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P17275

- JUNB_HUMAN

UniProt

P17275 - JUNB_HUMAN

Protein

Transcription factor jun-B

Gene

JUNB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[CG]TCA-3'.

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. double-stranded DNA binding Source: Ensembl
    3. protein binding Source: IntAct
    4. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl
    6. transcription coactivator activity Source: ProtInc
    7. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. cellular response to calcium ion Source: Ensembl
    2. cellular response to hormone stimulus Source: Ensembl
    3. decidualization Source: Ensembl
    4. embryonic process involved in female pregnancy Source: Ensembl
    5. gene expression Source: Reactome
    6. labyrinthine layer blood vessel development Source: Ensembl
    7. osteoblast differentiation Source: Ensembl
    8. osteoblast proliferation Source: Ensembl
    9. osteoclast differentiation Source: Ensembl
    10. positive regulation of cell differentiation Source: Ensembl
    11. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    12. regulation of cell cycle Source: Ensembl
    13. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    14. response to cAMP Source: Ensembl
    15. response to corticosterone Source: Ensembl
    16. response to cytokine Source: Ensembl
    17. response to drug Source: Ensembl
    18. response to light stimulus Source: Ensembl
    19. response to mechanical stimulus Source: Ensembl
    20. response to peptide hormone Source: Ensembl
    21. response to progesterone Source: Ensembl
    22. transcription, DNA-templated Source: Reactome
    23. transcription initiation from RNA polymerase II promoter Source: Reactome
    24. transforming growth factor beta receptor signaling pathway Source: Reactome
    25. trophectodermal cell differentiation Source: Ensembl
    26. vasculogenesis Source: Ensembl

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    SignaLinkiP17275.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor jun-B
    Gene namesi
    Name:JUNB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6205. JUNB.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin Source: ProtInc
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30007.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 347347Transcription factor jun-BPRO_0000076438Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021Phosphothreonine1 Publication
    Modified residuei104 – 1041Phosphothreonine2 Publications
    Modified residuei117 – 1171Phosphoserine2 Publications
    Modified residuei240 – 2401N6-acetyllysineBy similarity
    Modified residuei251 – 2511Phosphoserine2 Publications
    Modified residuei255 – 2551Phosphothreonine3 Publications
    Modified residuei259 – 2591Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated by ITCH, leading to its degradation.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP17275.
    PaxDbiP17275.
    PRIDEiP17275.

    PTM databases

    PhosphoSiteiP17275.

    Expressioni

    Inductioni

    By growth factors.

    Gene expression databases

    ArrayExpressiP17275.
    BgeeiP17275.
    CleanExiHS_JUNB.
    GenevestigatoriP17275.

    Organism-specific databases

    HPAiCAB004464.
    HPA019149.

    Interactioni

    Subunit structurei

    Binds DNA as a homodimer or as a heterodimer with another member of the Jun/Fos family. Interacts with ITCH (via its WW domains).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BATF2Q8N1L93EBI-748062,EBI-742695
    C19orf68Q86XI82EBI-748062,EBI-2682158
    FOSP011003EBI-748062,EBI-852851

    Protein-protein interaction databases

    BioGridi109929. 41 interactions.
    DIPiDIP-1052N.
    IntActiP17275. 26 interactions.
    MINTiMINT-205420.
    STRINGi9606.ENSP00000303315.

    Structurei

    3D structure databases

    ProteinModelPortaliP17275.
    SMRiP17275. Positions 272-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini268 – 33164bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni268 – 29528Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni296 – 32429Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bZIP family. Jun subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG283376.
    HOGENOMiHOG000006648.
    HOVERGENiHBG001722.
    InParanoidiP17275.
    KOiK09028.
    OMAiLNAYCPN.
    OrthoDBiEOG75MVXV.
    PhylomeDBiP17275.

    Family and domain databases

    Gene3Di1.10.880.10. 1 hit.
    InterProiIPR004827. bZIP.
    IPR005643. JNK.
    IPR002112. Leuzip_Jun.
    IPR008917. TF_DNA-bd.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    PF03957. Jun. 1 hit.
    [Graphical view]
    PRINTSiPR00043. LEUZIPPRJUN.
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47454. SSF47454. 1 hit.
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17275-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCTKMEQPFY HDDSYTATGY GRAPGGLSLH DYKLLKPSLA VNLADPYRSL    50
    KAPGARGPGP EGGGGGSYFS GQGSDTGASL KLASSELERL IVPNSNGVIT 100
    TTPTPPGQYF YPRGGGSGGG AGGAGGGVTE EQEGFADGFV KALDDLHKMN 150
    HVTPPNVSLG ATGGPPAGPG GVYAGPEPPP VYTNLSSYSP ASASSGGAGA 200
    AVGTGSSYPT TTISYLPHAP PFAGGHPAQL GLGRGASTFK EEPQTVPEAR 250
    SRDATPPVSP INMEDQERIK VERKRLRNRL AATKCRKRKL ERIARLEDKV 300
    KTLKAENAGL SSTAGLLREQ VAQLKQKVMT HVSNGCQLLL GVKGHAF 347
    Length:347
    Mass (Da):35,879
    Last modified:August 1, 1990 - v1
    Checksum:iDF8CD1CD4409C6BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241A → G in AAH09465. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti230 – 2301L → V.1 Publication
    Corresponds to variant rs17880705 [ dbSNP | Ensembl ].
    VAR_021081

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29039 Genomic DNA. Translation: AAA59198.1.
    X51345 mRNA. Translation: CAA35738.1.
    U20734 Genomic DNA. Translation: AAA74915.1.
    AY751746 Genomic DNA. Translation: AAU43800.1.
    BC004250 mRNA. Translation: AAH04250.1.
    BC009465 mRNA. Translation: AAH09465.1.
    BC009466 mRNA. Translation: AAH09466.1.
    CCDSiCCDS12280.1.
    PIRiS10183. TVHUJB.
    RefSeqiNP_002220.1. NM_002229.2.
    UniGeneiHs.25292.

    Genome annotation databases

    EnsembliENST00000302754; ENSP00000303315; ENSG00000171223.
    GeneIDi3726.
    KEGGihsa:3726.
    UCSCiuc002mvc.3. human.

    Polymorphism databases

    DMDMi135304.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29039 Genomic DNA. Translation: AAA59198.1 .
    X51345 mRNA. Translation: CAA35738.1 .
    U20734 Genomic DNA. Translation: AAA74915.1 .
    AY751746 Genomic DNA. Translation: AAU43800.1 .
    BC004250 mRNA. Translation: AAH04250.1 .
    BC009465 mRNA. Translation: AAH09465.1 .
    BC009466 mRNA. Translation: AAH09466.1 .
    CCDSi CCDS12280.1.
    PIRi S10183. TVHUJB.
    RefSeqi NP_002220.1. NM_002229.2.
    UniGenei Hs.25292.

    3D structure databases

    ProteinModelPortali P17275.
    SMRi P17275. Positions 272-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109929. 41 interactions.
    DIPi DIP-1052N.
    IntActi P17275. 26 interactions.
    MINTi MINT-205420.
    STRINGi 9606.ENSP00000303315.

    PTM databases

    PhosphoSitei P17275.

    Polymorphism databases

    DMDMi 135304.

    Proteomic databases

    MaxQBi P17275.
    PaxDbi P17275.
    PRIDEi P17275.

    Protocols and materials databases

    DNASUi 3726.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302754 ; ENSP00000303315 ; ENSG00000171223 .
    GeneIDi 3726.
    KEGGi hsa:3726.
    UCSCi uc002mvc.3. human.

    Organism-specific databases

    CTDi 3726.
    GeneCardsi GC19P012902.
    HGNCi HGNC:6205. JUNB.
    HPAi CAB004464.
    HPA019149.
    MIMi 165161. gene.
    neXtProti NX_P17275.
    PharmGKBi PA30007.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283376.
    HOGENOMi HOG000006648.
    HOVERGENi HBG001722.
    InParanoidi P17275.
    KOi K09028.
    OMAi LNAYCPN.
    OrthoDBi EOG75MVXV.
    PhylomeDBi P17275.

    Enzyme and pathway databases

    Reactomei REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    SignaLinki P17275.

    Miscellaneous databases

    GeneWikii JUNB.
    GenomeRNAii 3726.
    NextBioi 14587.
    PROi P17275.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17275.
    Bgeei P17275.
    CleanExi HS_JUNB.
    Genevestigatori P17275.

    Family and domain databases

    Gene3Di 1.10.880.10. 1 hit.
    InterProi IPR004827. bZIP.
    IPR005643. JNK.
    IPR002112. Leuzip_Jun.
    IPR008917. TF_DNA-bd.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    PF03957. Jun. 1 hit.
    [Graphical view ]
    PRINTSi PR00043. LEUZIPPRJUN.
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47454. SSF47454. 1 hit.
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "jun-B inhibits and c-fos stimulates the transforming and trans-activating activities of c-jun."
      Schuette J., Viallet J., Nau M., Segal S., Fedorko J., Minna J.
      Cell 59:987-997(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation of human cDNA clones of jun-related genes, jun-B and jun-D."
      Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.
      Nucleic Acids Res. 18:3047-3048(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Complex genetic organization of junB: multiple blocks of flanking evolutionarily conserved sequence at the murine and human junB loci."
      Phinney D.G., Tseng S.W., Ryder K.
      Genomics 28:228-234(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. NIEHS SNPs program
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-230.
    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: Pancreas.
    6. "Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation."
      Yang C., Zhou W., Jeon M.S., Demydenko D., Harada Y., Zhou H., Liu Y.C.
      Mol. Cell 21:135-141(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITCH, UBIQUITINATION.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102; THR-104 AND SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; THR-255 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-117; SER-251 AND THR-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiJUNB_HUMAN
    AccessioniPrimary (citable) accession number: P17275
    Secondary accession number(s): Q96GH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 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 19
      Human chromosome 19: 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