GTPB6_HUMAN
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 03-AUG-2022, entry version 161.
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;
CC Evidence={ECO:0000255|PROSITE-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_012227.3.
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 SMR; O43824; -.
DR BioGRID; 113858; 95.
DR IntAct; O43824; 7.
DR STRING; 9606.ENSP00000316598; -.
DR iPTMnet; O43824; -.
DR PhosphoSitePlus; O43824; -.
DR BioMuta; GTPBP6; -.
DR EPD; O43824; -.
DR jPOST; O43824; -.
DR MassIVE; O43824; -.
DR PaxDb; O43824; -.
DR PeptideAtlas; O43824; -.
DR PRIDE; O43824; -.
DR ProteomicsDB; 34343; -.
DR ProteomicsDB; 49190; -.
DR Antibodypedia; 23297; 42 antibodies from 11 providers.
DR DNASU; 8225; -.
DR Ensembl; ENST00000326153.9; ENSP00000316598.5; ENSG00000178605.13.
DR GeneID; 8225; -.
DR KEGG; hsa:8225; -.
DR MANE-Select; ENST00000326153.10; ENSP00000316598.5; NM_012227.4; NP_036359.3.
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 neXtProt; NX_O43824; -.
DR OpenTargets; ENSG00000178605; -.
DR VEuPathDB; HostDB:ENSG00000178605; -.
DR eggNOG; KOG0410; Eukaryota.
DR GeneTree; ENSGT00390000001397; -.
DR InParanoid; O43824; -.
DR OMA; MMHVVIS; -.
DR OrthoDB; 1121388at2759; -.
DR PhylomeDB; O43824; -.
DR TreeFam; TF315022; -.
DR PathwayCommons; O43824; -.
DR SignaLink; O43824; -.
DR BioGRID-ORCS; 8225; 27 hits in 162 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 RNAct; O43824; protein.
DR Bgee; ENSG00000178605; Expressed in left ovary and 175 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR CDD; cd01878; HflX; 1.
DR Gene3D; 3.40.50.11060; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR10229; PTHR10229; 1.
DR Pfam; PF16360; GTP-bdg_M; 1.
DR Pfam; PF13167; GTP-bdg_N; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03156; GTP_HflX; 1.
DR PROSITE; PS51705; G_HFLX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW 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 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
