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P31269

- HXA9_HUMAN

UniProt

P31269 - HXA9_HUMAN

Protein

Homeobox protein Hox-A9

Gene

HOXA9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 4 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei163 – 1642Breakpoint for translocation to form MSI2/HOXA9 fusion protein

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi206 – 26560HomeoboxPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. sequence-specific DNA binding Source: InterPro
    4. sequence-specific DNA binding transcription factor activity Source: InterPro

    GO - Biological processi

    1. endothelial cell activation Source: UniProtKB
    2. multicellular organismal development Source: ProtInc
    3. negative regulation of myeloid cell differentiation Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiP31269.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homeobox protein Hox-A9
    Alternative name(s):
    Homeobox protein Hox-1G
    Gene namesi
    Name:HOXA9
    Synonyms:HOX1G
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:5109. HOXA9.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: LIFEdb

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving HOXA9 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with NUP98.
    A chromosomal aberration involving HOXA9 may contribute to disease progression in chronic myeloid leukemia. Translocation t(7;17)(p15;q23) with MSI2.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi140 – 1401R → A: Results in loss of methylation. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA29386.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 272272Homeobox protein Hox-A9PRO_0000200081Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei140 – 1401Symmetric dimethylarginine1 Publication

    Post-translational modificationi

    Methylated on Arg-140 by PRMT5; methylation is critical for E-selectin induction.1 Publication

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP31269.
    PRIDEiP31269.

    PTM databases

    PhosphoSiteiP31269.

    Expressioni

    Gene expression databases

    ArrayExpressiP31269.
    BgeeiP31269.
    CleanExiHS_HOXA9.
    GenevestigatoriP31269.

    Organism-specific databases

    HPAiHPA061982.

    Interactioni

    Subunit structurei

    Transiently interacts with PRMT5 in TNF-alpha stimulated endothelial cells.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TRIP6Q156544EBI-742314,EBI-742327

    Protein-protein interaction databases

    BioGridi109445. 13 interactions.
    IntActiP31269. 6 interactions.
    MINTiMINT-2802430.
    STRINGi9606.ENSP00000343619.

    Structurei

    3D structure databases

    ProteinModelPortaliP31269.
    SMRiP31269. Positions 194-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Abd-B homeobox family.Curated
    Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Homeobox

    Phylogenomic databases

    eggNOGiNOG286554.
    HOGENOMiHOG000231180.
    HOVERGENiHBG016849.
    InParanoidiP31269.
    KOiK09294.
    OMAiVPAVYHP.
    OrthoDBiEOG722J9F.
    PhylomeDBiP31269.
    TreeFamiTF317819.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR017112. Homeobox_Hox9.
    IPR020479. Homeobox_metazoa.
    IPR009057. Homeodomain-like.
    IPR006711. Hox9_activation_N.
    [Graphical view]
    PfamiPF00046. Homeobox. 1 hit.
    PF04617. Hox9_act. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037109. Homeobox_Hox9. 1 hit.
    PRINTSiPR00024. HOMEOBOX.
    SMARTiSM00389. HOX. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    PROSITEiPS00027. HOMEOBOX_1. 1 hit.
    PS50071. HOMEOBOX_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P31269-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATTGALGNY YVDSFLLGAD AADELSVGRY APGTLGQPPR QAATLAEHPD    50
    FSPCSFQSKA TVFGASWNPV HAAGANAVPA AVYHHHHHHP YVHPQAPVAA 100
    AAPDGRYMRS WLEPTPGALS FAGLPSSRPY GIKPEPLSAR RGDCPTLDTH 150
    TLSLTDYACG SPPVDREKQP SEGAFSENNA ENESGGDKPP IDPNNPAANW 200
    LHARSTRKKR CPYTKHQTLE LEKEFLFNMY LTRDRRYEVA RLLNLTERQV 250
    KIWFQNRRMK MKKINKDRAK DE 272
    Length:272
    Mass (Da):30,172
    Last modified:July 15, 1999 - v4
    Checksum:i823A1A22BB07A881
    GO

    Sequence cautioni

    The sequence AAC50364.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641G → V in AAB40867. 1 PublicationCurated
    Sequence conflicti67 – 671W → R in AAD08713. (PubMed:9880515)Curated
    Sequence conflicti80 – 801Missing in AAB40867. 1 PublicationCurated
    Sequence conflicti243 – 2431L → F in AAB40867. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82759 mRNA. Translation: AAB40867.1.
    AF010258 Genomic DNA. Translation: AAD08713.1.
    BT006990 mRNA. Translation: AAP35636.1.
    AC004080 Genomic DNA. No translation available.
    BC006537 mRNA. Translation: AAH06537.1.
    BC010023 mRNA. Translation: AAH10023.1.
    U41813 mRNA. Translation: AAC50364.1. Different initiation.
    CCDSiCCDS5409.1.
    PIRiS14929.
    RefSeqiNP_689952.1. NM_152739.3.
    UniGeneiHs.659350.

    Genome annotation databases

    EnsembliENST00000343483; ENSP00000343619; ENSG00000078399.
    GeneIDi3205.
    KEGGihsa:3205.
    UCSCiuc003syt.3. human.

    Polymorphism databases

    DMDMi6166219.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82759 mRNA. Translation: AAB40867.1 .
    AF010258 Genomic DNA. Translation: AAD08713.1 .
    BT006990 mRNA. Translation: AAP35636.1 .
    AC004080 Genomic DNA. No translation available.
    BC006537 mRNA. Translation: AAH06537.1 .
    BC010023 mRNA. Translation: AAH10023.1 .
    U41813 mRNA. Translation: AAC50364.1 . Different initiation.
    CCDSi CCDS5409.1.
    PIRi S14929.
    RefSeqi NP_689952.1. NM_152739.3.
    UniGenei Hs.659350.

    3D structure databases

    ProteinModelPortali P31269.
    SMRi P31269. Positions 194-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109445. 13 interactions.
    IntActi P31269. 6 interactions.
    MINTi MINT-2802430.
    STRINGi 9606.ENSP00000343619.

    PTM databases

    PhosphoSitei P31269.

    Polymorphism databases

    DMDMi 6166219.

    Proteomic databases

    PaxDbi P31269.
    PRIDEi P31269.

    Protocols and materials databases

    DNASUi 3205.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343483 ; ENSP00000343619 ; ENSG00000078399 .
    GeneIDi 3205.
    KEGGi hsa:3205.
    UCSCi uc003syt.3. human.

    Organism-specific databases

    CTDi 3205.
    GeneCardsi GC07M027230.
    HGNCi HGNC:5109. HOXA9.
    HPAi HPA061982.
    MIMi 142956. gene.
    neXtProti NX_P31269.
    PharmGKBi PA29386.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG286554.
    HOGENOMi HOG000231180.
    HOVERGENi HBG016849.
    InParanoidi P31269.
    KOi K09294.
    OMAi VPAVYHP.
    OrthoDBi EOG722J9F.
    PhylomeDBi P31269.
    TreeFami TF317819.

    Enzyme and pathway databases

    SignaLinki P31269.

    Miscellaneous databases

    ChiTaRSi HOXA9. human.
    GeneWikii HOXA9.
    GenomeRNAii 3205.
    NextBioi 12752.
    PROi P31269.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31269.
    Bgeei P31269.
    CleanExi HS_HOXA9.
    Genevestigatori P31269.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR017112. Homeobox_Hox9.
    IPR020479. Homeobox_metazoa.
    IPR009057. Homeodomain-like.
    IPR006711. Hox9_activation_N.
    [Graphical view ]
    Pfami PF00046. Homeobox. 1 hit.
    PF04617. Hox9_act. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037109. Homeobox_Hox9. 1 hit.
    PRINTSi PR00024. HOMEOBOX.
    SMARTi SM00389. HOX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    PROSITEi PS00027. HOMEOBOX_1. 1 hit.
    PS50071. HOMEOBOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Rozenfeld S., Sauvageau G., Largman C.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone marrow.
    2. "Endothelial cells express a novel, tumor necrosis factor-alpha-regulated variant of HOXA9."
      Patel C.V., Sharangpani R., Bandyopadhyay S., DiCorleto P.E.
      J. Biol. Chem. 274:1415-1422(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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].
      Tissue: Colon.
    6. "The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9."
      Borrow J., Shearman A.M., Stanton V.P., Becher R., Collins T., Williams A.J., Dube I., Katz F., Kwong Y.L., Morris C., Ohyashiki K., Toyama K., Rowley J., Housman D.E.
      Nat. Genet. 12:159-167(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-272, CHROMOSOMAL TRANSLOCATION WITH NUP98.
    7. Cited for: NUCLEOTIDE SEQUENCE OF 206-271.
    8. "A novel gene, MSI2, encoding a putative RNA-binding protein is recurrently rearranged at disease progression of chronic myeloid leukemia and forms a fusion gene with HOXA9 as a result of the cryptic t(7;17)(p15;q23)."
      Barbouti A., Hoeglund M., Johansson B., Lassen C., Nilsson P.-G., Hagemeijer A., Mitelman F., Fioretos T.
      Cancer Res. 63:1202-1206(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH MSI2.
    9. "HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules."
      Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A., Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.
      Mol. Cell. Biol. 32:1202-1213(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRMT5, METHYLATION AT ARG-140, MUTAGENESIS OF ARG-140, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiHXA9_HUMAN
    AccessioniPrimary (citable) accession number: P31269
    Secondary accession number(s): O43369, O43429, Q99820
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Vertebrate homeotic Hox proteins
      Nomenclature of vertebrate homeotic Hox proteins and list of entries
    2. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3