dbPTM

SH24A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SH24A_HUMAN
UniProt AC	Q9H788
Protein Name	SH2 domain-containing protein 4A
Gene Name	SH2D4A
Organism	Homo sapiens (Human).
Sequence Length	454
Subcellular Localization	Cytoplasm . Located at podocyte foot processes..
Protein Description	Inhibits estrogen-induced cell proliferation by competing with PLCG for binding to ESR1, blocking the effect of estrogen on PLCG and repressing estrogen-induced proliferation. May play a role in T-cell development and function..
Protein Sequence	MLKQILSEMYIDPDLLAELSEEQKQILFFKMREEQIRRWKEREAAMERKESLPVKPRPKKENGKSVHWKLGADKEVWVWVMGEHHLDKPYDVLCNEIIAERARLKAEQEAEEPRKTHSEEFTNSLKTKSQYHDLQAPDNQQTKDIWKKVAEKEELEQGSRPAPTLEEEKIRSLSSSSRNIQQMLADSINRMKAYAFHQKKESMKKKQDEEINQIEEERTKQICKSWKEDSEWQASLRKSKAADEKRRSLAKQAREDYKRLSLGAQKGRGGERLQSPLRVPQKPERPPLPPKPQFLNSGAYPQKPLRNQGVVRTLSSSAQEDIIRWFKEEQLPLRAGYQKTSDTIAPWFHGILTLKKANELLLSTGMPGSFLIRVSERIKGYALSYLSEDGCKHFLIDASADAYSFLGVDQLQHATLADLVEYHKEEPITSLGKELLLYPCGQQDQLPDYLELFE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Sulfoxidation	LKQILSEMYIDPDLL HHHHHHHHCCCHHHH	2.98	30846556
10	Phosphorylation	KQILSEMYIDPDLLA HHHHHHHCCCHHHHH	9.71	22817900
24	Acetylation	AELSEEQKQILFFKM HHCCHHHHHHHHHHH	42.45	19608861
49	Ubiquitination	REAAMERKESLPVKP HHHHHHHHHCCCCCC	38.05	33845483
51	Phosphorylation	AAMERKESLPVKPRP HHHHHHHCCCCCCCC	40.80	26657352
55	Acetylation	RKESLPVKPRPKKEN HHHCCCCCCCCCCCC	33.11	27452117
55	Ubiquitination	RKESLPVKPRPKKEN HHHCCCCCCCCCCCC	33.11	33845483
60	Ubiquitination	PVKPRPKKENGKSVH CCCCCCCCCCCCCCE	60.12	29967540
69	Ubiquitination	NGKSVHWKLGADKEV CCCCCEEECCCCCEE	23.36	19608861
69	Acetylation	NGKSVHWKLGADKEV CCCCCEEECCCCCEE	23.36	19608861
70	Ubiquitination	GKSVHWKLGADKEVW CCCCEEECCCCCEEE	6.04	22817900
81	Ubiquitination	KEVWVWVMGEHHLDK CEEEEEEEECCCCCC	2.82	33845483
83	Ubiquitination	VWVWVMGEHHLDKPY EEEEEEECCCCCCCH	15.27	22817900
98	Ubiquitination	DVLCNEIIAERARLK HHHHHHHHHHHHHHH	2.38	29967540
105	Sumoylation	IAERARLKAEQEAEE HHHHHHHHHHHHHHC	44.30	-
105	Sumoylation	IAERARLKAEQEAEE HHHHHHHHHHHHHHC	44.30	-
105	Ubiquitination	IAERARLKAEQEAEE HHHHHHHHHHHHHHC	44.30	29967540
107	Ubiquitination	ERARLKAEQEAEEPR HHHHHHHHHHHHCCC	47.57	29967540
115	Ubiquitination	QEAEEPRKTHSEEFT HHHHCCCCCCCHHHH	62.39	21906983
116	Phosphorylation	EAEEPRKTHSEEFTN HHHCCCCCCCHHHHH	31.73	20873877
118	Phosphorylation	EEPRKTHSEEFTNSL HCCCCCCCHHHHHHH	44.01	26657352
122	Phosphorylation	KTHSEEFTNSLKTKS CCCCHHHHHHHHCHH	27.46	23927012
124	Phosphorylation	HSEEFTNSLKTKSQY CCHHHHHHHHCHHHH	28.34	28355574
124	Ubiquitination	HSEEFTNSLKTKSQY CCHHHHHHHHCHHHH	28.34	33845483
126	Ubiquitination	EEFTNSLKTKSQYHD HHHHHHHHCHHHHHC	54.44	21906983
127	Phosphorylation	EFTNSLKTKSQYHDL HHHHHHHCHHHHHCC	41.02	28857561
128	Ubiquitination	FTNSLKTKSQYHDLQ HHHHHHCHHHHHCCC	33.69	22817900
128	Methylation	FTNSLKTKSQYHDLQ HHHHHHCHHHHHCCC	33.69	115981329
129	Phosphorylation	TNSLKTKSQYHDLQA HHHHHCHHHHHCCCC	41.00	21945579
131	Phosphorylation	SLKTKSQYHDLQAPD HHHCHHHHHCCCCCC	12.37	21945579
143	Ubiquitination	APDNQQTKDIWKKVA CCCCHHHHHHHHHHH	42.76	29967540
152	Ubiquitination	IWKKVAEKEELEQGS HHHHHHHHHHHHCCC	46.91	29967540
152	Acetylation	IWKKVAEKEELEQGS HHHHHHHHHHHHCCC	46.91	26051181
154	Ubiquitination	KKVAEKEELEQGSRP HHHHHHHHHHCCCCC	69.54	29967540
169	Ubiquitination	APTLEEEKIRSLSSS CCCCCHHHHHHCCCC	46.85	33845483
172	Phosphorylation	LEEEKIRSLSSSSRN CCHHHHHHCCCCCHH	35.76	28555341
172	O-linked_Glycosylation	LEEEKIRSLSSSSRN CCHHHHHHCCCCCHH	35.76	30379171
177	Phosphorylation	IRSLSSSSRNIQQML HHHCCCCCHHHHHHH	31.15	-
187	Phosphorylation	IQQMLADSINRMKAY HHHHHHHHHHHHHHH	19.02	20068231
199	2-Hydroxyisobutyrylation	KAYAFHQKKESMKKK HHHHHHHHHHHHHHH	50.35	-
199	Ubiquitination	KAYAFHQKKESMKKK HHHHHHHHHHHHHHH	50.35	29967540
235	Phosphorylation	EDSEWQASLRKSKAA CCHHHHHHHHHHHHH	17.38	25159151
240	Methylation	QASLRKSKAADEKRR HHHHHHHHHHHHHHH	51.10	116253797
261	Phosphorylation	REDYKRLSLGAQKGR HHHHHHHHHHCCCCC	28.88	22167270
270	Phosphorylation	GAQKGRGGERLQSPL HCCCCCCCCCCCCCC	18.58	32645325
275	Phosphorylation	RGGERLQSPLRVPQK CCCCCCCCCCCCCCC	30.41	21815630
282	Ubiquitination	SPLRVPQKPERPPLP CCCCCCCCCCCCCCC	42.66	21963094
288	Phosphorylation	QKPERPPLPPKPQFL CCCCCCCCCCCCCCC	14.55	32645325
300	Ubiquitination	QFLNSGAYPQKPLRN CCCCCCCCCCCCCCC	15.10	21963094
303	Acetylation	NSGAYPQKPLRNQGV CCCCCCCCCCCCCCC	41.33	26051181
313	Phosphorylation	RNQGVVRTLSSSAQE CCCCCEEECCCCHHH	21.27	22167270
315	Phosphorylation	QGVVRTLSSSAQEDI CCCEEECCCCHHHHH	22.95	19664994
316	Phosphorylation	GVVRTLSSSAQEDII CCEEECCCCHHHHHH	32.57	22167270
317	Phosphorylation	VVRTLSSSAQEDIIR CEEECCCCHHHHHHH	30.51	22167270
327	Ubiquitination	EDIIRWFKEEQLPLR HHHHHHHHHCCCCCC	54.07	21963094
327	Sumoylation	EDIIRWFKEEQLPLR HHHHHHHHHCCCCCC	54.07	-
327	Sumoylation	EDIIRWFKEEQLPLR HHHHHHHHHCCCCCC	54.07	-
353	Phosphorylation	PWFHGILTLKKANEL HHHHHHHHHHHHHHH	34.31	22777824

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
261	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SH24A_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 SH24A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH3G1_HUMAN	SH3GL1	physical	19060904
DBNL_HUMAN	DBNL	physical	19060904
HDGF_HUMAN	HDGF	physical	22863883
HMBX1_HUMAN	HMBOX1	physical	25416956
CEP76_HUMAN	CEP76	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
UBX11_HUMAN	UBXN11	physical	25416956
FSD2_HUMAN	FSD2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
NUTM1_HUMAN	NUTM1	physical	25416956
CC172_HUMAN	CCDC172	physical	25416956
TRFE_HUMAN	TF	physical	26186194
PP1B_HUMAN	PPP1CB	physical	26186194
PP1R7_HUMAN	PPP1R7	physical	26186194
TBA3C_HUMAN	TUBA3C	physical	26186194
DTD1_HUMAN	DTD1	physical	26344197
NDRG1_HUMAN	NDRG1	physical	26344197
OLIG1_HUMAN	OLIG1	physical	25814554
PP1R7_HUMAN	PPP1R7	physical	28514442
PP1A_HUMAN	PPP1CA	physical	28514442
PP1B_HUMAN	PPP1CB	physical	28514442
TBA3C_HUMAN	TUBA3C	physical	28514442
TRFE_HUMAN	TF	physical	28514442
PP1G_HUMAN	PPP1CC	physical	28514442

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 SH24A_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-69, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-315, AND MASSSPECTROMETRY.	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-315, 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-315, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND MASSSPECTROMETRY.	17389395 [Abstract]