CAZA2_MOUSE - dbPTM
CAZA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAZA2_MOUSE
UniProt AC P47754
Protein Name F-actin-capping protein subunit alpha-2
Gene Name Capza2
Organism Mus musculus (Mouse).
Sequence Length 286
Subcellular Localization
Protein Description F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments..
Protein Sequence MADLEEQLSDEEKVRIAAKFIIHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNLDQFTPVKIEGYEDQVLITEHGDLGNGKFLDPKNRICFKFDHLRKEATDPRPYEAENAIESWRTSVETALRAYVKEHYPNGVCTVYGKKVDGQQTIIACIESHQFQAKNFWNGRWRSEWKFTVTPSTTQVVGILKIQVHYYEDGNVQLVSHKDIQDSLTVSNEVQTAKEFIKIVEAAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
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------MADLEEQLS
------CCCHHHHCC
30.05-
9PhosphorylationADLEEQLSDEEKVRI
CCHHHHCCHHHHHHH
42.5426824392
63PhosphorylationQYNLDQFTPVKIEGY
HCCCCCCCCEEEECC
22.8725521595
86AcetylationHGDLGNGKFLDPKNR
CCCCCCCCCCCCCCC
46.9122826441
86UbiquitinationHGDLGNGKFLDPKNR
CCCCCCCCCCCCCCC
46.9122790023
97AcetylationPKNRICFKFDHLRKE
CCCCEEEEHHHHHHC
45.5322826441
126PhosphorylationSWRTSVETALRAYVK
HHHHHHHHHHHHHHH
28.9228464351
133UbiquitinationTALRAYVKEHYPNGV
HHHHHHHHHHCCCCE
26.5422790023
141S-nitrosocysteineEHYPNGVCTVYGKKV
HHCCCCEEEEEEEEE
1.95-
141S-nitrosylationEHYPNGVCTVYGKKV
HHCCCCEEEEEEEEE
1.9520925432
157S-palmitoylationGQQTIIACIESHQFQ
CCEEEEEEEECCEEE
2.2128680068
157S-nitrosylationGQQTIIACIESHQFQ
CCEEEEEEEECCEEE
2.2120925432
157S-nitrosocysteineGQQTIIACIESHQFQ
CCEEEEEEEECCEEE
2.21-
180PhosphorylationWRSEWKFTVTPSTTQ
CCCEEEEEECCCCEE
21.5328576409
182PhosphorylationSEWKFTVTPSTTQVV
CEEEEEECCCCEEEE
14.4125521595
184PhosphorylationWKFTVTPSTTQVVGI
EEEEECCCCEEEEEE
34.4229514104
185PhosphorylationKFTVTPSTTQVVGIL
EEEECCCCEEEEEEE
23.5829472430
186PhosphorylationFTVTPSTTQVVGILK
EEECCCCEEEEEEEE
24.5729472430
198PhosphorylationILKIQVHYYEDGNVQ
EEEEEEEEEECCCEE
15.08-
215PhosphorylationSHKDIQDSLTVSNEV
EECCCCCCEEECHHH
15.0128464351
217PhosphorylationKDIQDSLTVSNEVQT
CCCCCCEEECHHHHH
26.3228464351
226SuccinylationSNEVQTAKEFIKIVE
CHHHHHHHHHHHHHH
57.4523954790
268UbiquitinationQLPVTRTKIDWNKIL
HCCCCCCEECHHHHH
35.06-
268MalonylationQLPVTRTKIDWNKIL
HCCCCCCEECHHHHH
35.0626320211
273UbiquitinationRTKIDWNKILSYKIG
CCEECHHHHHHHHCH
40.5522790023
273AcetylationRTKIDWNKILSYKIG
CCEECHHHHHHHHCH
40.55132803
277PhosphorylationDWNKILSYKIGKEMQ
CHHHHHHHHCHHHHC
11.8129514104
278MalonylationWNKILSYKIGKEMQN
HHHHHHHHCHHHHCC
41.4226320211
278UbiquitinationWNKILSYKIGKEMQN
HHHHHHHHCHHHHCC
41.4222790023

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 CAZA2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAZA2_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 CAZA2_MOUSE !!

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

Oops, there are no PPI records of CAZA2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAZA2_MOUSE

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Related Literatures of Post-Translational Modification

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