dbPTM

EFHD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EFHD2_HUMAN
UniProt AC	Q96C19
Protein Name	EF-hand domain-containing protein D2
Gene Name	EFHD2
Organism	Homo sapiens (Human).
Sequence Length	240
Subcellular Localization	Membrane raft. In a mouse immature B-cell line WEHI-231..
Protein Description	May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance..
Protein Sequence	MATDELATKLSRRLQMEGEGGGETPEQPGLNGAAAAAAGAPDEAAEALGSADCELSAKLLRRADLNQGIGEPQSPSRRVFNPYTEFKEFSRKQIKDMEKMFKQYDAGRDGFIDLMELKLMMEKLGAPQTHLGLKNMIKEVDEDFDSKLSFREFLLIFRKAAAGELQEDSGLCVLARLSEIDVSSEGVKGAKSFFEAKVQAINVSSRFEEEIKAEQEERKKQAEEMKQRKAAFKELQSTFK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATDELATK ------CCHHHHHHH	24.61	22814378
3	Phosphorylation	-----MATDELATKL -----CCHHHHHHHH	28.80	23090842
8	Phosphorylation	MATDELATKLSRRLQ CCHHHHHHHHHHHHH	45.18	23401153
9	Ubiquitination	ATDELATKLSRRLQM CHHHHHHHHHHHHHH	38.57	-
9	Acetylation	ATDELATKLSRRLQM CHHHHHHHHHHHHHH	38.57	23749302
11	Phosphorylation	DELATKLSRRLQMEG HHHHHHHHHHHHHCC	19.53	23401153
24	Phosphorylation	EGEGGGETPEQPGLN CCCCCCCCCCCCCCC	35.09	25159151
50	Phosphorylation	EAAEALGSADCELSA HHHHHHCCCCHHHHH	23.06	27251275
56	Phosphorylation	GSADCELSAKLLRRA CCCCHHHHHHHHHHC	10.89	27251275
74	Phosphorylation	QGIGEPQSPSRRVFN CCCCCCCCCCCCCCC	35.24	19664994
76	Phosphorylation	IGEPQSPSRRVFNPY CCCCCCCCCCCCCCC	37.66	29255136
83	Phosphorylation	SRRVFNPYTEFKEFS CCCCCCCCHHHHHHH	21.72	21945579
84	Phosphorylation	RRVFNPYTEFKEFSR CCCCCCCHHHHHHHH	35.88	21945579
87	Acetylation	FNPYTEFKEFSRKQI CCCCHHHHHHHHHHH	52.17	25953088
87	Ubiquitination	FNPYTEFKEFSRKQI CCCCHHHHHHHHHHH	52.17	21890473
90	Phosphorylation	YTEFKEFSRKQIKDM CHHHHHHHHHHHHHH	39.39	26074081
99	2-Hydroxyisobutyrylation	KQIKDMEKMFKQYDA HHHHHHHHHHHHHHC	42.89	-
99	Acetylation	KQIKDMEKMFKQYDA HHHHHHHHHHHHHHC	42.89	25953088
102	Ubiquitination	KDMEKMFKQYDAGRD HHHHHHHHHHHCCCC	44.44	-
102	Acetylation	KDMEKMFKQYDAGRD HHHHHHHHHHHCCCC	44.44	25953088
104	Phosphorylation	MEKMFKQYDAGRDGF HHHHHHHHHCCCCCH	14.35	22461510
115	Sulfoxidation	RDGFIDLMELKLMME CCCHHHHHHHHHHHH	5.13	21406390
118	Acetylation	FIDLMELKLMMEKLG HHHHHHHHHHHHHHC	22.49	26822725
123	Ubiquitination	ELKLMMEKLGAPQTH HHHHHHHHHCCCCCH	34.03	-
134	Acetylation	PQTHLGLKNMIKEVD CCCHHCHHHHHHHHC	42.54	25953088
138	Ubiquitination	LGLKNMIKEVDEDFD HCHHHHHHHHCCCHH	40.70	-
147	Methylation	VDEDFDSKLSFREFL HCCCHHCCCCHHHHH	50.42	-
147	2-Hydroxyisobutyrylation	VDEDFDSKLSFREFL HCCCHHCCCCHHHHH	50.42	-
147	Ubiquitination	VDEDFDSKLSFREFL HCCCHHCCCCHHHHH	50.42	-
149	Phosphorylation	EDFDSKLSFREFLLI CCHHCCCCHHHHHHH	26.45	23186163
159	Ubiquitination	EFLLIFRKAAAGELQ HHHHHHHHHHCCCCC	31.46	-
172	S-nitrosylation	LQEDSGLCVLARLSE CCCCCCEEEEEEHHH	2.41	22178444
178	Phosphorylation	LCVLARLSEIDVSSE EEEEEEHHHCCCCCC	27.27	23312004
183	Phosphorylation	RLSEIDVSSEGVKGA EHHHCCCCCCCCCCC	20.94	28450419
184	Phosphorylation	LSEIDVSSEGVKGAK HHHCCCCCCCCCCCH	37.91	29496963
188	Acetylation	DVSSEGVKGAKSFFE CCCCCCCCCCHHHHH	65.10	25953088
188	2-Hydroxyisobutyrylation	DVSSEGVKGAKSFFE CCCCCCCCCCHHHHH	65.10	-
188	Ubiquitination	DVSSEGVKGAKSFFE CCCCCCCCCCHHHHH	65.10	-
191	Ubiquitination	SEGVKGAKSFFEAKV CCCCCCCHHHHHHHH	57.36	-
192	Phosphorylation	EGVKGAKSFFEAKVQ CCCCCCHHHHHHHHH	34.33	21712546
204	Phosphorylation	KVQAINVSSRFEEEI HHHHHCCCHHHHHHH	16.00	25159151
205	Phosphorylation	VQAINVSSRFEEEIK HHHHCCCHHHHHHHH	36.38	29496963
229	Acetylation	AEEMKQRKAAFKELQ HHHHHHHHHHHHHHH	41.39	25953088
233	Acetylation	KQRKAAFKELQSTFK HHHHHHHHHHHHHCC	53.43	19608861
233	Ubiquitination	KQRKAAFKELQSTFK HHHHHHHHHHHHHCC	53.43	19608861
233	Methylation	KQRKAAFKELQSTFK HHHHHHHHHHHHHCC	53.43	19608861
238	Phosphorylation	AFKELQSTFK----- HHHHHHHHCC-----	23.60	-
240	Methylation	KELQSTFK------- HHHHHHCC-------	60.56	-

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
74	S	Phosphorylation	Kinase	CDK1	P06493	PSP
74	S	Phosphorylation	Kinase	CDK5	Q00535	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EFHD2_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 EFHD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
ENOG_HUMAN	ENO2	physical	22863883
GLRX3_HUMAN	GLRX3	physical	22863883
GUAA_HUMAN	GMPS	physical	22863883
IDHC_HUMAN	IDH1	physical	22863883
PTN11_HUMAN	PTPN11	physical	22863883
RCN1_HUMAN	RCN1	physical	22863883
FCL_HUMAN	TSTA3	physical	22863883
ARP2_HUMAN	ACTR2	physical	26344197
ARPC2_HUMAN	ARPC2	physical	26344197
ARPC3_HUMAN	ARPC3	physical	26344197
ARPC4_HUMAN	ARPC4	physical	26344197
TMOD1_HUMAN	TMOD1	physical	26344197
SYVC_HUMAN	VARS	physical	26344197

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 EFHD2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-74, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-233, 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-74, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-74, AND MASS SPECTROMETRY.	19413330 [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-74 AND SER-76, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.	17924679 [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-74, 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-74, AND MASSSPECTROMETRY.	17081983 [Abstract]