GPN1_HUMAN
ID GPN1_HUMAN Reviewed; 374 AA.
AC Q9HCN4; B4DQJ5; B4DQM4; B4DXU4; B5MBZ5; O76004;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=GPN-loop GTPase 1 {ECO:0000303|PubMed:20855544};
DE EC=3.6.5.- {ECO:0000269|PubMed:11058119, ECO:0000269|PubMed:21768307};
DE AltName: Full=MBD2-interacting protein;
DE Short=MBDin;
DE AltName: Full=RNAPII-associated protein 4 {ECO:0000303|PubMed:20855544};
DE AltName: Full=XPA-binding protein 1 {ECO:0000303|PubMed:11058119};
GN Name=GPN1 {ECO:0000303|PubMed:20855544, ECO:0000312|HGNC:HGNC:17030};
GN Synonyms=MBDIN, RPAP4 {ECO:0000303|PubMed:20855544},
GN XAB1 {ECO:0000303|PubMed:11058119}; ORFNames=HUSSY-23;
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] (ISOFORM 1), INTERACTION WITH XPA, SUBCELLULAR
RP LOCATION, AND CATALYTIC ACTIVITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=11058119; DOI=10.1093/nar/28.21.4212;
RA Nitta M., Saijo M., Kodo N., Matsuda T., Nakastu Y., Tamai H., Tanaka K.;
RT "A novel cytoplasmic GTPase XAB1 interacts with DNA repair protein XPA.";
RL Nucleic Acids Res. 28:4212-4218(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [5]
RP PROTEIN SEQUENCE OF 2-17; 182-190 AND 226-267, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-374 (ISOFORM 1).
RC TISSUE=Liver, and Spleen;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to yeast
RT sequences.";
RL Yeast 18:69-80(2001).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP RNA POLYMERASE II COMPLEX.
RX PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
RA Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
RA Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
RA Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
RT "Systematic analysis of the protein interaction network for the human
RT transcription machinery reveals the identity of the 7SK capping enzyme.";
RL Mol. Cell 27:262-274(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-314 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND BINDING TO RNA POYMERASE II.
RX PubMed=20855544; DOI=10.1074/mcp.m110.003616;
RA Forget D., Lacombe A.A., Cloutier P., Al-Khoury R., Bouchard A.,
RA Lavallee-Adam M., Faubert D., Jeronimo C., Blanchette M., Coulombe B.;
RT "The protein interaction network of the human transcription machinery
RT reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly
RT in nuclear import and biogenesis of RNA polymerase II.";
RL Mol. Cell. Proteomics 9:2827-2839(2010).
RN [13]
RP BINDING TO RNA POYMERASE 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP BINDING TO RNA POYMERASE II.
RX PubMed=21844196; DOI=10.1074/jbc.m111.286161;
RA Staresincic L., Walker J., Dirac-Svejstrup A.B., Mitter R., Svejstrup J.Q.;
RT "GTP-dependent binding and nuclear transport of RNA polymerase II by Npa3
RT protein.";
RL J. Biol. Chem. 286:35553-35561(2011).
RN [17]
RP FUNCTION, BINDING TO RNA POYMERASE II, INTERACTION WITH GPN3; RPB1; RPB4
RP AND RPB7, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 29-GLY--LYS-32.
RX PubMed=21768307; DOI=10.1128/mcb.05442-11;
RA Carre C., Shiekhattar R.;
RT "Human GTPases associate with RNA polymerase II to mediate its nuclear
RT import.";
RL Mol. Cell. Biol. 31:3953-3962(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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).
RN [20]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-314 AND THR-340, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; THR-328; SER-338 AND
RP THR-340, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Small GTPase required for proper nuclear import of RNA
CC polymerase II (RNAPII) (PubMed:20855544, PubMed:21768307). May act at
CC an RNAP assembly step prior to nuclear import (PubMed:21768307). Forms
CC an interface between the RNA polymerase II enzyme and
CC chaperone/scaffolding proteins, suggesting that it is required to
CC connect RNA polymerase II to regulators of protein complex formation
CC (PubMed:17643375). May be involved in nuclear localization of XPA
CC (PubMed:11058119). {ECO:0000269|PubMed:17643375,
CC ECO:0000269|PubMed:20855544, ECO:0000269|PubMed:21768307,
CC ECO:0000305|PubMed:11058119}.
CC -!- SUBUNIT: Heterodimer with GPN3 (PubMed:21768307). Binds to RNA
CC polymerase II (RNAPII) (PubMed:17643375, PubMed:20864038,
CC PubMed:21844196). Interacts directly with RNAPII subunits RPB4 and RPB7
CC and the CTD of RPB1 (PubMed:21768307). Interacts with XPA
CC (PubMed:11058119). {ECO:0000269|PubMed:11058119,
CC ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:20864038,
CC ECO:0000269|PubMed:21768307, ECO:0000269|PubMed:21844196}.
CC -!- INTERACTION:
CC Q9HCN4; Q9H9Y4: GPN2; NbExp=4; IntAct=EBI-745137, EBI-11603368;
CC Q9HCN4; Q9UHW5: GPN3; NbExp=3; IntAct=EBI-745137, EBI-395491;
CC Q9HCN4; Q8IXW5: RPAP2; NbExp=6; IntAct=EBI-745137, EBI-395878;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11058119,
CC ECO:0000269|PubMed:20855544}. Nucleus {ECO:0000269|PubMed:20855544}.
CC Note=Shuttles between the nucleus and the cytoplasm.
CC {ECO:0000269|PubMed:20855544}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9HCN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCN4-2; Sequence=VSP_042750;
CC Name=3;
CC IsoId=Q9HCN4-3; Sequence=VSP_042749;
CC Name=4;
CC IsoId=Q9HCN4-4; Sequence=VSP_046176;
CC Name=5;
CC IsoId=Q9HCN4-5; Sequence=VSP_054366;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR EMBL; AB044661; BAB17612.1; -; mRNA.
DR EMBL; AK298827; BAG60957.1; -; mRNA.
DR EMBL; AK298866; BAG60986.1; -; mRNA.
DR EMBL; AK302131; BAG63506.1; -; mRNA.
DR EMBL; AK310340; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK316404; BAH14775.1; -; mRNA.
DR EMBL; AC074091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007451; AAH07451.1; -; mRNA.
DR EMBL; AJ010842; CAA09376.1; -; mRNA.
DR CCDS; CCDS1760.2; -. [Q9HCN4-1]
DR CCDS; CCDS46248.1; -. [Q9HCN4-4]
DR CCDS; CCDS46249.1; -. [Q9HCN4-3]
DR CCDS; CCDS46250.1; -. [Q9HCN4-2]
DR RefSeq; NP_001138519.1; NM_001145047.1. [Q9HCN4-4]
DR RefSeq; NP_001138520.1; NM_001145048.1. [Q9HCN4-2]
DR RefSeq; NP_001138521.1; NM_001145049.1. [Q9HCN4-3]
DR RefSeq; NP_009197.2; NM_007266.3. [Q9HCN4-1]
DR AlphaFoldDB; Q9HCN4; -.
DR SMR; Q9HCN4; -.
DR BioGRID; 116452; 122.
DR IntAct; Q9HCN4; 30.
DR MINT; Q9HCN4; -.
DR STRING; 9606.ENSP00000264718; -.
DR iPTMnet; Q9HCN4; -.
DR MetOSite; Q9HCN4; -.
DR PhosphoSitePlus; Q9HCN4; -.
DR BioMuta; GPN1; -.
DR DMDM; 34925430; -.
DR CPTAC; CPTAC-1027; -.
DR EPD; Q9HCN4; -.
DR jPOST; Q9HCN4; -.
DR MassIVE; Q9HCN4; -.
DR MaxQB; Q9HCN4; -.
DR PaxDb; Q9HCN4; -.
DR PeptideAtlas; Q9HCN4; -.
DR PRIDE; Q9HCN4; -.
DR ProteomicsDB; 5961; -.
DR ProteomicsDB; 81775; -. [Q9HCN4-1]
DR ProteomicsDB; 81776; -. [Q9HCN4-2]
DR ProteomicsDB; 81777; -. [Q9HCN4-3]
DR Antibodypedia; 13832; 201 antibodies from 29 providers.
DR DNASU; 11321; -.
DR Ensembl; ENST00000264718.7; ENSP00000264718.3; ENSG00000198522.14. [Q9HCN4-5]
DR Ensembl; ENST00000407583.7; ENSP00000384255.3; ENSG00000198522.14. [Q9HCN4-4]
DR Ensembl; ENST00000424214.5; ENSP00000398115.1; ENSG00000198522.14. [Q9HCN4-2]
DR Ensembl; ENST00000458167.6; ENSP00000412170.2; ENSG00000198522.14. [Q9HCN4-3]
DR Ensembl; ENST00000503738.5; ENSP00000427269.1; ENSG00000198522.14. [Q9HCN4-3]
DR Ensembl; ENST00000515877.5; ENSP00000424678.1; ENSG00000198522.14. [Q9HCN4-2]
DR Ensembl; ENST00000610189.2; ENSP00000476446.1; ENSG00000198522.14. [Q9HCN4-1]
DR Ensembl; ENST00000616939.4; ENSP00000484680.1; ENSG00000198522.14. [Q9HCN4-5]
DR GeneID; 11321; -.
DR KEGG; hsa:11321; -.
DR MANE-Select; ENST00000610189.2; ENSP00000476446.1; NM_007266.4; NP_009197.3.
DR UCSC; uc010ezf.4; human. [Q9HCN4-1]
DR CTD; 11321; -.
DR DisGeNET; 11321; -.
DR GeneCards; GPN1; -.
DR HGNC; HGNC:17030; GPN1.
DR HPA; ENSG00000198522; Low tissue specificity.
DR MIM; 611479; gene.
DR neXtProt; NX_Q9HCN4; -.
DR OpenTargets; ENSG00000198522; -.
DR PharmGKB; PA162390148; -.
DR VEuPathDB; HostDB:ENSG00000198522; -.
DR eggNOG; KOG1532; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_1_2_1; -.
DR InParanoid; Q9HCN4; -.
DR OrthoDB; 1096688at2759; -.
DR PhylomeDB; Q9HCN4; -.
DR TreeFam; TF313204; -.
DR PathwayCommons; Q9HCN4; -.
DR SignaLink; Q9HCN4; -.
DR BioGRID-ORCS; 11321; 758 hits in 1085 CRISPR screens.
DR ChiTaRS; GPN1; human.
DR GenomeRNAi; 11321; -.
DR Pharos; Q9HCN4; Tbio.
DR PRO; PR:Q9HCN4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HCN4; protein.
DR Bgee; ENSG00000198522; Expressed in islet of Langerhans and 206 other tissues.
DR ExpressionAtlas; Q9HCN4; baseline and differential.
DR Genevisible; Q9HCN4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW GTP-binding; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..374
FT /note="GPN-loop GTPase 1"
FT /id="PRO_0000066001"
FT REGION 326..354
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 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:0000269|Ref.5, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..104
FT /note="MAASAAAAELQASGGPRHPVCLLVLGMAGSGKTTFVQRLTGHLHAQGTPPYV
FT INLDPAVHEVPFPANIDIRDTVKYKEVMKQYGLGPNGGIVTSLNLFATRFDQ -> MKF
FT PFLPIL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042749"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042750"
FT VAR_SEQ 1..37
FT /note="MAASAAAAELQASGGPRHPVCLLVLGMAGSGKTTFVQ -> MTGHTRSSLPR
FT CTGIVLLIKLRFSE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046176"
FT VAR_SEQ 1
FT /note="M -> MRCLYGRVGGARRKM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054366"
FT MUTAGEN 29..32
FT /note="GSGK->AAAA: Abolishes GTPase activity and decreases
FT association with GPN3."
FT /evidence="ECO:0000269|PubMed:21768307"
SQ SEQUENCE 374 AA; 41740 MW; 9B96F452FAFE955C CRC64;
MAASAAAAEL QASGGPRHPV CLLVLGMAGS GKTTFVQRLT GHLHAQGTPP YVINLDPAVH
EVPFPANIDI RDTVKYKEVM KQYGLGPNGG IVTSLNLFAT RFDQVMKFIE KAQNMSKYVL
IDTPGQIEVF TWSASGTIIT EALASSFPTV VIYVMDTSRS TNPVTFMSNM LYACSILYKT
KLPFIVVMNK TDIIDHSFAV EWMQDFEAFQ DALNQETTYV SNLTRSMSLV LDEFYSSLRV
VGVSAVLGTG LDELFVQVTS AAEEYEREYR PEYERLKKSL ANAESQQQRE QLERLRKDMG
SVALDAGTAK DSLSPVLHPS DLILTRGTLD EEDEEADSDT DDIDHRVTEE SHEEPAFQNF
MQESMAQYWK RNNK
