TCP4_RAT
ID TCP4_RAT Reviewed; 127 AA.
AC Q63396; Q5M805;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Activated RNA polymerase II transcriptional coactivator p15;
DE AltName: Full=Positive cofactor 4;
DE Short=PC4;
DE AltName: Full=SUB1 homolog;
DE AltName: Full=p14;
GN Name=Sub1; Synonyms=Pc4, Rpo2tc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-127.
RX PubMed=6208900; DOI=10.1016/0006-291x(84)90931-8;
RA Soma G., Kitahara N., Andoh T.;
RT "Molecular cloning and characterization of a cDNA clone for a protein
RT specifically expressed in embryo as well as in a chemically induced
RT pancreatic B cell tumor of rat.";
RL Biochem. Biophys. Res. Commun. 124:164-171(1984).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-17 AND SER-19, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: General coactivator that functions cooperatively with TAFs
CC and mediates functional interactions between upstream activators and
CC the general transcriptional machinery. May be involved in stabilizing
CC the multiprotein transcription complex. Binds single-stranded DNA. Also
CC binds, in vitro, non-specifically to double-stranded DNA (ds DNA) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with CSTF2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Activity is controlled by protein kinases that target the
CC regulatory region. Phosphorylation inactivates both ds DNA-binding and
CC cofactor function, but does not affect binding to ssDNA (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transcriptional coactivator PC4 family.
CC {ECO:0000305}.
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DR EMBL; BC088346; AAH88346.1; -; mRNA.
DR EMBL; K02816; AAA41758.1; -; mRNA.
DR PIR; A23063; A23063.
DR RefSeq; NP_001009618.1; NM_001009618.1.
DR RefSeq; XP_006232105.1; XM_006232043.3.
DR AlphaFoldDB; Q63396; -.
DR SMR; Q63396; -.
DR BioGRID; 251393; 2.
DR IntAct; Q63396; 2.
DR MINT; Q63396; -.
DR STRING; 10116.ENSRNOP00000067467; -.
DR iPTMnet; Q63396; -.
DR PhosphoSitePlus; Q63396; -.
DR jPOST; Q63396; -.
DR PaxDb; Q63396; -.
DR PRIDE; Q63396; -.
DR Ensembl; ENSRNOT00000113169; ENSRNOP00000092370; ENSRNOG00000067555.
DR GeneID; 192269; -.
DR KEGG; rno:192269; -.
DR CTD; 10923; -.
DR RGD; 621582; Sub1.
DR VEuPathDB; HostDB:ENSRNOG00000050563; -.
DR eggNOG; KOG2712; Eukaryota.
DR GeneTree; ENSGT00390000008802; -.
DR HOGENOM; CLU_104273_1_1_1; -.
DR InParanoid; Q63396; -.
DR OMA; WMNPDGE; -.
DR OrthoDB; 1616655at2759; -.
DR PhylomeDB; Q63396; -.
DR TreeFam; TF313859; -.
DR PRO; PR:Q63396; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000050563; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; Q63396; RN.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003678; F:DNA helicase activity; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:RGD.
DR GO; GO:0051053; P:negative regulation of DNA metabolic process; ISO:RGD.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; ISO:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
DR Gene3D; 2.30.31.10; -; 1.
DR InterPro; IPR003173; PC4_C.
DR InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR InterPro; IPR045125; Sub1/Tcp4-like.
DR PANTHER; PTHR13215; PTHR13215; 1.
DR Pfam; PF02229; PC4; 1.
DR SUPFAM; SSF54447; SSF54447; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..127
FT /note="Activated RNA polymerase II transcriptional
FT coactivator p15"
FT /id="PRO_0000045173"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..50
FT /note="Regulatory"
FT /evidence="ECO:0000250"
FT REGION 77..101
FT /note="Interaction with ssDNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 50..51
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11031"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P53999"
FT CONFLICT 43
FT /note="G -> S (in Ref. 2; AAA41758)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="G -> R (in Ref. 2; AAA41758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 14441 MW; 7B2B8CF34A54105C CRC64;
MPKSKELVSS SSSGSDSDSE VEKKLKRKKQ VVPEKPVKKQ KPGESSRALA SSKQSSSSRD
DNMFQIGKMR YVSVRDFKGK ILIDIREYWM DSEGEMKPGR KGISLNMEQW SQLKEQISDI
DDAVRKL
