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Protein

Guanine nucleotide-binding protein subunit alpha-14

Gene

Gna14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi49 – 491MagnesiumBy similarity
Metal bindingi182 – 1821MagnesiumBy similarity
Binding sitei327 – 3271GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 498GTPBy similarity
Nucleotide bindingi176 – 1827GTPBy similarity
Nucleotide bindingi201 – 2055GTPBy similarity
Nucleotide bindingi270 – 2734GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-399997. Acetylcholine regulates insulin secretion.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-418592. ADP signalling through P2Y purinoceptor 1.
R-MMU-428930. Thromboxane signalling through TP receptor.
R-MMU-432142. Platelet sensitization by LDL.
R-MMU-434316. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
R-MMU-456926. Thrombin signalling through proteinase activated receptors (PARs).

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit alpha-14
Short name:
G alpha-14
Short name:
G-protein subunit alpha-14
Gene namesi
Name:Gna14
Synonyms:Gna-14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:95769. Gna14.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Guanine nucleotide-binding protein subunit alpha-14PRO_0000203753Add
BLAST

Proteomic databases

EPDiP30677.
MaxQBiP30677.
PaxDbiP30677.
PRIDEiP30677.

PTM databases

iPTMnetiP30677.
PhosphoSiteiP30677.
SwissPalmiP30677.

Expressioni

Gene expression databases

BgeeiP30677.
CleanExiMM_GNA14.
GenevisibleiP30677. MM.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025602.

Structurei

3D structure databases

ProteinModelPortaliP30677.
SMRiP30677. Positions 31-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(q) subfamily.Curated

Phylogenomic databases

eggNOGiKOG0085. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP30677.
KOiK04636.
OMAiVEVDKVC.
OrthoDBiEOG7ZWD1W.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000654. Gprotein_alpha_Q.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00442. GPROTEINAQ.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

P30677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGCCCLSAE EKESQRISAE IERQLRRDKK DARRELKLLL LGTGESGKST
60 70 80 90 100
FIKQMRIIHG SGYSDEDRKG FTKLVYQNIF TAMQAMIRAM DTLRIQYMCE
110 120 130 140 150
QNKENAQIIR EVEVDKVTAL SRDQVAAIKQ LWLDPGIQEC YDRRREYQLS
160 170 180 190 200
DSAKYYLTDI ERIAMPSFVP TQQDVLRVRV PTTGIIEYPF DLENIIFRMV
210 220 230 240 250
DVGGQRSERR KWIHCFESVT SIIFLVALSE YDQVLAECDN ENRMEESKAL
260 270 280 290 300
FRTIITYPWF LNSSVILFLN KKDLLEEKIM YSHLISYFPE YTGPKQDVKA
310 320 330 340 350
ARDFILKLYQ DQNPDKEKVI YSHFTCATDT ENIRFVFAAV KDTILQLNLR

EFNLV
Length:355
Mass (Da):41,528
Last modified:July 27, 2011 - v2
Checksum:iD34B39ACD179AE82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 252QL → HV in AAA83222 (PubMed:1946421).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80631 mRNA. Translation: AAA83222.1.
AK160808 mRNA. Translation: BAE36026.1.
AK168498 mRNA. Translation: BAE40384.1.
CH466534 Genomic DNA. Translation: EDL41541.1.
BC027015 mRNA. Translation: AAH27015.1.
M57616 mRNA. Translation: AAA63304.1.
CCDSiCCDS29685.1.
PIRiA41534.
RefSeqiNP_032163.3. NM_008137.4.
UniGeneiMm.313181.

Genome annotation databases

EnsembliENSMUST00000025602; ENSMUSP00000025602; ENSMUSG00000024697.
GeneIDi14675.
KEGGimmu:14675.
UCSCiuc008gwu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80631 mRNA. Translation: AAA83222.1.
AK160808 mRNA. Translation: BAE36026.1.
AK168498 mRNA. Translation: BAE40384.1.
CH466534 Genomic DNA. Translation: EDL41541.1.
BC027015 mRNA. Translation: AAH27015.1.
M57616 mRNA. Translation: AAA63304.1.
CCDSiCCDS29685.1.
PIRiA41534.
RefSeqiNP_032163.3. NM_008137.4.
UniGeneiMm.313181.

3D structure databases

ProteinModelPortaliP30677.
SMRiP30677. Positions 31-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025602.

PTM databases

iPTMnetiP30677.
PhosphoSiteiP30677.
SwissPalmiP30677.

Proteomic databases

EPDiP30677.
MaxQBiP30677.
PaxDbiP30677.
PRIDEiP30677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025602; ENSMUSP00000025602; ENSMUSG00000024697.
GeneIDi14675.
KEGGimmu:14675.
UCSCiuc008gwu.2. mouse.

Organism-specific databases

CTDi9630.
MGIiMGI:95769. Gna14.

Phylogenomic databases

eggNOGiKOG0085. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP30677.
KOiK04636.
OMAiVEVDKVC.
OrthoDBiEOG7ZWD1W.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiR-MMU-399997. Acetylcholine regulates insulin secretion.
R-MMU-416476. G alpha (q) signalling events.
R-MMU-418592. ADP signalling through P2Y purinoceptor 1.
R-MMU-428930. Thromboxane signalling through TP receptor.
R-MMU-432142. Platelet sensitization by LDL.
R-MMU-434316. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
R-MMU-456926. Thrombin signalling through proteinase activated receptors (PARs).

Miscellaneous databases

PROiP30677.
SOURCEiSearch...

Gene expression databases

BgeeiP30677.
CleanExiMM_GNA14.
GenevisibleiP30677. MM.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000654. Gprotein_alpha_Q.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00442. GPROTEINAQ.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of G-protein alpha subunits in the Gq class: expression in murine tissues and in stromal and hematopoietic cell lines."
    Wilkie T.M., Scherle P.A., Strathmann M.P., Slepak V.Z., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 88:10049-10053(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Stomach.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 57-69; 74-88; 163-177 AND 199-206, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "Diversity of the G-protein family: sequences from five additional alpha subunits in the mouse."
    Strathmann M., Wilkie T.M., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 217-267.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Testis.

Entry informationi

Entry nameiGNA14_MOUSE
AccessioniPrimary (citable) accession number: P30677
Secondary accession number(s): Q8R2X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.