GPBP1_MOUSE
ID GPBP1_MOUSE Reviewed; 473 AA.
AC Q6NXH3; Q3TQR2; Q3TSN7; Q6TYE7; Q8C498; Q8R252;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Vasculin;
DE AltName: Full=GC-rich promoter-binding protein 1;
DE Short=mGPBP;
GN Name=Gpbp1; Synonyms=Gpbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH GTF2B; GTF2F2; RNA POLYMERASE II AND TBP, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=14612417; DOI=10.1128/mcb.23.23.8773-8785.2003;
RA Hsu L.-C., Liu S., Abedinpour F., Beech R.D., Lahti J.M., Kidd V.J.,
RA Greenspan J.A., Yeung C.-Y.;
RT "The murine G+C-rich promoter binding protein mGPBP is required for
RT promoter-specific transcription.";
RL Mol. Cell. Biol. 23:8773-8785(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Egg, Embryo, Olfactory bulb, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Retina;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274 AND SER-276, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions as a GC-rich promoter-specific transactivating
CC transcription factor. {ECO:0000269|PubMed:14612417}.
CC -!- SUBUNIT: Interacts with GTF2B, GTF2F2, RNA polymerase II and TBP.
CC {ECO:0000269|PubMed:14612417}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14612417}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6NXH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NXH3-2; Sequence=VSP_032139;
CC Name=3;
CC IsoId=Q6NXH3-3; Sequence=VSP_032138, VSP_032139;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC {ECO:0000269|PubMed:14612417}.
CC -!- SIMILARITY: Belongs to the vasculin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16083.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY382529; AAQ88446.1; -; mRNA.
DR EMBL; AK082704; BAC38578.1; -; mRNA.
DR EMBL; AK135728; BAE22631.1; -; mRNA.
DR EMBL; AK145318; BAE26364.1; -; mRNA.
DR EMBL; AK161928; BAE36638.1; -; mRNA.
DR EMBL; AK163370; BAE37320.1; -; mRNA.
DR EMBL; AK163390; BAE37330.1; -; mRNA.
DR EMBL; AK169406; BAE41152.1; -; mRNA.
DR EMBL; BC016083; AAH16083.1; ALT_INIT; mRNA.
DR EMBL; BC067075; AAH67075.1; -; mRNA.
DR EMBL; BC094888; AAH94888.1; -; mRNA.
DR CCDS; CCDS26769.1; -. [Q6NXH3-2]
DR CCDS; CCDS49362.1; -. [Q6NXH3-1]
DR RefSeq; NP_001116435.1; NM_001122963.1. [Q6NXH3-1]
DR RefSeq; NP_082763.3; NM_028487.4. [Q6NXH3-2]
DR RefSeq; XP_006517835.1; XM_006517772.1. [Q6NXH3-2]
DR RefSeq; XP_006517836.1; XM_006517773.3.
DR RefSeq; XP_017171102.1; XM_017315613.1.
DR RefSeq; XP_017171103.1; XM_017315614.1.
DR AlphaFoldDB; Q6NXH3; -.
DR BioGRID; 215884; 5.
DR IntAct; Q6NXH3; 1.
DR STRING; 10090.ENSMUSP00000048240; -.
DR iPTMnet; Q6NXH3; -.
DR PhosphoSitePlus; Q6NXH3; -.
DR EPD; Q6NXH3; -.
DR jPOST; Q6NXH3; -.
DR MaxQB; Q6NXH3; -.
DR PaxDb; Q6NXH3; -.
DR PeptideAtlas; Q6NXH3; -.
DR PRIDE; Q6NXH3; -.
DR ProteomicsDB; 267757; -. [Q6NXH3-1]
DR ProteomicsDB; 267758; -. [Q6NXH3-2]
DR ProteomicsDB; 267759; -. [Q6NXH3-3]
DR DNASU; 73274; -.
DR Ensembl; ENSMUST00000047627; ENSMUSP00000048240; ENSMUSG00000032745. [Q6NXH3-2]
DR Ensembl; ENSMUST00000091236; ENSMUSP00000088777; ENSMUSG00000032745. [Q6NXH3-1]
DR GeneID; 73274; -.
DR KEGG; mmu:73274; -.
DR UCSC; uc007rvv.2; mouse. [Q6NXH3-3]
DR UCSC; uc007rvw.2; mouse. [Q6NXH3-2]
DR UCSC; uc007rvx.2; mouse. [Q6NXH3-1]
DR CTD; 65056; -.
DR MGI; MGI:1920524; Gpbp1.
DR VEuPathDB; HostDB:ENSMUSG00000032745; -.
DR eggNOG; ENOG502QR5W; Eukaryota.
DR GeneTree; ENSGT00420000029753; -.
DR HOGENOM; CLU_045487_0_0_1; -.
DR InParanoid; Q6NXH3; -.
DR OMA; CNFKFSP; -.
DR OrthoDB; 662557at2759; -.
DR PhylomeDB; Q6NXH3; -.
DR TreeFam; TF332220; -.
DR BioGRID-ORCS; 73274; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Gpbp1; mouse.
DR PRO; PR:Q6NXH3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6NXH3; protein.
DR Bgee; ENSMUSG00000032745; Expressed in animal zygote and 250 other tissues.
DR ExpressionAtlas; Q6NXH3; baseline and differential.
DR Genevisible; Q6NXH3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR028128; Vasculin_fam.
DR PANTHER; PTHR14339; PTHR14339; 1.
DR Pfam; PF15337; Vasculin; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..473
FT /note="Vasculin"
FT /id="PRO_0000324111"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 87
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86WP2"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WP2"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WP2"
FT VAR_SEQ 3..137
FT /note="QHDFAPAWLNFPTPPSSTKSSLNFEKHSENFSWTENRYDVSRRRHNSSDGFD
FT SGIGRPNGGNFGRKEKNGWRTHGRNGTENINHRGGYHGGNSRSRSSIFHSGKSQGLHEN
FT SIPDNETGRKEDKRERRQFEAEDF -> LILVLDVLME (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032138"
FT VAR_SEQ 159
FT /note="W -> WGLHAQTHTYPTKKISQAPLL (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14612417,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_032139"
FT CONFLICT 204
FT /note="G -> S (in Ref. 1; AAQ88446)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="M -> I (in Ref. 1; AAQ88446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53423 MW; ADE2CF4F36D81E1C CRC64;
MAQHDFAPAW LNFPTPPSST KSSLNFEKHS ENFSWTENRY DVSRRRHNSS DGFDSGIGRP
NGGNFGRKEK NGWRTHGRNG TENINHRGGY HGGNSRSRSS IFHSGKSQGL HENSIPDNET
GRKEDKRERR QFEAEDFPSL NPEYEREPNQ NKSLAAGVWD YPPNPKSRTP RMLVIKKGNT
KDLQLSGFPV AGNLQSQPVK NGTGPSVYKG LVPKPAVPPT KPTQWKSQTK ENKVGTSFSH
ESTYGVGNFN TFKSTAKNIS PSTNSVKECN RSNSSSPVDK LNQQPRLTKL TRMRSDKKSE
FLKALKRDRV EEEHEDESHA GSEKDDDSFN LHNSNTTHQE RDINRNFDEN EIPQENGNAS
MISQQIIRSS TFPQTDVLSS SLEAEHRLLK EMGWQEDSEN DETCAPLTED EMREFQVISE
QLQKNGLRKN GILKNGLICD FKFGPWKNST FKPTIENDDT ETSSSDTSDD DDV
