Full text data of GBP6
GBP6
[Confidence: low (only semi-automatic identification from reviews)]
Guanylate-binding protein 6 (GTP-binding protein 6; GBP-6; Guanine nucleotide-binding protein 6)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Guanylate-binding protein 6 (GTP-binding protein 6; GBP-6; Guanine nucleotide-binding protein 6)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6ZN66
ID GBP6_HUMAN Reviewed; 633 AA.
AC Q6ZN66; A2RRM3; Q6ZN86; Q7Z3F0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=Guanylate-binding protein 6;
DE AltName: Full=GTP-binding protein 6;
DE Short=GBP-6;
DE AltName: Full=Guanine nucleotide-binding protein 6;
GN Name=GBP6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS PHE-344; VAL-355 AND VAL-520.
RC TISSUE=Esophageal carcinoma, and Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-331; PHE-344; VAL-355 AND VAL-520.
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-331; PHE-344; VAL-355 AND VAL-520.
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds GTP, GDP and GMP (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZN66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN66-2; Sequence=VSP_030155;
CC -!- SIMILARITY: Belongs to the GBP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK131329; BAD18489.1; -; mRNA.
DR EMBL; AK131356; BAD18509.1; -; mRNA.
DR EMBL; BX537949; CAD97917.1; -; mRNA.
DR EMBL; AL691464; CAI22141.1; -; Genomic_DNA.
DR EMBL; BC131713; AAI31714.1; -; mRNA.
DR RefSeq; NP_940862.2; NM_198460.2.
DR RefSeq; XP_005270605.1; XM_005270548.1.
DR UniGene; Hs.254338; -.
DR ProteinModelPortal; Q6ZN66; -.
DR SMR; Q6ZN66; 7-579.
DR STRING; 9606.ENSP00000359485; -.
DR PhosphoSite; Q6ZN66; -.
DR DMDM; 74749570; -.
DR PaxDb; Q6ZN66; -.
DR PRIDE; Q6ZN66; -.
DR DNASU; 163351; -.
DR Ensembl; ENST00000370456; ENSP00000359485; ENSG00000183347.
DR GeneID; 163351; -.
DR KEGG; hsa:163351; -.
DR UCSC; uc001dnf.2; human.
DR CTD; 163351; -.
DR GeneCards; GC01P089829; -.
DR H-InvDB; HIX0000767; -.
DR HGNC; HGNC:25395; GBP6.
DR HPA; HPA027744; -.
DR MIM; 612467; gene.
DR neXtProt; NX_Q6ZN66; -.
DR PharmGKB; PA134964409; -.
DR eggNOG; NOG288755; -.
DR HOGENOM; HOG000266974; -.
DR HOVERGEN; HBG001979; -.
DR InParanoid; Q6ZN66; -.
DR OMA; KNDDTPW; -.
DR OrthoDB; EOG7BW0J3; -.
DR PhylomeDB; Q6ZN66; -.
DR Reactome; REACT_6900; Immune System.
DR GenomeRNAi; 163351; -.
DR NextBio; 88351; -.
DR PRO; PR:Q6ZN66; -.
DR ArrayExpress; Q6ZN66; -.
DR Bgee; Q6ZN66; -.
DR CleanEx; HS_GBP6; -.
DR Genevestigator; Q6ZN66; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR InterPro; IPR003191; Guanylate-bd_C.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF02841; GBP_C; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; GTP-binding;
KW Nucleotide-binding; Polymorphism; Reference proteome.
FT CHAIN 1 633 Guanylate-binding protein 6.
FT /FTId=PRO_0000313811.
FT NP_BIND 45 52 GTP (By similarity).
FT NP_BIND 67 69 GTP (By similarity).
FT NP_BIND 97 101 GTP (By similarity).
FT REGION 1 310 GTPase domain (Globular) (By similarity).
FT COMPBIAS 38 41 Poly-Val.
FT VAR_SEQ 1 337 Missing (in isoform 2).
FT /FTId=VSP_030155.
FT VARIANT 278 278 T -> I (in dbSNP:rs4582772).
FT /FTId=VAR_037750.
FT VARIANT 331 331 A -> S (in dbSNP:rs4658359).
FT /FTId=VAR_037751.
FT VARIANT 344 344 L -> F (in dbSNP:rs4658360).
FT /FTId=VAR_037752.
FT VARIANT 355 355 M -> V (in dbSNP:rs4658146).
FT /FTId=VAR_037753.
FT VARIANT 520 520 D -> V (in dbSNP:rs959460).
FT /FTId=VAR_037754.
FT CONFLICT 13 13 L -> Q (in Ref. 2; CAD97917).
FT CONFLICT 313 313 N -> D (in Ref. 2; CAD97917).
SQ SEQUENCE 633 AA; 72427 MW; D3487659300D5678 CRC64;
MESGPKMLAP VCLVENNNEQ LLVNQQAIQI LEKISQPVVV VAIVGLYRTG KSYLMNHLAG
QNHGFPLGST VQSETKGIWM WCVPHPSKPN HTLVLLDTEG LGDVEKGDPK NDSWIFALAV
LLCSTFVYNS MSTINHQALE QLHYVTELTE LIKAKSSPRP DGVEDSTEFV SFFPDFLWTV
RDFTLELKLN GHPITEDEYL ENALKLIQGN NPRVQTSNFP RECIRRFFPK RKCFVFDRPT
NDKDLLANIE KVSEKQLDPK FQEQTNIFCS YIFTHARTKT LREGITVTGN RLGTLAVTYV
EAINSGAVPC LENAVITLAQ RENSAAVQRA ADYYSQQMAQ RVKLPTDTLQ ELLDMHAACE
REAIAIFMEH SFKDENQEFQ KKFMETTMNK KGDFLLQNEE SSVQYCQAKL NELSKGLMES
ISAGSFSVPG GHKLYMETKE RIEQDYWQVP RKGVKAKEVF QRFLESQMVI EESILQSDKA
LTDREKAVAV DRAKKEAAEK EQELLKQKLQ EQQQQMEAQD KSRKENIAQL KEKLQMEREH
LLREQIMMLE HTQKVQNDWL HEGFKKKYEE MNAEISQFKR MIDTTKNDDT PWIARTLDNL
ADELTAILSA PAKLIGHGVK GVSSLFKKHK LPF
//
ID GBP6_HUMAN Reviewed; 633 AA.
AC Q6ZN66; A2RRM3; Q6ZN86; Q7Z3F0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=Guanylate-binding protein 6;
DE AltName: Full=GTP-binding protein 6;
DE Short=GBP-6;
DE AltName: Full=Guanine nucleotide-binding protein 6;
GN Name=GBP6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS PHE-344; VAL-355 AND VAL-520.
RC TISSUE=Esophageal carcinoma, and Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-331; PHE-344; VAL-355 AND VAL-520.
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-331; PHE-344; VAL-355 AND VAL-520.
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds GTP, GDP and GMP (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZN66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN66-2; Sequence=VSP_030155;
CC -!- SIMILARITY: Belongs to the GBP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK131329; BAD18489.1; -; mRNA.
DR EMBL; AK131356; BAD18509.1; -; mRNA.
DR EMBL; BX537949; CAD97917.1; -; mRNA.
DR EMBL; AL691464; CAI22141.1; -; Genomic_DNA.
DR EMBL; BC131713; AAI31714.1; -; mRNA.
DR RefSeq; NP_940862.2; NM_198460.2.
DR RefSeq; XP_005270605.1; XM_005270548.1.
DR UniGene; Hs.254338; -.
DR ProteinModelPortal; Q6ZN66; -.
DR SMR; Q6ZN66; 7-579.
DR STRING; 9606.ENSP00000359485; -.
DR PhosphoSite; Q6ZN66; -.
DR DMDM; 74749570; -.
DR PaxDb; Q6ZN66; -.
DR PRIDE; Q6ZN66; -.
DR DNASU; 163351; -.
DR Ensembl; ENST00000370456; ENSP00000359485; ENSG00000183347.
DR GeneID; 163351; -.
DR KEGG; hsa:163351; -.
DR UCSC; uc001dnf.2; human.
DR CTD; 163351; -.
DR GeneCards; GC01P089829; -.
DR H-InvDB; HIX0000767; -.
DR HGNC; HGNC:25395; GBP6.
DR HPA; HPA027744; -.
DR MIM; 612467; gene.
DR neXtProt; NX_Q6ZN66; -.
DR PharmGKB; PA134964409; -.
DR eggNOG; NOG288755; -.
DR HOGENOM; HOG000266974; -.
DR HOVERGEN; HBG001979; -.
DR InParanoid; Q6ZN66; -.
DR OMA; KNDDTPW; -.
DR OrthoDB; EOG7BW0J3; -.
DR PhylomeDB; Q6ZN66; -.
DR Reactome; REACT_6900; Immune System.
DR GenomeRNAi; 163351; -.
DR NextBio; 88351; -.
DR PRO; PR:Q6ZN66; -.
DR ArrayExpress; Q6ZN66; -.
DR Bgee; Q6ZN66; -.
DR CleanEx; HS_GBP6; -.
DR Genevestigator; Q6ZN66; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR InterPro; IPR003191; Guanylate-bd_C.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF02841; GBP_C; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; GTP-binding;
KW Nucleotide-binding; Polymorphism; Reference proteome.
FT CHAIN 1 633 Guanylate-binding protein 6.
FT /FTId=PRO_0000313811.
FT NP_BIND 45 52 GTP (By similarity).
FT NP_BIND 67 69 GTP (By similarity).
FT NP_BIND 97 101 GTP (By similarity).
FT REGION 1 310 GTPase domain (Globular) (By similarity).
FT COMPBIAS 38 41 Poly-Val.
FT VAR_SEQ 1 337 Missing (in isoform 2).
FT /FTId=VSP_030155.
FT VARIANT 278 278 T -> I (in dbSNP:rs4582772).
FT /FTId=VAR_037750.
FT VARIANT 331 331 A -> S (in dbSNP:rs4658359).
FT /FTId=VAR_037751.
FT VARIANT 344 344 L -> F (in dbSNP:rs4658360).
FT /FTId=VAR_037752.
FT VARIANT 355 355 M -> V (in dbSNP:rs4658146).
FT /FTId=VAR_037753.
FT VARIANT 520 520 D -> V (in dbSNP:rs959460).
FT /FTId=VAR_037754.
FT CONFLICT 13 13 L -> Q (in Ref. 2; CAD97917).
FT CONFLICT 313 313 N -> D (in Ref. 2; CAD97917).
SQ SEQUENCE 633 AA; 72427 MW; D3487659300D5678 CRC64;
MESGPKMLAP VCLVENNNEQ LLVNQQAIQI LEKISQPVVV VAIVGLYRTG KSYLMNHLAG
QNHGFPLGST VQSETKGIWM WCVPHPSKPN HTLVLLDTEG LGDVEKGDPK NDSWIFALAV
LLCSTFVYNS MSTINHQALE QLHYVTELTE LIKAKSSPRP DGVEDSTEFV SFFPDFLWTV
RDFTLELKLN GHPITEDEYL ENALKLIQGN NPRVQTSNFP RECIRRFFPK RKCFVFDRPT
NDKDLLANIE KVSEKQLDPK FQEQTNIFCS YIFTHARTKT LREGITVTGN RLGTLAVTYV
EAINSGAVPC LENAVITLAQ RENSAAVQRA ADYYSQQMAQ RVKLPTDTLQ ELLDMHAACE
REAIAIFMEH SFKDENQEFQ KKFMETTMNK KGDFLLQNEE SSVQYCQAKL NELSKGLMES
ISAGSFSVPG GHKLYMETKE RIEQDYWQVP RKGVKAKEVF QRFLESQMVI EESILQSDKA
LTDREKAVAV DRAKKEAAEK EQELLKQKLQ EQQQQMEAQD KSRKENIAQL KEKLQMEREH
LLREQIMMLE HTQKVQNDWL HEGFKKKYEE MNAEISQFKR MIDTTKNDDT PWIARTLDNL
ADELTAILSA PAKLIGHGVK GVSSLFKKHK LPF
//
MIM
612467
*RECORD*
*FIELD* NO
612467
*FIELD* TI
*612467 GUANYLATE-BINDING PROTEIN 6; GBP6
;;GUANYLATE-BINDING PROTEIN 4, MOUSE, HOMOLOG OF; GBP4
read more*FIELD* TX
DESCRIPTION
Guanylate-binding proteins, such as GBP6, are induced by interferon and
hydrolyze GTP to both GDP and GMP (Olszewski et al., 2006).
CLONING
Olszewski et al. (2006) identified GBP6 within the GBP gene cluster on
chromosome 1. The 634-amino acid GBP6 protein shares 74% identity with
both GBP7 (612468) and GBP4 (612466). All GBPs, including GBP6, have a
conserved N-terminal globular GTP-binding domain containing 2 consensus
sequences and a third T(L/V)RD sequence not found in other GTPases. GBP6
lacks a C-terminal CaaX isoprenylation motif found in GBP1 (600411),
GBP2 (600412), and GBP5 (611467). EST database analysis indicated that
GBP6 expression was limited to larynx, muscle, and tongue.
GENE FUNCTION
Using RT-PCR, Tripal et al. (2007) detected expression of all GBPs
except GBP6 and GBP7 in endothelial cells after stimulation with IFNG
(147570), TNF (191160), or IL1B (147720).
GENE STRUCTURE
Olszewski et al. (2006) determined that, like other GBPs, the GBP6 gene
contains 11 exons and begins translation in exon 2.
MAPPING
By genomic sequence analysis, Olszewski et al. (2006) mapped the GBP6
gene to the GBP gene cluster on chromosome 1p22.2. It is located 91 kb
from GBP5 and is the most centromeric of the GBP genes.
*FIELD* RF
1. Olszewski, M. A.; Gray, J.; Vestal, D. J.: In silico genomic analysis
of the human and murine guanylate-binding protein (GBP) gene clusters. J.
Interferon Cytokine Res. 26: 328-352, 2006.
2. Tripal, P.; Bauer, M.; Naschberger, E.; Mortinger, T.; Hohenadl,
C.; Cornali, E.; Thurau, M.; Sturzl, M.: Unique features of different
members of the human guanylate-binding protein family. J. Interferon
Cytokine Res. 27: 44-52, 2007.
*FIELD* CD
Paul J. Converse: 12/11/2008
*FIELD* ED
alopez: 08/16/2011
terry: 7/26/2011
mgross: 12/11/2008
*RECORD*
*FIELD* NO
612467
*FIELD* TI
*612467 GUANYLATE-BINDING PROTEIN 6; GBP6
;;GUANYLATE-BINDING PROTEIN 4, MOUSE, HOMOLOG OF; GBP4
read more*FIELD* TX
DESCRIPTION
Guanylate-binding proteins, such as GBP6, are induced by interferon and
hydrolyze GTP to both GDP and GMP (Olszewski et al., 2006).
CLONING
Olszewski et al. (2006) identified GBP6 within the GBP gene cluster on
chromosome 1. The 634-amino acid GBP6 protein shares 74% identity with
both GBP7 (612468) and GBP4 (612466). All GBPs, including GBP6, have a
conserved N-terminal globular GTP-binding domain containing 2 consensus
sequences and a third T(L/V)RD sequence not found in other GTPases. GBP6
lacks a C-terminal CaaX isoprenylation motif found in GBP1 (600411),
GBP2 (600412), and GBP5 (611467). EST database analysis indicated that
GBP6 expression was limited to larynx, muscle, and tongue.
GENE FUNCTION
Using RT-PCR, Tripal et al. (2007) detected expression of all GBPs
except GBP6 and GBP7 in endothelial cells after stimulation with IFNG
(147570), TNF (191160), or IL1B (147720).
GENE STRUCTURE
Olszewski et al. (2006) determined that, like other GBPs, the GBP6 gene
contains 11 exons and begins translation in exon 2.
MAPPING
By genomic sequence analysis, Olszewski et al. (2006) mapped the GBP6
gene to the GBP gene cluster on chromosome 1p22.2. It is located 91 kb
from GBP5 and is the most centromeric of the GBP genes.
*FIELD* RF
1. Olszewski, M. A.; Gray, J.; Vestal, D. J.: In silico genomic analysis
of the human and murine guanylate-binding protein (GBP) gene clusters. J.
Interferon Cytokine Res. 26: 328-352, 2006.
2. Tripal, P.; Bauer, M.; Naschberger, E.; Mortinger, T.; Hohenadl,
C.; Cornali, E.; Thurau, M.; Sturzl, M.: Unique features of different
members of the human guanylate-binding protein family. J. Interferon
Cytokine Res. 27: 44-52, 2007.
*FIELD* CD
Paul J. Converse: 12/11/2008
*FIELD* ED
alopez: 08/16/2011
terry: 7/26/2011
mgross: 12/11/2008