ANXA2_RAT - dbPTM
ANXA2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANXA2_RAT
UniProt AC Q07936
Protein Name Annexin A2
Gene Name Anxa2
Organism Rattus norvegicus (Rat).
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. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9..
Protein Sequence MSTVHEILCKLSLEGDHSTPPSAYGSVKPYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELPSAMKSALSGHLETVMLGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGEFRKLLVALAKGKRAEDGSVIDYELIDQDARELYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYFIQQDTKGDYQKALLYLCGGDD
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
2Phosphorylation------MSTVHEILC
------CCCHHHHHH
38.8523984901
2Acetylation------MSTVHEILC
------CCCHHHHHH
38.85-
3Phosphorylation-----MSTVHEILCK
-----CCCHHHHHHH
25.2823984901
12PhosphorylationHEILCKLSLEGDHST
HHHHHHHHCCCCCCC
15.1824317
18PhosphorylationLSLEGDHSTPPSAYG
HHCCCCCCCCCHHCC
47.5523984901
19PhosphorylationSLEGDHSTPPSAYGS
HCCCCCCCCCHHCCC
35.4823984901
22PhosphorylationGDHSTPPSAYGSVKP
CCCCCCCHHCCCCCC
35.0125532521
24PhosphorylationHSTPPSAYGSVKPYT
CCCCCHHCCCCCCCC
17.8025532521
26PhosphorylationTPPSAYGSVKPYTNF
CCCHHCCCCCCCCCC
17.8130181290
28AcetylationPSAYGSVKPYTNFDA
CHHCCCCCCCCCCCH
33.7222902405
49AcetylationIETAIKTKGVDEVTI
HHHHHHCCCCCEEEE
52.5122902405
55PhosphorylationTKGVDEVTIVNILTN
CCCCCEEEEEEEECC
19.7023984901
89PhosphorylationELPSAMKSALSGHLE
HCCHHHHHHHHHCHH
22.7434801875
92PhosphorylationSAMKSALSGHLETVM
HHHHHHHHHCHHHHH
24.7123984901
104AcetylationTVMLGLLKTPAQYDA
HHHHHHHCCHHHCCH
58.4622902405
115AcetylationQYDASELKASMKGLG
HCCHHHHHHHHCCCC
34.0722902405
117PhosphorylationDASELKASMKGLGTD
CHHHHHHHHCCCCCC
21.3123984901
119AcetylationSELKASMKGLGTDED
HHHHHHHCCCCCCHH
48.7922902405
123PhosphorylationASMKGLGTDEDSLIE
HHHCCCCCCHHHHHH
41.0623984901
127PhosphorylationGLGTDEDSLIEIICS
CCCCCHHHHHHHHHH
29.2423984901
148AcetylationQEINRVYKEMYKTDL
HHHHHHHHHHHCCHH
32.9022902405
152AcetylationRVYKEMYKTDLEKDI
HHHHHHHCCHHHHHH
33.9622902405
157AcetylationMYKTDLEKDIISDTS
HHCCHHHHHHHCCCC
62.6222902405
169AcetylationDTSGEFRKLLVALAK
CCCHHHHHHHHHHHC
52.0426302492
184PhosphorylationGKRAEDGSVIDYELI
CCCCCCCCCCCCEEC
28.3728109543
188PhosphorylationEDGSVIDYELIDQDA
CCCCCCCCEECCHHH
11.0823984901
199PhosphorylationDQDARELYDAGVKRK
CHHHHHHHHHCCCCC
10.05-
212AcetylationRKGTDVPKWISIMTE
CCCCCCCHHHHHHHH
57.9422902405
227AcetylationRSVCHLQKVFERYKS
HHHHHHHHHHHHHHC
56.0825786129
234PhosphorylationKVFERYKSYSPYDML
HHHHHHHCCCHHHHH
23.1623984901
235PhosphorylationVFERYKSYSPYDMLE
HHHHHHCCCHHHHHH
14.9823984901
236PhosphorylationFERYKSYSPYDMLES
HHHHHCCCHHHHHHH
24.8723984901
238PhosphorylationRYKSYSPYDMLESIR
HHHCCCHHHHHHHHH
14.19-
279AcetylationDRLYDSMKGKGTRDK
HHHHHHHCCCCCCCH
62.5122902405
286AcetylationKGKGTRDKVLIRIMV
CCCCCCCHHHEEEEE
35.3322902405
302AcetylationRSEVDMLKIRSEFKR
HHHHCHHHHHHHHHH
29.4522902405
308AcetylationLKIRSEFKRKYGKSL
HHHHHHHHHHHCCCC
43.8822902405
313AcetylationEFKRKYGKSLYYFIQ
HHHHHHCCCCEEEHH
33.9122902405
314PhosphorylationFKRKYGKSLYYFIQQ
HHHHHCCCCEEEHHC
19.7623984901
324AcetylationYFIQQDTKGDYQKAL
EEHHCCCCCCHHHHH
59.0622902405

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
24YPhosphorylationKinaseSRCQ9WUD9
Uniprot
26SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANXA2_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ANXA2_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANXA2_RAT

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Related Literatures of Post-Translational Modification

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