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Protein

Guanine nucleotide-binding protein subunit alpha-14

Gene

GNA14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_18405. Acetylcholine regulates insulin secretion.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_20647. Thromboxane signalling through TP receptor.
REACT_21384. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:4382. GNA14.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • heterotrimeric G-protein complex Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28767.

Polymorphism and mutation databases

BioMutaiGNA14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Guanine nucleotide-binding protein subunit alpha-14PRO_0000203752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791ADP-ribosylarginine; by cholera toxinBy similarity

Keywords - PTMi

ADP-ribosylation

Proteomic databases

MaxQBiO95837.
PaxDbiO95837.
PRIDEiO95837.

PTM databases

PhosphoSiteiO95837.

Expressioni

Gene expression databases

BgeeiO95837.
CleanExiHS_GNA14.
GenevisibleiO95837. HS.

Organism-specific databases

HPAiHPA048886.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
DNAL4O960153EBI-7951023,EBI-742362

Protein-protein interaction databases

BioGridi114989. 3 interactions.
IntActiO95837. 3 interactions.
MINTiMINT-7944128.
STRINGi9606.ENSP00000365807.

Structurei

3D structure databases

ProteinModelPortaliO95837.
SMRiO95837. Positions 31-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322962.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiO95837.
KOiK04636.
OMAiDRIAMPS.
OrthoDBiEOG7ZWD1W.
PhylomeDBiO95837.
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.

O95837-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGCCCLSAE EKESQRISAE IERQLRRDKK DARRELKLLL LGTGESGKST
60 70 80 90 100
FIKQMRIIHG SGYSDEDRKG FTKLVYQNIF TAMQAMIRAM DTLRIQYVCE
110 120 130 140 150
QNKENAQIIR EVEVDKVSML SREQVEAIKQ LWQDPGIQEC YDRRREYQLS
160 170 180 190 200
DSAKYYLTDI DRIATPSFVP TQQDVLRVRV PTTGIIEYPF DLENIIFRMV
210 220 230 240 250
DVGGQRSERR KWIHCFESVT SIIFLVALSE YDQVLAECDN ENRMEESKAL
260 270 280 290 300
FKTIITYPWF LNSSVILFLN KKDLLEEKIM YSHLISYFPE YTGPKQDVRA
310 320 330 340 350
ARDFILKLYQ DQNPDKEKVI YSHFTCATDT DNIRFVFAAV KDTILQLNLR

EFNLV
Length:355
Mass (Da):41,571
Last modified:May 1, 1999 - v1
Checksum:iEAB73A9876E9C47E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105201 mRNA. Translation: AAD17944.1.
AF493903 mRNA. Translation: AAM12617.1.
AK312460 mRNA. Translation: BAG35367.1.
CH471089 Genomic DNA. Translation: EAW62603.1.
BC027886 mRNA. Translation: AAH27886.1.
CCDSiCCDS6657.1.
RefSeqiNP_004288.1. NM_004297.3.
UniGeneiHs.657795.

Genome annotation databases

EnsembliENST00000341700; ENSP00000365807; ENSG00000156049.
GeneIDi9630.
KEGGihsa:9630.
UCSCiuc004aku.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105201 mRNA. Translation: AAD17944.1.
AF493903 mRNA. Translation: AAM12617.1.
AK312460 mRNA. Translation: BAG35367.1.
CH471089 Genomic DNA. Translation: EAW62603.1.
BC027886 mRNA. Translation: AAH27886.1.
CCDSiCCDS6657.1.
RefSeqiNP_004288.1. NM_004297.3.
UniGeneiHs.657795.

3D structure databases

ProteinModelPortaliO95837.
SMRiO95837. Positions 31-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114989. 3 interactions.
IntActiO95837. 3 interactions.
MINTiMINT-7944128.
STRINGi9606.ENSP00000365807.

PTM databases

PhosphoSiteiO95837.

Polymorphism and mutation databases

BioMutaiGNA14.

Proteomic databases

MaxQBiO95837.
PaxDbiO95837.
PRIDEiO95837.

Protocols and materials databases

DNASUi9630.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341700; ENSP00000365807; ENSG00000156049.
GeneIDi9630.
KEGGihsa:9630.
UCSCiuc004aku.3. human.

Organism-specific databases

CTDi9630.
GeneCardsiGC09M080037.
HGNCiHGNC:4382. GNA14.
HPAiHPA048886.
MIMi604397. gene.
neXtProtiNX_O95837.
PharmGKBiPA28767.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG322962.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiO95837.
KOiK04636.
OMAiDRIAMPS.
OrthoDBiEOG7ZWD1W.
PhylomeDBiO95837.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_18405. Acetylcholine regulates insulin secretion.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_20647. Thromboxane signalling through TP receptor.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).

Miscellaneous databases

ChiTaRSiGNA14. human.
GenomeRNAii9630.
NextBioi36139.
PROiO95837.
SOURCEiSearch...

Gene expression databases

BgeeiO95837.
CleanExiHS_GNA14.
GenevisibleiO95837. HS.

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. "Genomic organization of the human G-alpha-14 and G-alpha-Q genes and mutation analysis in chorea-acanthocytosis (CHAC)."
    Rubio J.P., Levy E.R., Dobson-Stone C., Monaco A.P.
    Genomics 57:84-93(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Caudate nucleus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Pancreas and Spleen.

Entry informationi

Entry nameiGNA14_HUMAN
AccessioniPrimary (citable) accession number: O95837
Secondary accession number(s): B1ALW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.