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PAGR1_BOVIN
ID   PAGR1_BOVIN             Reviewed;         253 AA.
AC   Q1LZ80; A4FV67;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=PAXIP1-associated glutamate-rich protein 1;
DE   AltName: Full=PAXIP1-associated protein 1;
DE   AltName: Full=PTIP-associated protein 1;
GN   Name=PAGR1; Synonyms=PA1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia, and Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Its association with the histone methyltransferase MLL2/MLL3
CC       complex is suggesting a role in epigenetic transcriptional activation.
CC       However, in association with PAXIP1/PTIP is proposed to function at
CC       least in part independently of the MLL2/MLL3 complex. Proposed to be
CC       recruited by PAXIP1 to sites of DNA damage where the PAGR1:PAXIP1
CC       complex is required for cell survival in response to DNA damage
CC       independently of the MLL2/MLL3 complex. However, its function in DNA
CC       damage has been questioned. During immunoglobulin class switching in
CC       activated B-cells is involved in transcription regulation of downstream
CC       switch regions at the immunoglobulin heavy-chain (Igh) locus
CC       independently of the MLL2/MLL3 complex. Involved in both estrogen
CC       receptor-regulated gene transcription and estrogen-stimulated G1/S
CC       cell-cycle transition. Acts as transcriptional cofactor for nuclear
CC       hormone receptors. Inhibits the induction properties of several steroid
CC       receptors such as NR3C1, AR and PPARG; the mechanism of inhibition
CC       appears to be gene-dependent. {ECO:0000250|UniProtKB:Q99L02,
CC       ECO:0000250|UniProtKB:Q9BTK6}.
CC   -!- SUBUNIT: Component of the KMT2 family MLL2/MLL3 complex, at least
CC       composed of the histone methyltransferases KMT2D and/or KMT2C, the
CC       common complex subunits ASH2L, RBBP5, WDR5 and DPY30, and the complex
CC       type-specific subunits PAXIP1/PTIP, PAGR1, NCOA6 and KDM6A; PAXIP1 is
CC       required for the association with the MLL2/MLL3 complex (By
CC       similarity). Forms a constitutive complex with PAXIP1/PTIP
CC       independently of the MLL2/MLL3 complex. Interacts with NCOA1, ESR1,
CC       NR3C1, AR. {ECO:0000250|UniProtKB:Q99L02,
CC       ECO:0000250|UniProtKB:Q9BTK6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99L02,
CC       ECO:0000250|UniProtKB:Q9BTK6}.
CC   -!- CAUTION: The terminology of MLL proteins in mammalia is not consistent
CC       also concerning the terminology of MLL protein-containing complexes.
CC       The decribed MLL2/MLL3 complex is commonly described as MLL3/MLL4
CC       complex in literature. {ECO:0000305}.
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DR   EMBL; BC116156; AAI16157.1; -; mRNA.
DR   EMBL; BC118095; AAI18096.1; -; mRNA.
DR   EMBL; BC123802; AAI23803.1; -; mRNA.
DR   RefSeq; NP_001069100.1; NM_001075632.1.
DR   RefSeq; XP_005224957.1; XM_005224900.3.
DR   RefSeq; XP_015315856.1; XM_015460370.1.
DR   AlphaFoldDB; Q1LZ80; -.
DR   STRING; 9913.ENSBTAP00000014478; -.
DR   PaxDb; Q1LZ80; -.
DR   PRIDE; Q1LZ80; -.
DR   Ensembl; ENSBTAT00000014478; ENSBTAP00000014478; ENSBTAG00000010904.
DR   Ensembl; ENSBTAT00000045230; ENSBTAP00000042638; ENSBTAG00000010904.
DR   GeneID; 513650; -.
DR   KEGG; bta:513650; -.
DR   CTD; 79447; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010904; -.
DR   VGNC; VGNC:97294; PAGR1.
DR   eggNOG; ENOG502S0T8; Eukaryota.
DR   GeneTree; ENSGT00390000016049; -.
DR   HOGENOM; CLU_088613_1_0_1; -.
DR   InParanoid; Q1LZ80; -.
DR   OMA; QAWMPPP; -.
DR   OrthoDB; 1630689at2759; -.
DR   TreeFam; TF326621; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000010904; Expressed in anterior segment of eyeball and 106 other tissues.
DR   GO; GO:0044666; C:MLL3/4 complex; IBA:GO_Central.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR   GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IBA:GO_Central.
DR   GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   InterPro; IPR028213; PA1.
DR   PANTHER; PTHR28467; PTHR28467; 1.
DR   Pfam; PF15364; PAXIP1_C; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..253
FT                   /note="PAXIP1-associated glutamate-rich protein 1"
FT                   /id="PRO_0000248333"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..160
FT                   /note="Sufficient for interaction with NCOA1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTK6"
FT   REGION          128..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..253
FT                   /note="Sufficient for interaction with ESR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTK6"
FT   COMPBIAS        72..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         138
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5M865"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5M865"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5M865"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5M865"
SQ   SEQUENCE   253 AA;  27784 MW;  AC1F399520B92B42 CRC64;
     MSLVRGHGDI AATTAAPLSE EGEVTSGLQA LAVEDTGGPS ASADQAEEEG EGGREEAEHE
     GSGAEEVQGE APSPEGEERA KGESEDWCVP CSDEEVELPA DGQSWMPPPS EIQRLYELLA
     AHGTLELQAE ILPRRPPTPE AQSEEERSDE EPEAKEEEEE KPHMPTEFDF DDEPTTPKDS
     LIDRRRTPGS SARSQKREAR LDKVLSDMKR HKKLEEQILR TGRDLFSLDS EDASPASPPL
     RSSGSLFPRQ RKY
 
 
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