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P11031

- TCP4_MOUSE

UniProt

P11031 - TCP4_MOUSE

Protein

Activated RNA polymerase II transcriptional coactivator p15

Gene

Sub1

Organism
Mus musculus (Mouse)
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).

    Sites

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

    GO - Molecular functioni

    1. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    2. single-stranded DNA binding Source: Ensembl
    3. transcription coactivator activity Source: Ensembl

    GO - Biological processi

    1. positive regulation of transcription from RNA polymerase II promoter Source: GOC

    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
    Single-stranded DNA-binding protein p9
    p14
    Gene namesi
    Name:Sub1
    Synonyms:Pc4, Rpo2tc1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:104811. Sub1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleolus Source: Ensembl
    2. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 127126Activated RNA polymerase II transcriptional coactivator p15PRO_0000023286Add
    BLAST

    Amino acid modifications

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

    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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11031.
    PaxDbiP11031.
    PRIDEiP11031.

    PTM databases

    PhosphoSiteiP11031.

    Expressioni

    Gene expression databases

    BgeeiP11031.
    CleanExiMM_SUB1.
    GenevestigatoriP11031.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CSTF2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202999. 2 interactions.
    IntActiP11031. 2 interactions.
    MINTiMINT-4137265.

    Structurei

    3D structure databases

    ProteinModelPortaliP11031.
    SMRiP11031. Positions 63-127.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 1916Ser-richAdd
    BLAST
    Compositional biasi23 – 5331Lys-richAdd
    BLAST
    Compositional biasi51 – 588Ser-rich

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG299238.
    GeneTreeiENSGT00390000008802.
    HOGENOMiHOG000239157.
    HOVERGENiHBG028243.
    InParanoidiP11031.
    OMAiREYWMNQ.
    OrthoDBiEOG76MKBV.
    PhylomeDBiP11031.
    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.

    P11031-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKSKELVSS SSSGSDSDSE VEKKLKRKKQ AVPEKPVKKQ KPGETSRALA    50
    SSKQSSSSRD DNMFQIGKMR YVSVRDFKGK ILIDIREYWM DSEGEMKPGR 100
    KGISLNMEQW SQLKEQISDI DDAVRKL 127
    Length:127
    Mass (Da):14,427
    Last modified:January 23, 2007 - v3
    Checksum:i12D58716F40FEB1C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461S → P in BAE27090. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03750 mRNA. Translation: AAA37317.1.
    AK048371 mRNA. Translation: BAC33314.1.
    AK049260 mRNA. Translation: BAC33642.1.
    AK132021 mRNA. Translation: BAE20946.1.
    AK146335 mRNA. Translation: BAE27090.1.
    AK151734 mRNA. Translation: BAE30649.1.
    AK154114 mRNA. Translation: BAE32384.1.
    BC010967 mRNA. Translation: AAH10967.1.
    CCDSiCCDS27387.1.
    PIRiA28084.
    RefSeqiNP_035424.1. NM_011294.3.
    XP_006520105.1. XM_006520042.1.
    UniGeneiMm.41746.

    Genome annotation databases

    EnsembliENSMUST00000022816; ENSMUSP00000022816; ENSMUSG00000022205.
    ENSMUST00000110504; ENSMUSP00000106130; ENSMUSG00000022205.
    GeneIDi20024.
    KEGGimmu:20024.
    UCSCiuc007vhj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03750 mRNA. Translation: AAA37317.1 .
    AK048371 mRNA. Translation: BAC33314.1 .
    AK049260 mRNA. Translation: BAC33642.1 .
    AK132021 mRNA. Translation: BAE20946.1 .
    AK146335 mRNA. Translation: BAE27090.1 .
    AK151734 mRNA. Translation: BAE30649.1 .
    AK154114 mRNA. Translation: BAE32384.1 .
    BC010967 mRNA. Translation: AAH10967.1 .
    CCDSi CCDS27387.1.
    PIRi A28084.
    RefSeqi NP_035424.1. NM_011294.3.
    XP_006520105.1. XM_006520042.1.
    UniGenei Mm.41746.

    3D structure databases

    ProteinModelPortali P11031.
    SMRi P11031. Positions 63-127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202999. 2 interactions.
    IntActi P11031. 2 interactions.
    MINTi MINT-4137265.

    PTM databases

    PhosphoSitei P11031.

    Proteomic databases

    MaxQBi P11031.
    PaxDbi P11031.
    PRIDEi P11031.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022816 ; ENSMUSP00000022816 ; ENSMUSG00000022205 .
    ENSMUST00000110504 ; ENSMUSP00000106130 ; ENSMUSG00000022205 .
    GeneIDi 20024.
    KEGGi mmu:20024.
    UCSCi uc007vhj.1. mouse.

    Organism-specific databases

    CTDi 10923.
    MGIi MGI:104811. Sub1.

    Phylogenomic databases

    eggNOGi NOG299238.
    GeneTreei ENSGT00390000008802.
    HOGENOMi HOG000239157.
    HOVERGENi HBG028243.
    InParanoidi P11031.
    OMAi REYWMNQ.
    OrthoDBi EOG76MKBV.
    PhylomeDBi P11031.
    TreeFami TF313859.

    Miscellaneous databases

    ChiTaRSi SUB1. mouse.
    NextBioi 297547.
    PROi P11031.
    SOURCEi Search...

    Gene expression databases

    Bgeei P11031.
    CleanExi MM_SUB1.
    Genevestigatori P11031.

    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. "Identification of a novel 9-kDa polypeptide from nuclear extracts. DNA binding properties, primary structure, and in vitro expression."
      Ballard D.W., Philbrick W.M., Bothwell A.L.M.
      J. Biol. Chem. 263:8450-8457(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-81 AND 108-127, PROTEOLYTIC PROCESSING, DNA-BINDING.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J, DBA/2 and NOD.
      Tissue: Bone marrow.
    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].
      Strain: Czech II.
      Tissue: Mammary gland.
    4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTCP4_MOUSE
    AccessioniPrimary (citable) accession number: P11031
    Secondary accession number(s): Q3UJR5, Q543N2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3