ID   GTPB6_HUMAN             Reviewed;         516 AA.
AC   O43824; H0Y2S1; Q53F77; Q5HYX8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 4.
DT   28-JAN-2026, entry version 177.
DE   RecName: Full=Putative GTP-binding protein 6;
DE   AltName: Full=Pseudoautosomal GTP-binding protein-like;
GN   Name=GTPBP6; Synonyms=PGPL;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-516, AND TISSUE SPECIFICITY.
RX   PubMed=9466997; DOI=10.1093/hmg/7.3.407;
RA   Gianfrancesco F., Esposito T., Montanini L., Ciccodicola A., Mumm S.,
RA   Mazzarella R., Rao E., Giglio S., Rappold G., Forabosco A.;
RT   "A novel pseudoautosomal gene encoding a putative GTP-binding protein
RT   resides in the vicinity of the Xp/Yp telomere.";
RL   Hum. Mol. Genet. 7:407-414(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-516.
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-516.
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-516.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01042};
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:9466997}.
CC   -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC       pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. HflX GTPase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01042}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH14636.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD97132.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA74749.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC126759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX000483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO681518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Y14391; CAA74749.2; ALT_FRAME; mRNA.
DR   EMBL; AK223412; BAD97132.1; ALT_INIT; mRNA.
DR   EMBL; BC014636; AAH14636.1; ALT_INIT; mRNA.
DR   EMBL; BT007360; AAP36024.1; -; mRNA.
DR   CCDS; CCDS75943.1; -.
DR   RefSeq; NP_036359.3; NM_012227.4.
DR   PDB; 7OF2; EM; 2.70 A; C=1-516.
DR   PDB; 7OF4; EM; 2.70 A; C=1-516.
DR   PDB; 7OF6; EM; 2.60 A; C=1-516.
DR   PDBsum; 7OF2; -.
DR   PDBsum; 7OF4; -.
DR   PDBsum; 7OF6; -.
DR   AlphaFoldDB; O43824; -.
DR   EMDB; EMD-12867; -.
DR   EMDB; EMD-12869; -.
DR   EMDB; EMD-12871; -.
DR   SMR; O43824; -.
DR   BioGRID; 113858; 102.
DR   FunCoup; O43824; 446.
DR   IntAct; O43824; 36.
DR   STRING; 9606.ENSP00000316598; -.
DR   iPTMnet; O43824; -.
DR   PhosphoSitePlus; O43824; -.
DR   SwissPalm; O43824; -.
DR   BioMuta; GTPBP6; -.
DR   jPOST; O43824; -.
DR   MassIVE; O43824; -.
DR   PaxDb; 9606-ENSP00000316598; -.
DR   PeptideAtlas; O43824; -.
DR   ProteomicsDB; 34343; -.
DR   ProteomicsDB; 49190; -.
DR   Pumba; O43824; -.
DR   Antibodypedia; 23297; 46 antibodies from 13 providers.
DR   DNASU; 8225; -.
DR   Ensembl; ENST00000326153.10; ENSP00000316598.5; ENSG00000178605.16.
DR   Ensembl; ENST00000711233.2; ENSP00000518626.1; ENSG00000292358.3.
DR   Ensembl; ENST00000850592.1; ENSP00000520879.1; ENSG00000178605.16.
DR   GeneID; 8225; -.
DR   KEGG; hsa:8225; -.
DR   MANE-Select; ENST00000326153.10; ENSP00000316598.5; NM_012227.4; NP_036359.3.
DR   AGR; HGNC:30189; -.
DR   CTD; 8225; -.
DR   DisGeNET; 8225; -.
DR   GeneCards; GTPBP6; -.
DR   HGNC; HGNC:30189; GTPBP6.
DR   HPA; ENSG00000178605; Low tissue specificity.
DR   MIM; 300124; gene.
DR   OpenTargets; ENSG00000178605; -.
DR   VEuPathDB; HostDB:ENSG00000178605; -.
DR   eggNOG; KOG0410; Eukaryota.
DR   GeneTree; ENSGT00390000001397; -.
DR   InParanoid; O43824; -.
DR   OMA; IDVANKC; -.
DR   OrthoDB; 10268034at2759; -.
DR   PAN-GO; O43824; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; O43824; -.
DR   PathwayCommons; O43824; -.
DR   SignaLink; O43824; -.
DR   Agora; ENSG00000178605; -.
DR   BioGRID-ORCS; 8225; 28 hits in 204 CRISPR screens.
DR   ChiTaRS; GTPBP6; human.
DR   GeneWiki; GTPBP6; -.
DR   GenomeRNAi; 8225; -.
DR   Pharos; O43824; Tdark.
DR   PRO; PR:O43824; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Proteomes; UP000005640; Chromosome Y.
DR   RNAct; O43824; protein.
DR   Bgee; ENSG00000178605; Expressed in left ovary and 177 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IDA:FlyBase.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IDA:FlyBase.
DR   CDD; cd01878; HflX; 1.
DR   FunFam; 3.40.50.11060:FF:000002; GTP binding protein 6 (putative); 1.
DR   FunFam; 3.40.50.300:FF:000886; Putative GTP-binding protein 6; 1.
DR   Gene3D; 3.40.50.11060; GTPase HflX, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030394; G_HFLX_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR032305; GTP-bd_M.
DR   InterPro; IPR016496; GTPase_HflX.
DR   InterPro; IPR025121; GTPase_HflX_N.
DR   InterPro; IPR042108; GTPase_HflX_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03156; GTP_HflX; 1.
DR   PANTHER; PTHR10229:SF0; GTP-BINDING PROTEIN 6-RELATED; 1.
DR   PANTHER; PTHR10229; GTP-BINDING PROTEIN HFLX; 1.
DR   Pfam; PF16360; GTP-bdg_M; 1.
DR   Pfam; PF13167; GTP-bdg_N; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51705; G_HFLX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..516
FT                   /note="Putative GTP-binding protein 6"
FT                   /id="PRO_0000304798"
FT   DOMAIN          295..459
FT                   /note="Hflx-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   REGION          18..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..39
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..82
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         301..308
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   BINDING         327..331
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   BINDING         329
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   BINDING         349..352
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   BINDING         418..421
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   BINDING         437..439
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01042"
FT   CONFLICT        60
FT                   /note="D -> E (in Ref. 2; CAA74749)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="G -> R (in Ref. 3; BAD97132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="G -> E (in Ref. 2; CAA74749)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="E -> K (in Ref. 2; CAA74749)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="I -> V (in Ref. 4; AAH14636, 5; AAP36024 and 2;
FT                   CAA74749)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   516 AA;  56897 MW;  0BCF19A88FB5A984 CRC64;
     MWALRAAVRP GLRLSRVGRG RSAPRAAAPS CPARALAAVG RRSPGNLEGP WGGGRGLRAD
     GGRSRTGDDE EEPEDADENA EEELLRGEPL LPAGTQRVCL VHPDVKWGPG KSQMTRAEWQ
     VAEATALVHT LDGWSVVQTM VVSTKTPDRK LIFGKGNFEH LTEKIRGSPD ITCVFLNVER
     MAAPTKKELE AAWGVEVFDR FTVVLHIFRC NARTKEARLQ VALAEMPLHR SNLKRDVAHL
     YRGVGSRYIM GSGESFMQLQ QRLLREKEAK IRKALDRLRK KRHLLRRQRT RREFPVISVV
     GYTNCGKTTL IKALTGDAAI QPRDQLFATL DVTAHAGTLP SRMTVLYVDT IGFLSQLPHG
     LIESFSATLE DVAHSDLILH VRDVSHPEAE LQKCSVLSTL RGLQLPAPLL DSMVEVHNKV
     DLVPGYSPTE PNVVPVSALR GHGLQELKAE LDAAVLKATG RQILTLRVRL AGAQLSWLYK
     EATVQEVDVI PEDGAADVRV IISNSAYGKF RKLFPG
//