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   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.
DR   Genevisible; Q9H9Y4; HS.
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
//