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Protein

Guanine nucleotide-binding protein subunit alpha-15

Gene

GNA15

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 bindingi56 – 561MagnesiumBy similarity
Metal bindingi189 – 1891MagnesiumBy similarity
Binding sitei346 – 3461GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 568GTPBy similarity
Nucleotide bindingi183 – 1897GTPBy similarity
Nucleotide bindingi208 – 2125GTPBy similarity
Nucleotide bindingi277 – 2804GTPBy similarity

GO - Molecular functioni

  1. G-protein beta/gamma-subunit complex binding Source: GO_Central
  2. G-protein coupled receptor binding Source: GO_Central
  3. GTPase activity Source: GO_Central
  4. GTP binding Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. activation of phospholipase C activity Source: ProtInc
  2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: GO_Central
  3. blood coagulation Source: Reactome
  4. phospholipase C-activating dopamine receptor signaling pathway Source: GO_Central
  5. phospholipase C-activating G-protein coupled acetylcholine receptor signaling pathway Source: ProtInc
  6. platelet activation Source: Reactome
  7. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
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-15
Short name:
G alpha-15
Short name:
G-protein subunit alpha-15
Alternative name(s):
Epididymis tissue protein Li 17E
Guanine nucleotide-binding protein subunit alpha-16
Short name:
G alpha-16
Short name:
G-protein subunit alpha-16
Gene namesi
Name:GNA15
Synonyms:GNA16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:4383. GNA15.

Subcellular locationi

GO - Cellular componenti

  1. heterotrimeric G-protein complex Source: UniProtKB
  2. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Guanine nucleotide-binding protein subunit alpha-15PRO_0000203755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861ADP-ribosylarginine; by cholera toxinBy similarity

Keywords - PTMi

ADP-ribosylation

Proteomic databases

MaxQBiP30679.
PaxDbiP30679.
PRIDEiP30679.

PTM databases

PhosphoSiteiP30679.

Expressioni

Tissue specificityi

Specifically expressed in hematopoietic cells. Expressed in epididymis (at protein level).1 Publication

Gene expression databases

BgeeiP30679.
CleanExiHS_GNA15.
ExpressionAtlasiP30679. baseline and differential.
GenevestigatoriP30679.

Organism-specific databases

HPAiHPA043113.

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

BioGridi109031. 5 interactions.
IntActiP30679. 9 interactions.
STRINGi9606.ENSP00000262958.

Structurei

3D structure databases

ProteinModelPortaliP30679.
SMRiP30679. Positions 17-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG271464.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP30679.
KOiK04637.
OMAiMYAGCVD.
OrthoDBiEOG7ZWD1W.
PhylomeDBiP30679.
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.

P30679-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARSLTWRCC PWCLTEDEKA AARVDQEINR ILLEQKKQDR GELKLLLLGP
60 70 80 90 100
GESGKSTFIK QMRIIHGAGY SEEERKGFRP LVYQNIFVSM RAMIEAMERL
110 120 130 140 150
QIPFSRPESK HHASLVMSQD PYKVTTFEKR YAAAMQWLWR DAGIRAYYER
160 170 180 190 200
RREFHLLDSA VYYLSHLERI TEEGYVPTAQ DVLRSRMPTT GINEYCFSVQ
210 220 230 240 250
KTNLRIVDVG GQKSERKKWI HCFENVIALI YLASLSEYDQ CLEENNQENR
260 270 280 290 300
MKESLALFGT ILELPWFKST SVILFLNKTD ILEEKIPTSH LATYFPSFQG
310 320 330 340 350
PKQDAEAAKR FILDMYTRMY TGCVDGPEGS KKGARSRRLF SHYTCATDTQ
360 370
NIRKVFKDVR DSVLARYLDE INLL
Length:374
Mass (Da):43,568
Last modified:November 2, 2010 - v2
Checksum:iF32F8C9198FDC26A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti147 – 1471Y → C.6 Publications
Corresponds to variant rs310680 [ dbSNP | Ensembl ].
VAR_028000

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63904 mRNA. Translation: AAA35860.1.
GU727637 mRNA. Translation: ADU87639.1.
GU727645 mRNA. Translation: ADU87646.1.
AF493904 mRNA. Translation: AAM12618.1.
BT009850 mRNA. Translation: AAP88852.1.
AC005264 Genomic DNA. Translation: AAC25612.1.
AC005262 Genomic DNA. Translation: AAC25616.1.
CH471139 Genomic DNA. Translation: EAW69338.1.
BC013585 mRNA. Translation: AAH13585.1.
CCDSiCCDS12104.1.
PIRiA41096.
RefSeqiNP_002059.3. NM_002068.3.
UniGeneiHs.73797.

Genome annotation databases

EnsembliENST00000262958; ENSP00000262958; ENSG00000060558.
GeneIDi2769.
KEGGihsa:2769.
UCSCiuc002lxf.2. human.

Polymorphism databases

DMDMi311033388.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63904 mRNA. Translation: AAA35860.1.
GU727637 mRNA. Translation: ADU87639.1.
GU727645 mRNA. Translation: ADU87646.1.
AF493904 mRNA. Translation: AAM12618.1.
BT009850 mRNA. Translation: AAP88852.1.
AC005264 Genomic DNA. Translation: AAC25612.1.
AC005262 Genomic DNA. Translation: AAC25616.1.
CH471139 Genomic DNA. Translation: EAW69338.1.
BC013585 mRNA. Translation: AAH13585.1.
CCDSiCCDS12104.1.
PIRiA41096.
RefSeqiNP_002059.3. NM_002068.3.
UniGeneiHs.73797.

3D structure databases

ProteinModelPortaliP30679.
SMRiP30679. Positions 17-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109031. 5 interactions.
IntActiP30679. 9 interactions.
STRINGi9606.ENSP00000262958.

Chemistry

BindingDBiP30679.

PTM databases

PhosphoSiteiP30679.

Polymorphism databases

DMDMi311033388.

Proteomic databases

MaxQBiP30679.
PaxDbiP30679.
PRIDEiP30679.

Protocols and materials databases

DNASUi2769.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262958; ENSP00000262958; ENSG00000060558.
GeneIDi2769.
KEGGihsa:2769.
UCSCiuc002lxf.2. human.

Organism-specific databases

CTDi2769.
GeneCardsiGC19P003142.
HGNCiHGNC:4383. GNA15.
HPAiHPA043113.
MIMi139314. gene.
neXtProtiNX_P30679.
PharmGKBiPA28768.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG271464.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP30679.
KOiK04637.
OMAiMYAGCVD.
OrthoDBiEOG7ZWD1W.
PhylomeDBiP30679.
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

ChiTaRSiGNA15. human.
GenomeRNAii2769.
NextBioi10892.
PROiP30679.
SOURCEiSearch...

Gene expression databases

BgeeiP30679.
CleanExiHS_GNA15.
ExpressionAtlasiP30679. baseline and differential.
GenevestigatoriP30679.

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. "G alpha 16, a G protein alpha subunit specifically expressed in hematopoietic cells."
    Amatruda T.T. III, Steele D.A., Slepak V.Z., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 88:5587-5591(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-147.
  2. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
    Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
    Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT CYS-147.
    Tissue: Epididymis.
  3. "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], VARIANT CYS-147.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-147.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT CYS-147.
  7. "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], VARIANT CYS-147.
    Tissue: Lung.

Entry informationi

Entry nameiGNA15_HUMAN
AccessioniPrimary (citable) accession number: P30679
Secondary accession number(s): E9KL40
, E9KL47, O75247, Q53XK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 2, 2010
Last modified: February 4, 2015
This is version 153 of the entry and version 2 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.