dbPTM

ANXA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANXA4_HUMAN
UniProt AC	P09525
Protein Name	Annexin A4
Gene Name	ANXA4
Organism	Homo sapiens (Human).
Sequence Length	319
Subcellular Localization
Protein Description	Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis..
Protein Sequence	MATKGGTVKAASGFNAMEDAQTLRKAMKGLGTDEDAIISVLAYRNTAQRQEIRTAYKSTIGRDLIDDLKSELSGNFEQVIVGMMTPTVLYDVQELRRAMKGAGTDEGCLIEILASRTPEEIRRISQTYQQQYGRSLEDDIRSDTSFMFQRVLVSLSAGGRDEGNYLDDALVRQDAQDLYEAGEKKWGTDEVKFLTVLCSRNRNHLLHVFDEYKRISQKDIEQSIKSETSGSFEDALLAIVKCMRNKSAYFAEKLYKSMKGLGTDDNTLIRVMVSRAEIDMLDIRAHFKRLYGKSLYSFIKGDTSGDYRKVLLVLCGGDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATKGGTVK ------CCCCCCCEE	20.30	22814378
7	Phosphorylation	-MATKGGTVKAASGF -CCCCCCCEECCCCC	27.74	28857561
12	Phosphorylation	GGTVKAASGFNAMED CCCEECCCCCCHHHH	49.10	25159151
14	Phosphorylation	TVKAASGFNAMEDAQ CEECCCCCCHHHHHH	4.96	20166139
17	Sulfoxidation	AASGFNAMEDAQTLR CCCCCCHHHHHHHHH	5.13	21406390
18	Ubiquitination	ASGFNAMEDAQTLRK CCCCCHHHHHHHHHH	48.02	-
22	Phosphorylation	NAMEDAQTLRKAMKG CHHHHHHHHHHHHCC	30.19	46164693
30	Ubiquitination	LRKAMKGLGTDEDAI HHHHHCCCCCCHHHH	5.79	-
43	Phosphorylation	AIISVLAYRNTAQRQ HHHHHHHHCCHHHHH	10.55	27259358
56	Phosphorylation	RQEIRTAYKSTIGRD HHHHHHHHHHHHCHH	12.59	23312004
57	Succinylation	QEIRTAYKSTIGRDL HHHHHHHHHHHCHHH	38.36	23954790
58	Phosphorylation	EIRTAYKSTIGRDLI HHHHHHHHHHCHHHH	16.75	23312004
59	Phosphorylation	IRTAYKSTIGRDLID HHHHHHHHHCHHHHH	24.25	23312004
59	Ubiquitination	IRTAYKSTIGRDLID HHHHHHHHHCHHHHH	24.25	-
69	Acetylation	RDLIDDLKSELSGNF HHHHHHHHHHHCCCH	49.21	-
71	Sumoylation	LIDDLKSELSGNFEQ HHHHHHHHHCCCHHH	45.42	-
85	Phosphorylation	QVIVGMMTPTVLYDV HHHHHCCCHHHHHCH	13.60	26552605
87	Phosphorylation	IVGMMTPTVLYDVQE HHHCCCHHHHHCHHH	17.61	26552605
90	Phosphorylation	MMTPTVLYDVQELRR CCCHHHHHCHHHHHH	15.10	26552605
100	Acetylation	QELRRAMKGAGTDEG HHHHHHHCCCCCCCC	44.62	-
102	Ubiquitination	LRRAMKGAGTDEGCL HHHHHCCCCCCCCHH	16.52	-
108	S-nitrosylation	GAGTDEGCLIEILAS CCCCCCCHHHHHHHC	3.05	25040305
115	Phosphorylation	CLIEILASRTPEEIR HHHHHHHCCCHHHHH	32.99	28857561
117	Phosphorylation	IEILASRTPEEIRRI HHHHHCCCHHHHHHH	32.34	28857561
125	Phosphorylation	PEEIRRISQTYQQQY HHHHHHHHHHHHHHH	18.04	28152594
127	Phosphorylation	EIRRISQTYQQQYGR HHHHHHHHHHHHHCC	19.26	24719451
128	Phosphorylation	IRRISQTYQQQYGRS HHHHHHHHHHHHCCC	9.18	28152594
130	Phosphorylation	RISQTYQQQYGRSLE HHHHHHHHHHCCCHH	28.22	-
132	Phosphorylation	SQTYQQQYGRSLEDD HHHHHHHHCCCHHHH	15.35	28152594
134	Phosphorylation	TYQQQYGRSLEDDIR HHHHHHCCCHHHHHH	32.89	-
142	Phosphorylation	SLEDDIRSDTSFMFQ CHHHHHHCCCHHHHH	45.64	28857561
144	Phosphorylation	EDDIRSDTSFMFQRV HHHHHCCCHHHHHHH	25.72	28857561
147	Sulfoxidation	IRSDTSFMFQRVLVS HHCCCHHHHHHHHHH	2.54	21406390
165	Phosphorylation	GGRDEGNYLDDALVR CCCCCCCCCCHHHHH	23.51	38513
167	Phosphorylation	RDEGNYLDDALVRQD CCCCCCCCHHHHHHC	28.86	-
179	Phosphorylation	RQDAQDLYEAGEKKW HHCHHHHHHHHHHHC	16.42	27362937
181	Phosphorylation	DAQDLYEAGEKKWGT CHHHHHHHHHHHCCC	20.21	-
184	Ubiquitination	DLYEAGEKKWGTDEV HHHHHHHHHCCCCHH	53.56	21890473
186	Ubiquitination	YEAGEKKWGTDEVKF HHHHHHHCCCCHHHH	26.45	-
187	Ubiquitination	EAGEKKWGTDEVKFL HHHHHHCCCCHHHHH	31.97	-
199	Phosphorylation	KFLTVLCSRNRNHLL HHHHHHHHCCCCCHH	28.56	46164687
211	Ubiquitination	HLLHVFDEYKRISQK CHHHHHHHHHHCCHH	41.30	-
212	Phosphorylation	LLHVFDEYKRISQKD HHHHHHHHHHCCHHH	13.86	20560755
213	Acetylation	LHVFDEYKRISQKDI HHHHHHHHHCCHHHH	41.00	19608861
215	Acetylation	VFDEYKRISQKDIEQ HHHHHHHCCHHHHHH	4.47	19608861
218	Succinylation	EYKRISQKDIEQSIK HHHHCCHHHHHHHHH	54.61	23954790
218	Acetylation	EYKRISQKDIEQSIK HHHHCCHHHHHHHHH	54.61	-
220	Ubiquitination	KRISQKDIEQSIKSE HHCCHHHHHHHHHHC	7.17	-
223	Phosphorylation	SQKDIEQSIKSETSG CHHHHHHHHHHCCCC	21.13	28450419
225	Acetylation	KDIEQSIKSETSGSF HHHHHHHHHCCCCCH	47.70	19608861
226	Phosphorylation	DIEQSIKSETSGSFE HHHHHHHHCCCCCHH	44.42	28450419
227	Ubiquitination	IEQSIKSETSGSFED HHHHHHHCCCCCHHH	41.83	19608861
227	Acetylation	IEQSIKSETSGSFED HHHHHHHCCCCCHHH	41.83	19608861
228	Phosphorylation	EQSIKSETSGSFEDA HHHHHHCCCCCHHHH	45.54	28450419
229	Phosphorylation	QSIKSETSGSFEDAL HHHHHCCCCCHHHHH	28.52	28857561
231	Phosphorylation	IKSETSGSFEDALLA HHHCCCCCHHHHHHH	25.82	27251275
248	Ubiquitination	KCMRNKSAYFAEKLY HHHHCCCHHHHHHHH	12.69	-
253	Acetylation	KSAYFAEKLYKSMKG CCHHHHHHHHHHHCC	54.40	25825284
255	Phosphorylation	AYFAEKLYKSMKGLG HHHHHHHHHHHCCCC	16.46	6975611
255	Acetylation	AYFAEKLYKSMKGLG HHHHHHHHHHHCCCC	16.46	-
257	Phosphorylation	FAEKLYKSMKGLGTD HHHHHHHHHCCCCCC	16.51	22468782
259	Acetylation	EKLYKSMKGLGTDDN HHHHHHHCCCCCCCC	59.06	7691955
259	Malonylation	EKLYKSMKGLGTDDN HHHHHHHCCCCCCCC	59.06	26320211
261	Ubiquitination	LYKSMKGLGTDDNTL HHHHHCCCCCCCCHH	5.79	-
263	Phosphorylation	KSMKGLGTDDNTLIR HHHCCCCCCCCHHHH	45.26	18510355
265	Phosphorylation	MKGLGTDDNTLIRVM HCCCCCCCCHHHHHH	50.26	18510355
267	Phosphorylation	GLGTDDNTLIRVMVS CCCCCCCHHHHHHHH	30.47	23312004
269	Phosphorylation	GTDDNTLIRVMVSRA CCCCCHHHHHHHHHH	2.69	-
280	Sulfoxidation	VSRAEIDMLDIRAHF HHHHHCCHHHHHHHH	4.44	30846556
293	Ubiquitination	HFKRLYGKSLYSFIK HHHHHHCCHHHHHHH	24.59	21890473
293	Acetylation	HFKRLYGKSLYSFIK HHHHHHCCHHHHHHH	24.59	19608861
293	Ubiquitination	HFKRLYGKSLYSFIK HHHHHHCCHHHHHHH	24.59	21890473
294	Phosphorylation	FKRLYGKSLYSFIKG HHHHHCCHHHHHHHC	28.33	28152594
295	Ubiquitination	KRLYGKSLYSFIKGD HHHHCCHHHHHHHCC	4.77	19608861
295	Acetylation	KRLYGKSLYSFIKGD HHHHCCHHHHHHHCC	4.77	19608861
296	Phosphorylation	RLYGKSLYSFIKGDT HHHCCHHHHHHHCCC	14.50	28152594
297	Phosphorylation	LYGKSLYSFIKGDTS HHCCHHHHHHHCCCC	26.28	28152594
298	Phosphorylation	YGKSLYSFIKGDTSG HCCHHHHHHHCCCCC	4.17	-
299	Phosphorylation	GKSLYSFIKGDTSGD CCHHHHHHHCCCCCC	3.92	20068231
300	Malonylation	KSLYSFIKGDTSGDY CHHHHHHHCCCCCCC	49.04	26320211
300	Acetylation	KSLYSFIKGDTSGDY CHHHHHHHCCCCCCC	49.04	19608861
302	Acetylation	LYSFIKGDTSGDYRK HHHHHHCCCCCCCCE	32.47	19608861

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
Oops, there are no upstream regulatory protein records of ANXA4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANXA4_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 ANXA4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NFKB1_HUMAN	NFKB1	physical	20237821
ASM_HUMAN	SMPD1	physical	21900206
NMT2_HUMAN	NMT2	physical	21900206
DJB11_HUMAN	DNAJB11	physical	22939629
ANXA7_HUMAN	ANXA7	physical	22939629
THTM_HUMAN	MPST	physical	22939629
PADI4_HUMAN	PADI4	physical	25416956
SF3A3_HUMAN	SF3A3	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 ANXA4_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-213; LYS-225; LYS-293 ANDLYS-300, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-165, AND MASSSPECTROMETRY.	19534553 [Abstract]