GPN1_MOUSE
ID GPN1_MOUSE Reviewed; 372 AA.
AC Q8VCE2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=GPN-loop GTPase 1 {ECO:0000250|UniProtKB:Q9HCN4};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q9HCN4};
DE AltName: Full=MBD2-interacting protein {ECO:0000250|UniProtKB:Q9HCN4};
DE Short=MBDin {ECO:0000250|UniProtKB:Q9HCN4};
DE AltName: Full=XPA-binding protein 1 {ECO:0000250|UniProtKB:Q9HCN4};
GN Name=Gpn1 {ECO:0000250|UniProtKB:Q9HCN4};
GN Synonyms=Mbdin {ECO:0000250|UniProtKB:Q9HCN4},
GN Xab1 {ECO:0000250|UniProtKB:Q9HCN4};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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: Small GTPase required for proper nuclear import of RNA
CC polymerase II (RNAPII). May act at an RNAP assembly step prior to
CC nuclear import. Forms an interface between the RNA polymerase II enzyme
CC and chaperone/scaffolding proteins, suggesting that it is required to
CC connect RNA polymerase II to regulators of protein complex formation.
CC May be involved in nuclear localization of XPA.
CC {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SUBUNIT: Heterodimer with GPN3. Binds to RNA polymerase II (RNAPII).
CC Interacts directly with RNAPII subunits RPB4 and RPB7 and the CTD of
CC RPB1. Interacts with XPA. {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HCN4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9HCN4}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q9HCN4}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; AK077645; BAC36923.1; -; mRNA.
DR EMBL; BC020174; AAH20174.1; -; mRNA.
DR CCDS; CCDS19185.1; -.
DR RefSeq; NP_598517.1; NM_133756.4.
DR AlphaFoldDB; Q8VCE2; -.
DR SMR; Q8VCE2; -.
DR IntAct; Q8VCE2; 3.
DR STRING; 10090.ENSMUSP00000076217; -.
DR iPTMnet; Q8VCE2; -.
DR PhosphoSitePlus; Q8VCE2; -.
DR EPD; Q8VCE2; -.
DR jPOST; Q8VCE2; -.
DR MaxQB; Q8VCE2; -.
DR PaxDb; Q8VCE2; -.
DR PRIDE; Q8VCE2; -.
DR ProteomicsDB; 271318; -.
DR Antibodypedia; 13832; 201 antibodies from 29 providers.
DR DNASU; 74254; -.
DR Ensembl; ENSMUST00000076949; ENSMUSP00000076217; ENSMUSG00000064037.
DR GeneID; 74254; -.
DR KEGG; mmu:74254; -.
DR UCSC; uc008wyi.1; mouse.
DR CTD; 11321; -.
DR MGI; MGI:1921504; Gpn1.
DR VEuPathDB; HostDB:ENSMUSG00000064037; -.
DR eggNOG; KOG1532; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_1_2_1; -.
DR InParanoid; Q8VCE2; -.
DR OMA; MIIVFNK; -.
DR OrthoDB; 1096688at2759; -.
DR PhylomeDB; Q8VCE2; -.
DR TreeFam; TF313204; -.
DR BioGRID-ORCS; 74254; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Gpn1; mouse.
DR PRO; PR:Q8VCE2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VCE2; protein.
DR Bgee; ENSMUSG00000064037; Expressed in ileal epithelium and 254 other tissues.
DR ExpressionAtlas; Q8VCE2; baseline and differential.
DR Genevisible; Q8VCE2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF8; PTHR21231:SF8; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT CHAIN 2..372
FT /note="GPN-loop GTPase 1"
FT /id="PRO_0000066002"
FT REGION 303..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..88
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT COMPBIAS 341..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 189..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 88
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN4"
SQ SEQUENCE 372 AA; 41598 MW; 8AD50C8B6E5D1E6A CRC64;
MAAPVAPSEP QASRAPQPPV CLLVLGMAGS GKTTFVQRLT GHLHNKGCPP YVINLDPAVH
EVPFPANIDI RDTVKYKEVM KQYGLGPNGG IVTSLNLFAT RFDQVMKFIE KAQNTFRYVL
IDTPGQIEVF TWSASGTIIT EALASSFPTV VIYVMDTSRS TNPVTFMSNM LYACSILYKT
KLPFIVVMNK TDIIDHSFAV EWMQDFEAFQ DALNQETTYV SNLTRSMSLV LDEFYSSLRV
VGVSAVVGTG FDELCTQVTS AAEEYEREYR PEYERLKKSL ANAQSNQQKE QLERLRKDMG
SVALDPEAGK GNASPVLDPS DLILTRGTLD EEDEEADSDT DDIDHRVTEE SREEPAFQNF
MEESMAHWKR NK
