ANXA2_MOUSE - dbPTM
ANXA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANXA2_MOUSE
UniProt AC P07356
Protein Name Annexin A2
Gene Name Anxa2
Organism Mus musculus (Mouse).
Sequence Length 339
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome. In the lamina beneath the plasma membrane.
Protein Description Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response (By similarity). Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9. [PubMed: 22848640]
Protein Sequence MSTVHEILCKLSLEGDHSTPPSAYGSVKPYTNFDAERDALNIETAVKTKGVDEVTIVNILTNRSNVQRQDIAFAYQRRTKKELPSALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARELYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
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------MSTVHEILC
------CCCHHHHHH
38.85-
2Phosphorylation------MSTVHEILC
------CCCHHHHHH
38.8526824392
3Phosphorylation-----MSTVHEILCK
-----CCCHHHHHHH
25.2826824392
10SumoylationTVHEILCKLSLEGDH
CHHHHHHHHHCCCCC
37.35-
12PhosphorylationHEILCKLSLEGDHST
HHHHHHHHCCCCCCC
15.1826824392
18PhosphorylationLSLEGDHSTPPSAYG
HHCCCCCCCCCHHCC
47.5521082442
19PhosphorylationSLEGDHSTPPSAYGS
HCCCCCCCCCHHCCC
35.4825619855
22PhosphorylationGDHSTPPSAYGSVKP
CCCCCCCHHCCCCCC
35.019403731
24PhosphorylationHSTPPSAYGSVKPYT
CCCCCHHCCCCCCCC
17.8026824392
26PhosphorylationTPPSAYGSVKPYTNF
CCCHHCCCCCCCCCC
17.8125619855
28AcetylationPSAYGSVKPYTNFDA
CHHCCCCCCCCCCCH
33.7223806337
30PhosphorylationAYGSVKPYTNFDAER
HCCCCCCCCCCCHHH
14.4825619855
31PhosphorylationYGSVKPYTNFDAERD
CCCCCCCCCCCHHHH
37.6325619855
44PhosphorylationRDALNIETAVKTKGV
HHCCCHHHHHHCCCC
32.7122499769
49UbiquitinationIETAVKTKGVDEVTI
HHHHHHCCCCCEEEE
51.7422790023
49AcetylationIETAVKTKGVDEVTI
HHHHHHCCCCCEEEE
51.7423806337
75PhosphorylationRQDIAFAYQRRTKKE
HHHHHHHHHHCCHHH
8.9729514104
81AcetylationAYQRRTKKELPSALK
HHHHCCHHHHCHHHH
64.9622826441
89PhosphorylationELPSALKSALSGHLE
HHCHHHHHHHHCCHH
34.9823984901
92PhosphorylationSALKSALSGHLETVI
HHHHHHHHCCHHHHH
24.7127180971
97PhosphorylationALSGHLETVILGLLK
HHHCCHHHHHHHHHC
21.1423984901
112PhosphorylationTPAQYDASELKASMK
CHHHCCHHHHHHHHC
40.3325338131
115UbiquitinationQYDASELKASMKGLG
HCCHHHHHHHHCCCC
34.0722790023
115AcetylationQYDASELKASMKGLG
HCCHHHHHHHHCCCC
34.0722733758
123PhosphorylationASMKGLGTDEDSLIE
HHHCCCCCCHHHHHH
41.0623984901
127PhosphorylationGLGTDEDSLIEIICS
CCCCCHHHHHHHHHH
29.2426824392
133S-nitrosocysteineDSLIEIICSRTNQEL
HHHHHHHHHCCHHHH
2.50-
133GlutathionylationDSLIEIICSRTNQEL
HHHHHHHHHCCHHHH
2.5024333276
133S-nitrosylationDSLIEIICSRTNQEL
HHHHHHHHHCCHHHH
2.5022588120
136PhosphorylationIEIICSRTNQELQEI
HHHHHHCCHHHHHHH
25.5926239621
148UbiquitinationQEINRVYKEMYKTDL
HHHHHHHHHHHCCHH
32.9022790023
148AcetylationQEINRVYKEMYKTDL
HHHHHHHHHHHCCHH
32.9022826441
152AcetylationRVYKEMYKTDLEKDI
HHHHHHHCCHHHHHH
33.9623806337
157AcetylationMYKTDLEKDIISDTS
HHCCHHHHHHHCCCC
62.6222826441
161PhosphorylationDLEKDIISDTSGDFR
HHHHHHHCCCCHHHH
34.8626060331
163PhosphorylationEKDIISDTSGDFRKL
HHHHHCCCCHHHHHH
28.0226824392
164PhosphorylationKDIISDTSGDFRKLM
HHHHCCCCHHHHHHH
41.1627180971
169AcetylationDTSGDFRKLMVALAK
CCCHHHHHHHHHHHC
40.7122733758
176AcetylationKLMVALAKGRRAEDG
HHHHHHHCCCCCCCC
54.5223236377
184PhosphorylationGRRAEDGSVIDYELI
CCCCCCCCCCCCEEC
28.3725619855
188PhosphorylationEDGSVIDYELIDQDA
CCCCCCCCEECCHHH
11.0825619855
199PhosphorylationDQDARELYDAGVKRK
CHHHHHHHHHCCCCC
10.0522499769
204AcetylationELYDAGVKRKGTDVP
HHHHHCCCCCCCCCC
47.697612875
212AcetylationRKGTDVPKWISIMTE
CCCCCCCHHHHHHHH
57.9422826441
215PhosphorylationTDVPKWISIMTERSV
CCCCHHHHHHHHHHH
12.7527180971
223GlutathionylationIMTERSVCHLQKVFE
HHHHHHHHHHHHHHH
2.5324333276
227AcetylationRSVCHLQKVFERYKS
HHHHHHHHHHHHHHC
56.0823806337
227MalonylationRSVCHLQKVFERYKS
HHHHHHHHHHHHHHC
56.0826320211
233AcetylationQKVFERYKSYSPYDM
HHHHHHHHCCCHHHH
49.4923806337
233SuccinylationQKVFERYKSYSPYDM
HHHHHHHHCCCHHHH
49.4923806337
234PhosphorylationKVFERYKSYSPYDML
HHHHHHHCCCHHHHH
23.1629514104
235PhosphorylationVFERYKSYSPYDMLE
HHHHHHCCCHHHHHH
14.9829514104
236PhosphorylationFERYKSYSPYDMLES
HHHHHCCCHHHHHHH
24.8730460009
238PhosphorylationRYKSYSPYDMLESIK
HHHCCCHHHHHHHHH
14.1916873679
245AcetylationYDMLESIKKEVKGDL
HHHHHHHHHHHCCHH
52.7623236377
262S-nitrosylationAFLNLVQCIQNKPLY
HHHHHHHHHHCCCCH
2.4220925432
262S-nitrosocysteineAFLNLVQCIQNKPLY
HHHHHHHHHHCCCCH
2.42-
262GlutathionylationAFLNLVQCIQNKPLY
HHHHHHHHHHCCCCH
2.4224333276
275PhosphorylationLYFADRLYDSMKGKG
CHHHHHHHHHHCCCC
13.5822499769
277PhosphorylationFADRLYDSMKGKGTR
HHHHHHHHHCCCCCC
14.6122499769
279AcetylationDRLYDSMKGKGTRDK
HHHHHHHCCCCCCCH
62.5123236377
279MalonylationDRLYDSMKGKGTRDK
HHHHHHHCCCCCCCH
62.5126320211
302UbiquitinationRSEVDMLKIRSEFKR
HHHHHHHHHHHHHHH
29.4522790023
302AcetylationRSEVDMLKIRSEFKR
HHHHHHHHHHHHHHH
29.4523236377
310AcetylationIRSEFKRKYGKSLYY
HHHHHHHHHCCCCEE
59.9722826441
311PhosphorylationRSEFKRKYGKSLYYY
HHHHHHHHCCCCEEE
33.5422817900
313MalonylationEFKRKYGKSLYYYIQ
HHHHHHCCCCEEEEE
33.9126320211
313AcetylationEFKRKYGKSLYYYIQ
HHHHHHCCCCEEEEE
33.9123806337
314PhosphorylationFKRKYGKSLYYYIQQ
HHHHHCCCCEEEEEC
19.7622499769
316PhosphorylationRKYGKSLYYYIQQDT
HHHCCCCEEEEECCC
11.0020116462
317PhosphorylationKYGKSLYYYIQQDTK
HHCCCCEEEEECCCC
10.2122499769
318PhosphorylationYGKSLYYYIQQDTKG
HCCCCEEEEECCCCC
4.4322499769
324AcetylationYYIQQDTKGDYQKAL
EEEECCCCCCHHHHH
59.0622826441
324UbiquitinationYYIQQDTKGDYQKAL
EEEECCCCCCHHHHH
59.0622790023
329AcetylationDTKGDYQKALLYLCG
CCCCCHHHHHHHHCC
34.4722826441

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
24YPhosphorylationKinaseSRCP05480
Uniprot
26SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANXA2_MOUSE !!

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 ANXA2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYSF_MOUSEDysfphysical
14506282
PLOD1_HUMANPLOD1physical
26496610
PLOD2_HUMANPLOD2physical
26496610
PEPL_HUMANPPLphysical
26496610
S10AA_HUMANS100A10physical
26496610
PLOD3_HUMANPLOD3physical
26496610
AHNK_HUMANAHNAKphysical
26496610
GT251_HUMANCOLGALT1physical
26496610
AHNK2_HUMANAHNAK2physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANXA2_MOUSE

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Related Literatures of Post-Translational Modification

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