位置:首页 > 蛋白库 > TCP4_PONAB
TCP4_PONAB
ID   TCP4_PONAB              Reviewed;         127 AA.
AC   Q5R6D0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Activated RNA polymerase II transcriptional coactivator p15;
DE   AltName: Full=SUB1 homolog;
GN   Name=SUB1; Synonyms=RPO2TC1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR860561; CAH92686.1; -; mRNA.
DR   RefSeq; NP_001126574.1; NM_001133102.1.
DR   AlphaFoldDB; Q5R6D0; -.
DR   BMRB; Q5R6D0; -.
DR   SMR; Q5R6D0; -.
DR   STRING; 9601.ENSPPYP00000017177; -.
DR   Ensembl; ENSPPYT00000017876; ENSPPYP00000017177; ENSPPYG00000015379.
DR   GeneID; 100173565; -.
DR   KEGG; pon:100173565; -.
DR   CTD; 10923; -.
DR   eggNOG; KOG2712; Eukaryota.
DR   GeneTree; ENSGT00390000008802; -.
DR   HOGENOM; CLU_104273_1_1_1; -.
DR   InParanoid; Q5R6D0; -.
DR   OMA; WMNPDGE; -.
DR   OrthoDB; 1525616at2759; -.
DR   TreeFam; TF313859; -.
DR   Proteomes; UP000001595; Chromosome 5.
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_0000291884"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024