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Protein

Putative GTP-binding protein 6

Gene

GTPBP6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

Mg2+PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi308 – 3081MagnesiumPROSITE-ProRule annotation
Metal bindingi329 – 3291MagnesiumPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi301 – 3088GTPPROSITE-ProRule annotation
Nucleotide bindingi327 – 3315GTPPROSITE-ProRule annotation
Nucleotide bindingi349 – 3524GTPPROSITE-ProRule annotation
Nucleotide bindingi418 – 4214GTPPROSITE-ProRule annotation
Nucleotide bindingi437 – 4393GTPPROSITE-ProRule annotation

GO - Molecular functioni

  • GTP binding Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative GTP-binding protein 6
Alternative name(s):
Pseudoautosomal GTP-binding protein-like
Gene namesi
Name:GTPBP6
Synonyms:PGPL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:30189. GTPBP6.

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiGTPBP6.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 516516Putative GTP-binding protein 6PRO_0000304798Add
BLAST

Proteomic databases

MaxQBiO43824.
PaxDbiO43824.
PRIDEiO43824.

PTM databases

PhosphoSiteiO43824.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiO43824.
CleanExiHS_GTPBP6.
GenevestigatoriO43824.

Organism-specific databases

HPAiHPA035467.
HPA055418.

Interactioni

Protein-protein interaction databases

BioGridi113858. 15 interactions.
STRINGi9606.ENSP00000405410.

Structurei

3D structure databases

ProteinModelPortaliO43824.
SMRiO43824. Positions 175-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini295 – 459165Hflx-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family.PROSITE-ProRule annotation
Contains 1 Hflx-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2262.
HOGENOMiHOG000260368.
HOVERGENiHBG052970.
InParanoidiO43824.
PhylomeDBiO43824.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030394. G_HFLX_dom.
IPR006073. GTP_binding_domain.
IPR016496. GTPase_HflX.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10229. PTHR10229. 1 hit.
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03156. GTP_HflX. 1 hit.
PROSITEiPS51705. G_HFLX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWALRAAVRP GLRLSRVGRG RSAPRAAAPS CPARALAAVG RRSPGNLEGP
60 70 80 90 100
WGGGRGLRAD GGRSRTGDDE EEPEDADENA EEELLRGEPL LPAGTQRVCL
110 120 130 140 150
VHPDVKWGPG KSQMTRAEWQ VAEATALVHT LDGWSVVQTM VVSTKTPDRK
160 170 180 190 200
LIFGKGNFEH LTEKIRGSPD VTCVFLNVER MAAPTKKELE AAWGVEVFDR
210 220 230 240 250
FTVVLHIFRC NARTKEARLQ VALAEMPLHR SNLKRDVAHL YRGVGSRYIM
260 270 280 290 300
GSGESFMQLQ QRLLREKEAK IRKALDRLRK KRHLLRRQRT RREFPVISVV
310 320 330 340 350
GYTNCGKTTL IKALTGDAAI QPRDQLFATL DVTAHAGTLP SRMTVLYVDT
360 370 380 390 400
IGFLSQLPHG LIESFSATLE DVAHSDLILH VRDVSHPEAE LQKCSVLSTL
410 420 430 440 450
RGLQLPAPLL DSMVEVHNKV DLVPGYSPTE PNVVPVSALR GHGLQELKAE
460 470 480 490 500
LDAAVLKATG RQILTLRVRL AGAQLSWLYK EATVQEVDVI PEDGAADVRV
510
IISNSAYGKF RKLFPG
Length:516
Mass (Da):56,883
Last modified:October 5, 2010 - v3
Checksum:iAA81CEA655F579C7
GO

Sequence cautioni

The sequence AAH14636.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAP36024.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD97132.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA74749.2 differs from that shown.Has an upstream in-frame stop codon because of a region of poor sequence quality.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711V → I in BAD97132 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC126759 Genomic DNA. No translation available.
BX000483 Genomic DNA. Translation: CAI41972.1.
AK223412 mRNA. Translation: BAD97132.1. Different initiation.
BC014636 mRNA. Translation: AAH14636.1. Different initiation.
BT007360 mRNA. Translation: AAP36024.1. Different initiation.
Y14391 mRNA. Translation: CAA74749.2. Sequence problems.
CCDSiCCDS75943.1.
RefSeqiNP_036359.3. NM_012227.3.
UniGeneiHs.437145.

Genome annotation databases

GeneIDi8225.
KEGGihsa:8225.
UCSCiuc004cpe.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC126759 Genomic DNA. No translation available.
BX000483 Genomic DNA. Translation: CAI41972.1.
AK223412 mRNA. Translation: BAD97132.1. Different initiation.
BC014636 mRNA. Translation: AAH14636.1. Different initiation.
BT007360 mRNA. Translation: AAP36024.1. Different initiation.
Y14391 mRNA. Translation: CAA74749.2. Sequence problems.
CCDSiCCDS75943.1.
RefSeqiNP_036359.3. NM_012227.3.
UniGeneiHs.437145.

3D structure databases

ProteinModelPortaliO43824.
SMRiO43824. Positions 175-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113858. 15 interactions.
STRINGi9606.ENSP00000405410.

PTM databases

PhosphoSiteiO43824.

Polymorphism and mutation databases

BioMutaiGTPBP6.

Proteomic databases

MaxQBiO43824.
PaxDbiO43824.
PRIDEiO43824.

Protocols and materials databases

DNASUi8225.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8225.
KEGGihsa:8225.
UCSCiuc004cpe.1. human.

Organism-specific databases

CTDi8225.
GeneCardsiGC0XM000161.
HGNCiHGNC:30189. GTPBP6.
HPAiHPA035467.
HPA055418.
MIMi300124. gene.
neXtProtiNX_O43824.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2262.
HOGENOMiHOG000260368.
HOVERGENiHBG052970.
InParanoidiO43824.
PhylomeDBiO43824.

Miscellaneous databases

ChiTaRSiGTPBP6. human.
GeneWikiiGTPBP6.
GenomeRNAii8225.
NextBioi30958.
PROiO43824.
SOURCEiSearch...

Gene expression databases

BgeeiO43824.
CleanExiHS_GTPBP6.
GenevestigatoriO43824.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030394. G_HFLX_dom.
IPR006073. GTP_binding_domain.
IPR016496. GTPase_HflX.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10229. PTHR10229. 1 hit.
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03156. GTP_HflX. 1 hit.
PROSITEiPS51705. G_HFLX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-516.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-516.
    Tissue: Muscle.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-516.
  5. "A novel pseudoautosomal gene encoding a putative GTP-binding protein resides in the vicinity of the Xp/Yp telomere."
    Gianfrancesco F., Esposito T., Montanini L., Ciccodicola A., Mumm S., Mazzarella R., Rao E., Giglio S., Rappold G., Forabosco A.
    Hum. Mol. Genet. 7:407-414(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Entry informationi

Entry nameiGTPB6_HUMAN
AccessioniPrimary (citable) accession number: O43824
Secondary accession number(s): Q53F77, Q5HYX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 5, 2010
Last modified: April 29, 2015
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.