Full text data of GNA14
GNA14
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Guanine nucleotide-binding protein subunit alpha-14; G alpha-14; G-protein subunit alpha-14
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Guanine nucleotide-binding protein subunit alpha-14; G alpha-14; G-protein subunit alpha-14
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00000695
IPI00000695 Guanine nucleotide-binding protein, alpha-14 subunit Guanine nucleotide-binding protein, alpha-14 subunit membrane n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a 1 n/a n/a inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
IPI00000695 Guanine nucleotide-binding protein, alpha-14 subunit Guanine nucleotide-binding protein, alpha-14 subunit membrane n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a 1 n/a n/a inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
UniProt
O95837
ID GNA14_HUMAN Reviewed; 355 AA.
AC O95837;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-14;
DE Short=G alpha-14;
DE Short=G-protein subunit alpha-14;
GN Name=GNA14;
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 [MRNA].
RX PubMed=10191087; DOI=10.1006/geno.1999.5758;
RA Rubio J.P., Levy E.R., Dobson-Stone C., Monaco A.P.;
RT "Genomic organization of the human G-alpha-14 and G-alpha-Q genes and
RT mutation analysis in chorea-acanthocytosis (CHAC).";
RL Genomics 57:84-93(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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: Guanine nucleotide-binding proteins (G proteins) are
CC involved as modulators or transducers in various transmembrane
CC signaling systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC gamma. The alpha chain contains the guanine nucleotide binding
CC site.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
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; AF105201; AAD17944.1; -; mRNA.
DR EMBL; AF493903; AAM12617.1; -; mRNA.
DR EMBL; BC027886; AAH27886.1; -; mRNA.
DR RefSeq; NP_004288.1; NM_004297.3.
DR UniGene; Hs.657795; -.
DR ProteinModelPortal; O95837; -.
DR SMR; O95837; 33-350.
DR IntAct; O95837; 2.
DR MINT; MINT-7944128; -.
DR STRING; 9606.ENSP00000365807; -.
DR PhosphoSite; O95837; -.
DR PaxDb; O95837; -.
DR PRIDE; O95837; -.
DR DNASU; 9630; -.
DR Ensembl; ENST00000341700; ENSP00000365807; ENSG00000156049.
DR GeneID; 9630; -.
DR KEGG; hsa:9630; -.
DR UCSC; uc004aku.3; human.
DR CTD; 9630; -.
DR GeneCards; GC09M080037; -.
DR HGNC; HGNC:4382; GNA14.
DR HPA; HPA048886; -.
DR MIM; 604397; gene.
DR neXtProt; NX_O95837; -.
DR PharmGKB; PA28767; -.
DR eggNOG; NOG322962; -.
DR HOGENOM; HOG000038729; -.
DR HOVERGEN; HBG063184; -.
DR InParanoid; O95837; -.
DR KO; K04636; -.
DR OMA; DRIAMPS; -.
DR OrthoDB; EOG7ZWD1W; -.
DR PhylomeDB; O95837; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; GNA14; human.
DR GenomeRNAi; 9630; -.
DR NextBio; 36139; -.
DR PRO; PR:O95837; -.
DR ArrayExpress; O95837; -.
DR Bgee; O95837; -.
DR CleanEx; HS_GNA14; -.
DR Genevestigator; O95837; -.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome.
DR GO; GO:0001664; F:G-protein coupled receptor binding; IBA:RefGenome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004871; F:signal transducer activity; IBA:RefGenome.
DR GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:RefGenome.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR Gene3D; 1.10.400.10; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Complete proteome; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1 355 Guanine nucleotide-binding protein
FT subunit alpha-14.
FT /FTId=PRO_0000203752.
FT NP_BIND 42 49 GTP (By similarity).
FT NP_BIND 176 182 GTP (By similarity).
FT NP_BIND 201 205 GTP (By similarity).
FT NP_BIND 270 273 GTP (By similarity).
FT METAL 49 49 Magnesium (By similarity).
FT METAL 182 182 Magnesium (By similarity).
FT BINDING 327 327 GTP; via amide nitrogen (By similarity).
FT MOD_RES 179 179 ADP-ribosylarginine; by cholera toxin (By
FT similarity).
SQ SEQUENCE 355 AA; 41571 MW; EAB73A9876E9C47E CRC64;
MAGCCCLSAE EKESQRISAE IERQLRRDKK DARRELKLLL LGTGESGKST FIKQMRIIHG
SGYSDEDRKG FTKLVYQNIF TAMQAMIRAM DTLRIQYVCE QNKENAQIIR EVEVDKVSML
SREQVEAIKQ LWQDPGIQEC YDRRREYQLS DSAKYYLTDI DRIATPSFVP TQQDVLRVRV
PTTGIIEYPF DLENIIFRMV DVGGQRSERR KWIHCFESVT SIIFLVALSE YDQVLAECDN
ENRMEESKAL FKTIITYPWF LNSSVILFLN KKDLLEEKIM YSHLISYFPE YTGPKQDVRA
ARDFILKLYQ DQNPDKEKVI YSHFTCATDT DNIRFVFAAV KDTILQLNLR EFNLV
//
ID GNA14_HUMAN Reviewed; 355 AA.
AC O95837;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-14;
DE Short=G alpha-14;
DE Short=G-protein subunit alpha-14;
GN Name=GNA14;
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 [MRNA].
RX PubMed=10191087; DOI=10.1006/geno.1999.5758;
RA Rubio J.P., Levy E.R., Dobson-Stone C., Monaco A.P.;
RT "Genomic organization of the human G-alpha-14 and G-alpha-Q genes and
RT mutation analysis in chorea-acanthocytosis (CHAC).";
RL Genomics 57:84-93(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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: Guanine nucleotide-binding proteins (G proteins) are
CC involved as modulators or transducers in various transmembrane
CC signaling systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC gamma. The alpha chain contains the guanine nucleotide binding
CC site.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
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; AF105201; AAD17944.1; -; mRNA.
DR EMBL; AF493903; AAM12617.1; -; mRNA.
DR EMBL; BC027886; AAH27886.1; -; mRNA.
DR RefSeq; NP_004288.1; NM_004297.3.
DR UniGene; Hs.657795; -.
DR ProteinModelPortal; O95837; -.
DR SMR; O95837; 33-350.
DR IntAct; O95837; 2.
DR MINT; MINT-7944128; -.
DR STRING; 9606.ENSP00000365807; -.
DR PhosphoSite; O95837; -.
DR PaxDb; O95837; -.
DR PRIDE; O95837; -.
DR DNASU; 9630; -.
DR Ensembl; ENST00000341700; ENSP00000365807; ENSG00000156049.
DR GeneID; 9630; -.
DR KEGG; hsa:9630; -.
DR UCSC; uc004aku.3; human.
DR CTD; 9630; -.
DR GeneCards; GC09M080037; -.
DR HGNC; HGNC:4382; GNA14.
DR HPA; HPA048886; -.
DR MIM; 604397; gene.
DR neXtProt; NX_O95837; -.
DR PharmGKB; PA28767; -.
DR eggNOG; NOG322962; -.
DR HOGENOM; HOG000038729; -.
DR HOVERGEN; HBG063184; -.
DR InParanoid; O95837; -.
DR KO; K04636; -.
DR OMA; DRIAMPS; -.
DR OrthoDB; EOG7ZWD1W; -.
DR PhylomeDB; O95837; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; GNA14; human.
DR GenomeRNAi; 9630; -.
DR NextBio; 36139; -.
DR PRO; PR:O95837; -.
DR ArrayExpress; O95837; -.
DR Bgee; O95837; -.
DR CleanEx; HS_GNA14; -.
DR Genevestigator; O95837; -.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome.
DR GO; GO:0001664; F:G-protein coupled receptor binding; IBA:RefGenome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004871; F:signal transducer activity; IBA:RefGenome.
DR GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:RefGenome.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR Gene3D; 1.10.400.10; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Complete proteome; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1 355 Guanine nucleotide-binding protein
FT subunit alpha-14.
FT /FTId=PRO_0000203752.
FT NP_BIND 42 49 GTP (By similarity).
FT NP_BIND 176 182 GTP (By similarity).
FT NP_BIND 201 205 GTP (By similarity).
FT NP_BIND 270 273 GTP (By similarity).
FT METAL 49 49 Magnesium (By similarity).
FT METAL 182 182 Magnesium (By similarity).
FT BINDING 327 327 GTP; via amide nitrogen (By similarity).
FT MOD_RES 179 179 ADP-ribosylarginine; by cholera toxin (By
FT similarity).
SQ SEQUENCE 355 AA; 41571 MW; EAB73A9876E9C47E CRC64;
MAGCCCLSAE EKESQRISAE IERQLRRDKK DARRELKLLL LGTGESGKST FIKQMRIIHG
SGYSDEDRKG FTKLVYQNIF TAMQAMIRAM DTLRIQYVCE QNKENAQIIR EVEVDKVSML
SREQVEAIKQ LWQDPGIQEC YDRRREYQLS DSAKYYLTDI DRIATPSFVP TQQDVLRVRV
PTTGIIEYPF DLENIIFRMV DVGGQRSERR KWIHCFESVT SIIFLVALSE YDQVLAECDN
ENRMEESKAL FKTIITYPWF LNSSVILFLN KKDLLEEKIM YSHLISYFPE YTGPKQDVRA
ARDFILKLYQ DQNPDKEKVI YSHFTCATDT DNIRFVFAAV KDTILQLNLR EFNLV
//
MIM
604397
*RECORD*
*FIELD* NO
604397
*FIELD* TI
*604397 GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-14; GNA14
*FIELD* TX
For background information on G proteins, see 600874.
read more
Rubio et al. (1999) constructed a YAC contig of the choreoacanthocytosis
(CHAC; 200150) critical region on chromosome 9q21. Using a PCR-based
strategy with primers from the mouse G-alpha-14 gene, they cloned a
full-length human G-alpha-14 (GNA14) cDNA from the contig. GNA14, which
contains 7 exons, encodes a predicted 355-amino acid protein that is 98%
and 99% identical to the mouse and bovine proteins, respectively. Rubio
et al. (1999) established the genetic structure of both the GNA14 and
GNAQ (600998) genes, which are situated in a head-to-tail arrangement
(cen--GNAQ--GNA14--qter). Northern blot analysis revealed that
expression of GNAQ is ubiquitous, whereas that of GNA14 is restricted to
fetal lung and kidney. Mutation analysis of GNAQ and GNA14 in 10 CHAC
individuals identified no changes likely to cause the disease.
By fluorescence in situ hybridization, Rubio et al. (1999) confirmed the
assignment of the GNA14 gene to 9q21.
*FIELD* RF
1. Rubio, J. P.; Levy, E. R.; Dobson-Stone, C.; Monaco, A. P.: Genomic
organization of the human G-alpha-14 and G-alpha-Q genes and mutation
analysis in chorea-acanthocytosis (CHAC). Genomics 57: 84-93, 1999.
*FIELD* CD
Paul J. Converse: 1/3/2000
*FIELD* ED
carol: 01/03/2000
carol: 1/3/2000
*RECORD*
*FIELD* NO
604397
*FIELD* TI
*604397 GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-14; GNA14
*FIELD* TX
For background information on G proteins, see 600874.
read more
Rubio et al. (1999) constructed a YAC contig of the choreoacanthocytosis
(CHAC; 200150) critical region on chromosome 9q21. Using a PCR-based
strategy with primers from the mouse G-alpha-14 gene, they cloned a
full-length human G-alpha-14 (GNA14) cDNA from the contig. GNA14, which
contains 7 exons, encodes a predicted 355-amino acid protein that is 98%
and 99% identical to the mouse and bovine proteins, respectively. Rubio
et al. (1999) established the genetic structure of both the GNA14 and
GNAQ (600998) genes, which are situated in a head-to-tail arrangement
(cen--GNAQ--GNA14--qter). Northern blot analysis revealed that
expression of GNAQ is ubiquitous, whereas that of GNA14 is restricted to
fetal lung and kidney. Mutation analysis of GNAQ and GNA14 in 10 CHAC
individuals identified no changes likely to cause the disease.
By fluorescence in situ hybridization, Rubio et al. (1999) confirmed the
assignment of the GNA14 gene to 9q21.
*FIELD* RF
1. Rubio, J. P.; Levy, E. R.; Dobson-Stone, C.; Monaco, A. P.: Genomic
organization of the human G-alpha-14 and G-alpha-Q genes and mutation
analysis in chorea-acanthocytosis (CHAC). Genomics 57: 84-93, 1999.
*FIELD* CD
Paul J. Converse: 1/3/2000
*FIELD* ED
carol: 01/03/2000
carol: 1/3/2000