Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10242

- MYB_HUMAN

UniProt

P10242 - MYB_HUMAN

Protein

Transcriptional activator Myb

Gene

MYB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi63 – 8624H-T-H motifPROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi115 – 13824H-T-H motifPROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi166 – 18924H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB

    GO - Biological processi

    1. B cell differentiation Source: Ensembl
    2. blood coagulation Source: Reactome
    3. calcium ion transport Source: Ensembl
    4. chromatin remodeling Source: UniProtKB
    5. embryonic digestive tract development Source: Ensembl
    6. G1/S transition of mitotic cell cycle Source: Ensembl
    7. homeostasis of number of cells Source: Ensembl
    8. in utero embryonic development Source: Ensembl
    9. negative regulation of transcription, DNA-templated Source: BHF-UCL
    10. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. positive regulation of histone H3-K4 methylation Source: UniProtKB
    12. positive regulation of histone H3-K9 methylation Source: UniProtKB
    13. positive regulation of T-helper cell differentiation Source: UniProtKB
    14. positive regulation of transcription, DNA-templated Source: UniProtKB
    15. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. regulation of transcription, DNA-templated Source: UniProtKB
    17. thymus development Source: Ensembl

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinkiP10242.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional activator Myb
    Alternative name(s):
    Proto-oncogene c-Myb
    Gene namesi
    Name:MYB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7545. MYB.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nuclear matrix Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti86849. Acute basophilic leukemia.
    99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBiPA31345.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 640640Transcriptional activator MybPRO_0000197048Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei471 – 4711N6-acetyllysine1 Publication
    Modified residuei480 – 4801N6-acetyllysine1 Publication

    Post-translational modificationi

    Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation.Curated
    Phosphorylated by NLK on multiple sites, which induces proteasomal degradation.By similarity
    Phosphorylated by HIPK1. This phosphorylation reduces MYB transcription factor activity but not MYB protein levels.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP10242.
    PaxDbiP10242.
    PRIDEiP10242.

    PTM databases

    PhosphoSiteiP10242.

    Expressioni

    Inductioni

    Negatively regulated by microRNA-155 (miR-155).1 Publication

    Gene expression databases

    ArrayExpressiP10242.
    BgeeiP10242.
    CleanExiHS_MYB.
    GenevestigatoriP10242.

    Organism-specific databases

    HPAiCAB017704.

    Interactioni

    Subunit structurei

    Binds MYBBP1A. Interacts with HIPK2, MAF and NLK By similarity. Binds to HIPK1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLTCQ006104EBI-298355,EBI-354967
    ERC2O150832EBI-298355,EBI-2684336
    SUMO1P631653EBI-298355,EBI-80140
    SUMO2P619563EBI-298355,EBI-473220
    ZFC3H1O602932EBI-298355,EBI-746701

    Protein-protein interaction databases

    BioGridi110687. 50 interactions.
    DIPiDIP-1057N.
    IntActiP10242. 33 interactions.
    MINTiMINT-6772664.
    STRINGi9606.ENSP00000339992.

    Structurei

    3D structure databases

    ProteinModelPortaliP10242.
    SMRiP10242. Positions 38-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 8652HTH myb-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini87 – 14256HTH myb-type 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini143 – 19351HTH myb-type 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni90 – 193104Interaction with HIPK2 and NLKBy similarityAdd
    BLAST
    Regioni275 – 32753Transcription activation domain (PubMed:2189102)1 PublicationAdd
    BLAST
    Regioni328 – 465138Negative regulatory domainBy similarityAdd
    BLAST
    Regioni376 – 39722Leucine-zipperAdd
    BLAST

    Domaini

    Comprised of 3 domains; an N-terminal DNA-binding domain, a centrally located transcriptional activation domain and a C-terminal domain involved in transcriptional repression.1 Publication

    Sequence similaritiesi

    Contains 3 HTH myb-type DNA-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5147.
    HOVERGENiHBG007964.
    KOiK09420.
    OMAiHGCLPEE.
    OrthoDBiEOG7H791P.
    PhylomeDBiP10242.
    TreeFamiTF326257.

    Family and domain databases

    Gene3Di1.10.10.60. 3 hits.
    InterProiIPR015395. C-myb_C.
    IPR009057. Homeodomain-like.
    IPR017930. Myb_dom.
    IPR001005. SANT/Myb.
    IPR012642. Tscrpt_reg_Wos2-domain.
    [Graphical view]
    PfamiPF09316. Cmyb_C. 1 hit.
    PF07988. LMSTEN. 1 hit.
    PF00249. Myb_DNA-binding. 1 hit.
    [Graphical view]
    SMARTiSM00717. SANT. 3 hits.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 2 hits.
    PROSITEiPS51294. HTH_MYB. 3 hits.
    [Graphical view]

    Sequences (12)i

    Sequence statusi: Complete.

    This entry describes 12 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P10242-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK    50
    LKKLVEQNGT DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED 100
    QRVIELVQKY GPKRWSVIAK HLKGRIGKQC RERWHNHLNP EVKKTSWTEE 150
    EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA IKNHWNSTMR RKVEQEGYLQ 200
    ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV NNDYSYYHIS 250
    EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 300
    LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE 350
    HHSTPSLPAD PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID 400
    SFLNTSSNHE NSDLEMPSLT STPLIGHKLT VTTPFHRDQT VKTQKENTVF 450
    RTPAIKRSIL ESSPRTPTPF KHALAAQEIK YGPLKMLPQT PSHLVEDLQD 500
    VIKQESDESG IVAEFQENGP PLLKKIKQEV ESPTDKSGNF FCSHHWEGDS 550
    LNTQLFTQTS PVADAPNILT SSVLMAPASE DEDNVLKAFT VPKNRSLASP 600
    LQPCSSTWEP ASCGKMEEQM TSSSQARKYV NAFSARTLVM 640
    Length:640
    Mass (Da):72,341
    Last modified:November 1, 1997 - v2
    Checksum:iFD5E6694020426ED
    GO
    Isoform 2 (identifier: P10242-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         314-316: Missing.

    Show »
    Length:637
    Mass (Da):72,032
    Checksum:i75D8144FEEC381C5
    GO
    Isoform 3 (identifier: P10242-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         317-350: TQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGE → LCGPLLNSDIFSDWAANWDGSLCFATYIVNQQRQ
         351-640: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:350
    Mass (Da):40,620
    Checksum:i60632631CFEE51FF
    GO
    Isoform 4 (identifier: P10242-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-401: S → SDSSSWCDLS...VKSLPFSPSQ

    Show »
    Length:761
    Mass (Da):85,475
    Checksum:i9D11661393B1A85B
    GO
    Isoform 5 (identifier: P10242-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         402-402: F → M
         403-640: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:402
    Mass (Da):46,065
    Checksum:i331FC406EC1C335C
    GO
    Isoform 6 (identifier: P10242-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         567-640: NILTSSVLMA...NAFSARTLVM → TGVQWHDFGS...LRFNGTSIRR

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:666
    Mass (Da):75,526
    Checksum:iBF91C8F858EA12DF
    GO
    Isoform 7 (identifier: P10242-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         314-316: Missing.
         401-401: S → SDSSSWCDLS...VKSLPFSPSQ

    Show »
    Length:758
    Mass (Da):85,166
    Checksum:i0F2142F19B9D4E48
    GO
    Isoform 8 (identifier: P10242-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         386-401: VKNLLEFAETLQFIDS → DSSSWCDLSS...VKSLPFSPSQ

    Show »
    Length:745
    Mass (Da):83,626
    Checksum:i9B6C4EBD083ED7CF
    GO
    Isoform 9 (identifier: P10242-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         282-316: Missing.

    Show »
    Length:605
    Mass (Da):68,135
    Checksum:i6078B295869F3BDA
    GO
    Isoform 10 (identifier: P10242-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         530-566: Missing.

    Show »
    Length:603
    Mass (Da):68,308
    Checksum:i560AF3F759C690F1
    GO
    Isoform 11 (identifier: P10242-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         317-401: Missing.

    Show »
    Length:555
    Mass (Da):63,198
    Checksum:iD29BCA8DD3CDA8FE
    GO
    Isoform 12 (identifier: P10242-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         317-640: TQNHTCSYPG...NAFSARTLVM → VRLSSCA

    Note: No experimental confirmation available.

    Show »
    Length:323
    Mass (Da):37,507
    Checksum:i52D7B7EA3EDB98E1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti511 – 5111I → F in AAA52032. (PubMed:3540945)Curated
    Sequence conflicti511 – 5111I → F in AY787447. 1 PublicationCurated
    Sequence conflicti511 – 5111I → F in AY787448. 1 PublicationCurated
    Sequence conflicti563 – 5631A → R in AAA52032. (PubMed:3540945)Curated
    Sequence conflicti563 – 5631A → R in AY787447. 1 PublicationCurated
    Sequence conflicti563 – 5631A → R in AY787448. 1 PublicationCurated
    Isoform 4 (identifier: P10242-4)
    Sequence conflicti433 – 4331L → F in CAA35503. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti336 – 3361T → I.
    Corresponds to variant rs2229999 [ dbSNP | Ensembl ].
    VAR_050188
    Natural varianti422 – 4221T → N.
    Corresponds to variant rs2230000 [ dbSNP | Ensembl ].
    VAR_050189

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei282 – 31635Missing in isoform 9. 1 PublicationVSP_046658Add
    BLAST
    Alternative sequencei314 – 3163Missing in isoform 2 and isoform 7. 3 PublicationsVSP_003293
    Alternative sequencei317 – 640324TQNHT…RTLVM → VRLSSCA in isoform 12. 1 PublicationVSP_053389Add
    BLAST
    Alternative sequencei317 – 40185Missing in isoform 11. 1 PublicationVSP_046659Add
    BLAST
    Alternative sequencei317 – 35034TQNHT…SCLGE → LCGPLLNSDIFSDWAANWDG SLCFATYIVNQQRQ in isoform 3. CuratedVSP_003294Add
    BLAST
    Alternative sequencei351 – 640290Missing in isoform 3. CuratedVSP_003295Add
    BLAST
    Alternative sequencei386 – 40116VKNLL…QFIDS → DSSSWCDLSSFEFFEEADFS PSQHHTGKALQLQQREGNGT KPAGEPSPRVNKRMLSESSL DPPKVLPPARHSTIPLVILR KKRGQASPLATGDCSSFIFA DVSSSTPKRSPVKSLPFSPS Q in isoform 8. 1 PublicationVSP_046660Add
    BLAST
    Alternative sequencei401 – 4011S → SDSSSWCDLSSFEFFEEADF SPSQHHTGKALQLQQREGNG TKPAGEPSPRVNKRMLSESS LDPPKVLPPARHSTIPLVIL RKKRGQASPLATGDCSSFIF ADVSSSTPKRSPVKSLPFSP SQ in isoform 4 and isoform 7. 2 PublicationsVSP_003296
    Alternative sequencei402 – 4021F → M in isoform 5. CuratedVSP_003297
    Alternative sequencei403 – 640238Missing in isoform 5. CuratedVSP_003298Add
    BLAST
    Alternative sequencei530 – 56637Missing in isoform 10. 1 PublicationVSP_046661Add
    BLAST
    Alternative sequencei567 – 64074NILTS…RTLVM → TGVQWHDFGSLQPLPPGFKR FSCLSLPRSWDYRHPPPRPA NFEFLVETGFLHVGQAGLEL LTSGDLPASASQSARITGVS HRARPEYSYKLRFNGTSIRR in isoform 6. CuratedVSP_003299Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15024 mRNA. Translation: AAA52032.1.
    X52125 mRNA. Translation: CAA36371.1.
    AJ606319 mRNA. Translation: CAE55170.1.
    AJ606320 mRNA. Translation: CAE55171.1.
    AJ616791 mRNA. Translation: CAF04482.1.
    AJ616791 mRNA. Translation: CAF04479.1.
    U22376 Genomic DNA. Translation: AAB49034.1.
    U22376 Genomic DNA. Translation: AAB49035.1.
    U22376 Genomic DNA. Translation: AAB49036.1.
    U22376 Genomic DNA. Translation: AAB49037.1.
    U22376 Genomic DNA. Translation: AAB49038.1.
    U22376 Genomic DNA. Translation: AAB49039.1.
    AF104863 mRNA. Translation: AAC96326.1.
    AY787443 mRNA. No translation available.
    AY787447 mRNA. No translation available.
    AY787448 mRNA. No translation available.
    AY787461 mRNA. No translation available.
    AY787468 mRNA. No translation available.
    AL023693 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW47969.1.
    CH471051 Genomic DNA. Translation: EAW47973.1.
    BC064955 mRNA. Translation: AAH64955.1.
    M13665 mRNA. Translation: AAA52030.1.
    M13666 mRNA. Translation: AAA52031.1.
    X17469 mRNA. Translation: CAA35503.1.
    CCDSiCCDS47481.1. [P10242-4]
    CCDS47482.1. [P10242-2]
    CCDS5174.1. [P10242-1]
    CCDS55058.1. [P10242-7]
    CCDS55059.1. [P10242-8]
    CCDS55060.1. [P10242-10]
    CCDS55061.1. [P10242-11]
    CCDS55062.1. [P10242-9]
    PIRiA26661. TVHUMB.
    RefSeqiNP_001123644.1. NM_001130172.1. [P10242-2]
    NP_001123645.1. NM_001130173.1. [P10242-4]
    NP_001155128.1. NM_001161656.1. [P10242-7]
    NP_001155129.1. NM_001161657.1. [P10242-11]
    NP_001155130.1. NM_001161658.1. [P10242-8]
    NP_001155131.1. NM_001161659.1. [P10242-10]
    NP_001155132.1. NM_001161660.1. [P10242-9]
    NP_005366.2. NM_005375.2. [P10242-1]
    XP_006715558.1. XM_006715495.1.
    UniGeneiHs.606320.

    Genome annotation databases

    EnsembliENST00000341911; ENSP00000339992; ENSG00000118513. [P10242-4]
    ENST00000367812; ENSP00000356786; ENSG00000118513. [P10242-6]
    ENST00000367814; ENSP00000356788; ENSG00000118513. [P10242-1]
    ENST00000430686; ENSP00000390460; ENSG00000118513.
    ENST00000442647; ENSP00000410825; ENSG00000118513. [P10242-2]
    ENST00000525369; ENSP00000435938; ENSG00000118513. [P10242-11]
    ENST00000525477; ENSP00000437081; ENSG00000118513. [P10242-3]
    ENST00000525514; ENSP00000435578; ENSG00000118513. [P10242-3]
    ENST00000528774; ENSP00000434723; ENSG00000118513. [P10242-7]
    ENST00000529586; ENSP00000437264; ENSG00000118513. [P10242-3]
    ENST00000533384; ENSP00000432811; ENSG00000118513. [P10242-5]
    ENST00000533624; ENSP00000436605; ENSG00000118513. [P10242-9]
    ENST00000533808; ENSP00000435293; ENSG00000118513. [P10242-5]
    ENST00000533837; ENSP00000434639; ENSG00000118513. [P10242-5]
    ENST00000534044; ENSP00000435055; ENSG00000118513. [P10242-10]
    ENST00000534121; ENSP00000432851; ENSG00000118513. [P10242-8]
    GeneIDi4602.
    KEGGihsa:4602.
    UCSCiuc003qfc.3. human. [P10242-1]
    uc003qfh.3. human. [P10242-4]
    uc003qfu.3. human. [P10242-2]

    Polymorphism databases

    DMDMi2815504.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15024 mRNA. Translation: AAA52032.1 .
    X52125 mRNA. Translation: CAA36371.1 .
    AJ606319 mRNA. Translation: CAE55170.1 .
    AJ606320 mRNA. Translation: CAE55171.1 .
    AJ616791 mRNA. Translation: CAF04482.1 .
    AJ616791 mRNA. Translation: CAF04479.1 .
    U22376 Genomic DNA. Translation: AAB49034.1 .
    U22376 Genomic DNA. Translation: AAB49035.1 .
    U22376 Genomic DNA. Translation: AAB49036.1 .
    U22376 Genomic DNA. Translation: AAB49037.1 .
    U22376 Genomic DNA. Translation: AAB49038.1 .
    U22376 Genomic DNA. Translation: AAB49039.1 .
    AF104863 mRNA. Translation: AAC96326.1 .
    AY787443 mRNA. No translation available.
    AY787447 mRNA. No translation available.
    AY787448 mRNA. No translation available.
    AY787461 mRNA. No translation available.
    AY787468 mRNA. No translation available.
    AL023693 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW47969.1 .
    CH471051 Genomic DNA. Translation: EAW47973.1 .
    BC064955 mRNA. Translation: AAH64955.1 .
    M13665 mRNA. Translation: AAA52030.1 .
    M13666 mRNA. Translation: AAA52031.1 .
    X17469 mRNA. Translation: CAA35503.1 .
    CCDSi CCDS47481.1. [P10242-4 ]
    CCDS47482.1. [P10242-2 ]
    CCDS5174.1. [P10242-1 ]
    CCDS55058.1. [P10242-7 ]
    CCDS55059.1. [P10242-8 ]
    CCDS55060.1. [P10242-10 ]
    CCDS55061.1. [P10242-11 ]
    CCDS55062.1. [P10242-9 ]
    PIRi A26661. TVHUMB.
    RefSeqi NP_001123644.1. NM_001130172.1. [P10242-2 ]
    NP_001123645.1. NM_001130173.1. [P10242-4 ]
    NP_001155128.1. NM_001161656.1. [P10242-7 ]
    NP_001155129.1. NM_001161657.1. [P10242-11 ]
    NP_001155130.1. NM_001161658.1. [P10242-8 ]
    NP_001155131.1. NM_001161659.1. [P10242-10 ]
    NP_001155132.1. NM_001161660.1. [P10242-9 ]
    NP_005366.2. NM_005375.2. [P10242-1 ]
    XP_006715558.1. XM_006715495.1.
    UniGenei Hs.606320.

    3D structure databases

    ProteinModelPortali P10242.
    SMRi P10242. Positions 38-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110687. 50 interactions.
    DIPi DIP-1057N.
    IntActi P10242. 33 interactions.
    MINTi MINT-6772664.
    STRINGi 9606.ENSP00000339992.

    PTM databases

    PhosphoSitei P10242.

    Polymorphism databases

    DMDMi 2815504.

    Proteomic databases

    MaxQBi P10242.
    PaxDbi P10242.
    PRIDEi P10242.

    Protocols and materials databases

    DNASUi 4602.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341911 ; ENSP00000339992 ; ENSG00000118513 . [P10242-4 ]
    ENST00000367812 ; ENSP00000356786 ; ENSG00000118513 . [P10242-6 ]
    ENST00000367814 ; ENSP00000356788 ; ENSG00000118513 . [P10242-1 ]
    ENST00000430686 ; ENSP00000390460 ; ENSG00000118513 .
    ENST00000442647 ; ENSP00000410825 ; ENSG00000118513 . [P10242-2 ]
    ENST00000525369 ; ENSP00000435938 ; ENSG00000118513 . [P10242-11 ]
    ENST00000525477 ; ENSP00000437081 ; ENSG00000118513 . [P10242-3 ]
    ENST00000525514 ; ENSP00000435578 ; ENSG00000118513 . [P10242-3 ]
    ENST00000528774 ; ENSP00000434723 ; ENSG00000118513 . [P10242-7 ]
    ENST00000529586 ; ENSP00000437264 ; ENSG00000118513 . [P10242-3 ]
    ENST00000533384 ; ENSP00000432811 ; ENSG00000118513 . [P10242-5 ]
    ENST00000533624 ; ENSP00000436605 ; ENSG00000118513 . [P10242-9 ]
    ENST00000533808 ; ENSP00000435293 ; ENSG00000118513 . [P10242-5 ]
    ENST00000533837 ; ENSP00000434639 ; ENSG00000118513 . [P10242-5 ]
    ENST00000534044 ; ENSP00000435055 ; ENSG00000118513 . [P10242-10 ]
    ENST00000534121 ; ENSP00000432851 ; ENSG00000118513 . [P10242-8 ]
    GeneIDi 4602.
    KEGGi hsa:4602.
    UCSCi uc003qfc.3. human. [P10242-1 ]
    uc003qfh.3. human. [P10242-4 ]
    uc003qfu.3. human. [P10242-2 ]

    Organism-specific databases

    CTDi 4602.
    GeneCardsi GC06P135503.
    HGNCi HGNC:7545. MYB.
    HPAi CAB017704.
    MIMi 189990. gene.
    neXtProti NX_P10242.
    Orphaneti 86849. Acute basophilic leukemia.
    99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBi PA31345.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5147.
    HOVERGENi HBG007964.
    KOi K09420.
    OMAi HGCLPEE.
    OrthoDBi EOG7H791P.
    PhylomeDBi P10242.
    TreeFami TF326257.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinki P10242.

    Miscellaneous databases

    ChiTaRSi MYB. human.
    GeneWikii MYB_(gene).
    GenomeRNAii 4602.
    NextBioi 17700.
    PROi P10242.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10242.
    Bgeei P10242.
    CleanExi HS_MYB.
    Genevestigatori P10242.

    Family and domain databases

    Gene3Di 1.10.10.60. 3 hits.
    InterProi IPR015395. C-myb_C.
    IPR009057. Homeodomain-like.
    IPR017930. Myb_dom.
    IPR001005. SANT/Myb.
    IPR012642. Tscrpt_reg_Wos2-domain.
    [Graphical view ]
    Pfami PF09316. Cmyb_C. 1 hit.
    PF07988. LMSTEN. 1 hit.
    PF00249. Myb_DNA-binding. 1 hit.
    [Graphical view ]
    SMARTi SM00717. SANT. 3 hits.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 2 hits.
    PROSITEi PS51294. HTH_MYB. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human c-myb protooncogene: nucleotide sequence of cDNA and organization of the genomic locus."
      Majello B., Kenyon L.C., Dalla-Favera R.
      Proc. Natl. Acad. Sci. U.S.A. 83:9636-9640(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Alternative splicing of the human c-myb gene."
      Westin E.H., Gorse K.M., Clarke M.F.
      Oncogene 5:1117-1124(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Genome annotation of a 1.5 Mb region of human chromosome 6q23 encompassing a quantitative trait locus for fetal hemoglobin expression in adults."
      Close J.P., Game L., Clark B., Bergounioux J., Gerovassili A., Thein S.L.
      BMC Genomics 5:33-33(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
    4. "Characterization of the complete sequence structure of the human c-myb gene."
      Westin E.H., Gorse K.M.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6).
      Tissue: Liver and Placenta.
    5. Gaillard C., Perbal B.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "Complex RNA splicing produces multiple forms of c-Myb with distinct transcriptional activities."
      O'Rourke J.P. Jr., Ness S.A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 8; 9; 10 AND 11), ALTERNATIVE SPLICING.
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 1).
      Tissue: Testis.
    10. "Identification of a second promoter in the human c-myb proto-oncogene."
      Jacobs S.M., Gorse K.M., Westin E.H.
      Oncogene 9:227-235(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1).
    11. "Positive autoregulation of c-myb expression via Myb binding sites in the 5' flanking region of the human c-myb gene."
      Nicolaides N.C., Gualdi R., Casadevall C., Manzella L., Calabretta B.
      Mol. Cell. Biol. 11:6166-6176(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
    12. "Studies of the human c-myb gene and its product in human acute leukemias."
      Slamon D.J., Boone T.C., Murdock D.C., Keith D.E., Press M.F., Larson R.A., Souza L.M.
      Science 233:347-351(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-640 (ISOFORMS 1 AND 12).
    13. "Identification of alternatively spliced transcripts for human c-myb: molecular cloning and sequence analysis of human c-myb exon 9A sequences."
      Dasgupta P., Reddy E.P.
      Oncogene 4:1419-1423(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    14. "Transcriptional activation by human c-myb and v-myb genes."
      Kalkbrenner F., Guehmann S., Moelling K.
      Oncogene 5:657-661(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    15. "p53 suppresses the c-Myb-induced activation of heat shock transcription factor 3."
      Tanikawa J., Ichikawa-Iwata E., Kanei-Ishii C., Nakai A., Matsuzawa S., Reed J.C., Ishii S.
      J. Biol. Chem. 275:15578-15585(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH1, DEGRADATION.
    16. "HIPK1 interacts with c-Myb and modulates its activity through phosphorylation."
      Matre V., Nordgaard O., Alm-Kristiansen A.H., Ledsaak M., Gabrielsen O.S.
      Biochem. Biophys. Res. Commun. 388:150-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY HIPK1, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "BCL6 positively regulates AID and germinal center gene expression via repression of miR-155."
      Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C., Dalla-Favera R.
      J. Exp. Med. 209:2455-2465(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiMYB_HUMAN
    AccessioniPrimary (citable) accession number: P10242
    Secondary accession number(s): E9PI07
    , E9PLZ5, E9PNA4, E9PNL6, E9PRS2, P78391, P78392, P78525, P78526, Q14023, Q14024, Q708E4, Q708E7, Q9UE83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 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. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3