR   PROSITE; PS50102; RRM; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Differentiation; Erythrocyte maturation;
KW   Isopeptide bond; mRNA processing; mRNA splicing; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; RNA-binding; Ubl conjugation.
FT   CHAIN           1..523
FT                   /note="Polypyrimidine tract-binding protein 3"
FT                   /id="PRO_0000081874"
FT   DOMAIN          30..114
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          153..229
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          329..403
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          446..521
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         98
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P26599"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P26599"
FT   MOD_RES         394
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O95758"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95758"
FT   CROSSLNK        36
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26599"
FT   CROSSLNK        187
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26599"
FT   VAR_SEQ         8..10
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010869"
SQ   SEQUENCE   523 AA;  56701 MW;  2CED3B84B745AA25 CRC64;
     MNSSTSAGVY ANGNDNKKFK GDRPPCSPSR VLHLRKIPCD VTEAEVISLG LPFGKVTNLL
     MLKGKSQAFL EMASEEAAVT MINYYTPVTP HLRSQPVYIQ YSNHRELKTD NLPNQARAQA
     ALQAVSAVQS GNLSLPGATA NEGTLLPGQS PVLRIIIENL FYPVTLEVLH QIFSKFGTVL
     KIITFTKNNQ FQALLQYADP VNAQYAKMAL DGQNIYNACC TLRIDFSKLT SLNVKYNNDK
     SRDFTRLDLP TGDGQPSLEP PMAAAFGAPG IMSSPYAGAA GFAPAIAFPQ AAGLSVPAVP
     GALGPLTLTS SAVSGRMAIP GASGMPGNSV LLVTNLNPDF ITPHGLFILF GVYGDVHRVK
     IMFNKKENAL VQMADASQAQ LAMNHLSGQR LYGKVLRATL SKHQAVQLPR EGQEDQGLTK
     DFSNSPLHRF KKPGSKNFQN IFPPSATLHL SNIPPSVTMD DLKNLFTEAG CSVKAFKFFQ
     KDRKMALIQL GSVEEAIQAL IELHNHDLGE NHHLRVSFSK STI
 
 
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