TCP4_MACFA
ID TCP4_MACFA Reviewed; 127 AA.
AC Q4R947;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Activated RNA polymerase II transcriptional coactivator p15;
DE AltName: Full=SUB1 homolog;
GN Name=SUB1; Synonyms=RPO2TC1; ORFNames=QtsA-10726;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168249; BAE00374.1; -; mRNA.
DR RefSeq; NP_001272042.1; NM_001285113.1.
DR RefSeq; XP_015306641.1; XM_015451155.1.
DR RefSeq; XP_015306642.1; XM_015451156.1.
DR AlphaFoldDB; Q4R947; -.
DR BMRB; Q4R947; -.
DR SMR; Q4R947; -.
DR STRING; 9541.XP_005556712.1; -.
DR Ensembl; ENSMFAT00000078022; ENSMFAP00000049298; ENSMFAG00000062564.
DR GeneID; 101926874; -.
DR KEGG; mcf:101926874; -.
DR CTD; 10923; -.
DR VEuPathDB; HostDB:ENSMFAG00000040728; -.
DR eggNOG; KOG2712; Eukaryota.
DR GeneTree; ENSGT00390000008802; -.
DR OMA; WMNPDGE; -.
DR OrthoDB; 1616655at2759; -.
DR Proteomes; UP000233100; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:InterPro.
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 2: Evidence at transcript 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_0000291883"
FT REGION 1..64
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 43..63
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:0000250|UniProtKB:P53999"
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:0000250|UniProtKB:P53999"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53999"
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"
SQ SEQUENCE 127 AA; 14395 MW; 0DAE0CAAAD5E4E15 CRC64;
MPKSKELVSS SSSGSDSDSE VDKKLKRKKQ VAPEKPVKKQ KTGETSRALS SSKQSSSSRD
DNMFQIGKMR YVSVRDFKGK VLIDIREYWM DPEGEMKPGR KGISLNPEQW SQLKEQISDI
DDAVRKL
