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Q99081

- HTF4_HUMAN

UniProt

Q99081 - HTF4_HUMAN

Protein

Transcription factor 12

Gene

TCF12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3').

    GO - Molecular functioni

    1. bHLH transcription factor binding Source: BHF-UCL
    2. E-box binding Source: Ensembl
    3. enhancer binding Source: BHF-UCL
    4. protein binding Source: BHF-UCL
    5. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    6. SMAD binding Source: BHF-UCL
    7. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. immune response Source: ProtInc
    2. muscle organ development Source: ProtInc
    3. positive regulation of neuron differentiation Source: Ensembl
    4. positive regulation of transcription, DNA-templated Source: Ensembl
    5. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_21402. CDO in myogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor 12
    Short name:
    TCF-12
    Alternative name(s):
    Class B basic helix-loop-helix protein 20
    Short name:
    bHLHb20
    DNA-binding protein HTF4
    E-box-binding protein
    Transcription factor HTF-4
    Gene namesi
    Name:TCF12
    Synonyms:BHLHB20, HEB, HTF4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:11623. TCF12.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. nuclear chromatin Source: BHF-UCL
    3. nucleus Source: BHF-UCL
    4. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Craniosynostosis 3 (CRS3) [MIM:615314]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti600 – 6001L → P in CRS3. 1 Publication
    VAR_070096
    Natural varianti614 – 6141Q → E in CRS3. 1 Publication
    VAR_070097

    Keywords - Diseasei

    Craniosynostosis, Disease mutation

    Organism-specific databases

    MIMi615314. phenotype.
    Orphaneti209916. Extraskeletal myxoid chondrosarcoma.
    35099. Isolated brachycephaly.
    35098. Isolated plagiocephaly.
    PharmGKBiPA36381.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 682682Transcription factor 12PRO_0000127228Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphoserine1 Publication
    Modified residuei313 – 3131Phosphothreonine1 Publication
    Modified residuei333 – 3331Phosphoserine1 Publication
    Modified residuei557 – 5571Phosphothreonine1 Publication
    Modified residuei559 – 5591Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99081.
    PaxDbiQ99081.
    PRIDEiQ99081.

    Expressioni

    Tissue specificityi

    Expressed in several tissues and cell types including skeletal muscle, thymus, and a B-cell line.

    Gene expression databases

    ArrayExpressiQ99081.
    BgeeiQ99081.
    CleanExiHS_TCF12.
    GenevestigatoriQ99081.

    Organism-specific databases

    HPAiCAB004432.
    HPA002103.

    Interactioni

    Subunit structurei

    Efficient DNA binding requires dimerization with another bHLH protein. Forms homo- or heterooligomers with myogenin, E12 and ITF2 proteins. Interacts with PTF1A. Interacts with NEUROD2 By similarity. Interacts with RUNX1T1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FOXH1O755932EBI-722877,EBI-1759806

    Protein-protein interaction databases

    BioGridi112798. 27 interactions.
    DIPiDIP-29403N.
    IntActiQ99081. 15 interactions.
    MINTiMINT-4713897.
    STRINGi9606.ENSP00000331057.

    Structurei

    Secondary structure

    1
    682
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 184
    Turni24 – 263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KNHNMR-B11-28[»]
    4JOLX-ray2.91E/F/G/H177-200[»]
    ProteinModelPortaliQ99081.
    SMRiQ99081. Positions 578-637.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99081.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini577 – 63054bHLHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 14022Leucine-zipperAdd
    BLAST
    Regioni632 – 65524Class A specific domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 2799aaTAD

    Domaini

    the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

    Sequence similaritiesi

    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG282899.
    HOGENOMiHOG000234180.
    HOVERGENiHBG003854.
    KOiK15603.
    OMAiYYSFSAT.
    OrthoDBiEOG72G16Q.
    PhylomeDBiQ99081.
    TreeFamiTF321672.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    InterProiIPR011598. bHLH_dom.
    [Graphical view]
    PfamiPF00010. HLH. 1 hit.
    [Graphical view]
    SMARTiSM00353. HLH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    PROSITEiPS50888. BHLH. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99081-1) [UniParc]FASTAAdd to Basket

    Also known as: a

    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

    MNPQQQRMAA IGTDKELSDL LDFSAMFSPP VNSGKTRPTT LGSSQFSGSG    50
    IDERGGTTSW GTSGQPSPSY DSSRGFTDSP HYSDHLNDSR LGAHEGLSPT 100
    PFMNSNLMGK TSERGSFSLY SRDTGLPGCQ SSLLRQDLGL GSPAQLSSSG 150
    KPGTAYYSFS ATSSRRRPLH DSAALDPLQA KKVRKVPPGL PSSVYAPSPN 200
    SDDFNRESPS YPSPKPPTSM FASTFFMQDG THNSSDLWSS SNGMSQPGFG 250
    GILGTSTSHM SQSSSYGNLH SHDRLSYPPH SVSPTDINTS LPPMSSFHRG 300
    STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD 350
    HTSSSFPSNP STPVGSPSPL TGTSQWPRPG GQAPSSPSYE NSLHSLQSRM 400
    EDRLDRLDDA IHVLRNHAVG PSTSLPAGHS DIHSLLGPSH NAPIGSLNSN 450
    YGGSSLVASS RSASMVGTHR EDSVSLNGNH SVLSSTVTTS STDLNHKTQE 500
    NYRGGLQSQS GTVVTTEIKT ENKEKDENLH EPPSSDDMKS DDESSQKDIK 550
    VSSRGRTSST NEDEDLNPEQ KIEREKERRM ANNARERLRV RDINEAFKEL 600
    GRMCQLHLKS EKPQTKLLIL HQAVAVILSL EQQVRERNLN PKAACLKRRE 650
    EEKVSAVSAE PPTTLPGTHP GLSETTNPMG HM 682
    Length:682
    Mass (Da):72,965
    Last modified:October 1, 1996 - v1
    Checksum:i9736113D9361D3F5
    GO
    Isoform 2 (identifier: Q99081-2) [UniParc]FASTAAdd to Basket

    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-170: Missing.
         171-193: DSAALDPLQAKKVRKVPPGLPSS → MYCAYPVPGMGSNSLMYYYNGKT

    Show »
    Length:512
    Mass (Da):55,142
    Checksum:i98AF7F83F8A2AEF4
    GO
    Isoform 3 (identifier: Q99081-3) [UniParc]FASTAAdd to Basket

    Also known as: c

    The sequence of this isoform differs from the canonical sequence as follows:
         396-396: L → LKNRVEQQLHEHLQDAMSFLKDVCE

    Show »
    Length:706
    Mass (Da):75,845
    Checksum:i75B7B4173C9B660D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti523 – 5231K → E in CAD89914. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti300 – 3001G → S.
    Corresponds to variant rs12442879 [ dbSNP | Ensembl ].
    VAR_049543
    Natural varianti600 – 6001L → P in CRS3. 1 Publication
    VAR_070096
    Natural varianti614 – 6141Q → E in CRS3. 1 Publication
    VAR_070097

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 170170Missing in isoform 2. 1 PublicationVSP_039109Add
    BLAST
    Alternative sequencei171 – 19323DSAAL…GLPSS → MYCAYPVPGMGSNSLMYYYN GKT in isoform 2. 1 PublicationVSP_039110Add
    BLAST
    Alternative sequencei396 – 3961L → LKNRVEQQLHEHLQDAMSFL KDVCE in isoform 3. 1 PublicationVSP_040024

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83233 mRNA. Translation: AAB62389.1.
    M80627 mRNA. Translation: AAA58632.1.
    AL831981 mRNA. Translation: CAD89914.1.
    BX537967 mRNA. Translation: CAD97931.1.
    AC010999 Genomic DNA. No translation available.
    AC016525 Genomic DNA. No translation available.
    AC090511 Genomic DNA. No translation available.
    AC090532 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77512.1.
    BC050556 mRNA. Translation: AAH50556.1.
    M65209 mRNA. Translation: AAC37571.1.
    BK001049 mRNA. Translation: DAA01129.1.
    CCDSiCCDS10159.1. [Q99081-1]
    CCDS10160.1. [Q99081-3]
    CCDS42042.1. [Q99081-2]
    PIRiA42121.
    RefSeqiNP_003196.1. NM_003205.3. [Q99081-1]
    NP_996919.1. NM_207036.1. [Q99081-3]
    NP_996920.1. NM_207037.1. [Q99081-3]
    NP_996921.1. NM_207038.1. [Q99081-1]
    NP_996923.1. NM_207040.1. [Q99081-2]
    UniGeneiHs.511504.

    Genome annotation databases

    EnsembliENST00000267811; ENSP00000267811; ENSG00000140262. [Q99081-1]
    ENST00000333725; ENSP00000331057; ENSG00000140262. [Q99081-3]
    ENST00000343827; ENSP00000342459; ENSG00000140262. [Q99081-2]
    ENST00000438423; ENSP00000388940; ENSG00000140262. [Q99081-3]
    ENST00000557843; ENSP00000453737; ENSG00000140262. [Q99081-1]
    GeneIDi6938.
    KEGGihsa:6938.
    UCSCiuc002aea.3. human. [Q99081-3]
    uc002aec.3. human. [Q99081-1]
    uc002aee.3. human. [Q99081-2]

    Polymorphism databases

    DMDMi1708332.

    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
    M83233 mRNA. Translation: AAB62389.1 .
    M80627 mRNA. Translation: AAA58632.1 .
    AL831981 mRNA. Translation: CAD89914.1 .
    BX537967 mRNA. Translation: CAD97931.1 .
    AC010999 Genomic DNA. No translation available.
    AC016525 Genomic DNA. No translation available.
    AC090511 Genomic DNA. No translation available.
    AC090532 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77512.1 .
    BC050556 mRNA. Translation: AAH50556.1 .
    M65209 mRNA. Translation: AAC37571.1 .
    BK001049 mRNA. Translation: DAA01129.1 .
    CCDSi CCDS10159.1. [Q99081-1 ]
    CCDS10160.1. [Q99081-3 ]
    CCDS42042.1. [Q99081-2 ]
    PIRi A42121.
    RefSeqi NP_003196.1. NM_003205.3. [Q99081-1 ]
    NP_996919.1. NM_207036.1. [Q99081-3 ]
    NP_996920.1. NM_207037.1. [Q99081-3 ]
    NP_996921.1. NM_207038.1. [Q99081-1 ]
    NP_996923.1. NM_207040.1. [Q99081-2 ]
    UniGenei Hs.511504.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KNH NMR - B 11-28 [» ]
    4JOL X-ray 2.91 E/F/G/H 177-200 [» ]
    ProteinModelPortali Q99081.
    SMRi Q99081. Positions 578-637.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112798. 27 interactions.
    DIPi DIP-29403N.
    IntActi Q99081. 15 interactions.
    MINTi MINT-4713897.
    STRINGi 9606.ENSP00000331057.

    Polymorphism databases

    DMDMi 1708332.

    Proteomic databases

    MaxQBi Q99081.
    PaxDbi Q99081.
    PRIDEi Q99081.

    Protocols and materials databases

    DNASUi 6938.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267811 ; ENSP00000267811 ; ENSG00000140262 . [Q99081-1 ]
    ENST00000333725 ; ENSP00000331057 ; ENSG00000140262 . [Q99081-3 ]
    ENST00000343827 ; ENSP00000342459 ; ENSG00000140262 . [Q99081-2 ]
    ENST00000438423 ; ENSP00000388940 ; ENSG00000140262 . [Q99081-3 ]
    ENST00000557843 ; ENSP00000453737 ; ENSG00000140262 . [Q99081-1 ]
    GeneIDi 6938.
    KEGGi hsa:6938.
    UCSCi uc002aea.3. human. [Q99081-3 ]
    uc002aec.3. human. [Q99081-1 ]
    uc002aee.3. human. [Q99081-2 ]

    Organism-specific databases

    CTDi 6938.
    GeneCardsi GC15P057210.
    HGNCi HGNC:11623. TCF12.
    HPAi CAB004432.
    HPA002103.
    MIMi 600480. gene.
    615314. phenotype.
    neXtProti NX_Q99081.
    Orphaneti 209916. Extraskeletal myxoid chondrosarcoma.
    35099. Isolated brachycephaly.
    35098. Isolated plagiocephaly.
    PharmGKBi PA36381.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282899.
    HOGENOMi HOG000234180.
    HOVERGENi HBG003854.
    KOi K15603.
    OMAi YYSFSAT.
    OrthoDBi EOG72G16Q.
    PhylomeDBi Q99081.
    TreeFami TF321672.

    Enzyme and pathway databases

    Reactomei REACT_21402. CDO in myogenesis.

    Miscellaneous databases

    ChiTaRSi TCF12. human.
    EvolutionaryTracei Q99081.
    GeneWikii TCF12.
    GenomeRNAii 6938.
    NextBioi 27145.
    PROi Q99081.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99081.
    Bgeei Q99081.
    CleanExi HS_TCF12.
    Genevestigatori Q99081.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    [Graphical view ]
    Pfami 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. "The nucleotide sequence of the human transcription factor HTF4a cDNA."
      Zhang Y., Bina M.
      DNA Seq. 2:397-403(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "HEB, a helix-loop-helix protein related to E2A and ITF2 that can modulate the DNA-binding ability of myogenic regulatory factors."
      Hu J.S., Olson E.N., Kingston R.E.
      Mol. Cell. Biol. 12:1031-1042(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Endometrium and Skeletal muscle.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 3).
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-682.
    8. "Genomic organization of human TCF12 gene and spliced mRNA variants producing isoforms of transcription factor HTF4."
      Gan T.I., Rowen L., Nesbitt R., Roe B.A., Wu H., Hu P., Yao Z., Kim U.J., O'Sickey T., Bina M.
      Cytogenet. Genome Res. 98:245-248(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE ORGANIZATION, ALTERNATIVE SPLICING.
    9. "The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity."
      Liu Y., Cheney M.D., Gaudet J.J., Chruszcz M., Lukasik S.M., Sugiyama D., Lary J., Cole J., Dauter Z., Minor W., Speck N.A., Bushweller J.H.
      Cancer Cell 9:249-260(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RUNX1T1.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
      Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
      Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-67; SER-333 AND THR-557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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-559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity."
      Park S., Chen W., Cierpicki T., Tonelli M., Cai X., Speck N.A., Bushweller J.H.
      Blood 113:3558-3567(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 11-28 IN COMPLEX WITH RUNX1T1, SUBUNIT.
    19. Cited for: VARIANTS CRS3 PRO-600 AND GLU-614.

    Entry informationi

    Entry nameiHTF4_HUMAN
    AccessioniPrimary (citable) accession number: Q99081
    Secondary accession number(s): Q7Z3D9, Q86TC1, Q86VM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 134 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3