Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92786 (PROX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prospero homeobox protein 1
Alternative name(s):
Homeobox prospero-like protein PROX1
Short name=PROX-1
Gene names
Name:PROX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a fundamental role in early development of CNS. May regulate gene expression and development of postmitotic undifferentiated young neurons By similarity.

Subcellular location

Nucleus Probable.

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.

Sequence similarities

Belongs to the Prospero homeobox family.

Contains 1 Prospero-type homeobox DNA-binding domain.

Sequence caution

The sequence CAI15309.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainHomeobox
   LigandDNA-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaorta smooth muscle tissue morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

atrial cardiac muscle tissue morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

brain development

Inferred from expression pattern Ref.1. Source: BHF-UCL

cell fate determination

Inferred from electronic annotation. Source: Ensembl

cerebellar granule cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

dentate gyrus development

Inferred from sequence or structural similarity. Source: BHF-UCL

dorsal spinal cord development

Inferred from sequence or structural similarity PubMed 11789987. Source: BHF-UCL

embryonic retina morphogenesis in camera-type eye

Inferred from expression pattern PubMed 12692551. Source: BHF-UCL

endocardium formation

Inferred from sequence or structural similarity. Source: BHF-UCL

hepatocyte cell migration

Inferred from electronic annotation. Source: Ensembl

hepatocyte differentiation

Inferred from expression pattern PubMed 15232737. Source: BHF-UCL

hepatocyte proliferation

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from expression pattern Ref.1. Source: BHF-UCL

lens development in camera-type eye

Inferred from expression pattern Ref.1. Source: BHF-UCL

lens fiber cell morphogenesis

Inferred from expression pattern PubMed 11850194. Source: BHF-UCL

liver development

Inferred from expression pattern PubMed 11789987. Source: BHF-UCL

lung development

Inferred from expression pattern Ref.1. Source: BHF-UCL

lymphangiogenesis

Inferred from direct assay PubMed 12412020. Source: BHF-UCL

lymphatic endothelial cell differentiation

Inferred from direct assay PubMed 12198161. Source: BHF-UCL

negative regulation of bile acid biosynthetic process

Inferred from mutant phenotype PubMed 16488887. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 17062673. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15205472PubMed 16488887. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15205472. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15143342PubMed 15205472. Source: BHF-UCL

negative regulation of viral genome replication

Inferred from direct assay PubMed 19264593. Source: BHF-UCL

neural tube development

Inferred from sequence or structural similarity PubMed 11789987. Source: BHF-UCL

neuronal stem cell maintenance

Inferred from sequence or structural similarity. Source: BHF-UCL

olfactory placode formation

Inferred from sequence or structural similarity PubMed 11789987. Source: BHF-UCL

optic placode formation involved in camera-type eye formation

Inferred from sequence or structural similarity PubMed 11850194. Source: BHF-UCL

otic placode formation

Inferred from sequence or structural similarity PubMed 11789987. Source: BHF-UCL

pancreas development

Inferred from expression pattern PubMed 11789987. Source: BHF-UCL

positive regulation of cell cycle

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell cycle checkpoint

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 12198161. Source: BHF-UCL

positive regulation of cyclin-dependent protein kinase activity

Inferred from direct assay PubMed 19210544. Source: BHF-UCL

positive regulation of endothelial cell migration

Inferred from direct assay PubMed 19210544. Source: BHF-UCL

positive regulation of endothelial cell proliferation

Inferred from direct assay PubMed 19210544. Source: BHF-UCL

positive regulation of forebrain neuron differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of heart growth

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neural precursor cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of sarcomere organization

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 18815287. Source: BHF-UCL

regulation of gene expression

Inferred from direct assay PubMed 12198161. Source: BHF-UCL

regulation of transcription involved in lymphatic endothelial cell fate commitment

Inferred from mutant phenotype PubMed 18815287. Source: BHF-UCL

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

retina morphogenesis in camera-type eye

Inferred from sequence or structural similarity PubMed 11789987. Source: BHF-UCL

skeletal muscle thin filament assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

venous blood vessel morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

ventricular cardiac muscle tissue morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

ventricular cardiac myofibril assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

ventricular septum morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11850194. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 11850194PubMed 15143342PubMed 15205472PubMed 19210544. Source: BHF-UCL

   Molecular_functionDBD domain binding

Inferred from physical interaction PubMed 15205472. Source: BHF-UCL

DNA binding

Inferred from mutant phenotype PubMed 18815287. Source: BHF-UCL

LBD domain binding

Inferred from physical interaction PubMed 15143342PubMed 15205472. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

ligand-dependent nuclear receptor binding

Inferred from physical interaction PubMed 15143342PubMed 15205472PubMed 16488887. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 19264593PubMed 21988832. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred by curator PubMed 19210544. Source: BHF-UCL

transcription corepressor activity

Inferred from direct assay PubMed 15143342PubMed 15205472PubMed 16488887PubMed 19264593. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from direct assay PubMed 19210544. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 737737Prospero homeobox protein 1
PRO_0000208880

Regions

DNA binding573 – 63563Prospero-type homeobox
Region636 – 737102Prospero-like
Compositional bias215 – 2195Poly-Gln

Amino acid modifications

Modified residue1791Phosphoserine By similarity
Modified residue5111Phosphoserine By similarity
Modified residue5141Phosphoserine By similarity

Natural variations

Natural variant5841H → R.
Corresponds to variant rs12121210 [ dbSNP | Ensembl ].
VAR_049362

Experimental info

Sequence conflict251 – 2533RQL → LHV in AAC50656. Ref.1
Sequence conflict455 – 4573PAA → LV in AAC50656. Ref.1
Sequence conflict7241I → F in AAC50656. Ref.1

Secondary structure

.................... 737
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92786 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: D243CEB421B313CA

FASTA73783,203
        10         20         30         40         50         60 
MPDHDSTALL SRQTKRRRVD IGVKRTVGTA SAFFAKARAT FFSAMNPQGS EQDVEYSVVQ 

        70         80         90        100        110        120 
HADGEKSNVL RKLLKRANSY EDAMMPFPGA TIISQLLKNN MNKNGGTEPS FQASGLSSTG 

       130        140        150        160        170        180 
SEVHQEDICS NSSRDSPPEC LSPFGRPTMS QFDMDRLCDE HLRAKRARVE NIIRGMSHSP 

       190        200        210        220        230        240 
SVALRGNENE REMAPQSVSP RESYRENKRK QKLPQQQQQS FQQLVSARKE QKREERRQLK 

       250        260        270        280        290        300 
QQLEDMQKQL RQLQEKFYQI YDSTDSENDE DGNLSEDSMR SEILDARAQD SVGRSDNEMC 

       310        320        330        340        350        360 
ELDPGQFIDR ARALIREQEM AENKPKREGN NKERDHGPNS LQPEGKHLAE TLKQELNTAM 

       370        380        390        400        410        420 
SQVVDTVVKV FSAKPSRQVP QVFPPLQIPQ ARFAVNGENH NFHTANQRLQ CFGDVIIPNP 

       430        440        450        460        470        480 
LDTFGNVQMA SSTDQTEALP LVVRKNSSDQ SASGPAAGGH HQPLHQSPLS ATTGFTTSTF 

       490        500        510        520        530        540 
RHPFPLPLMA YPFQSPLGAP SGSFSGKDRA SPESLDLTRD TTSLRTKMSS HHLSHHPCSP 

       550        560        570        580        590        600 
AHPPSTAEGL SLSLIKSECG DLQDMSEISP YSGSAMQEGL SPNHLKKAKL MFFYTRYPSS 

       610        620        630        640        650        660 
NMLKTYFSDV KFNRCITSQL IKWFSNFREF YYIQMEKYAR QAINDGVTST EELSITRDCE 

       670        680        690        700        710        720 
LYRALNMHYN KANDFEVPER FLEVAQITLR EFFNAIIAGK DVDPSWKKAI YKVICKLDSE 

       730 
VPEIFKSPNC LQELLHE 

« Hide

References

« Hide 'large scale' references
[1]"Structure and chromosomal localization of the human homeobox gene Prox 1."
Zinovieva R.D., Duncan M.K., Johnson T.R., Torres R., Polymeropoulos M.H., Tomarev S.I.
Genomics 35:517-522(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryonic brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[6]"Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:10873-10878(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 575-737.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U44060 mRNA. Translation: AAC50656.1.
AK290176 mRNA. Translation: BAF82865.1.
AL606537, AC011700 Genomic DNA. Translation: CAI15309.1. Sequence problems.
CH471100 Genomic DNA. Translation: EAW93360.1.
BC024201 mRNA. Translation: AAH24201.1.
CCDSCCDS31021.1.
RefSeqNP_001257545.1. NM_001270616.1.
NP_002754.2. NM_002763.4.
UniGeneHs.741808.
Hs.744931.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LMDNMR-A575-737[»]
ProteinModelPortalQ92786.
SMRQ92786. Positions 575-737.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111613. 16 interactions.
IntActQ92786. 7 interactions.
MINTMINT-2813285.
STRING9606.ENSP00000261454.

PTM databases

PhosphoSiteQ92786.

Polymorphism databases

DMDM85702224.

Proteomic databases

MaxQBQ92786.
PaxDbQ92786.
PRIDEQ92786.

Protocols and materials databases

DNASU5629.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261454; ENSP00000261454; ENSG00000117707.
ENST00000366958; ENSP00000355925; ENSG00000117707.
ENST00000435016; ENSP00000400694; ENSG00000117707.
ENST00000498508; ENSP00000420283; ENSG00000117707.
GeneID5629.
KEGGhsa:5629.
UCSCuc001hkg.2. human.

Organism-specific databases

CTD5629.
GeneCardsGC01P214156.
HGNCHGNC:9459. PROX1.
MIM601546. gene.
neXtProtNX_Q92786.
PharmGKBPA33812.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323972.
HOGENOMHOG000115708.
HOVERGENHBG053693.
OMAQECLSPF.
OrthoDBEOG7MSMNK.
PhylomeDBQ92786.
TreeFamTF316638.

Gene expression databases

ArrayExpressQ92786.
BgeeQ92786.
CleanExHS_PROX1.
GenevestigatorQ92786.

Family and domain databases

Gene3D1.10.10.500. 1 hit.
InterProIPR023082. Homeo_prospero_dom.
IPR009057. Homeodomain-like.
IPR007738. Prox1.
[Graphical view]
PANTHERPTHR12198. PTHR12198. 1 hit.
PfamPF05044. HPD. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
ProtoNetSearch...

Other

GeneWikiPROX1.
GenomeRNAi5629.
NextBio21878.
PROQ92786.
SOURCESearch...

Entry information

Entry namePROX1_HUMAN
AccessionPrimary (citable) accession number: Q92786
Secondary accession number(s): A6NK29 expand/collapse secondary AC list , A8K2B1, Q5SW76, Q8TB91
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM