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P19532

- TFE3_HUMAN

UniProt

P19532 - TFE3_HUMAN

Protein

Transcription factor E3

Gene

TFE3

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 4 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF. In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4+ T-cells and thymus-dependent humoral immunity. Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer. It also binds very well to a USF/MLTF site.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei178 – 1792Breakpoint for translocation to form PRCC-TFE3 oncogene
    Sitei260 – 2612Breakpoint for translocation to form ASPSCR1-TFE3 oncogene
    Sitei295 – 2962Breakpoint for translocation to form NONO-TFE3, PSF-TFE3 and ASPSCR1-TFE3 oncogenes

    GO - Molecular functioni

    1. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    2. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. humoral immune response Source: UniProtKB
    2. positive regulation of cell adhesion Source: UniProtKB
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. regulation of osteoclast differentiation Source: Ensembl
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Adaptive immunity, Immunity, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E3
    Alternative name(s):
    Class E basic helix-loop-helix protein 33
    Short name:
    bHLHe33
    Gene namesi
    Name:TFE3
    Synonyms:BHLHE33
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11752. TFE3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving TFE3 is found in patients with alveolar soft part sarcoma. Translocation t(X;17)(p11;q25) with ASPSCR1 forms a ASPSCR1-TFE3 fusion protein.
    Chromosomal aberrations involving TFE3 are found in patients with papillary renal cell carcinoma. Translocation t(X;1)(p11.2;q21.2) with PRCC; translocation t(X;1)(p11.2;p34) with PSF; inversion inv(X)(p11.2;q12) that fuses NONO to TFE3.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti163699. Alveolar soft-tissue sarcoma.
    319308. Translocation renal cell carcinoma.
    PharmGKBiPA36467.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 575575Transcription factor E3PRO_0000127471Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei548 – 5481Phosphoserine1 Publication
    Modified residuei556 – 5561Phosphoserine2 Publications
    Modified residuei560 – 5601Phosphoserine2 Publications
    Modified residuei568 – 5681Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated; does not affect dimerization with MITF.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP19532.
    PaxDbiP19532.
    PRIDEiP19532.

    PTM databases

    PhosphoSiteiP19532.

    Expressioni

    Tissue specificityi

    Ubiquitous in fetal and adult tissues.

    Gene expression databases

    ArrayExpressiP19532.
    BgeeiP19532.
    CleanExiHS_TFE3.
    GenevestigatoriP19532.

    Organism-specific databases

    HPAiHPA023881.

    Interactioni

    Subunit structurei

    Homodimer and heterodimer; with TFEB or MITF.

    Protein-protein interaction databases

    BioGridi112888. 22 interactions.
    IntActiP19532. 1 interaction.
    STRINGi9606.ENSP00000314129.

    Structurei

    3D structure databases

    ProteinModelPortaliP19532.
    SMRiP19532. Positions 347-437.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini346 – 39954bHLHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni260 – 27112Strong transcription activation domainSequence AnalysisAdd
    BLAST
    Regioni409 – 43022Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MiT/TFE family.Curated
    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG251286.
    HOGENOMiHOG000231368.
    HOVERGENiHBG006768.
    KOiK09105.
    OMAiPGTATFH.
    OrthoDBiEOG72G182.
    PhylomeDBiP19532.
    TreeFamiTF317174.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    InterProiIPR011598. bHLH_dom.
    IPR021802. bHLH_ZIP_TF_MiT/TFE.
    IPR024100. TFE3.
    [Graphical view]
    PANTHERiPTHR10014:SF37. PTHR10014:SF37. 1 hit.
    PfamiPF11851. DUF3371. 1 hit.
    PF00010. HLH. 1 hit.
    [Graphical view]
    SMARTiSM00353. HLH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    PROSITEiPS50888. BHLH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19532-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHAAEPARD GVEASAEGPR AVFVLLEERR PADSAQLLSL NSLLPESGIV    50
    ADIELENVLD PDSFYELKSQ PLPLRSSLPI SLQATPATPA TLSASSSAGG 100
    SRTPAMSSSS SSRVLLRQQL MRAQAQEQER RERREQAAAA PFPSPAPASP 150
    AISVVGVSAG GHTLSRPPPA QVPREVLKVQ THLENPTRYH LQQARRQQVK 200
    QYLSTTLGPK LASQALTPPP GPASAQPLPA PEAAHTTGPT GSAPNSPMAL 250
    LTIGSSSEKE IDDVIDEIIS LESSYNDEML SYLPGGTTGL QLPSTLPVSG 300
    NLLDVYSSQG VATPAITVSN SCPAELPNIK REISETEAKA LLKERQKKDN 350
    HNLIERRRRF NINDRIKELG TLIPKSSDPE MRWNKGTILK ASVDYIRKLQ 400
    KEQQRSKDLE SRQRSLEQAN RSLQLRIQEL ELQAQIHGLP VPPTPGLLSL 450
    ATTSASDSLK PEQLDIEEEG RPGAATFHVG GGPAQNAPHQ QPPAPPSDAL 500
    LDLHFPSDHL GDLGDPFHLG LEDILMEEEE GVVGGLSGGA LSPLRAASDP 550
    LLSSVSPAVS KASSRRSSFS MEEES 575
    Length:575
    Mass (Da):61,521
    Last modified:November 13, 2007 - v4
    Checksum:iEF1F11AB624C6BE1
    GO

    Sequence cautioni

    The sequence CAA35714.1 differs from that shown. Reason: Frameshift at position 557.
    The sequence CAA65800.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti172 – 1721V → M in CAA65800. (PubMed:8872474)Curated
    Sequence conflicti219 – 2191P → S in CAA65800. (PubMed:8872474)Curated
    Sequence conflicti222 – 2221P → K in CAA35714. (PubMed:2338243)Curated
    Sequence conflicti229 – 2291P → L in CAA65800. (PubMed:8872474)Curated
    Sequence conflicti443 – 4431P → G in CAA35714. (PubMed:2338243)Curated
    Sequence conflicti455 – 4551A → T in CAA65800. (PubMed:8872474)Curated
    Sequence conflicti455 – 4551A → T in CAA35714. (PubMed:2338243)Curated
    Sequence conflicti475 – 4751A → R in CAA35714. (PubMed:2338243)Curated
    Sequence conflicti575 – 5751S → M in CAA65800. (PubMed:8872474)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961S → C.
    Corresponds to variant rs5953258 [ dbSNP | Ensembl ].
    VAR_027501
    Natural varianti313 – 3131T → A.
    Corresponds to variant rs3027470 [ dbSNP | Ensembl ].
    VAR_027502

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96717 mRNA. Translation: CAA65478.1.
    BX572102 Genomic DNA. No translation available.
    X99721 Genomic DNA. Translation: CAA68061.1.
    X97160, X97161, X97162 Genomic DNA. Translation: CAA65800.1. Sequence problems.
    X51330 mRNA. Translation: CAA35714.1. Sequence problems.
    CCDSiCCDS14315.3.
    PIRiA34596.
    RefSeqiNP_006512.2. NM_006521.5.
    UniGeneiHs.730740.

    Genome annotation databases

    EnsembliENST00000315869; ENSP00000314129; ENSG00000068323.
    GeneIDi7030.
    KEGGihsa:7030.
    UCSCiuc004dmb.3. human.

    Polymorphism databases

    DMDMi160113240.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, 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
    X96717 mRNA. Translation: CAA65478.1 .
    BX572102 Genomic DNA. No translation available.
    X99721 Genomic DNA. Translation: CAA68061.1 .
    X97160 , X97161 , X97162 Genomic DNA. Translation: CAA65800.1 . Sequence problems.
    X51330 mRNA. Translation: CAA35714.1 . Sequence problems.
    CCDSi CCDS14315.3.
    PIRi A34596.
    RefSeqi NP_006512.2. NM_006521.5.
    UniGenei Hs.730740.

    3D structure databases

    ProteinModelPortali P19532.
    SMRi P19532. Positions 347-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112888. 22 interactions.
    IntActi P19532. 1 interaction.
    STRINGi 9606.ENSP00000314129.

    PTM databases

    PhosphoSitei P19532.

    Polymorphism databases

    DMDMi 160113240.

    Proteomic databases

    MaxQBi P19532.
    PaxDbi P19532.
    PRIDEi P19532.

    Protocols and materials databases

    DNASUi 7030.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315869 ; ENSP00000314129 ; ENSG00000068323 .
    GeneIDi 7030.
    KEGGi hsa:7030.
    UCSCi uc004dmb.3. human.

    Organism-specific databases

    CTDi 7030.
    GeneCardsi GC0XM048886.
    HGNCi HGNC:11752. TFE3.
    HPAi HPA023881.
    MIMi 314310. gene.
    neXtProti NX_P19532.
    Orphaneti 163699. Alveolar soft-tissue sarcoma.
    319308. Translocation renal cell carcinoma.
    PharmGKBi PA36467.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251286.
    HOGENOMi HOG000231368.
    HOVERGENi HBG006768.
    KOi K09105.
    OMAi PGTATFH.
    OrthoDBi EOG72G182.
    PhylomeDBi P19532.
    TreeFami TF317174.

    Miscellaneous databases

    ChiTaRSi TFE3. human.
    GeneWikii TFE3.
    GenomeRNAii 7030.
    NextBioi 27465.
    PROi P19532.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19532.
    Bgeei P19532.
    CleanExi HS_TFE3.
    Genevestigatori P19532.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    IPR021802. bHLH_ZIP_TF_MiT/TFE.
    IPR024100. TFE3.
    [Graphical view ]
    PANTHERi PTHR10014:SF37. PTHR10014:SF37. 1 hit.
    Pfami PF11851. DUF3371. 1 hit.
    PF00010. HLH. 1 hit.
    [Graphical view ]
    SMARTi SM00353. HLH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma."
      Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.
      Oncogene 15:2233-2239(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH PSF AND NONO.
    2. Clark J.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Fusion of the transcription factor TFE3 gene to a novel gene, PRCC, in t(X;1)(p11;q21)-positive papillary renal cell carcinomas."
      Weterman M.A.J., Wilbrink M., Geurts van Kessel A.
      Proc. Natl. Acad. Sci. U.S.A. 93:15294-15298(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-219, CHROMOSOMAL TRANSLOCATION WITH PRCC.
    5. "The t(X;1)(p11.2;q21.2) translocation in papillary renal cell carcinoma fuses a novel gene PRCC to the TFE3 transcription factor gene."
      Sidhar S.K., Clark J., Gill S., Hamoudi R., Crew A.J., Gwilliam R., Ross M., Linehan W.M., Birdsall S., Shipley J., Cooper C.S.
      Hum. Mol. Genet. 5:1333-1338(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-575, CHROMOSOMAL TRANSLOCATION WITH PRCC.
      Tissue: Monocyte.
    6. "TFE3: a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif."
      Beckmann H., Su L.-K., Kadesch T.
      Genes Dev. 4:167-179(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 212-575.
      Tissue: Leukemia.
    7. "Fusion of a novel gene, RCC17, to the TFE3 gene in t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas."
      Heimann P., El Housni H., Ogur G., Weterman M.A.J., Petty E.M., Vassart G.
      Cancer Res. 61:4130-4135(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH ASPSCR1.
    8. "The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses the TFE3 transcription factor gene to ASPL, a novel gene at 17q25."
      Ladanyi M., Lui M.Y., Antonescu C.R., Krause-Boehm A., Meindl A., Argani P., Healey J.H., Ueda T., Yoshikawa H., Meloni-Ehrig A., Sorensen P.H.B., Mertens F., Mandahl N., van den Berghe H., Sciot R., Dal Cin P., Bridge J.
      Oncogene 20:48-57(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH ASPSCR1, INVOLVEMENT IN ASPS.
    9. "Sumoylation of MITF and its related family members TFE3 and TFEB."
      Miller A.J., Levy C., Davis I.J., Razin E., Fisher D.E.
      J. Biol. Chem. 280:146-155(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH MITF.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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 SER-548; SER-556 AND SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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 SER-556 AND SER-568, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTFE3_HUMAN
    AccessioniPrimary (citable) accession number: P19532
    Secondary accession number(s): A8MZL6
    , Q92757, Q92758, Q99964
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 158 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. Human chromosome X
      Human chromosome X: 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