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P40424 (PBX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-B-cell leukemia transcription factor 1
Alternative name(s):
Homeobox protein PBX1
Homeobox protein PRL
Gene names
Name:PBX1
Synonyms:PRL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds the sequence 5'-ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in complex with MEIS1. Converted into a potent transcriptional activator by the (1;19) translocation. May have a role in steroidogenesis and, subsequently, sexual development and differentiation. Isoform PBX1b as part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Probably in complex with MEIS2, is involved in transcriptional regulation by KLF4. Acts as a transcriptional activator of NKX2-5 and a transcriptional repressor of CDKN2B. Together with NKX2-5, it is required for spleen development through a mechanism that involves CDKN2B repression By similarity. Ref.11 Ref.15

Subunit structure

Forms a heterodimer with MEIS1 which binds DNA including a cAMP-responsive sequence in CYP17. Also forms heterotrimers with MEIS1 and a number of HOX proteins including HOXA9, HOXD4, HOXD9 and HOXD10. Interacts with PBXIP1 and TLX1. Isoform PBX1a interacts with MEIS2 isoform 4 SP1, SP3 and KLF4. Isoform PBX1b is part of a PDX1:PBX1b:MEIS2b complex; PBX1b recruits Meis2B to the complex. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in all tissues except in cells of the B and T lineage.

Involvement in disease

A chromosomal aberration involving PBX1 is a cause of pre-B-cell acute lymphoblastic leukemia (B-ALL). Translocation t(1;19)(q23;p13.3) with TCF3. TCF3-PBX1 transforms cells by constitutively activating transcription of genes regulated by PBX1 or by other members of the PBX protein family.

Sequence similarities

Belongs to the TALE/PBX homeobox family.

Contains 1 homeobox DNA-binding domain.

Sequence caution

The sequence AAA36764.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDifferentiation
Sexual differentiation
Steroidogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainHomeobox
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
Repressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadrenal gland development

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

embryonic limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system development

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15684392. Source: UniProtKB

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

proximal/distal pattern formation

Inferred from electronic annotation. Source: Ensembl

regulation of ossification

Inferred from electronic annotation. Source: Ensembl

sex differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

spleen development

Inferred from electronic annotation. Source: Ensembl

steroid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

thymus development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18973687. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 18973687PubMed 15684392. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay Ref.16. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.13. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Non-traceable author statement PubMed 10500199. Source: ProtInc

transcription factor binding

Inferred from physical interaction PubMed 15684392. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform PBX1a (identifier: P40424-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform PBX1b (identifier: P40424-2)

The sequence of this isoform differs from the canonical sequence as follows:
     334-347: SSSSFNMSNSGDLF → GYPSPCYQPDRRIQ
     348-430: Missing.
Isoform 3 (identifier: P40424-3)

The sequence of this isoform differs from the canonical sequence as follows:
     401-430: ANGGWQDATTPSSVTSPTEGPGSVHSDTSN → HLPRHPRQAHYHFRLPTWHP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Pre-B-cell leukemia transcription factor 1
PRO_0000049235

Regions

DNA binding233 – 29563Homeobox; TALE-type
Compositional bias127 – 1359Poly-Ala

Sites

Site88 – 892Breakpoint for translocation to form TCF3-PBX1 oncogene

Natural variations

Alternative sequence334 – 34714SSSSF…SGDLF → GYPSPCYQPDRRIQ in isoform PBX1b.
VSP_002271
Alternative sequence348 – 43083Missing in isoform PBX1b.
VSP_002272
Alternative sequence401 – 43030ANGGW…SDTSN → HLPRHPRQAHYHFRLPTWHP in isoform 3.
VSP_044499
Natural variant311G → S. Ref.3
Corresponds to variant rs2275558 [ dbSNP | Ensembl ].
VAR_068904

Experimental info

Sequence conflict3511Q → H in BAG61583. Ref.3

Secondary structure

........... 430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PBX1a [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: AD3FFACBC5A9E715

FASTA43046,626
        10         20         30         40         50         60 
MDEQPRLMHS HAGVGMAGHP GLSQHLQDGA GGTEGEGGRK QDIGDILQQI MTITDQSLDE 

        70         80         90        100        110        120 
AQARKHALNC HRMKPALFNV LCEIKEKTVL SIRGAQEEEP TDPQLMRLDN MLLAEGVAGP 

       130        140        150        160        170        180 
EKGGGSAAAA AAAAASGGAG SDNSVEHSDY RAKLSQIRQI YHTELEKYEQ ACNEFTTHVM 

       190        200        210        220        230        240 
NLLREQSRTR PISPKEIERM VSIIHRKFSS IQMQLKQSTC EAVMILRSRF LDARRKRRNF 

       250        260        270        280        290        300 
NKQATEILNE YFYSHLSNPY PSEEAKEELA KKCGITVSQV SNWFGNKRIR YKKNIGKFQE 

       310        320        330        340        350        360 
EANIYAAKTA VTATNVSAHG SQANSPSTPN SAGSSSSFNM SNSGDLFMSV QSLNGDSYQG 

       370        380        390        400        410        420 
AQVGANVQSQ VDTLRHVISQ TGGYSDGLAA SQMYSPQGIS ANGGWQDATT PSSVTSPTEG 

       430 
PGSVHSDTSN 

« Hide

Isoform PBX1b [UniParc].

Checksum: C4A2BDDD4A410C20
Show »

FASTA34738,427
Isoform 3 [UniParc].

Checksum: 1CC4B8B2EA51E509
Show »

FASTA42046,265

References

« Hide 'large scale' references
[1]"PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1."
Monica K., Galili N., Nourse J., Saltman D., Cleary M.L.
Mol. Cell. Biol. 11:6149-6157(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1A).
[2]"Analysis of PBX1 as a candidate gene for type 2 diabetes mellitus in Pima Indians."
Thameem F., Wolford J.K., Bogardus C., Prochazka M.
Biochim. Biophys. Acta 1518:215-220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PBX1A).
[3]"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] (ISOFORM 3), VARIANT SER-31.
Tissue: Brain.
[4]"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].
[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] (ISOFORM PBX1A).
Tissue: Brain.
[6]"A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL."
Kamps M.P., Murre C., Sun X.-H., Baltimore D.
Cell 60:547-555(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 89-430, CHROMOSOMAL TRANSLOCATION WITH TCF3.
[7]"The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1 coding sequences in acute lymphoblastic leukemias."
Hunger S.P., Galili N., Carroll A.J., Crist W.M., Link M.P., Cleary M.L.
Blood 77:687-693(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH TCF3.
[8]"Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastoid leukemia."
van Dijk M.A., Voorhoeve P.M., Murre C.
Proc. Natl. Acad. Sci. U.S.A. 90:6061-6065(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation."
Lu Q., Wright D.D., Kamps M.P.
Mol. Cell. Biol. 14:3938-3948(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA."
Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., Largman C., Humphries R.K.
J. Biol. Chem. 275:26172-26177(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PBXIP1.
[11]"Homeodomain proteins MEIS1 and PBXs regulate the lineage-specific transcription of the platelet factor 4 gene."
Okada Y., Nagai R., Sato T., Matsuura E., Minami T., Morita I., Doi T.
Blood 101:4748-4756(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEIS1.
[12]"An autoinhibitory effect of the homothorax domain of Meis2."
Hyman-Walsh C., Bjerke G.A., Wotton D.
FEBS J. 277:2584-2597(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEIS2.
[13]"MEIS proteins as partners of the TLX1/HOX11 oncoprotein."
Milech N., Gottardo N.G., Ford J., D'Souza D., Greene W.K., Kees U.R., Watt P.M.
Leuk. Res. 34:358-363(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TLX1.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1."
Bjerke G.A., Hyman-Walsh C., Wotton D.
Mol. Cell. Biol. 31:3723-3733(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SP1; SP3 AND KLF4.
[16]"Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation."
Piper D.E., Batchelor A.H., Chang C.-P., Cleary M.L., Wolberger C.
Cell 96:587-597(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 233-319 IN COMPLEX WITH HOXB1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86546 mRNA. Translation: AAA60031.1.
AF313404 expand/collapse EMBL AC list , AF313396, AF313397, AF313398, AF313399, AF313400, AF313401, AF313402, AF313403 Genomic DNA. Translation: AAG30941.1.
AK299673 mRNA. Translation: BAG61583.1.
AL359255, AL357568, AL390119 Genomic DNA. Translation: CAI14854.1.
AL390119, AL359255, AL357568 Genomic DNA. Translation: CAH73499.1.
AL357568, AL390119, AL359255 Genomic DNA. Translation: CAI14908.1.
AL391001 Genomic DNA. No translation available.
BC101578 mRNA. Translation: AAI01579.1.
M31522 mRNA. Translation: AAA36764.1. Different initiation.
CCDSCCDS1246.1. [P40424-1]
CCDS55653.1. [P40424-3]
CCDS55654.1. [P40424-2]
PIRB34734.
RefSeqNP_001191892.1. NM_001204963.1. [P40424-3]
NP_002576.1. NM_002585.3. [P40424-1]
XP_005245286.1. XM_005245229.1. [P40424-1]
UniGeneHs.557097.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B72X-ray2.35B233-319[»]
1PUFX-ray1.90B233-305[»]
ProteinModelPortalP40424.
SMRP40424. Positions 233-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111120. 30 interactions.
IntActP40424. 7 interactions.
MINTMINT-1532549.
STRING9606.ENSP00000405890.

Chemistry

BindingDBP40424.

PTM databases

PhosphoSiteP40424.

Polymorphism databases

DMDM730279.

Proteomic databases

MaxQBP40424.
PaxDbP40424.
PRIDEP40424.

Protocols and materials databases

DNASU5087.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367897; ENSP00000356872; ENSG00000185630. [P40424-2]
ENST00000401534; ENSP00000384856; ENSG00000185630. [P40424-2]
ENST00000420696; ENSP00000405890; ENSG00000185630. [P40424-1]
ENST00000540236; ENSP00000439943; ENSG00000185630. [P40424-3]
GeneID5087.
KEGGhsa:5087.
UCSCuc001gct.3. human. [P40424-1]
uc010pku.2. human. [P40424-3]

Organism-specific databases

CTD5087.
GeneCardsGC01P164524.
HGNCHGNC:8632. PBX1.
HPACAB018768.
HPA003505.
HPA003881.
MIM176310. gene.
neXtProtNX_P40424.
Orphanet99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBPA32970.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248144.
HOGENOMHOG000266972.
HOVERGENHBG000122.
InParanoidP40424.
KOK09355.
OMANIQSQVD.
PhylomeDBP40424.
TreeFamTF314340.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkP40424.

Gene expression databases

ArrayExpressP40424.
BgeeP40424.
CleanExHS_PBX1.
HS_PRL.
GenevestigatorP40424.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR005542. PBX.
[Graphical view]
PfamPF00046. Homeobox. 1 hit.
PF03792. PBC. 1 hit.
[Graphical view]
SMARTSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPBX1. human.
EvolutionaryTraceP40424.
GeneWikiPBX1.
GenomeRNAi5087.
NextBio19618.
PROP40424.
SOURCESearch...

Entry information

Entry namePBX1_HUMAN
AccessionPrimary (citable) accession number: P40424
Secondary accession number(s): B4DSC1, F5H4U9, Q5T488
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 154 of the entry and version 1 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