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Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14)

 TCP4_RAT                Reviewed;         127 AA.
Q63396; Q5M805;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 125.
RecName: Full=Activated RNA polymerase II transcriptional coactivator p15;
AltName: Full=Positive cofactor 4;
Short=PC4;
AltName: Full=SUB1 homolog;
AltName: Full=p14;
Name=Sub1; Synonyms=Pc4, Rpo2tc1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-127.
PubMed=6208900; DOI=10.1016/0006-291X(84)90931-8;
Soma G., Kitahara N., Andoh T.;
"Molecular cloning and characterization of a cDNA clone for a protein
specifically expressed in embryo as well as in a chemically induced
pancreatic B cell tumor of rat.";
Biochem. Biophys. Res. Commun. 124:164-171(1984).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-17 AND SER-19,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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) (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with CSTF2 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- SIMILARITY: Belongs to the transcriptional coactivator PC4 family.
{ECO:0000305}.
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EMBL; BC088346; AAH88346.1; -; mRNA.
EMBL; K02816; AAA41758.1; -; mRNA.
PIR; A23063; A23063.
RefSeq; NP_001009618.1; NM_001009618.1.
RefSeq; XP_006232105.1; XM_006232043.3.
UniGene; Rn.160776; -.
UniGene; Rn.8706; -.
ProteinModelPortal; Q63396; -.
SMR; Q63396; -.
BioGrid; 251393; 1.
IntAct; Q63396; 2.
MINT; Q63396; -.
STRING; 10116.ENSRNOP00000067467; -.
iPTMnet; Q63396; -.
PhosphoSitePlus; Q63396; -.
PaxDb; Q63396; -.
PRIDE; Q63396; -.
Ensembl; ENSRNOT00000074446; ENSRNOP00000067467; ENSRNOG00000050563.
GeneID; 192269; -.
KEGG; rno:192269; -.
CTD; 10923; -.
RGD; 621582; Sub1.
eggNOG; KOG2712; Eukaryota.
eggNOG; ENOG410XUB8; LUCA.
GeneTree; ENSGT00390000008802; -.
HOGENOM; HOG000239157; -.
HOVERGEN; HBG028243; -.
InParanoid; Q63396; -.
OMA; MVDIREH; -.
OrthoDB; EOG091G14VO; -.
PhylomeDB; Q63396; -.
TreeFam; TF313859; -.
PRO; PR:Q63396; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000050563; -.
Genevisible; Q63396; RN.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; ISO:RGD.
GO; GO:0033613; F:activating transcription factor binding; IEA:Ensembl.
GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific DNA binding; ISO:RGD.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
Gene3D; 2.30.31.10; -; 1.
InterPro; IPR003173; PC4.
InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
Pfam; PF02229; PC4; 1.
SUPFAM; SSF54447; SSF54447; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 127 Activated RNA polymerase II
transcriptional coactivator p15.
/FTId=PRO_0000045173.
REGION 1 50 Regulatory. {ECO:0000250}.
REGION 77 101 Interaction with ssDNA. {ECO:0000250}.
COMPBIAS 4 19 Ser-rich.
COMPBIAS 23 53 Lys-rich.
COMPBIAS 43 58 Ser-rich.
SITE 50 51 Cleavage. {ECO:0000250}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 35 35 N6-acetyllysine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11031}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 68 68 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P53999}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:P53999}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P53999}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P53999}.
CONFLICT 43 43 G -> S (in Ref. 2; AAA41758).
{ECO:0000305}.
CONFLICT 99 99 G -> R (in Ref. 2; AAA41758).
{ECO:0000305}.
SEQUENCE 127 AA; 14441 MW; 7B2B8CF34A54105C CRC64;
MPKSKELVSS SSSGSDSDSE VEKKLKRKKQ VVPEKPVKKQ KPGESSRALA SSKQSSSSRD
DNMFQIGKMR YVSVRDFKGK ILIDIREYWM DSEGEMKPGR KGISLNMEQW SQLKEQISDI
DDAVRKL


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