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Prospero homeobox protein 1 (Homeobox prospero-like protein PROX1) (PROX-1)

 PROX1_HUMAN             Reviewed;         737 AA.
Q92786; A6NK29; A8K2B1; Q5SW76; Q8TB91;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 2.
12-SEP-2018, entry version 158.
RecName: Full=Prospero homeobox protein 1;
AltName: Full=Homeobox prospero-like protein PROX1;
Short=PROX-1;
Name=PROX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Embryonic brain;
PubMed=8812486; DOI=10.1006/geno.1996.0392;
Zinovieva R.D., Duncan M.K., Johnson T.R., Torres R.,
Polymeropoulos M.H., Tomarev S.I.;
"Structure and chromosomal localization of the human homeobox gene
Prox 1.";
Genomics 35:517-522(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
REVIEW.
PubMed=22733308; DOI=10.1007/s10555-012-9390-8;
Elsir T., Smits A., Lindstroem M.S., Nister M.;
"Transcription factor PROX1: its role in development and cancer.";
Cancer Metastasis Rev. 31:793-805(2012).
[7]
FUNCTION.
PubMed=23723244; DOI=10.1093/nar/gkt447;
Takeda Y., Jetten A.M.;
"Prospero-related homeobox 1 (Prox1) functions as a novel modulator of
retinoic acid-related orphan receptors alpha- and gamma-mediated
transactivation.";
Nucleic Acids Res. 41:6992-7008(2013).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-199; SER-295
AND SER-557, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-324, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[10]
STRUCTURE BY NMR OF 575-737.
PubMed=22733734; DOI=10.1073/pnas.1203013109;
Lange O.F., Rossi P., Sgourakis N.G., Song Y., Lee H.W., Aramini J.M.,
Ertekin A., Xiao R., Acton T.B., Montelione G.T., Baker D.;
"Determination of solution structures of proteins up to 40 kDa using
CS-Rosetta with sparse NMR data from deuterated samples.";
Proc. Natl. Acad. Sci. U.S.A. 109:10873-10878(2012).
-!- FUNCTION: Transcription factor involved in developmental processes
such as cell fate determination, gene transcriptional regulation
and progenitor cell regulation in a number of organs. Plays a
critical role in embryonic development and functions as a key
regulatory protein in neurogenesis and the development of the
heart, eye lens, liver, pancreas and the lymphatic system.
Involved in the regulation of the circadian rhythm. Represses:
transcription of the retinoid-related orphan receptor RORG,
transcriptional activator activity of RORA and RORG and the
expression of RORA/G-target genes including core clock components:
ARNTL/BMAL1, NPAS2 and CRY1 and metabolic genes: AVPR1A and
ELOVL3. {ECO:0000269|PubMed:23723244,
ECO:0000303|PubMed:22733308}.
-!- SUBUNIT: Interacts with RORA and RORG (via AF-2 motif).
{ECO:0000250|UniProtKB:P48437}.
-!- INTERACTION:
P56545:CTBP2; NbExp=2; IntAct=EBI-3912635, EBI-741533;
P20823:HNF1A; NbExp=3; IntAct=EBI-3912635, EBI-636034;
P41235:HNF4A; NbExp=3; IntAct=EBI-3912635, EBI-1049011;
O00482-2:NR5A2; NbExp=9; IntAct=EBI-3912635, EBI-9257474;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P48437}.
Note=RORG promotes its nuclear localization.
{ECO:0000250|UniProtKB:P48437}.
-!- TISSUE SPECIFICITY: Most actively expressed in the developing
lens. Detected also in embryonic brain, lung, liver and kidney. In
adult, it is more abundant in heart and liver than in brain,
skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:8812486}.
-!- DOMAIN: The Prospero-type homeodomain and the adjacent Prospero
domain act as a single structural unit, the Homeo-Prospero domain.
The Prospero-type homeodomain is essential for repression of RORG
transcriptional activator activity. {ECO:0000250|UniProtKB:P48437,
ECO:0000255|PROSITE-ProRule:PRU01162}.
-!- SIMILARITY: Belongs to the Prospero homeodomain family.
{ECO:0000255|PROSITE-ProRule:PRU01162}.
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EMBL; U44060; AAC50656.1; -; mRNA.
EMBL; AK290176; BAF82865.1; -; mRNA.
EMBL; AC011700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL606537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471100; EAW93360.1; -; Genomic_DNA.
EMBL; BC024201; AAH24201.1; -; mRNA.
CCDS; CCDS31021.1; -.
RefSeq; NP_001257545.1; NM_001270616.1.
RefSeq; NP_002754.2; NM_002763.4.
RefSeq; XP_016857322.1; XM_017001833.1.
UniGene; Hs.741808; -.
UniGene; Hs.744931; -.
PDB; 2LMD; NMR; -; A=575-737.
PDBsum; 2LMD; -.
ProteinModelPortal; Q92786; -.
SMR; Q92786; -.
BioGrid; 111613; 17.
IntAct; Q92786; 10.
MINT; Q92786; -.
STRING; 9606.ENSP00000261454; -.
iPTMnet; Q92786; -.
PhosphoSitePlus; Q92786; -.
DMDM; 85702224; -.
MaxQB; Q92786; -.
PaxDb; Q92786; -.
PeptideAtlas; Q92786; -.
PRIDE; Q92786; -.
ProteomicsDB; 75470; -.
DNASU; 5629; -.
Ensembl; ENST00000261454; ENSP00000261454; ENSG00000117707.
Ensembl; ENST00000366958; ENSP00000355925; ENSG00000117707.
Ensembl; ENST00000435016; ENSP00000400694; ENSG00000117707.
Ensembl; ENST00000498508; ENSP00000420283; ENSG00000117707.
GeneID; 5629; -.
KEGG; hsa:5629; -.
UCSC; uc001hkg.3; human.
CTD; 5629; -.
DisGeNET; 5629; -.
EuPathDB; HostDB:ENSG00000117707.15; -.
GeneCards; PROX1; -.
HGNC; HGNC:9459; PROX1.
HPA; HPA000842; -.
HPA; HPA001030; -.
MIM; 601546; gene.
neXtProt; NX_Q92786; -.
OpenTargets; ENSG00000117707; -.
PharmGKB; PA33812; -.
eggNOG; KOG3779; Eukaryota.
eggNOG; ENOG410ZE21; LUCA.
GeneTree; ENSGT00530000063507; -.
HOGENOM; HOG000115708; -.
HOVERGEN; HBG053693; -.
InParanoid; Q92786; -.
KO; K20211; -.
OMA; SCFMSRN; -.
OrthoDB; EOG091G02KS; -.
PhylomeDB; Q92786; -.
TreeFam; TF316638; -.
SIGNOR; Q92786; -.
ChiTaRS; PROX1; human.
GeneWiki; PROX1; -.
GenomeRNAi; 5629; -.
PRO; PR:Q92786; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117707; Expressed in 168 organ(s), highest expression level in liver.
CleanEx; HS_PROX1; -.
ExpressionAtlas; Q92786; baseline and differential.
Genevisible; Q92786; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0050692; F:DBD domain binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IMP:BHF-UCL.
GO; GO:0003700; F:DNA-binding transcription factor activity; IC:BHF-UCL.
GO; GO:0050693; F:LBD domain binding; IPI:BHF-UCL.
GO; GO:0016922; F:nuclear receptor binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISS:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0007420; P:brain development; IEP:BHF-UCL.
GO; GO:0061114; P:branching involved in pancreas morphogenesis; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; IBA:GO_Central.
GO; GO:0001709; P:cell fate determination; IEA:Ensembl.
GO; GO:0021707; P:cerebellar granule cell differentiation; ISS:BHF-UCL.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0021542; P:dentate gyrus development; ISS:BHF-UCL.
GO; GO:0021516; P:dorsal spinal cord development; ISS:BHF-UCL.
GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEP:BHF-UCL.
GO; GO:0060214; P:endocardium formation; ISS:BHF-UCL.
GO; GO:0002194; P:hepatocyte cell migration; IEA:Ensembl.
GO; GO:0070365; P:hepatocyte differentiation; IEP:BHF-UCL.
GO; GO:0072574; P:hepatocyte proliferation; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEP:BHF-UCL.
GO; GO:0002088; P:lens development in camera-type eye; IEP:BHF-UCL.
GO; GO:0070309; P:lens fiber cell morphogenesis; IEP:BHF-UCL.
GO; GO:0001889; P:liver development; IEP:BHF-UCL.
GO; GO:0030324; P:lung development; IEP:BHF-UCL.
GO; GO:0001946; P:lymphangiogenesis; IDA:BHF-UCL.
GO; GO:0060836; P:lymphatic endothelial cell differentiation; IDA:BHF-UCL.
GO; GO:0070858; P:negative regulation of bile acid biosynthetic process; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
GO; GO:0021915; P:neural tube development; ISS:BHF-UCL.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:BHF-UCL.
GO; GO:0030910; P:olfactory placode formation; ISS:BHF-UCL.
GO; GO:0046619; P:optic placode formation involved in camera-type eye formation; ISS:BHF-UCL.
GO; GO:0043049; P:otic placode formation; ISS:BHF-UCL.
GO; GO:0031016; P:pancreas development; IEP:BHF-UCL.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL.
GO; GO:1901978; P:positive regulation of cell cycle checkpoint; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:2000979; P:positive regulation of forebrain neuron differentiation; ISS:BHF-UCL.
GO; GO:0060421; P:positive regulation of heart growth; ISS:BHF-UCL.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:BHF-UCL.
GO; GO:0060298; P:positive regulation of sarcomere organization; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IDA:BHF-UCL.
GO; GO:0060849; P:regulation of transcription involved in lymphatic endothelial cell fate commitment; IMP:BHF-UCL.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISS:BHF-UCL.
GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0048845; P:venous blood vessel morphogenesis; ISS:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0055005; P:ventricular cardiac myofibril assembly; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
Gene3D; 1.10.10.500; -; 1.
InterPro; IPR023082; Homeo_prospero_dom.
InterPro; IPR037131; Homeo_prospero_dom_sf.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR039350; Prospero_homeodomain.
InterPro; IPR007738; Prox1.
PANTHER; PTHR12198; PTHR12198; 1.
PANTHER; PTHR12198:SF6; PTHR12198:SF6; 1.
Pfam; PF05044; HPD; 1.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS51818; HOMEO_PROSPERO; 1.
1: Evidence at protein level;
3D-structure; Biological rhythms; Complete proteome;
Developmental protein; DNA-binding; Homeobox; Isopeptide bond;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 737 Prospero homeobox protein 1.
/FTId=PRO_0000208880.
DOMAIN 577 635 Prospero-type homeo.
{ECO:0000255|PROSITE-ProRule:PRU01162}.
DOMAIN 636 735 Prospero. {ECO:0000255|PROSITE-
ProRule:PRU01162}.
REGION 1 28 Interaction with RORG.
{ECO:0000250|UniProtKB:P48437}.
REGION 577 735 Homeo-Prospero. {ECO:0000255|PROSITE-
ProRule:PRU01162}.
REGION 723 729 Essential for nuclear localization,
interaction with RORG, repression of RORG
transcriptional activator activity.
{ECO:0000250|UniProtKB:P48437}.
COMPBIAS 215 219 Poly-Gln.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:P48437}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:P48437}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000250|UniProtKB:P48437}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000250|UniProtKB:P48437}.
MOD_RES 557 557 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 324 324 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297}.
VARIANT 584 584 H -> R (in dbSNP:rs12121210).
/FTId=VAR_049362.
CONFLICT 251 253 RQL -> LHV (in Ref. 1; AAC50656).
{ECO:0000305}.
CONFLICT 455 457 PAA -> LV (in Ref. 1; AAC50656).
{ECO:0000305}.
CONFLICT 724 724 I -> F (in Ref. 1; AAC50656).
{ECO:0000305}.
HELIX 582 592 {ECO:0000244|PDB:2LMD}.
HELIX 599 606 {ECO:0000244|PDB:2LMD}.
HELIX 614 645 {ECO:0000244|PDB:2LMD}.
HELIX 650 652 {ECO:0000244|PDB:2LMD}.
STRAND 653 656 {ECO:0000244|PDB:2LMD}.
HELIX 660 669 {ECO:0000244|PDB:2LMD}.
HELIX 679 698 {ECO:0000244|PDB:2LMD}.
HELIX 705 715 {ECO:0000244|PDB:2LMD}.
HELIX 728 730 {ECO:0000244|PDB:2LMD}.
HELIX 732 734 {ECO:0000244|PDB:2LMD}.
SEQUENCE 737 AA; 83203 MW; D243CEB421B313CA CRC64;
MPDHDSTALL SRQTKRRRVD IGVKRTVGTA SAFFAKARAT FFSAMNPQGS EQDVEYSVVQ
HADGEKSNVL RKLLKRANSY EDAMMPFPGA TIISQLLKNN MNKNGGTEPS FQASGLSSTG
SEVHQEDICS NSSRDSPPEC LSPFGRPTMS QFDMDRLCDE HLRAKRARVE NIIRGMSHSP
SVALRGNENE REMAPQSVSP RESYRENKRK QKLPQQQQQS FQQLVSARKE QKREERRQLK
QQLEDMQKQL RQLQEKFYQI YDSTDSENDE DGNLSEDSMR SEILDARAQD SVGRSDNEMC
ELDPGQFIDR ARALIREQEM AENKPKREGN NKERDHGPNS LQPEGKHLAE TLKQELNTAM
SQVVDTVVKV FSAKPSRQVP QVFPPLQIPQ ARFAVNGENH NFHTANQRLQ CFGDVIIPNP
LDTFGNVQMA SSTDQTEALP LVVRKNSSDQ SASGPAAGGH HQPLHQSPLS ATTGFTTSTF
RHPFPLPLMA YPFQSPLGAP SGSFSGKDRA SPESLDLTRD TTSLRTKMSS HHLSHHPCSP
AHPPSTAEGL SLSLIKSECG DLQDMSEISP YSGSAMQEGL SPNHLKKAKL MFFYTRYPSS
NMLKTYFSDV KFNRCITSQL IKWFSNFREF YYIQMEKYAR QAINDGVTST EELSITRDCE
LYRALNMHYN KANDFEVPER FLEVAQITLR EFFNAIIAGK DVDPSWKKAI YKVICKLDSE
VPEIFKSPNC LQELLHE


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