GPCRDB: Swiss-Prot entry
ID GNA14_HUMAN STANDARD; PRT; 355 AA.
AC O95837;
DT 15-JUL-1999 (Rel. 38, Created)
DT 15-JUL-1999 (Rel. 38, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Guanine nucleotide-binding protein, alpha-14 subunit (G-protein alpha
DE subunit 14).
GN Name=GNA14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=99208664; PubMed=10191087 [NCBI, ExPASy, EBI, Israel, Japan]; 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 MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
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 This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; AF105201; AAD17944.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF493903; AAM12617.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC027886; AAH27886.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P10824; 1BOF. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR Ensembl; ENSG00000156049; Homo_sapiens
DR Genew; HGNC:4382; GNA14.
DR CleanEx; HGNC:4382; GNA14.
DR MIM; 604397; -. [NCBI / EBI]
DR GeneCards; GNA14.
DR GeneLynx; GNA14.
DR GenAtlas; GNA14.
DR SOURCE; GNA14.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; TAS.
DR GO; GO:0005886; C:plasma membrane; TAS.
DR GO; GO:0003924; F:GTPase activity; TAS.
DR GO; GO:0004871; F:signal transducer activity; NAS.
DR GO; GO:0007165; P:signal transduction; TAS.
DR InterPro; IPR001019; Gprotein_alpha.
DR InterPro; IPR000654; Gprotein_alpha_Q.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00503; G-alpha; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
DR ProDom; PD000281; Gprotein_alpha; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR CMR; O95837.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O95837.
DR ProtoNet; O95837.
DR ProtoMap; O95837.
DR PRESAGE; O95837.
DR DIP; O95837.
DR ModBase; O95837.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW ADP-ribosylation; GTP-binding; Multigene family; Transducer.
FT NP_BIND 42 49 GTP (By similarity).
FT NP_BIND 201 205 GTP (By similarity).
FT NP_BIND 270 273 GTP (By similarity).
FT MOD_RES 179 179 ADP-ribosylarginine (by cholera toxin)
FT (By 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
//