Q14344 (GNA13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein subunit alpha-13
Short name=G alpha-13
Short name=G-protein subunit alpha-13

Gene names

Name:

GNA13

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UBXD5. Interacts with HAX1. Ref.8 Ref.9
Subcellular location	Membrane; Lipid-anchor. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.10
Post-translational modification	Palmitoylation is critical for proper membrane localization and signaling. Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation.
Sequence similarities	Belongs to the G-alpha family. G(12) subfamily.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Inferred from Biological aspect of Ancestor. Source: RefGenome activation of adenylate cyclase activity by G-protein signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome activation of phospholipase D activity Inferred from Biological aspect of Ancestor. Source: RefGenome cellular component movement Traceable author statement. Source: ProtInc platelet activation Traceable author statement. Source: Reactome
Cellular component	brush border membrane Inferred from Biological aspect of Ancestor. Source: RefGenome heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D5 dopamine receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from Biological aspect of Ancestor. Source: RefGenome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome type 1 angiotensin receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGEF1	Q92888	2	EBI-465387,EBI-465400

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Guanine nucleotide-binding protein subunit alpha-13		PRO_0000203773
Regions
	Nucleotide binding	55 – 62	8	GTP By similarity
	Nucleotide binding	197 – 203	7	GTP By similarity
	Nucleotide binding	222 – 226	5	GTP By similarity
	Nucleotide binding	291 – 294	4	GTP By similarity
Sites
	Metal binding	62	1	Magnesium By similarity
	Metal binding	203	1	Magnesium By similarity
	Binding site	349	1	GTP; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	203	1	Phosphothreonine; by PKA Ref.7
	Lipidation	14	1	S-palmitoyl cysteine Ref.6
	Lipidation	18	1	S-palmitoyl cysteine Ref.6
Natural variations
	Natural variant	221	1	V → L. Ref.1 Corresponds to variant rs1062597 [ dbSNP | Ensembl ].		VAR_017160
Experimental info
	Mutagenesis	14	1	C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. Ref.6
	Mutagenesis	18	1	C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. Ref.6
	Mutagenesis	203	1	T → A: Abolishes phosphorylation by PKA; disrupts heterotrimer stability. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q14344 [UniParc]. Last modified October 31, 2003. Version 2. Checksum: 929B7B6473C54F2E	FASTA	377	44,050
	10 20 30 40 50 60 MADFLPSRSV LSVCFPGCLL TSGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG 70 80 90 100 110 120 KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNSNQQHGD 130 140 150 160 170 180 KMMSFDTRAP MAAQGMVETR VFLQYLPAIR ALWADSGIQN AYDRRREFQL GESVKYFLDN 190 200 210 220 230 240 LDKLGEPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV 250 260 270 280 290 300 TSILFLVSSS EFDQVLMEDR LTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV 310 320 330 340 350 360 QIVSIKDYFL EFEGDPHCLR DVQKFLVECF RNKRRDQQQK PLYHHFTTAI NTENIRLVFR 370 DVKDTILHDN LKQLMLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of GTP-binding protein alpha subunits in human thymocytes." Kabouridis P.S., Waters S.T., Escobar S., Stanners J., Tsoukas C.D. Mol. Cell. Biochem. 144:45-51(1995) [PubMed: 7791744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-221. Tissue: Thymus.
[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]. Tissue: Brain.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hippocampus.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Melanoma.
[6]	"Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding." Bhattacharyya R., Wedegaertner P.B. J. Biol. Chem. 275:14992-14999(2000) [PubMed: 10747909] [Abstract] Cited for: PALMITOYLATION AT CYS-14 AND CYS-18, MUTAGENESIS OF CYS-14 AND CYS-18.
[7]	"PKA-mediated phosphorylation of Galpha 13 switch I region alters the Galpha beta gamma 13-GPCR complex and inhibits Rho activation." Manganello J.M., Huang J.-S., Kozasa T., Voyno-Yasenetskaya T.A., Le Breton G.C. J. Biol. Chem. 278:124-130(2003) [PubMed: 12399457] [Abstract] Cited for: PHOSPHORYLATION AT THR-203, MUTAGENESIS OF THR-203.
[8]	"Galpha13 stimulates cell migration through cortactin-interacting protein Hax-1." Radhika V., Onesime D., Ha J.H., Dhanasekaran N. J. Biol. Chem. 279:49406-49413(2004) [PubMed: 15339924] [Abstract] Cited for: INTERACTION WITH HAX1.
[9]	"Socius, a novel binding partner of Galpha12/13, promotes the Galpha12-induced RhoA activation." Tateiwa K., Katoh H., Negishi M. Biochem. Biophys. Res. Commun. 337:615-620(2005) [PubMed: 16202387] [Abstract] Cited for: INTERACTION WITH UBXD5.
[10]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L22075 mRNA. Translation: AAA74235.1. AF493902 mRNA. Translation: AAM12616.1. AK313672 mRNA. Translation: BAG36424.1. CH471099 Genomic DNA. Translation: EAW88993.1. BC036756 mRNA. Translation: AAH36756.1.
IPI	IPI00290928.
PIR	I57490.
RefSeq	NP_006563.2. NM_006572.4.
UniGene	Hs.515018.
3D structure databases
ProteinModelPortal	Q14344.
SMR	Q14344. Positions 47-369.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14344. 2 interactions.
STRING	Q14344.
PTM databases
PhosphoSite	Q14344.
Polymorphism databases
DMDM	38258936.
Proteomic databases
PeptideAtlas	Q14344.
PRIDE	Q14344.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000439174; ENSP00000400717; ENSG00000120063.
GeneID	10672.
KEGG	hsa:10672.
UCSC	uc002jfc.1. human.
Organism-specific databases
CTD	10672.
GeneCards	GC17M063005.
H-InvDB	HIX0014101.
HGNC	HGNC:4381. GNA13.
HPA	HPA010087.
MIM	604406. gene.
neXtProt	NX_Q14344.
PharmGKB	PA28766.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18849.
GeneTree	ENSGT00560000077005.
HOGENOM	HBG444960.
HOVERGEN	HBG063184.
InParanoid	Q14344.
OMA	CFPGCVL.
OrthoDB	EOG444KKJ.
PhylomeDB	Q14344.
Enzyme and pathway databases
Pathway_Interaction_DB	lysophospholipid_pathway. LPA receptor mediated events. er_nongenomic_pathway. Plasma membrane estrogen receptor signaling. s1p_s1p2_pathway. S1P2 pathway. s1p_s1p3_pathway. S1P3 pathway. s1p_s1p4_pathway. S1P4 pathway. s1p_meta_pathway. Sphingosine 1-phosphate (S1P) pathway. txa2pathway. Thromboxane A2 receptor signaling.
Reactome	REACT_111102. Signal Transduction. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q14344.
Bgee	Q14344.
CleanEx	HS_GNA13.
Genevestigator	Q14344.
GermOnline	ENSG00000120063. Homo sapiens.
Family and domain databases
InterPro	IPR000469. Gprotein_alpha12. IPR001019. Gprotein_alpha_su. IPR011025. GproteinA_insert. [Graphical view]
Gene3D	G3DSA:1.10.400.10. GproteinA_insert. 1 hit.
KO	K04639.
PANTHER	PTHR10218. Gprotein_alph_bd. 1 hit.
Pfam	PF00503. G-alpha. 1 hit. [Graphical view]
PRINTS	PR00318. GPROTEINA. PR00440. GPROTEINA12.
SMART	SM00275. G_alpha. 1 hit. [Graphical view]
SUPFAM	SSF47895. Transducn_insert. 1 hit.
ProtoNet	Search...
Other
NextBio	40583.
SOURCE	Search...

Entry information

Entry name

GNA13_HUMAN

Accession

Primary (citable) accession number: Q14344
Secondary accession number(s): B2R977, Q8TD70

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 31, 2003
Last modified:	January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.