Full text data of GTPBP1
GTPBP1
[Confidence: low (only semi-automatic identification from reviews)]
GTP-binding protein 1; G-protein 1; GP-1; GP1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
GTP-binding protein 1; G-protein 1; GP-1; GP1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00178
ID GTPB1_HUMAN Reviewed; 669 AA.
AC O00178; Q6IC67;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-JUL-2007, sequence version 3.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=GTP-binding protein 1;
DE Short=G-protein 1;
DE Short=GP-1;
DE Short=GP1;
GN Name=GTPBP1;
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 GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-669.
RC TISSUE=Brain;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-669.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-669.
RX PubMed=9070279; DOI=10.1006/bbrc.1997.6103;
RA Senju S., Nishimura Y.;
RT "Identification of human and mouse GP-1, a putative member of a novel
RT G-protein family.";
RL Biochem. Biophys. Res. Commun. 231:360-364(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-44; SER-47 AND
RP SER-580, AND MASS SPECTROMETRY.
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 [6]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-47, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Promotes degradation of target mRNA species. Plays a
CC role in the regulation of circadian mRNA stability. Binds GTP and
CC has GTPase activity (By similarity).
CC -!- SUBUNIT: Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46,
CC HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with AANAT
CC mRNA, but does not bind mRNA by itself (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the GTPBP1 GTP-binding protein family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51273.1; Type=Erroneous initiation;
CC Sequence=CAG30387.1; Type=Erroneous initiation;
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; AL021707; CAI21603.2; -; Genomic_DNA.
DR EMBL; BC014075; AAH14075.3; -; mRNA.
DR EMBL; CR456501; CAG30387.1; ALT_INIT; mRNA.
DR EMBL; U87964; AAB51273.1; ALT_INIT; mRNA.
DR PIR; JC5291; JC5291.
DR RefSeq; NP_004277.2; NM_004286.4.
DR UniGene; Hs.276925; -.
DR ProteinModelPortal; O00178; -.
DR SMR; O00178; 161-574.
DR IntAct; O00178; 3.
DR MINT; MINT-7944705; -.
DR STRING; 9606.ENSP00000216044; -.
DR PhosphoSite; O00178; -.
DR PaxDb; O00178; -.
DR PRIDE; O00178; -.
DR DNASU; 9567; -.
DR Ensembl; ENST00000216044; ENSP00000216044; ENSG00000100226.
DR GeneID; 9567; -.
DR KEGG; hsa:9567; -.
DR UCSC; uc003awg.3; human.
DR CTD; 9567; -.
DR GeneCards; GC22P039101; -.
DR H-InvDB; HIX0016477; -.
DR HGNC; HGNC:4669; GTPBP1.
DR HPA; HPA003166; -.
DR MIM; 602245; gene.
DR neXtProt; NX_O00178; -.
DR PharmGKB; PA29057; -.
DR eggNOG; COG5258; -.
DR HOGENOM; HOG000176635; -.
DR HOVERGEN; HBG004471; -.
DR InParanoid; O00178; -.
DR OMA; PPGDEAC; -.
DR OrthoDB; EOG70KGPM; -.
DR ChiTaRS; GTPBP1; human.
DR GeneWiki; GTPBP1; -.
DR GenomeRNAi; 9567; -.
DR NextBio; 35877; -.
DR PRO; PR:O00178; -.
DR ArrayExpress; O00178; -.
DR Bgee; O00178; -.
DR CleanEx; HS_GTPBP1; -.
DR Genevestigator; O00178; -.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 669 GTP-binding protein 1.
FT /FTId=PRO_0000122469.
FT NP_BIND 167 174 GTP (Potential).
FT NP_BIND 252 256 GTP (Potential).
FT NP_BIND 308 311 GTP (Potential).
FT COMPBIAS 28 36 Poly-Ala.
FT MOD_RES 6 6 Phosphoserine (By similarity).
FT MOD_RES 12 12 Phosphoserine (By similarity).
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 47 47 Phosphoserine.
FT MOD_RES 580 580 Phosphoserine.
FT VARIANT 91 91 G -> R (in dbSNP:rs11547402).
FT /FTId=VAR_049496.
SQ SEQUENCE 669 AA; 72454 MW; 0814F4DC03740ABE CRC64;
MATERSRSAM DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD
LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV
KSMAEQIEAD VILLRERQEA GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL
THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI
CEKSTKVITF IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN
VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT ASNFSSERMC
PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID DTYSVPGVGT VVSGTTLRGL
IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM PVKEVRGGQT ASFALKKIKR SSIRKGMVMV
SPRLNPQASW EFEAEILVLH HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV
HFRFIKTPEY LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLT
KRDEGGPSGG PAVGAPPPGD EASSVGAGQP AASSNLQPQP KPSSGGRRRG GQRHKVKSQG
ACVTPASGC
//
ID GTPB1_HUMAN Reviewed; 669 AA.
AC O00178; Q6IC67;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-JUL-2007, sequence version 3.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=GTP-binding protein 1;
DE Short=G-protein 1;
DE Short=GP-1;
DE Short=GP1;
GN Name=GTPBP1;
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 GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-669.
RC TISSUE=Brain;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-669.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-669.
RX PubMed=9070279; DOI=10.1006/bbrc.1997.6103;
RA Senju S., Nishimura Y.;
RT "Identification of human and mouse GP-1, a putative member of a novel
RT G-protein family.";
RL Biochem. Biophys. Res. Commun. 231:360-364(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-44; SER-47 AND
RP SER-580, AND MASS SPECTROMETRY.
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 [6]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-47, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Promotes degradation of target mRNA species. Plays a
CC role in the regulation of circadian mRNA stability. Binds GTP and
CC has GTPase activity (By similarity).
CC -!- SUBUNIT: Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46,
CC HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with AANAT
CC mRNA, but does not bind mRNA by itself (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the GTPBP1 GTP-binding protein family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51273.1; Type=Erroneous initiation;
CC Sequence=CAG30387.1; Type=Erroneous initiation;
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; AL021707; CAI21603.2; -; Genomic_DNA.
DR EMBL; BC014075; AAH14075.3; -; mRNA.
DR EMBL; CR456501; CAG30387.1; ALT_INIT; mRNA.
DR EMBL; U87964; AAB51273.1; ALT_INIT; mRNA.
DR PIR; JC5291; JC5291.
DR RefSeq; NP_004277.2; NM_004286.4.
DR UniGene; Hs.276925; -.
DR ProteinModelPortal; O00178; -.
DR SMR; O00178; 161-574.
DR IntAct; O00178; 3.
DR MINT; MINT-7944705; -.
DR STRING; 9606.ENSP00000216044; -.
DR PhosphoSite; O00178; -.
DR PaxDb; O00178; -.
DR PRIDE; O00178; -.
DR DNASU; 9567; -.
DR Ensembl; ENST00000216044; ENSP00000216044; ENSG00000100226.
DR GeneID; 9567; -.
DR KEGG; hsa:9567; -.
DR UCSC; uc003awg.3; human.
DR CTD; 9567; -.
DR GeneCards; GC22P039101; -.
DR H-InvDB; HIX0016477; -.
DR HGNC; HGNC:4669; GTPBP1.
DR HPA; HPA003166; -.
DR MIM; 602245; gene.
DR neXtProt; NX_O00178; -.
DR PharmGKB; PA29057; -.
DR eggNOG; COG5258; -.
DR HOGENOM; HOG000176635; -.
DR HOVERGEN; HBG004471; -.
DR InParanoid; O00178; -.
DR OMA; PPGDEAC; -.
DR OrthoDB; EOG70KGPM; -.
DR ChiTaRS; GTPBP1; human.
DR GeneWiki; GTPBP1; -.
DR GenomeRNAi; 9567; -.
DR NextBio; 35877; -.
DR PRO; PR:O00178; -.
DR ArrayExpress; O00178; -.
DR Bgee; O00178; -.
DR CleanEx; HS_GTPBP1; -.
DR Genevestigator; O00178; -.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 669 GTP-binding protein 1.
FT /FTId=PRO_0000122469.
FT NP_BIND 167 174 GTP (Potential).
FT NP_BIND 252 256 GTP (Potential).
FT NP_BIND 308 311 GTP (Potential).
FT COMPBIAS 28 36 Poly-Ala.
FT MOD_RES 6 6 Phosphoserine (By similarity).
FT MOD_RES 12 12 Phosphoserine (By similarity).
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 47 47 Phosphoserine.
FT MOD_RES 580 580 Phosphoserine.
FT VARIANT 91 91 G -> R (in dbSNP:rs11547402).
FT /FTId=VAR_049496.
SQ SEQUENCE 669 AA; 72454 MW; 0814F4DC03740ABE CRC64;
MATERSRSAM DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD
LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV
KSMAEQIEAD VILLRERQEA GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL
THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI
CEKSTKVITF IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN
VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT ASNFSSERMC
PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID DTYSVPGVGT VVSGTTLRGL
IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM PVKEVRGGQT ASFALKKIKR SSIRKGMVMV
SPRLNPQASW EFEAEILVLH HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV
HFRFIKTPEY LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLT
KRDEGGPSGG PAVGAPPPGD EASSVGAGQP AASSNLQPQP KPSSGGRRRG GQRHKVKSQG
ACVTPASGC
//
MIM
602245
*RECORD*
*FIELD* NO
602245
*FIELD* TI
*602245 GTP-BINDING PROTEIN 1; GTPBP1
;;GP1
*FIELD* TX
CLONING
To identify genes induced in monocytes by interferon-gamma (IFNG;
read more147570), Senju and Nishimura (1997) carried out PCR-based cDNA
subtraction and subsequent differential display on mRNA isolated from a
human monocytic leukemia cell line, THP-1. They detected a novel gene
encoding a protein bearing GTP-binding motifs characteristic of G
proteins. They also identified the mouse homolog of this gene and
designated the gene GP1. The predicted 584-amino acid human protein is
97% identical to the mouse homolog. Northern blot analysis revealed that
the 4-kb GP1 mRNA was expressed in mouse brain, thymus, lung, and
kidney, but was rarely expressed in liver.
MAPPING
By radiation hybrid and genomic sequence analyses, Kudo et al. (2000)
mapped the GTPBP1 gene to chromosome 22q12-q13.1. By FISH, they mapped
the mouse gene to chromosome 15E3.
*FIELD* RF
1. Kudo, H.; Senju, S.; Mitsuya, H.; Nishimura, Y.: Mouse and human
GTPBP2, newly identified members of the GP-1 family of GTPase. Biochem.
Biophys. Res. Commun. 272: 456-465, 2000.
2. Senju, S.; Nishimura, Y.: Identification of human and mouse GP-1,
a putative member of a novel G-protein family. Biochem. Biophys.
Res. Commun. 231: 360-364, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 12/20/2002
*FIELD* CD
Rebekah S. Rasooly: 1/8/1998
*FIELD* ED
mgross: 12/20/2002
carol: 4/22/1999
alopez: 1/14/1998
*RECORD*
*FIELD* NO
602245
*FIELD* TI
*602245 GTP-BINDING PROTEIN 1; GTPBP1
;;GP1
*FIELD* TX
CLONING
To identify genes induced in monocytes by interferon-gamma (IFNG;
read more147570), Senju and Nishimura (1997) carried out PCR-based cDNA
subtraction and subsequent differential display on mRNA isolated from a
human monocytic leukemia cell line, THP-1. They detected a novel gene
encoding a protein bearing GTP-binding motifs characteristic of G
proteins. They also identified the mouse homolog of this gene and
designated the gene GP1. The predicted 584-amino acid human protein is
97% identical to the mouse homolog. Northern blot analysis revealed that
the 4-kb GP1 mRNA was expressed in mouse brain, thymus, lung, and
kidney, but was rarely expressed in liver.
MAPPING
By radiation hybrid and genomic sequence analyses, Kudo et al. (2000)
mapped the GTPBP1 gene to chromosome 22q12-q13.1. By FISH, they mapped
the mouse gene to chromosome 15E3.
*FIELD* RF
1. Kudo, H.; Senju, S.; Mitsuya, H.; Nishimura, Y.: Mouse and human
GTPBP2, newly identified members of the GP-1 family of GTPase. Biochem.
Biophys. Res. Commun. 272: 456-465, 2000.
2. Senju, S.; Nishimura, Y.: Identification of human and mouse GP-1,
a putative member of a novel G-protein family. Biochem. Biophys.
Res. Commun. 231: 360-364, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 12/20/2002
*FIELD* CD
Rebekah S. Rasooly: 1/8/1998
*FIELD* ED
mgross: 12/20/2002
carol: 4/22/1999
alopez: 1/14/1998