Gna13
entrez
14674
canonical
uniprot
P27601
canonical
ensembl
ENSMUSG00000020611
resolver
ensp
ENSMUSP00000020930
resolver
ensp
ENSMUSP00000102313
resolver
enst
ENSMUST00000020930
resolver
enst
ENSMUST00000106702
resolver
genesymbol
Gna13
resolver
genesymbol_syn
Gna-13
resolver
uniprot
F6Z5J2
resolver
uniprot
Q3UE40
resolver
uniprot
Q6PF99
resolver
uniprot
Q8K086
resolver
uniprot
Q9D034
resolver
uniprot_entry
F6Z5J2_MOUSE
resolver
uniprot_entry
GNA13_MOUSE
resolver
uniprot_entry
Q3UE40_MOUSE
resolver
uniprot_entry
Q8K086_MOUSE
resolver
uniprot_entry
Q9D034_MOUSE
resolver
uniprot_sec
Q6PF99
resolver
amino_acid_sequence
MADFLPSRSVLSVCFPGCVLTNGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNKNQLHGDKLMAFDTRAPMAAQGMVETRVFLQYLPAIRALWEDSGIQNAYDRRREFQLGESVKYFLDNLDKLGVPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEFDQVLMEDRQTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKVQVVSIKDYFLEFEGDPHCLRDVQKFLVECFRGKRRDQQQRPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ
uniprot
proteins
function
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (PubMed:16388592, PubMed:19151758, PubMed:21212405). Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) (PubMed:16388592). GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) (PubMed:19151758, PubMed:21212405). Promotes tumor cell invasion and metastasis by activating Rho/ROCK signaling pathway (By similarity). Inhibits CDH1-mediated cell adhesion in a process independent from Rho activation (By similarity). In lymphoid follicles, transmits P2RY8- and S1PR2-dependent signals that lead to inhibition of germinal center (GC) B cell growth and migration outside the GC niche. {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:19151758, ECO:0000269|PubMed:21212405, ECO:0000269|PubMed:25274307}.
uniprot
proteins
mass_dalton
44055
uniprot
proteins
post_translational_modification
PTM: Palmitoylation is critical for proper membrane localization and signaling. {ECO:0000250|UniProtKB:Q14344}.; PTM: Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation. {ECO:0000250|UniProtKB:Q14344}.
uniprot
proteins
protein_family
G(12) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
15240885
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16388592
uniprot
proteins
pubmed
18703424
uniprot
proteins
pubmed
18940608
uniprot
proteins
pubmed
1905812
uniprot
proteins
pubmed
19151758
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21212405
uniprot
proteins
pubmed
23994616
uniprot
proteins
pubmed
2508088
uniprot
proteins
pubmed
25274307
uniprot
proteins
pubmed
31875850
uniprot
proteins
sequence_length
377
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14344}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14344}; Cytoplasmic side {ECO:0000250|UniProtKB:Q14344}. Cytoplasm {ECO:0000269|PubMed:18703424}. Nucleus {ECO:0000269|PubMed:18703424}. Note=Associated to the plasma membrane via lipid-anchor (By similarity). Detected in the cytoplasm of Leydig cells and in the seminiferous epithelium, including differentiating cells from the spermatogonia to mature spermatozoa stages (PubMed:18703424). In round spermatids, also present in the nuclei (PubMed:18703424). {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:18703424}.
uniprot
proteins