ID GPN2_HUMAN Reviewed; 310 AA.
AC Q9H9Y4; Q96HG4; Q9NUE1; Q9NW30;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 24-JAN-2024, entry version 164.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000305};
DE AltName: Full=ATP-binding domain 1 family member B;
GN Name=GPN2 {ECO:0000303|PubMed:20864038, ECO:0000312|HGNC:HGNC:25513};
GN Synonyms=ATPBD1B; ORFNames=UNQ5828/PRO19647;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-264.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-264.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-227 AND GLY-264.
RC TISSUE=Cervix, and Eye;
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 [6]
RP BINDING TO RNA POLYMERASE II.
RX PubMed=20864038; DOI=10.1016/j.molcel.2010.08.023;
RA Boulon S., Pradet-Balade B., Verheggen C., Molle D., Boireau S.,
RA Georgieva M., Azzag K., Robert M.C., Ahmad Y., Neel H., Lamond A.I.,
RA Bertrand E.;
RT "HSP90 and its R2TP/Prefoldin-like cochaperone are involved in the
RT cytoplasmic assembly of RNA polymerase II.";
RL Mol. Cell 39:912-924(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Small GTPase required for proper localization of RNA
CC polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC step prior to nuclear import. {ECO:0000250|UniProtKB:Q08726}.
CC -!- SUBUNIT: Heterodimers with GPN1 or GPN3 (By similarity). Binds to RNA
CC polymerase II (RNAPII) (PubMed:20864038).
CC {ECO:0000250|UniProtKB:Q08726, ECO:0000269|PubMed:20864038}.
CC -!- INTERACTION:
CC Q9H9Y4; Q9HCN4: GPN1; NbExp=4; IntAct=EBI-11603368, EBI-745137;
CC Q9H9Y4; O14901: KLF11; NbExp=3; IntAct=EBI-11603368, EBI-948266;
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; AY364261; AAQ76820.1; -; mRNA.
DR EMBL; AY358864; AAQ89223.1; -; mRNA.
DR EMBL; AK001211; BAA91556.1; -; mRNA.
DR EMBL; AK022535; BAB14084.1; -; mRNA.
DR EMBL; AL034380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007815; AAH07815.1; -; mRNA.
DR EMBL; BC008634; AAH08634.1; -; mRNA.
DR CCDS; CCDS289.1; -.
DR RefSeq; NP_060536.3; NM_018066.3.
DR AlphaFoldDB; Q9H9Y4; -.
DR SMR; Q9H9Y4; -.
DR BioGRID; 120104; 24.
DR IntAct; Q9H9Y4; 9.
DR STRING; 9606.ENSP00000363250; -.
DR iPTMnet; Q9H9Y4; -.
DR PhosphoSitePlus; Q9H9Y4; -.
DR BioMuta; GPN2; -.
DR DMDM; 110832767; -.
DR EPD; Q9H9Y4; -.
DR jPOST; Q9H9Y4; -.
DR MassIVE; Q9H9Y4; -.
DR MaxQB; Q9H9Y4; -.
DR PaxDb; 9606-ENSP00000363250; -.
DR PeptideAtlas; Q9H9Y4; -.
DR ProteomicsDB; 81368; -.
DR Pumba; Q9H9Y4; -.
DR Antibodypedia; 30698; 52 antibodies from 13 providers.
DR DNASU; 54707; -.
DR Ensembl; ENST00000374135.9; ENSP00000363250.3; ENSG00000142751.15.
DR GeneID; 54707; -.
DR KEGG; hsa:54707; -.
DR MANE-Select; ENST00000374135.9; ENSP00000363250.3; NM_018066.4; NP_060536.3.
DR UCSC; uc001bnd.2; human.
DR AGR; HGNC:25513; -.
DR CTD; 54707; -.
DR DisGeNET; 54707; -.
DR GeneCards; GPN2; -.
DR HGNC; HGNC:25513; GPN2.
DR HPA; ENSG00000142751; Low tissue specificity.
DR neXtProt; NX_Q9H9Y4; -.
DR OpenTargets; ENSG00000142751; -.
DR PharmGKB; PA162390149; -.
DR VEuPathDB; HostDB:ENSG00000142751; -.
DR eggNOG; KOG1533; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_0_2_1; -.
DR InParanoid; Q9H9Y4; -.
DR OMA; ATHNYFL; -.
DR OrthoDB; 168004at2759; -.
DR PhylomeDB; Q9H9Y4; -.
DR TreeFam; TF300828; -.
DR PathwayCommons; Q9H9Y4; -.
DR SignaLink; Q9H9Y4; -.
DR BioGRID-ORCS; 54707; 826 hits in 1168 CRISPR screens.
DR ChiTaRS; GPN2; human.
DR GenomeRNAi; 54707; -.
DR Pharos; Q9H9Y4; Tdark.
DR PRO; PR:Q9H9Y4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H9Y4; Protein.
DR Bgee; ENSG00000142751; Expressed in mucosa of transverse colon and 178 other cell types or tissues.
DR ExpressionAtlas; Q9H9Y4; baseline and differential.
DR Genevisible; Q9H9Y4; HS.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR CDD; cd17871; GPN2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030231; Gpn2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW Acetylation; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..310
FT /note="GPN-loop GTPase 2"
FT /id="PRO_0000247829"
FT MOTIF 76..78
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 19..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 78
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:0007744|PubMed:22223895"
FT VARIANT 227
FT /note="Q -> R (in dbSNP:rs17856257)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027153"
FT VARIANT 264
FT /note="R -> G (in dbSNP:rs3170660)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_027154"
FT CONFLICT 15
FT /note="I -> T (in Ref. 1; AAQ76820 and 3; BAA91556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 34561 MW; F73EAF808DA692CA CRC64;
MAGAAPTTAF GQAVIGPPGS GKTTYCLGMS EFLRALGRRV AVVNLDPANE GLPYECAVDV
GELVGLGDVM DALRLGPNGG LLYCMEYLEA NLDWLRAKLD PLRGHYFLFD CPGQVELCTH
HGALRSIFSQ MAQWDLRLTA VHLVDSHYCT DPAKFISVLC TSLATMLHVE LPHINLLSKM
DLIEHYGKLA FNLDYYTEVL DLSYLLDHLA SDPFFRHYRQ LNEKLVQLIE DYSLVSFIPL
NIQDKESIQR VLQAVDKANG YCFRAQEQRS LEAMMSAAMG ADFHFSSTLG IQEKYLAPSN
QSVEQEAMQL
//
