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P53999

- TCP4_HUMAN

UniProt

P53999 - TCP4_HUMAN

Protein

Activated RNA polymerase II transcriptional coactivator p15

Gene

SUB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA).7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei50 – 512Cleavage

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. single-stranded DNA binding Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activated RNA polymerase II transcriptional coactivator p15
    Alternative name(s):
    Positive cofactor 4
    Short name:
    PC4
    SUB1 homolog
    p14
    Gene namesi
    Name:SUB1
    Synonyms:PC4, RPO2TC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:19985. SUB1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleolus Source: HPA
    3. nucleus Source: HPA
    4. transcription factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi68 – 681K → G: Reduced ssDNA binding. 1 Publication
    Mutagenesisi75 – 751R → G: Reduced ssDNA binding. 1 Publication
    Mutagenesisi77 – 804FKGK → AGG: Loss of ssDNA binding.
    Mutagenesisi86 – 861R → G: Loss of ssDNA binding. 1 Publication
    Mutagenesisi101 – 1011K → G: Loss of ssDNA binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670858.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 127126Activated RNA polymerase II transcriptional coactivator p15PRO_0000215944Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine1 Publication
    Modified residuei13 – 131Phosphoserine1 Publication
    Modified residuei15 – 151Phosphoserine1 Publication
    Modified residuei17 – 171Phosphoserine2 Publications
    Modified residuei19 – 191Phosphoserine2 Publications
    Modified residuei35 – 351N6-acetyllysine1 Publication
    Modified residuei53 – 531N6-acetyllysineBy similarity
    Modified residuei68 – 681N6-acetyllysine1 Publication
    Modified residuei118 – 1181Phosphoserine3 Publications

    Post-translational modificationi

    Activity is controlled by protein kinases that target the regulatory region. Phosphorylation inactivates both ds DNA-binding and cofactor function, but does not affect binding to ssDNA. Seems to be phosphorylated in vivo by CK2 in at least 7 sites in the N-terminal Ser-rich region.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP53999.
    PaxDbiP53999.
    PeptideAtlasiP53999.
    PRIDEiP53999.

    PTM databases

    PhosphoSiteiP53999.

    Expressioni

    Gene expression databases

    ArrayExpressiP53999.
    BgeeiP53999.
    CleanExiHS_SUB1.
    GenevestigatoriP53999.

    Organism-specific databases

    HPAiCAB015351.
    HPA001311.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CSTF2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSTF2P33240-13EBI-998260,EBI-711374
    Rep68P031323EBI-998260,EBI-7387242From a different organism.

    Protein-protein interaction databases

    BioGridi116127. 32 interactions.
    DIPiDIP-29044N.
    IntActiP53999. 10 interactions.
    MINTiMINT-138673.
    STRINGi9606.ENSP00000265073.

    Structurei

    Secondary structure

    1
    127
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi63 – 675
    Beta strandi70 – 778
    Beta strandi80 – 9011
    Beta strandi92 – 943
    Beta strandi96 – 10510
    Helixi107 – 12620

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PCFX-ray1.74A/B/C/D/E/F/G/H63-127[»]
    2C62X-ray1.74A/B63-127[»]
    2PHENMR-A/B63-127[»]
    ProteinModelPortaliP53999.
    SMRiP53999. Positions 63-127.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53999.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 5049RegulatoryAdd
    BLAST
    Regioni77 – 10125Interaction with ssDNAAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 1916Ser-richAdd
    BLAST
    Compositional biasi23 – 5331Lys-richAdd
    BLAST
    Compositional biasi50 – 589Ser-rich

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG299238.
    HOVERGENiHBG028243.
    InParanoidiP53999.
    OMAiREYWMNQ.
    OrthoDBiEOG76MKBV.
    PhylomeDBiP53999.
    TreeFamiTF313859.

    Family and domain databases

    Gene3Di2.30.31.10. 1 hit.
    InterProiIPR003173. PC4.
    IPR009044. ssDNA-bd_transcriptional_reg.
    [Graphical view]
    PfamiPF02229. PC4. 1 hit.
    [Graphical view]
    SUPFAMiSSF54447. SSF54447. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P53999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKSKELVSS SSSGSDSDSE VDKKLKRKKQ VAPEKPVKKQ KTGETSRALS    50
    SSKQSSSSRD DNMFQIGKMR YVSVRDFKGK VLIDIREYWM DPEGEMKPGR 100
    KGISLNPEQW SQLKEQISDI DDAVRKL 127
    Length:127
    Mass (Da):14,395
    Last modified:January 23, 2007 - v3
    Checksum:i0DAE0CAAAD5E4E15
    GO

    Mass spectrometryi

    Molecular mass is 14266±4 Da from positions 2 - 127. Determined by MALDI. 1 Publication
    Molecular mass is 14263 Da from positions 2 - 127. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111S → G.1 Publication
    Corresponds to variant rs17850527 [ dbSNP | Ensembl ].
    VAR_032870

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79805 mRNA. Translation: CAA56200.1.
    U12979 mRNA. Translation: AAA20980.1.
    BC009610 mRNA. Translation: AAH09610.1.
    BC010537 mRNA. Translation: AAH10537.1.
    BC018189 mRNA. Translation: AAH18189.1.
    BC022339 mRNA. Translation: AAH22339.1.
    CCDSiCCDS3897.1.
    PIRiA54670.
    RefSeqiNP_006704.3. NM_006713.3.
    UniGeneiHs.229641.

    Genome annotation databases

    EnsembliENST00000265073; ENSP00000265073; ENSG00000113387.
    ENST00000502897; ENSP00000427100; ENSG00000113387.
    ENST00000506237; ENSP00000422078; ENSG00000113387.
    ENST00000512913; ENSP00000422806; ENSG00000113387.
    ENST00000515355; ENSP00000426850; ENSG00000113387.
    GeneIDi10923.
    KEGGihsa:10923.
    UCSCiuc003jhs.2. human.

    Polymorphism databases

    DMDMi1709514.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79805 mRNA. Translation: CAA56200.1 .
    U12979 mRNA. Translation: AAA20980.1 .
    BC009610 mRNA. Translation: AAH09610.1 .
    BC010537 mRNA. Translation: AAH10537.1 .
    BC018189 mRNA. Translation: AAH18189.1 .
    BC022339 mRNA. Translation: AAH22339.1 .
    CCDSi CCDS3897.1.
    PIRi A54670.
    RefSeqi NP_006704.3. NM_006713.3.
    UniGenei Hs.229641.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PCF X-ray 1.74 A/B/C/D/E/F/G/H 63-127 [» ]
    2C62 X-ray 1.74 A/B 63-127 [» ]
    2PHE NMR - A/B 63-127 [» ]
    ProteinModelPortali P53999.
    SMRi P53999. Positions 63-127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116127. 32 interactions.
    DIPi DIP-29044N.
    IntActi P53999. 10 interactions.
    MINTi MINT-138673.
    STRINGi 9606.ENSP00000265073.

    PTM databases

    PhosphoSitei P53999.

    Polymorphism databases

    DMDMi 1709514.

    Proteomic databases

    MaxQBi P53999.
    PaxDbi P53999.
    PeptideAtlasi P53999.
    PRIDEi P53999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265073 ; ENSP00000265073 ; ENSG00000113387 .
    ENST00000502897 ; ENSP00000427100 ; ENSG00000113387 .
    ENST00000506237 ; ENSP00000422078 ; ENSG00000113387 .
    ENST00000512913 ; ENSP00000422806 ; ENSG00000113387 .
    ENST00000515355 ; ENSP00000426850 ; ENSG00000113387 .
    GeneIDi 10923.
    KEGGi hsa:10923.
    UCSCi uc003jhs.2. human.

    Organism-specific databases

    CTDi 10923.
    GeneCardsi GC05P032622.
    HGNCi HGNC:19985. SUB1.
    HPAi CAB015351.
    HPA001311.
    MIMi 600503. gene.
    neXtProti NX_P53999.
    PharmGKBi PA142670858.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299238.
    HOVERGENi HBG028243.
    InParanoidi P53999.
    OMAi REYWMNQ.
    OrthoDBi EOG76MKBV.
    PhylomeDBi P53999.
    TreeFami TF313859.

    Miscellaneous databases

    ChiTaRSi SUB1. human.
    EvolutionaryTracei P53999.
    GeneWikii SUB1.
    GenomeRNAii 10923.
    NextBioi 41499.
    PROi P53999.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53999.
    Bgeei P53999.
    CleanExi HS_SUB1.
    Genevestigatori P53999.

    Family and domain databases

    Gene3Di 2.30.31.10. 1 hit.
    InterProi IPR003173. PC4.
    IPR009044. ssDNA-bd_transcriptional_reg.
    [Graphical view ]
    Pfami PF02229. PC4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54447. SSF54447. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A novel mediator of class II gene transcription with homology to viral immediate-early transcriptional regulators."
      Kretzschmar M., Kaiser K., Lottspeich F., Meisterernst M.
      Cell 78:525-534(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
    2. "Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes."
      Ge H., Roeder R.G.
      Cell 78:513-523(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11 AND 81-97, FUNCTION.
    3. "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], VARIANT GLY-11.
      Tissue: Bone marrow, Cervix, Lung and Prostate.
    4. "Phosphorylation negatively regulates the function of coactivator PC4."
      Ge H., Zhao Y., Chait B.T., Roeder R.G.
      Proc. Natl. Acad. Sci. U.S.A. 91:12691-12695(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MASS SPECTROMETRY.
    5. "The coactivator p15 (PC4) initiates transcriptional activation during TFIIA-TFIID-promoter complex formation."
      Kaiser K., Stelzer G., Meisterernst M.
      EMBO J. 14:3520-3527(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    6. "A dynamic model for PC4 coactivator function in RNA polymerase II transcription."
      Malik S., Guermah M., Roeder R.G.
      Proc. Natl. Acad. Sci. U.S.A. 95:2192-2197(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY CK2.
    7. "Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination."
      Calvo O., Manley J.L.
      Mol. Cell 7:1013-1023(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSTF2.
    8. "Gradual phosphorylation regulates PC4 coactivator function."
      Jonker H.R.A., Wechselberger R.W., Pinkse M., Kaptein R., Folkers G.E.
      FEBS J. 273:1430-1444(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY, FUNCTION, DNA-BINDING, PHOSPHORYLATION AT SER-11; SER-13; SER-15; SER-17 AND SER-19.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-35 AND LYS-68, 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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site."
      Brandsen J., Werten S., van der Vliet P.C., Meisterernst M., Kroon J., Gros P.
      Nat. Struct. Biol. 4:900-903(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127, FUNCTION, SUBUNIT.
    17. "The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions."
      Jonker H.R.A., Wechselberger R.W., Boelens R., Kaptein R., Folkers G.E.
      Biochemistry 45:5067-5081(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, FUNCTION, MUTAGENESIS OF LYS-68; ARG-75; 77-PHE--LYS-80; ARG-86 AND LYS-101.
    18. "A global transcription cofactor bound to juxtaposed strands of unwound DNA."
      Werten S., Moras D.
      Nat. Struct. Biol. 13:181-182(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127 IN COMPLEX WITH SINGLE-STRANDED DNA, SUBUNIT.

    Entry informationi

    Entry nameiTCP4_HUMAN
    AccessioniPrimary (citable) accession number: P53999
    Secondary accession number(s): Q96L29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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