PITH1_MOUSE
ID PITH1_MOUSE Reviewed; 211 AA.
AC Q8BWR2; Q8BMZ1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=PITH domain-containing protein 1;
GN Name=Pithd1; Synonyms=Trp26;
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).
RA Kondo N., Yodoi J., Tagaya Y.;
RT "Molecular cloning of TRP26, a novel member of the thioredoxin family,
RT which is related to TRP32.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [6]
RP FUNCTION.
RX PubMed=25134913; DOI=10.1007/s00018-014-1704-2;
RA Lu B., Sun X., Chen Y., Jin Q., Liang Q., Liu S., Li Y., Zhou Y., Li W.,
RA Huang Z.;
RT "Novel function of PITH domain-containing 1 as an activator of internal
RT ribosomal entry site to enhance RUNX1 expression and promote megakaryocyte
RT differentiation.";
RL Cell. Mol. Life Sci. 72:821-832(2015).
CC -!- FUNCTION: Promotes megakaryocyte differentiation by up-regulating RUNX1
CC expression (PubMed:25134913). Regulates RUNX1 expression by activating
CC the proximal promoter of the RUNX1 gene and by enhancing the
CC translation activity of an internal ribosome entry site (IRES) element
CC in the RUNX1 gene (By similarity). {ECO:0000250|UniProtKB:Q9GZP4,
CC ECO:0000269|PubMed:25134913}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZP4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BWR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BWR2-2; Sequence=VSP_024808;
CC -!- SIMILARITY: Belongs to the PITHD1 family. {ECO:0000305}.
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DR EMBL; AF400670; AAO85407.1; -; mRNA.
DR EMBL; AK004208; BAC25071.1; -; mRNA.
DR EMBL; AK050261; BAC34151.1; -; mRNA.
DR EMBL; AL672076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052695; AAH52695.1; -; mRNA.
DR CCDS; CCDS51330.1; -. [Q8BWR2-1]
DR RefSeq; NP_079687.3; NM_025411.4. [Q8BWR2-1]
DR AlphaFoldDB; Q8BWR2; -.
DR SMR; Q8BWR2; -.
DR BioGRID; 211285; 2.
DR STRING; 10090.ENSMUSP00000101477; -.
DR PhosphoSitePlus; Q8BWR2; -.
DR SwissPalm; Q8BWR2; -.
DR EPD; Q8BWR2; -.
DR MaxQB; Q8BWR2; -.
DR PaxDb; Q8BWR2; -.
DR PeptideAtlas; Q8BWR2; -.
DR PRIDE; Q8BWR2; -.
DR ProteomicsDB; 288169; -. [Q8BWR2-1]
DR ProteomicsDB; 288170; -. [Q8BWR2-2]
DR Antibodypedia; 2117; 11 antibodies from 8 providers.
DR DNASU; 66193; -.
DR Ensembl; ENSMUST00000105851; ENSMUSP00000101477; ENSMUSG00000028669. [Q8BWR2-1]
DR GeneID; 66193; -.
DR KEGG; mmu:66193; -.
DR UCSC; uc012dnd.1; mouse. [Q8BWR2-1]
DR CTD; 57095; -.
DR MGI; MGI:1913443; Pithd1.
DR VEuPathDB; HostDB:ENSMUSG00000028669; -.
DR eggNOG; KOG1730; Eukaryota.
DR GeneTree; ENSGT00490000043398; -.
DR HOGENOM; CLU_072377_2_0_1; -.
DR InParanoid; Q8BWR2; -.
DR OMA; YHGVTIC; -.
DR OrthoDB; 1561790at2759; -.
DR PhylomeDB; Q8BWR2; -.
DR TreeFam; TF314669; -.
DR BioGRID-ORCS; 66193; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Pithd1; mouse.
DR PRO; PR:Q8BWR2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BWR2; protein.
DR Bgee; ENSMUSG00000028669; Expressed in dorsomedial nucleus of hypothalamus and 284 other tissues.
DR ExpressionAtlas; Q8BWR2; baseline and differential.
DR Genevisible; Q8BWR2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097598; C:sperm cytoplasmic droplet; IDA:MGI.
DR GO; GO:0061956; P:penetration of cumulus oophorus; IMP:MGI.
DR GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR Gene3D; 2.60.120.470; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045099; PITH1-like.
DR InterPro; IPR010400; PITH_dom.
DR InterPro; IPR037047; PITH_dom_sf.
DR PANTHER; PTHR12175; PTHR12175; 1.
DR Pfam; PF06201; PITH; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51532; PITH; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..211
FT /note="PITH domain-containing protein 1"
FT /id="PRO_0000285033"
FT DOMAIN 20..192
FT /note="PITH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00864"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZP4"
FT VAR_SEQ 193..211
FT /note="ANPADHRVHQVTPQTHFIS -> PNQQTTGCIRSLRRHTSFLKGQPGLPQMR
FT C (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024808"
SQ SEQUENCE 211 AA; 24192 MW; 159409B77F6F3C3D CRC64;
MSHGHSHGGG GCRCAAEREE PPEQRGLAYG LYLRIDLERL QCLNESREGS GRGVFKPWEE
RTDRSKFVES DADEELLFNI PFTGNVKLKG VIIMGEDDDS HPSEMRLYKN IPQMSFDDTE
REPEQTFSLN RDITGELEYA TKISRFSNVY HLSIHISKNF GADTTKIFYI GLRGEWTELR
RHEVTICNYE ASANPADHRV HQVTPQTHFI S
