PKNX1_MOUSE
ID PKNX1_MOUSE Reviewed; 436 AA.
AC O70477; Q7TT01;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Homeobox protein PKNOX1;
DE AltName: Full=PBX/knotted homeobox 1;
GN Name=Pknox1 {ECO:0000312|MGI:MGI:1201409};
GN Synonyms=Prep1 {ECO:0000303|PubMed:12529389};
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].
RC STRAIN=Swiss Webster;
RA Nakamura T., Yamazaki Y.;
RT "Isolation of the mouse Pknox1 homeobox gene.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION (MICROBIAL INFECTION).
RX PubMed=12529389; DOI=10.1128/mcb.23.3.831-841.2003;
RA Chao S.H., Walker J.R., Chanda S.K., Gray N.S., Caldwell J.S.;
RT "Identification of homeodomain proteins, PBX1 and PREP1, involved in the
RT transcription of murine leukemia virus.";
RL Mol. Cell. Biol. 23:831-841(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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=29465778; DOI=10.1002/1873-3468.13015;
RA Draime A., Bridoux L., Belpaire M., Pringels T., Degand H., Morsomme P.,
RA Rezsohazy R.;
RT "The O-GlcNAc transferase OGT interacts with and post-translationally
RT modifies the transcription factor HOXA1.";
RL FEBS Lett. 592:1185-1201(2018).
CC -!- FUNCTION: Activates transcription in the presence of PBX1A and HOXA1.
CC {ECO:0000269|PubMed:29465778}.
CC -!- FUNCTION: (Microbial infection) In complex with PBX1, binds to the 5'-
CC TGATTGAC-3' consensus sequence in the U5 region of Moloney murine
CC leukemia virus and promotes viral transcription.
CC {ECO:0000269|PubMed:12529389}.
CC -!- SUBUNIT: Interacts with MN1. {ECO:0000250|UniProtKB:P55347}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TALE/MEIS homeobox family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC15990.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF061270; AAC15990.1; ALT_INIT; mRNA.
DR EMBL; AK131788; BAE20805.1; -; mRNA.
DR EMBL; AK134000; BAE21975.1; -; mRNA.
DR EMBL; BC052701; AAH52701.1; -; mRNA.
DR CCDS; CCDS28608.1; -.
DR RefSeq; NP_057879.2; NM_016670.3.
DR RefSeq; XP_006523917.1; XM_006523854.2.
DR RefSeq; XP_006523918.1; XM_006523855.2.
DR AlphaFoldDB; O70477; -.
DR SMR; O70477; -.
DR BioGRID; 202211; 12.
DR IntAct; O70477; 3.
DR STRING; 10090.ENSMUSP00000094966; -.
DR iPTMnet; O70477; -.
DR PhosphoSitePlus; O70477; -.
DR EPD; O70477; -.
DR MaxQB; O70477; -.
DR PaxDb; O70477; -.
DR PeptideAtlas; O70477; -.
DR PRIDE; O70477; -.
DR ProteomicsDB; 289607; -.
DR Antibodypedia; 3800; 235 antibodies from 29 providers.
DR DNASU; 18771; -.
DR Ensembl; ENSMUST00000097352; ENSMUSP00000094966; ENSMUSG00000006705.
DR Ensembl; ENSMUST00000175806; ENSMUSP00000134852; ENSMUSG00000006705.
DR Ensembl; ENSMUST00000176701; ENSMUSP00000135804; ENSMUSG00000006705.
DR GeneID; 18771; -.
DR KEGG; mmu:18771; -.
DR UCSC; uc008bvh.2; mouse.
DR CTD; 5316; -.
DR MGI; MGI:1201409; Pknox1.
DR VEuPathDB; HostDB:ENSMUSG00000006705; -.
DR eggNOG; KOG0773; Eukaryota.
DR GeneTree; ENSGT00940000159505; -.
DR HOGENOM; CLU_023139_0_2_1; -.
DR InParanoid; O70477; -.
DR OMA; QHVTMPD; -.
DR OrthoDB; 1221551at2759; -.
DR PhylomeDB; O70477; -.
DR TreeFam; TF318093; -.
DR BioGRID-ORCS; 18771; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Pknox1; mouse.
DR PRO; PR:O70477; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O70477; protein.
DR Bgee; ENSMUSG00000006705; Expressed in rostral migratory stream and 255 other tissues.
DR ExpressionAtlas; O70477; baseline and differential.
DR Genevisible; O70477; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR InterPro; IPR032453; PKNOX/Meis_N.
DR Pfam; PF05920; Homeobox_KN; 1.
DR Pfam; PF16493; Meis_PKNOX_N; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..436
FT /note="Homeobox protein PKNOX1"
FT /id="PRO_0000049249"
FT DOMAIN 80..163
FT /note="MEIS N-terminal"
FT /evidence="ECO:0000255"
FT DNA_BIND 259..321
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 23..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55347"
FT CONFLICT 251
FT /note="I -> T (in Ref. 1; AAC15990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 47539 MW; AC549642781DFCA0 CRC64;
MMATQTLSID SYQDGQQMQV VTELKTEQDP NCSDPDAEGV SPPPIESQTP MDADKQAIYR
HPLFPLLALL FEKCEQSTQG SEGTTSASFD VDIENFVRKQ EKDGKPFFCE DPETDNLMVK
AIQVLRIHLL ELEKVNELCK DFCSRYIACL KTKMNSETLL SGEPGSPYSP VQSQQIQSAI
TGTLSPQGIV VPASALQQGN VTMATVAGGT VYQPVTVVTP QGQVVTQALS PGTIRIQNSQ
LQLQLNQDLS ILHQEDGSSK NKRGVLPKHA TNVMRSWLFQ HIGHPYPTED EKKQIAAQTN
LTLLQVNNWF INARRRILQP MLDSSCSETP KTKKKPAQNR PVQRFWPDSL ASGVAQATPS
ELAMSEGAVV TITTPVNMNV DSLQSLSSDG ATLAVQQVMM AGQSEDESVD STEDEGGALA
PTHISGLVLE NSDSLQ
