ANXA3_HUMAN - dbPTM
ANXA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANXA3_HUMAN
UniProt AC P12429
Protein Name Annexin A3
Gene Name ANXA3
Organism Homo sapiens (Human).
Sequence Length 323
Subcellular Localization
Protein Description Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate..
Protein Sequence MASIWVGHRGTVRDYPDFSPSVDAEAIQKAIRGIGTDEKMLISILTERSNAQRQLIVKEYQAAYGKELKDDLKGDLSGHFEHLMVALVTPPAVFDAKQLKKSMKGAGTNEDALIEILTTRTSRQMKDISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKQDAQILYKAGENRWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIVDSIKGELSGHFEDLLLAIVNCVRNTPAFLAERLHRALKGIGTDEFTLNRIMVSRSEIDLLDIRTEFKKHYGYSLYSAIKSDTSGDYEITLLKICGGDD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MASIWVGHR
------CCCEEECCC
15.10-
11PhosphorylationIWVGHRGTVRDYPDF
EEECCCCCCCCCCCC
16.6028152594
15PhosphorylationHRGTVRDYPDFSPSV
CCCCCCCCCCCCCCC
8.3028152594
19PhosphorylationVRDYPDFSPSVDAEA
CCCCCCCCCCCCHHH
24.5225159151
21PhosphorylationDYPDFSPSVDAEAIQ
CCCCCCCCCCHHHHH
31.2828450419
29AcetylationVDAEAIQKAIRGIGT
CCHHHHHHHHHCCCC
39.4023954790
29UbiquitinationVDAEAIQKAIRGIGT
CCHHHHHHHHHCCCC
39.4021906983
58AcetylationAQRQLIVKEYQAAYG
HHHHHHHHHHHHHHC
43.6523954790
58UbiquitinationAQRQLIVKEYQAAYG
HHHHHHHHHHHHHHC
43.6522817900
58SuccinylationAQRQLIVKEYQAAYG
HHHHHHHHHHHHHHC
43.6523954790
66UbiquitinationEYQAAYGKELKDDLK
HHHHHHCHHHHHHHC
47.3927667366
89PhosphorylationHLMVALVTPPAVFDA
HHHHHHHCCCCCCCH
25.14110740895
97AcetylationPPAVFDAKQLKKSMK
CCCCCCHHHHHHHHC
58.9923954790
100UbiquitinationVFDAKQLKKSMKGAG
CCCHHHHHHHHCCCC
40.0622817900
101UbiquitinationFDAKQLKKSMKGAGT
CCHHHHHHHHCCCCC
65.4622817900
104MethylationKQLKKSMKGAGTNED
HHHHHHHCCCCCCHH
53.34-
104UbiquitinationKQLKKSMKGAGTNED
HHHHHHHCCCCCCHH
53.3421906983
121PhosphorylationIEILTTRTSRQMKDI
HHHHHHCCHHHHHCH
26.6024719451
122PhosphorylationEILTTRTSRQMKDIS
HHHHHCCHHHHHCHH
19.7524719451
129PhosphorylationSRQMKDISQAYYTVY
HHHHHCHHHHHHHHH
20.9226074081
132PhosphorylationMKDISQAYYTVYKKS
HHCHHHHHHHHHHHH
7.6428152594
133PhosphorylationKDISQAYYTVYKKSL
HCHHHHHHHHHHHHH
7.8626074081
134PhosphorylationDISQAYYTVYKKSLG
CHHHHHHHHHHHHHC
12.5126074081
136PhosphorylationSQAYYTVYKKSLGDD
HHHHHHHHHHHHCCC
12.6126074081
137AcetylationQAYYTVYKKSLGDDI
HHHHHHHHHHHCCCC
31.3926051181
137SuccinylationQAYYTVYKKSLGDDI
HHHHHHHHHHHCCCC
31.3923954790
138UbiquitinationAYYTVYKKSLGDDIS
HHHHHHHHHHCCCCC
32.9729967540
139PhosphorylationYYTVYKKSLGDDISS
HHHHHHHHHCCCCCC
33.1728985074
145PhosphorylationKSLGDDISSETSGDF
HHHCCCCCCCCCHHH
29.1725159151
146PhosphorylationSLGDDISSETSGDFR
HHCCCCCCCCCHHHH
45.2725159151
148PhosphorylationGDDISSETSGDFRKA
CCCCCCCCCHHHHHH
39.70110740911
149PhosphorylationDDISSETSGDFRKAL
CCCCCCCCHHHHHHH
32.1125159151
154UbiquitinationETSGDFRKALLTLAD
CCCHHHHHHHHHHHC
43.3029967540
167PhosphorylationADGRRDESLKVDEHL
HCCCCCCCCCCCHHH
37.4720873877
169UbiquitinationGRRDESLKVDEHLAK
CCCCCCCCCCHHHHH
57.8533845483
169AcetylationGRRDESLKVDEHLAK
CCCCCCCCCCHHHHH
57.8526051181
176SuccinylationKVDEHLAKQDAQILY
CCCHHHHHHHHHHHH
55.8823954790
176UbiquitinationKVDEHLAKQDAQILY
CCCHHHHHHHHHHHH
55.8827667366
183PhosphorylationKQDAQILYKAGENRW
HHHHHHHHHCCCCCC
10.6227273156
184UbiquitinationQDAQILYKAGENRWG
HHHHHHHHCCCCCCC
46.6121906983
196UbiquitinationRWGTDEDKFTEILCL
CCCCCHHHHHHHHHH
52.7329967540
210UbiquitinationLRSFPQLKLTFDEYR
HHCCCCCEEEHHHHC
39.9923000965
216PhosphorylationLKLTFDEYRNISQKD
CEEEHHHHCCCCHHH
15.71110740919
222UbiquitinationEYRNISQKDIVDSIK
HHCCCCHHHHHHHHC
42.5027667366
222AcetylationEYRNISQKDIVDSIK
HHCCCCHHHHHHHHC
42.5023954790
222SuccinylationEYRNISQKDIVDSIK
HHCCCCHHHHHHHHC
42.5023954790
233PhosphorylationDSIKGELSGHFEDLL
HHHCHHHCHHHHHHH
26.3928348404
263AcetylationERLHRALKGIGTDEF
HHHHHHHCCCCCCCH
47.7125825284
263UbiquitinationERLHRALKGIGTDEF
HHHHHHHCCCCCCCH
47.7127667366
267PhosphorylationRALKGIGTDEFTLNR
HHHCCCCCCCHHHHC
30.36-
271PhosphorylationGIGTDEFTLNRIMVS
CCCCCCHHHHCCCCC
22.5227050516
280PhosphorylationNRIMVSRSEIDLLDI
HCCCCCHHHCEEHHH
31.2521712546
295PhosphorylationRTEFKKHYGYSLYSA
HHHHHHHHCCCHHHH
27.0028152594
297PhosphorylationEFKKHYGYSLYSAIK
HHHHHHCCCHHHHHH
6.5828152594
298PhosphorylationFKKHYGYSLYSAIKS
HHHHHCCCHHHHHHC
19.2328152594
300PhosphorylationKHYGYSLYSAIKSDT
HHHCCCHHHHHHCCC
7.0727273156
301PhosphorylationHYGYSLYSAIKSDTS
HHCCCHHHHHHCCCC
28.8930815365
307PhosphorylationYSAIKSDTSGDYEIT
HHHHHCCCCCCEEEE
41.5228152594
308PhosphorylationSAIKSDTSGDYEITL
HHHHCCCCCCEEEEE
34.3628152594
311PhosphorylationKSDTSGDYEITLLKI
HCCCCCCEEEEEEEE
16.8628152594
314PhosphorylationTSGDYEITLLKICGG
CCCCEEEEEEEECCC
17.6928152594

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 ANXA3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANXA3_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 ANXA3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IGS21_HUMANIGSF21physical
16169070
P53_HUMANTP53physical
16169070
UBR1_HUMANUBR1physical
16169070
U119A_HUMANUNC119physical
16169070
STX4_HUMANSTX4physical
22939629
STXB2_HUMANSTXBP2physical
22939629
ANXA4_HUMANANXA4physical
22939629
SNP23_HUMANSNAP23physical
22939629
SSNA1_HUMANSSNA1physical
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 ANXA3_HUMAN

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Related Literatures of Post-Translational Modification

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