dbPTM

ANXA5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANXA5_HUMAN
UniProt AC	P08758
Protein Name	Annexin A5
Gene Name	ANXA5
Organism	Homo sapiens (Human).
Sequence Length	320
Subcellular Localization
Protein Description	This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade..
Protein Sequence	MAQVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQVLRGTV ------CCCHHHCCC	14.27	19413330
6	Methylation	--MAQVLRGTVTDFP --CCCHHHCCCCCCC	39.62	-
8	Phosphorylation	MAQVLRGTVTDFPGF CCCHHHCCCCCCCCC	17.50	30087585
10	Phosphorylation	QVLRGTVTDFPGFDE CHHHCCCCCCCCCCH	31.59	110740065
18	Methylation	DFPGFDERADAETLR CCCCCCHHCCHHHHH	39.34	-
23	Phosphorylation	DERADAETLRKAMKG CHHCCHHHHHHHHHC	33.32	4715451
26	Ubiquitination	ADAETLRKAMKGLGT CCHHHHHHHHHCCCC	56.81	-
29	Sumoylation	ETLRKAMKGLGTDEE HHHHHHHHCCCCCHH	56.71	-
29	Sumoylation	ETLRKAMKGLGTDEE HHHHHHHHCCCCCHH	56.71	25114211
29	Ubiquitination	ETLRKAMKGLGTDEE HHHHHHHHCCCCCHH	56.71	21890473
29	Ubiquitination	ETLRKAMKGLGTDEE HHHHHHHHCCCCCHH	56.71	21890473
33	Phosphorylation	KAMKGLGTDEESILT HHHHCCCCCHHHHHH	45.33	29255136
37	Phosphorylation	GLGTDEESILTLLTS CCCCCHHHHHHHHHC	22.35	26657352
40	Phosphorylation	TDEESILTLLTSRSN CCHHHHHHHHHCCCH	20.32	29255136
43	Phosphorylation	ESILTLLTSRSNAQR HHHHHHHHCCCHHHH	25.80	29255136
44	Phosphorylation	SILTLLTSRSNAQRQ HHHHHHHCCCHHHHH	33.41	29507054
58	Acetylation	QEISAAFKTLFGRDL HHHHHHHHHHHCHHH	39.32	23236377
58	Ubiquitination	QEISAAFKTLFGRDL HHHHHHHHHHHCHHH	39.32	21906983
58	Ubiquitination	QEISAAFKTLFGRDL HHHHHHHHHHHCHHH	39.32	21890473
70	Acetylation	RDLLDDLKSELTGKF HHHHHHHHHHHCCHH	49.21	19608861
70	Sumoylation	RDLLDDLKSELTGKF HHHHHHHHHHHCCHH	49.21	19608861
70	Ubiquitination	RDLLDDLKSELTGKF HHHHHHHHHHHCCHH	49.21	19608861
74	Phosphorylation	DDLKSELTGKFEKLI HHHHHHHCCHHHHHH	33.98	113305251
76	Acetylation	LKSELTGKFEKLIVA HHHHHCCHHHHHHHH	45.15	19608861
76	Malonylation	LKSELTGKFEKLIVA HHHHHCCHHHHHHHH	45.15	26320211
76	Ubiquitination	LKSELTGKFEKLIVA HHHHHCCHHHHHHHH	45.15	21890473
76	Ubiquitination	LKSELTGKFEKLIVA HHHHHCCHHHHHHHH	45.15	21890473
79	Acetylation	ELTGKFEKLIVALMK HHCCHHHHHHHHHHC	46.80	19608861
79	Malonylation	ELTGKFEKLIVALMK HHCCHHHHHHHHHHC	46.80	26320211
79	Ubiquitination	ELTGKFEKLIVALMK HHCCHHHHHHHHHHC	46.80	21890473
79	Ubiquitination	ELTGKFEKLIVALMK HHCCHHHHHHHHHHC	46.80	21890473
86	Acetylation	KLIVALMKPSRLYDA HHHHHHHCHHHHHHH	40.46	23236377
86	Malonylation	KLIVALMKPSRLYDA HHHHHHHCHHHHHHH	40.46	26320211
86	Ubiquitination	KLIVALMKPSRLYDA HHHHHHHCHHHHHHH	40.46	21890473
86	Ubiquitination	KLIVALMKPSRLYDA HHHHHHHCHHHHHHH	40.46	21890473
88	O-linked_Glycosylation	IVALMKPSRLYDAYE HHHHHCHHHHHHHHH	29.42	30379171
88	Phosphorylation	IVALMKPSRLYDAYE HHHHHCHHHHHHHHH	29.42	21406692
91	Phosphorylation	LMKPSRLYDAYELKH HHCHHHHHHHHHHHH	9.45	21698337
94	Phosphorylation	PSRLYDAYELKHALK HHHHHHHHHHHHHHC	20.92	25159151
97	Acetylation	LYDAYELKHALKGAG HHHHHHHHHHHCCCC	18.19	19608861
97	Malonylation	LYDAYELKHALKGAG HHHHHHHHHHHCCCC	18.19	26320211
97	Ubiquitination	LYDAYELKHALKGAG HHHHHHHHHHHCCCC	18.19	21890473
97	Ubiquitination	LYDAYELKHALKGAG HHHHHHHHHHHCCCC	18.19	21890473
101	Acetylation	YELKHALKGAGTNEK HHHHHHHCCCCCCHH	47.72	16916647
101	Succinylation	YELKHALKGAGTNEK HHHHHHHCCCCCCHH	47.72	23954790
101	Ubiquitination	YELKHALKGAGTNEK HHHHHHHCCCCCCHH	47.72	-
105	Phosphorylation	HALKGAGTNEKVLTE HHHCCCCCCHHHHHH	39.40	68696949
108	Acetylation	KGAGTNEKVLTEIIA CCCCCCHHHHHHHHH	44.61	23954790
108	Ubiquitination	KGAGTNEKVLTEIIA CCCCCCHHHHHHHHH	44.61	21906983
108	Ubiquitination	KGAGTNEKVLTEIIA CCCCCCHHHHHHHHH	44.61	21890473
111	Phosphorylation	GTNEKVLTEIIASRT CCCHHHHHHHHHCCC	28.29	25106551
116	Phosphorylation	VLTEIIASRTPEELR HHHHHHHCCCHHHHH	26.69	29514088
118	Phosphorylation	TEIIASRTPEELRAI HHHHHCCCHHHHHHH	32.34	24670416
126	Sumoylation	PEELRAIKQVYEEEY HHHHHHHHHHHHHHH	32.50	-
126	Ubiquitination	PEELRAIKQVYEEEY HHHHHHHHHHHHHHH	32.50	21906983
129	Phosphorylation	LRAIKQVYEEEYGSS HHHHHHHHHHHHCCC	18.35	28450419
133	Phosphorylation	KQVYEEEYGSSLEDD HHHHHHHHCCCCCCC	26.11	28450419
135	Phosphorylation	VYEEEYGSSLEDDVV HHHHHHCCCCCCCCC	30.74	26657352
136	Phosphorylation	YEEEYGSSLEDDVVG HHHHHCCCCCCCCCC	31.26	28450419
145	Phosphorylation	EDDVVGDTSGYYQRM CCCCCCCCCHHHHHH	20.37	27251275
146	Phosphorylation	DDVVGDTSGYYQRML CCCCCCCCHHHHHHH	29.54	27251275
152	Sulfoxidation	TSGYYQRMLVVLLQA CCHHHHHHHHHHHHH	1.64	28183972
186	Ubiquitination	LFQAGELKWGTDEEK HHHHCCCCCCCCHHH	39.00	21906983
193	Acetylation	KWGTDEEKFITIFGT CCCCCHHHEEEEEEC	39.76	26051181
193	Ubiquitination	KWGTDEEKFITIFGT CCCCCHHHEEEEEEC	39.76	21890473
193	Ubiquitination	KWGTDEEKFITIFGT CCCCCHHHEEEEEEC	39.76	21890473
196	Phosphorylation	TDEEKFITIFGTRSV CCHHHEEEEEECCCH	17.24	20068231
200	Phosphorylation	KFITIFGTRSVSHLR HEEEEEECCCHHHHH	14.71	28348404
204	Phosphorylation	IFGTRSVSHLRKVFD EEECCCHHHHHHHHH	20.32	24719451
214	Sulfoxidation	RKVFDKYMTISGFQI HHHHHHCCCCCCCEE	3.10	30846556
229	Phosphorylation	EETIDRETSGNLEQL EEECCCCCCCCHHHH	42.71	26657352
230	Phosphorylation	ETIDRETSGNLEQLL EECCCCCCCCHHHHH	22.41	27732954
242	Ubiquitination	QLLLAVVKSIRSIPA HHHHHHHHHHHCHHH	33.30	-
243	Phosphorylation	LLLAVVKSIRSIPAY HHHHHHHHHHCHHHH	16.18	24275569
246	Phosphorylation	AVVKSIRSIPAYLAE HHHHHHHCHHHHHHH	31.11	46164699
250	Phosphorylation	SIRSIPAYLAETLYY HHHCHHHHHHHHHHH	10.90	30576142
254	Phosphorylation	IPAYLAETLYYAMKG HHHHHHHHHHHHHHC	17.91	46164711
256	Phosphorylation	AYLAETLYYAMKGAG HHHHHHHHHHHHCCC	9.15	26356563
257	Phosphorylation	YLAETLYYAMKGAGT HHHHHHHHHHHCCCC	11.88	30576142
259	Sulfoxidation	AETLYYAMKGAGTDD HHHHHHHHHCCCCCC	2.08	30846556
260	Ubiquitination	ETLYYAMKGAGTDDH HHHHHHHHCCCCCCC	37.12	-
264	Phosphorylation	YAMKGAGTDDHTLIR HHHHCCCCCCCHHEE	37.41	29255136
268	Phosphorylation	GAGTDDHTLIRVMVS CCCCCCCHHEEEEEE	30.76	29255136
275	Phosphorylation	TLIRVMVSRSEIDLF HHEEEEEEHHHCCHH	16.40	46164705
277	Phosphorylation	IRVMVSRSEIDLFNI EEEEEEHHHCCHHHH	31.25	20068231
290	Malonylation	NIRKEFRKNFATSLY HHCHHHHHHHHHHHH	62.83	26320211
290	Succinylation	NIRKEFRKNFATSLY HHCHHHHHHHHHHHH	62.83	-
290	Succinylation	NIRKEFRKNFATSLY HHCHHHHHHHHHHHH	62.83	-
290	Ubiquitination	NIRKEFRKNFATSLY HHCHHHHHHHHHHHH	62.83	21890473
290	Ubiquitination	NIRKEFRKNFATSLY HHCHHHHHHHHHHHH	62.83	21890473
294	Phosphorylation	EFRKNFATSLYSMIK HHHHHHHHHHHHHHH	18.35	28348404
295	Phosphorylation	FRKNFATSLYSMIKG HHHHHHHHHHHHHHC	23.14	20873877
297	Phosphorylation	KNFATSLYSMIKGDT HHHHHHHHHHHHCCC	8.92	21712546
298	Phosphorylation	NFATSLYSMIKGDTS HHHHHHHHHHHCCCC	21.23	21712546
299	Sulfoxidation	FATSLYSMIKGDTSG HHHHHHHHHHCCCCC	2.01	28465586
301	Acetylation	TSLYSMIKGDTSGDY HHHHHHHHCCCCCCH	41.93	26051181
301	Malonylation	TSLYSMIKGDTSGDY HHHHHHHHCCCCCCH	41.93	26320211
301	Ubiquitination	TSLYSMIKGDTSGDY HHHHHHHHCCCCCCH	41.93	21890473
301	Ubiquitination	TSLYSMIKGDTSGDY HHHHHHHHCCCCCCH	41.93	21890473
309	Acetylation	GDTSGDYKKALLLLC CCCCCCHHHHHHHHH	35.99	21339330
309	Succinylation	GDTSGDYKKALLLLC CCCCCCHHHHHHHHH	35.99	23954790
310	Ubiquitination	DTSGDYKKALLLLCG CCCCCHHHHHHHHHC	37.73	-

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 ANXA5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANXA5_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 ANXA5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ITB5_HUMAN	ITGB5	physical	12769841
FDFT_HUMAN	FDFT1	physical	16169070
A4_HUMAN	APP	physical	21832049
NDRG1_HUMAN	NDRG1	physical	22939629
SYHC_HUMAN	HARS	physical	22939629
PPT2_HUMAN	PPT2	physical	22939629
PUM1_HUMAN	PUM1	physical	22939629
LAMC3_HUMAN	LAMC3	physical	21988832
LRC15_HUMAN	LRRC15	physical	26186194
GCN1_HUMAN	GCN1L1	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
PDIA3_HUMAN	PDIA3	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
LRC15_HUMAN	LRRC15	physical	28514442
G6PI_HUMAN	GPI	physical	27173435
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	physical	27173435
PLST_HUMAN	PLS3	physical	27173435
IF2P_HUMAN	EIF5B	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435
CRNN_HUMAN	CRNN	physical	27173435
HPRT_HUMAN	HPRT1	physical	27173435
CPNE3_HUMAN	CPNE3	physical	27173435
PYGL_HUMAN	PYGL	physical	27173435
SF3A3_HUMAN	SF3A3	physical	27173435
CPSF6_HUMAN	CPSF6	physical	27173435
SF3A1_HUMAN	SF3A1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614391	Pregnancy loss, recurrent, 3 (RPRGL3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ANXA5_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, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Primary structure of human placental anticoagulant protein."; Funakoshi T., Hendrickson L.E., McMullen B.A., Fujikawa K.; Biochemistry 26:8087-8092(1987). Cited for: NUCLEOTIDE SEQUENCE [MRNA].	2964863 [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-70; LYS-76; LYS-79 ANDLYS-97, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, AND MASSSPECTROMETRY.	18083107 [Abstract]