PAGR1_RAT
ID PAGR1_RAT Reviewed; 253 AA.
AC Q5M865;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
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;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137; SER-142; SER-147 AND
RP SER-236, AND 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: 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 subunits ASH2L, RBBP5, WDR5 and DPY30, and the complex type-
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5M865-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5M865-2; Sequence=VSP_020244;
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; AABR03004725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088203; AAH88203.1; -; mRNA.
DR RefSeq; NP_001013923.1; NM_001013901.1. [Q5M865-2]
DR AlphaFoldDB; Q5M865; -.
DR STRING; 10116.ENSRNOP00000027392; -.
DR iPTMnet; Q5M865; -.
DR PhosphoSitePlus; Q5M865; -.
DR PaxDb; Q5M865; -.
DR PRIDE; Q5M865; -.
DR GeneID; 293500; -.
DR KEGG; rno:293500; -.
DR UCSC; RGD:1305592; rat. [Q5M865-1]
DR CTD; 79447; -.
DR RGD; 1305592; RGD1305592.
DR VEuPathDB; HostDB:ENSRNOG00000029366; -.
DR eggNOG; ENOG502S0T8; Eukaryota.
DR HOGENOM; CLU_088613_1_0_1; -.
DR InParanoid; Q5M865; -.
DR OMA; QAWMPPP; -.
DR OrthoDB; 1630689at2759; -.
DR PhylomeDB; Q5M865; -.
DR TreeFam; TF326621; -.
DR PRO; PR:Q5M865; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020217; Expressed in cerebellum and 19 other tissues.
DR Genevisible; Q5M865; RN.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:RGD.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD.
DR GO; GO:0060717; P:chorion development; ISO:RGD.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0071557; P:histone H3-K27 demethylation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; ISO:RGD.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; ISO:RGD.
DR InterPro; IPR028213; PA1.
DR PANTHER; PTHR28467; PTHR28467; 1.
DR Pfam; PF15364; PAXIP1_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..253
FT /note="PAXIP1-associated glutamate-rich protein 1"
FT /id="PRO_0000248336"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..159
FT /note="Sufficient for interaction with NCOA1"
FT /evidence="ECO:0000250|UniProtKB:Q9BTK6"
FT REGION 126..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..253
FT /note="Sufficient for interaction with ESR1"
FT /evidence="ECO:0000250|UniProtKB:Q9BTK6"
FT COMPBIAS 48..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 161..253
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020244"
SQ SEQUENCE 253 AA; 27683 MW; BF5C8549355D152C CRC64;
MSLALGHGTI AGSTAAPLSE EGEVTSGLQA LAVEDTGGPS VSASKAEEEG KGSQEEAGRE
ASRAEEALEA SSAVSDERAE GESEDWCVPC SDEEVELPAN GQSWMPPPSE IQRLYELLAT
QGTLELQAEI LPRRPPTPEA QSEEERSDEE PEAKEEEEEK PHMPTEFDFD DEPVTPKDSL
IDRRRTPGSS ARSQKREARL DKVLSDMKRH KKLEEQILRT GRDLFSLDSE GPSPASPPLR
SSGNSLFPRQ RKY
