dbPTM

SGTA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SGTA_HUMAN
UniProt AC	O43765
Protein Name	Small glutamine-rich tetratricopeptide repeat-containing protein alpha
Gene Name	SGTA
Organism	Homo sapiens (Human).
Sequence Length	313
Subcellular Localization	Cytoplasm . Nucleus . Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis.
Protein Description	Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. [PubMed: 28104892 Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module]
Protein Sequence	MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Acetylation	----MDNKKRLAYAI ----CCHHHHHHHHH	34.70	7430831
9	Phosphorylation	DNKKRLAYAIIQFLH CHHHHHHHHHHHHHH	11.70	-
67	Phosphorylation	EIFEAAATGKEMPQD HHHHHHHHCCCCCCH	44.02	26074081
76	Methylation	KEMPQDLRSPARTPP CCCCCHHCCCCCCCC	49.21	115916829
77	Phosphorylation	EMPQDLRSPARTPPS CCCCHHCCCCCCCCC	30.15	29255136
81	Phosphorylation	DLRSPARTPPSEEDS HHCCCCCCCCCHHHH	41.48	29255136
84	Phosphorylation	SPARTPPSEEDSAEA CCCCCCCCHHHHHHH	55.62	29255136
88	Phosphorylation	TPPSEEDSAEAERLK CCCCHHHHHHHHHHH	31.15	30266825
95	Acetylation	SAEAERLKTEGNEQM HHHHHHHHCCCCHHH	51.23	26051181
95	Ubiquitination	SAEAERLKTEGNEQM HHHHHHHHCCCCHHH	51.23	21906983
103	Acetylation	TEGNEQMKVENFEAA CCCCHHHEECCHHHH	46.20	25953088
103	Ubiquitination	TEGNEQMKVENFEAA CCCCHHHEECCHHHH	46.20	32015554
116	Ubiquitination	AAVHFYGKAIELNPA HHHHHHHHHEECCHH	34.51	21963094
127	Phosphorylation	LNPANAVYFCNRAAA CCHHHHHHEEHHHHH	10.45	28152594
129	Glutathionylation	PANAVYFCNRAAAYS HHHHHHEEHHHHHHH	1.52	22555962
129	S-nitrosylation	PANAVYFCNRAAAYS HHHHHHEEHHHHHHH	1.52	19483679
129	S-nitrosocysteine	PANAVYFCNRAAAYS HHHHHHEEHHHHHHH	1.52	-
137	Malonylation	NRAAAYSKLGNYAGA HHHHHHHHHCCCHHH	47.97	26320211
137	Ubiquitination	NRAAAYSKLGNYAGA HHHHHHHHHCCCHHH	47.97	27667366
137	Acetylation	NRAAAYSKLGNYAGA HHHHHHHHHCCCHHH	47.97	19608861
141	Phosphorylation	AYSKLGNYAGAVQDC HHHHHCCCHHHHCCC	12.47	28152594
148	Glutathionylation	YAGAVQDCERAICID CHHHHCCCCCEEECC	1.82	22555962
148	S-nitrosylation	YAGAVQDCERAICID CHHHHCCCCCEEECC	1.82	19483679
148	S-nitrosocysteine	YAGAVQDCERAICID CHHHHCCCCCEEECC	1.82	-
153	S-nitrosylation	QDCERAICIDPAYSK CCCCCEEECCHHHHH	2.55	19483679
153	S-nitrosocysteine	QDCERAICIDPAYSK CCCCCEEECCHHHHH	2.55	-
158	Phosphorylation	AICIDPAYSKAYGRM EEECCHHHHHHHHHH	18.98	28152594
159	Phosphorylation	ICIDPAYSKAYGRMG EECCHHHHHHHHHHH	16.96	28152594
160	Acetylation	CIDPAYSKAYGRMGL ECCHHHHHHHHHHHH	32.71	23749302
160	Ubiquitination	CIDPAYSKAYGRMGL ECCHHHHHHHHHHHH	32.71	27667366
160	Neddylation	CIDPAYSKAYGRMGL ECCHHHHHHHHHHHH	32.71	32015554
160	Malonylation	CIDPAYSKAYGRMGL ECCHHHHHHHHHHHH	32.71	26320211
162	Phosphorylation	DPAYSKAYGRMGLAL CHHHHHHHHHHHHHH	14.70	-
171	Phosphorylation	RMGLALSSLNKHVEA HHHHHHHHHHHHHHH	36.49	20068231
174	Ubiquitination	LALSSLNKHVEAVAY HHHHHHHHHHHHHHH	55.08	33845483
181	Phosphorylation	KHVEAVAYYKKALEL HHHHHHHHHHHHHHC	14.82	26074081
182	Phosphorylation	HVEAVAYYKKALELD HHHHHHHHHHHHHCC	9.04	26074081
183	Ubiquitination	VEAVAYYKKALELDP HHHHHHHHHHHHCCC	20.92	21906983
184	Acetylation	EAVAYYKKALELDPD HHHHHHHHHHHCCCC	41.92	27452117
184	Ubiquitination	EAVAYYKKALELDPD HHHHHHHHHHHCCCC	41.92	22817900
194	Phosphorylation	ELDPDNETYKSNLKI HCCCCCCHHHHHHHH	42.37	26074081
195	Nitration	LDPDNETYKSNLKIA CCCCCCHHHHHHHHE	13.26	-
195	Phosphorylation	LDPDNETYKSNLKIA CCCCCCHHHHHHHHE	13.26	26074081
196	Ubiquitination	DPDNETYKSNLKIAE CCCCCHHHHHHHHEE	40.04	23000965
200	Acetylation	ETYKSNLKIAELKLR CHHHHHHHHEEEEEC	44.09	25953088
200	Neddylation	ETYKSNLKIAELKLR CHHHHHHHHEEEEEC	44.09	32015554
200	Ubiquitination	ETYKSNLKIAELKLR CHHHHHHHHEEEEEC	44.09	23000965
205	Ubiquitination	NLKIAELKLREAPSP HHHHEEEEECCCCCC	36.68	23000965
211	Phosphorylation	LKLREAPSPTGGVGS EEECCCCCCCCCCCC	41.99	26074081
213	Phosphorylation	LREAPSPTGGVGSFD ECCCCCCCCCCCCCC	51.40	26074081
263	Phosphorylation	NPLGTPGTSPSQNDL CCCCCCCCCCCHHHH	38.37	26074081
264	Phosphorylation	PLGTPGTSPSQNDLA CCCCCCCCCCHHHHH	28.59	26074081
266	Phosphorylation	GTPGTSPSQNDLASL CCCCCCCCHHHHHHH	41.19	26074081
272	Phosphorylation	PSQNDLASLIQAGQQ CCHHHHHHHHHHHHH	33.05	26074081
297	Phosphorylation	ELIEQLRSQIRSRTP HHHHHHHHHHHHCCC	38.25	25159151
301	Phosphorylation	QLRSQIRSRTPSASN HHHHHHHHCCCCCCC	41.98	29255136
303	Phosphorylation	RSQIRSRTPSASNDD HHHHHHCCCCCCCCC	23.88	29255136
305	Phosphorylation	QIRSRTPSASNDDQQ HHHHCCCCCCCCCCC	43.65	29255136
307	Phosphorylation	RSRTPSASNDDQQE- HHCCCCCCCCCCCC-	45.16	30266825

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
305	S	Phosphorylation	Kinase	AKT2	Q60823	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SGTA_HUMAN !!

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 SGTA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OSTP_HUMAN	SPP1	physical	16189514
JAM1_HUMAN	F11R	physical	16189514
FBLN4_HUMAN	EFEMP2	physical	16189514
C1QT1_HUMAN	C1QTNF1	physical	16189514
SPP2A_HUMAN	SPPL2A	physical	16189514
SYT4_HUMAN	SYT4	physical	16189514
GHR_HUMAN	GHR	physical	12735788
PROF2_HUMAN	PFN2	physical	16169070
PTN_HUMAN	PTN	physical	16169070
HS90A_HUMAN	HSP90AA1	physical	12482202
HSP7C_HUMAN	HSPA8	physical	16777091
HSP74_HUMAN	HSPA4	physical	16777091
BAG6_HUMAN	BAG6	physical	16777091
SMC5_HUMAN	SMC5	physical	22939629
BAG6_HUMAN	BAG6	physical	23246001
UBL4A_HUMAN	UBL4A	physical	23246001
HSP7C_HUMAN	HSPA8	physical	23246001
OSTP_HUMAN	SPP1	physical	21988832
TNR1A_HUMAN	TNFRSF1A	physical	21988832
ADPPT_HUMAN	AASDHPPT	physical	22863883
THIM_HUMAN	ACAA2	physical	22863883
CAZA1_HUMAN	CAPZA1	physical	22863883
CAZA2_HUMAN	CAPZA2	physical	22863883
CTBP2_HUMAN	CTBP2	physical	22863883
DPP3_HUMAN	DPP3	physical	22863883
GGH_HUMAN	GGH	physical	22863883
HXK1_HUMAN	HK1	physical	22863883
PABP1_HUMAN	PABPC1	physical	22863883
PCNA_HUMAN	PCNA	physical	22863883
PDC10_HUMAN	PDCD10	physical	22863883
PCH2_HUMAN	TRIP13	physical	22863883
TRIP6_HUMAN	TRIP6	physical	22863883
1433B_HUMAN	YWHAB	physical	22863883
BAG2_HUMAN	BAG2	physical	25036637
UBL4A_HUMAN	UBL4A	physical	25036637
GET4_HUMAN	GET4	physical	25036637
ASNA_HUMAN	ASNA1	physical	25036637
BAG6_HUMAN	BAG6	physical	25036637
DJB12_HUMAN	DNAJB12	physical	25036637
HS74L_HUMAN	HSPA4L	physical	25036637
SLPI_HUMAN	SLPI	physical	25416956
SODE_HUMAN	SOD3	physical	25416956
OSTP_HUMAN	SPP1	physical	25416956
HSP13_HUMAN	HSPA13	physical	25416956
SYT4_HUMAN	SYT4	physical	25416956
TFF3_HUMAN	TFF3	physical	25416956
TFR1_HUMAN	TFRC	physical	25416956
TGFA_HUMAN	TGFA	physical	25416956
UPK3A_HUMAN	UPK3A	physical	25416956
VIP_HUMAN	VIP	physical	25416956
BAG6_HUMAN	BAG6	physical	25416956
ADIPO_HUMAN	ADIPOQ	physical	25416956
SYT11_HUMAN	SYT11	physical	25416956
TR13B_HUMAN	TNFRSF13B	physical	25416956
LAT_HUMAN	LAT	physical	25416956
FBLN4_HUMAN	EFEMP2	physical	25416956
JAM1_HUMAN	F11R	physical	25416956
TXD12_HUMAN	TXNDC12	physical	25416956
GALA_HUMAN	GAL	physical	25416956
FKBP7_HUMAN	FKBP7	physical	25416956
FXYD7_HUMAN	FXYD7	physical	25416956
WBP1L_HUMAN	WBP1L	physical	25416956
EVA1B_HUMAN	EVA1B	physical	25416956
NNRD_HUMAN	CARKD	physical	25416956
MYDGF_HUMAN	C19orf10	physical	25416956
PCDA4_HUMAN	PCDHA4	physical	25416956
TWSG1_HUMAN	TWSG1	physical	25416956
SMAGP_HUMAN	SMAGP	physical	25416956
PBIP1_HUMAN	PBXIP1	physical	25416956
TMUB2_HUMAN	TMUB2	physical	25416956
TTMP_HUMAN	C3orf52	physical	25416956
FIP1_HUMAN	FIP1L1	physical	25416956
SPP2A_HUMAN	SPPL2A	physical	25416956
C1QT1_HUMAN	C1QTNF1	physical	25416956
C1QT6_HUMAN	C1QTNF6	physical	25416956
PRAP1_HUMAN	PRAP1	physical	25416956
ERP27_HUMAN	ERP27	physical	25416956
ZG16B_HUMAN	ZG16B	physical	25416956
TM174_HUMAN	TMEM174	physical	25416956
KASH5_HUMAN	CCDC155	physical	25416956
IPIL1_HUMAN	ITPRIPL1	physical	25416956
AGR3_HUMAN	AGR3	physical	25416956
TMM31_HUMAN	TMEM31	physical	25416956
FER3L_HUMAN	FERD3L	physical	25416956
ZG16_HUMAN	ZG16	physical	25416956
UBL4A_HUMAN	UBL4A	physical	25415308
BAG6_HUMAN	BAG6	physical	25415308
GCR_HUMAN	NR3C1	physical	24753260
PRGR_HUMAN	PGR	physical	24753260
HSP74_HUMAN	HSPA4	physical	24753260
HS90A_HUMAN	HSP90AA1	physical	24753260
BAG6_HUMAN	BAG6	physical	24424410
SC6B1_YEAST	SBH1	physical	25535373
GET4_HUMAN	GET4	physical	26186194
CGL_HUMAN	CTH	physical	26344197
LSM7_HUMAN	LSM7	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
HSP13_HUMAN	HSPA13	physical	21516116
TMUB2_HUMAN	TMUB2	physical	21516116
ADRM1_MOUSE	Adrm1	physical	26169395
ADRM1_HUMAN	ADRM1	physical	27827410
BAG6_HUMAN	BAG6	physical	27193484

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 SGTA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-305,AND MASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81; SER-301;THR-303 AND SER-305, AND MASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-305, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, AND MASSSPECTROMETRY.	15302935 [Abstract]