dbPTM

GNA13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GNA13_HUMAN
UniProt AC	Q14344
Protein Name	Guanine nucleotide-binding protein subunit alpha-13
Gene Name	GNA13
Organism	Homo sapiens (Human).
Sequence Length	377
Subcellular Localization	Cell membrane Lipid-anchor . Melanosome . Cytoplasm . Nucleus . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Detected in the cytoplasm of Leydig cells and in the seminiferous epithelium, includ
Protein Description	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. [PubMed: 15240885]
Protein Sequence	MADFLPSRSVLSVCFPGCLLTSGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNSNQQHGDKMMSFDTRAPMAAQGMVETRVFLQYLPAIRALWADSGIQNAYDRRREFQLGESVKYFLDNLDKLGEPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEFDQVLMEDRLTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKVQIVSIKDYFLEFEGDPHCLRDVQKFLVECFRNKRRDQQQKPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	ADFLPSRSVLSVCFP CCCCCCCHHHHHCCC	31.57	28111955
12	Phosphorylation	LPSRSVLSVCFPGCL CCCCHHHHHCCCCCC	18.06	28111955
14	S-palmitoylation	SRSVLSVCFPGCLLT CCHHHHHCCCCCCCC	2.83	10747909
18	S-palmitoylation	LSVCFPGCLLTSGEA HHHCCCCCCCCCCHH	2.61	10747909
21	Phosphorylation	CFPGCLLTSGEAEQQ CCCCCCCCCCHHHHH	23.03	28111955
22	Phosphorylation	FPGCLLTSGEAEQQR CCCCCCCCCHHHHHH	34.31	28111955
31	Phosphorylation	EAEQQRKSKEIDKCL HHHHHHHHHHHHHHH	37.40	28111955
36	Ubiquitination	RKSKEIDKCLSREKT HHHHHHHHHHHCCHH	42.61	-
43	Phosphorylation	KCLSREKTYVKRLVK HHHHCCHHHHHHHHH	28.88	20068231
44	Phosphorylation	CLSREKTYVKRLVKI HHHCCHHHHHHHHHH	18.29	20068231
59	Phosphorylation	LLLGAGESGKSTFLK HHHCCCCCCHHHHHH	51.07	20068231
61	Ubiquitination	LGAGESGKSTFLKQM HCCCCCCHHHHHHHH	56.45	-
66	Ubiquitination	SGKSTFLKQMRIIHG CCHHHHHHHHHHHHC	37.55	-
87	Phosphorylation	AREEFRPTIYSNVIK HHHHHHHHHHHHHHC	28.43	20068231
88	Ubiquitination	REEFRPTIYSNVIKG HHHHHHHHHHHHHCC	3.83	-
90	Phosphorylation	EFRPTIYSNVIKGMR HHHHHHHHHHHCCCE	22.29	20068231
105	Ubiquitination	VLVDAREKLHIPWGD EEEECHHHCCCCCCC	39.55	-
119	Ubiquitination	DNSNQQHGDKMMSFD CCCCCCCCCEECCCC	31.71	21906983
124	Ubiquitination	QHGDKMMSFDTRAPM CCCCEECCCCCCCHH	19.24	-
131	Sulfoxidation	SFDTRAPMAAQGMVE CCCCCCHHHHCCCHH	4.75	21406390
183	Ubiquitination	YFLDNLDKLGEPDYI HHHHCHHHCCCCCCC	62.65	21890473
189	Phosphorylation	DKLGEPDYIPSQQDI HHCCCCCCCCCHHHE	26.00	-
190	Ubiquitination	KLGEPDYIPSQQDIL HCCCCCCCCCHHHEE	3.27	21890473
203	Phosphorylation	ILLARRPTKGIHEYD EEECCCCCCCCEECC	39.84	12399457
204	Malonylation	LLARRPTKGIHEYDF EECCCCCCCCEECCE	59.56	26320211
204	Ubiquitination	LLARRPTKGIHEYDF EECCCCCCCCEECCE	59.56	-
214	Ubiquitination	HEYDFEIKNVPFKMV EECCEEEECCCCEEE	44.70	21890473
214	Ubiquitination	HEYDFEIKNVPFKMV EECCEEEECCCCEEE	44.70	21890473
219	Ubiquitination	EIKNVPFKMVDVGGQ EEECCCCEEEECCCC	31.76	-
262	Phosphorylation	VLMEDRLTNRLTESL HHCHHHHHHHHHHHH	21.13	26074081
266	Phosphorylation	DRLTNRLTESLNIFE HHHHHHHHHHHCHHH	21.94	26074081
268	Phosphorylation	LTNRLTESLNIFETI HHHHHHHHHCHHHHH	22.83	26074081
268	Ubiquitination	LTNRLTESLNIFETI HHHHHHHHHCHHHHH	22.83	-
274	Phosphorylation	ESLNIFETIVNNRVF HHHCHHHHHHHCCCC	21.34	26074081
277	Ubiquitination	NIFETIVNNRVFSNV CHHHHHHHCCCCCCC	27.09	-
285	Phosphorylation	NRVFSNVSIILFLNK CCCCCCCEEEEEECC	14.25	-
363	Ubiquitination	RLVFRDVKDTILHDN EEEEECHHHHHHCHH	54.14	-
363	Acetylation	RLVFRDVKDTILHDN EEEEECHHHHHHCHH	54.14	7695247
363	Malonylation	RLVFRDVKDTILHDN EEEEECHHHHHHCHH	54.14	26320211
372	Ubiquitination	TILHDNLKQLMLQ-- HHHCHHHHHHHCC--	47.87	21890473
372	Acetylation	TILHDNLKQLMLQ-- HHHCHHHHHHHCC--	47.87	7695257

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
203	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
203	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
203	T	Phosphorylation	Kinase	PKA	-	Uniprot
203	T	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
203	T	Phosphorylation		12399457
Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of GNA13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AKAP3_HUMAN	AKAP3	physical	11696326
ARHG1_HUMAN	ARHGEF1	physical	12681510
ARHG1_HUMAN	ARHGEF1	physical	9641916
RADI_HUMAN	RDX	physical	10816569
FAK2_HUMAN	PTK2B	physical	10821841
KAP2_HUMAN	PRKAR2A	physical	11696326
ARHGC_HUMAN	ARHGEF12	physical	11094164
PAR1_HUMAN	F2R	physical	8290554
TA2R_HUMAN	TBXA2R	physical	8290554
ARHGB_HUMAN	ARHGEF11	physical	10026210
M3K5_HUMAN	MAP3K5	physical	17595347
ARG28_HUMAN	ARHGEF28	physical	17595347
AIP_HUMAN	AIP	physical	19390533
CXCR5_HUMAN	CXCR5	physical	23773523
CXCR4_HUMAN	CXCR4	physical	23773523
PAR1_HUMAN	F2R	physical	23773523

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GNA13_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Galpha 13 requires palmitoylation for plasma membrane localization,Rho-dependent signaling, and promotion of p115-RhoGEF membranebinding."; Bhattacharyya R., Wedegaertner P.B.; J. Biol. Chem. 275:14992-14999(2000). Cited for: PALMITOYLATION AT CYS-14 AND CYS-18, AND MUTAGENESIS OF CYS-14 ANDCYS-18.	10747909 [Abstract]
Phosphorylation
Reference	PubMed
"PKA-mediated phosphorylation of Galpha 13 switch I region alters theGalpha 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). Cited for: PHOSPHORYLATION AT THR-203, AND MUTAGENESIS OF THR-203.	12399457 [Abstract]

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