PITH1_HUMAN
ID PITH1_HUMAN Reviewed; 211 AA.
AC Q9GZP4; B2R7J4; Q5QPN6; Q5QPN7; Q9NRI8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=PITH domain-containing protein 1;
GN Name=PITHD1; Synonyms=C1orf128; ORFNames=AD039, HT014, PP603;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 (PubMed:25134913). {ECO:0000269|PubMed:25134913}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25134913}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZP4-2; Sequence=VSP_024807;
CC -!- TISSUE SPECIFICITY: Down-regulated in primary acute myeloid leukemia
CC (AML) patients. {ECO:0000269|PubMed:25134913}.
CC -!- INDUCTION: Up-regulated in K562 and HEL cells undergoing megakaryocyte
CC differentiation induced by phorbol myristate acetate (PMA).
CC {ECO:0000269|PubMed:25134913}.
CC -!- SIMILARITY: Belongs to the PITHD1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF271784; AAG44795.1; -; mRNA.
DR EMBL; AF221595; AAF91232.1; -; mRNA.
DR EMBL; AF218024; AAG17266.1; -; mRNA.
DR EMBL; AK313005; BAG35841.1; -; mRNA.
DR EMBL; AL031295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW95075.1; -; Genomic_DNA.
DR EMBL; BC017208; AAH17208.1; -; mRNA.
DR CCDS; CCDS240.1; -. [Q9GZP4-1]
DR RefSeq; NP_065095.2; NM_020362.4. [Q9GZP4-1]
DR AlphaFoldDB; Q9GZP4; -.
DR SMR; Q9GZP4; -.
DR BioGRID; 121363; 45.
DR IntAct; Q9GZP4; 9.
DR MINT; Q9GZP4; -.
DR STRING; 9606.ENSP00000246151; -.
DR GlyGen; Q9GZP4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZP4; -.
DR PhosphoSitePlus; Q9GZP4; -.
DR BioMuta; PITHD1; -.
DR DMDM; 74752536; -.
DR REPRODUCTION-2DPAGE; IPI00015351; -.
DR EPD; Q9GZP4; -.
DR jPOST; Q9GZP4; -.
DR MassIVE; Q9GZP4; -.
DR MaxQB; Q9GZP4; -.
DR PaxDb; Q9GZP4; -.
DR PeptideAtlas; Q9GZP4; -.
DR PRIDE; Q9GZP4; -.
DR ProteomicsDB; 80105; -. [Q9GZP4-1]
DR ProteomicsDB; 80106; -. [Q9GZP4-2]
DR Antibodypedia; 2117; 11 antibodies from 8 providers.
DR DNASU; 57095; -.
DR Ensembl; ENST00000246151.9; ENSP00000246151.4; ENSG00000057757.10. [Q9GZP4-1]
DR GeneID; 57095; -.
DR KEGG; hsa:57095; -.
DR MANE-Select; ENST00000246151.9; ENSP00000246151.4; NM_020362.5; NP_065095.2.
DR UCSC; uc001bhq.4; human. [Q9GZP4-1]
DR CTD; 57095; -.
DR DisGeNET; 57095; -.
DR GeneCards; PITHD1; -.
DR HGNC; HGNC:25022; PITHD1.
DR HPA; ENSG00000057757; Low tissue specificity.
DR MIM; 618784; gene.
DR neXtProt; NX_Q9GZP4; -.
DR OpenTargets; ENSG00000057757; -.
DR PharmGKB; PA142672446; -.
DR VEuPathDB; HostDB:ENSG00000057757; -.
DR eggNOG; KOG1730; Eukaryota.
DR GeneTree; ENSGT00490000043398; -.
DR HOGENOM; CLU_072377_2_0_1; -.
DR InParanoid; Q9GZP4; -.
DR OMA; YHGVTIC; -.
DR OrthoDB; 1561790at2759; -.
DR PhylomeDB; Q9GZP4; -.
DR TreeFam; TF314669; -.
DR PathwayCommons; Q9GZP4; -.
DR SignaLink; Q9GZP4; -.
DR BioGRID-ORCS; 57095; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; PITHD1; human.
DR GenomeRNAi; 57095; -.
DR Pharos; Q9GZP4; Tdark.
DR PRO; PR:Q9GZP4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9GZP4; protein.
DR Bgee; ENSG00000057757; Expressed in secondary oocyte and 181 other tissues.
DR ExpressionAtlas; Q9GZP4; baseline and differential.
DR Genevisible; Q9GZP4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0097598; C:sperm cytoplasmic droplet; IEA:Ensembl.
DR GO; GO:0061956; P:penetration of cumulus oophorus; IEA:Ensembl.
DR GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
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_0000285032"
FT DOMAIN 20..192
FT /note="PITH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00864"
FT MOD_RES 189
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT VAR_SEQ 53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_024807"
SQ SEQUENCE 211 AA; 24178 MW; CFB3B6A0D75685FA CRC64;
MSHGHSHGGG GCRCAAEREE PPEQRGLAYG LYLRIDLERL QCLNESREGS GRGVFKPWEE
RTDRSKFVES DADEELLFNI PFTGNVKLKG IIIMGEDDDS HPSEMRLYKN IPQMSFDDTE
REPDQTFSLN RDLTGELEYA TKISRFSNVY HLSIHISKNF GADTTKVFYI GLRGEWTELR
RHEVTICNYE ASANPADHRV HQVTPQTHFI S
