UniProt ID | CAZA2_HUMAN | |
---|---|---|
UniProt AC | P47755 | |
Protein Name | F-actin-capping protein subunit alpha-2 | |
Gene Name | CAPZA2 | |
Organism | Homo sapiens (Human). | |
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 | MADLEEQLSDEEKVRIAAKFIIHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNLDQFTPVKIEGYEDQVLITEHGDLGNGKFLDPKNRICFKFDHLRKEATDPRPCEVENAVESWRTSVETALRAYVKEHYPNGVCTVYGKKIDGQQTIIACIESHQFQAKNFWNGRWRSEWKFTITPSTTQVVGILKIQVHYYEDGNVQLVSHKDIQDSLTVSNEVQTAKEFIKIVEAAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MADLEEQLS ------CCCHHHHCC | 30.05 | 22223895 | |
9 | Phosphorylation | ADLEEQLSDEEKVRI CCHHHHCCHHHHHHH | 42.54 | 29255136 | |
13 | Ubiquitination | EQLSDEEKVRIAAKF HHCCHHHHHHHEEEE | 34.46 | - | |
13 | Ubiquitination | EQLSDEEKVRIAAKF HHCCHHHHHHHEEEE | 34.46 | - | |
19 | Acetylation | EKVRIAAKFIIHAPP HHHHHEEEEEEECCC | 28.24 | 25953088 | |
19 | Ubiquitination | EKVRIAAKFIIHAPP HHHHHEEEEEEECCC | 28.24 | 21890473 | |
19 | Ubiquitination | EKVRIAAKFIIHAPP HHHHHEEEEEEECCC | 28.24 | 21890473 | |
63 | Phosphorylation | QYNLDQFTPVKIEGY HCCCCCCCCEEEECC | 22.87 | 25850435 | |
70 | Phosphorylation | TPVKIEGYEDQVLIT CCEEEECCCCEEEEE | 11.98 | - | |
86 | Acetylation | HGDLGNGKFLDPKNR CCCCCCCCCCCCCCC | 46.91 | 23954790 | |
86 | Ubiquitination | HGDLGNGKFLDPKNR CCCCCCCCCCCCCCC | 46.91 | 21906983 | |
86 | Acetylation | HGDLGNGKFLDPKNR CCCCCCCCCCCCCCC | 46.91 | - | |
86 | Ubiquitination | HGDLGNGKFLDPKNR CCCCCCCCCCCCCCC | 46.91 | - | |
91 | Ubiquitination | NGKFLDPKNRICFKF CCCCCCCCCCEEEEH | 59.53 | - | |
91 | Ubiquitination | NGKFLDPKNRICFKF CCCCCCCCCCEEEEH | 59.53 | - | |
97 | Ubiquitination | PKNRICFKFDHLRKE CCCCEEEEHHHHHCC | 45.53 | 19608861 | |
97 | Acetylation | PKNRICFKFDHLRKE CCCCEEEEHHHHHCC | 45.53 | 25825284 | |
103 | Ubiquitination | FKFDHLRKEATDPRP EEHHHHHCCCCCCCC | 59.05 | - | |
133 | Ubiquitination | TALRAYVKEHYPNGV HHHHHHHHHHCCCCE | 26.54 | 21890473 | |
133 | Acetylation | TALRAYVKEHYPNGV HHHHHHHHHHCCCCE | 26.54 | 26051181 | |
133 | Ubiquitination | TALRAYVKEHYPNGV HHHHHHHHHHCCCCE | 26.54 | 21890473 | |
142 | Phosphorylation | HYPNGVCTVYGKKID HCCCCEEEEEEEEEC | 17.85 | - | |
144 | Phosphorylation | PNGVCTVYGKKIDGQ CCCEEEEEEEEECCC | 12.69 | - | |
146 | 2-Hydroxyisobutyrylation | GVCTVYGKKIDGQQT CEEEEEEEEECCCEE | 28.94 | - | |
146 | Ubiquitination | GVCTVYGKKIDGQQT CEEEEEEEEECCCEE | 28.94 | - | |
146 | Acetylation | GVCTVYGKKIDGQQT CEEEEEEEEECCCEE | 28.94 | 25953088 | |
166 | Ubiquitination | ESHQFQAKNFWNGRW ECCEEEEECCCCCCC | 41.72 | - | |
180 | Phosphorylation | WRSEWKFTITPSTTQ CCCEEEEEECCCCCE | 21.88 | 20068231 | |
184 | Phosphorylation | WKFTITPSTTQVVGI EEEEECCCCCEEEEE | 35.12 | 24719451 | |
185 | Phosphorylation | KFTITPSTTQVVGIL EEEECCCCCEEEEEE | 23.58 | 28348404 | |
186 | Phosphorylation | FTITPSTTQVVGILK EEECCCCCEEEEEEE | 24.57 | 28348404 | |
198 | Phosphorylation | ILKIQVHYYEDGNVQ EEEEEEEEEECCCEE | 15.08 | 22817900 | |
215 | Phosphorylation | SHKDIQDSLTVSNEV EECCCCCCEEECHHH | 15.01 | 21406692 | |
217 | Phosphorylation | KDIQDSLTVSNEVQT CCCCCCEEECHHHHH | 26.32 | 21406692 | |
219 | Phosphorylation | IQDSLTVSNEVQTAK CCCCEEECHHHHHHH | 23.26 | 21406692 | |
224 | Phosphorylation | TVSNEVQTAKEFIKI EECHHHHHHHHHHHH | 44.89 | 21406692 | |
226 | Ubiquitination | SNEVQTAKEFIKIVE CHHHHHHHHHHHHHH | 57.45 | 21890473 | |
230 | Ubiquitination | QTAKEFIKIVEAAEN HHHHHHHHHHHHHHH | 46.12 | - | |
247 | Phosphorylation | QTAISENYQTMSDTT HHHHHHHCCCCCHHH | 10.99 | - | |
250 | Sulfoxidation | ISENYQTMSDTTFKA HHHHCCCCCHHHHHH | 1.69 | 30846556 | |
256 | Ubiquitination | TMSDTTFKALRRQLP CCCHHHHHHHHHHCC | 44.40 | 21890473 | |
256 | Methylation | TMSDTTFKALRRQLP CCCHHHHHHHHHHCC | 44.40 | - | |
268 | Ubiquitination | QLPVTRTKIDWNKIL HCCCCCCEECHHHHH | 35.06 | - | |
268 | Sumoylation | QLPVTRTKIDWNKIL HCCCCCCEECHHHHH | 35.06 | - | |
268 | Malonylation | QLPVTRTKIDWNKIL HCCCCCCEECHHHHH | 35.06 | 26320211 | |
268 | Sumoylation | QLPVTRTKIDWNKIL HCCCCCCEECHHHHH | 35.06 | - | |
268 | 2-Hydroxyisobutyrylation | QLPVTRTKIDWNKIL HCCCCCCEECHHHHH | 35.06 | - | |
273 | Malonylation | RTKIDWNKILSYKIG CCEECHHHHHHHHCH | 40.55 | 26320211 | |
273 | 2-Hydroxyisobutyrylation | RTKIDWNKILSYKIG CCEECHHHHHHHHCH | 40.55 | - | |
273 | Sumoylation | RTKIDWNKILSYKIG CCEECHHHHHHHHCH | 40.55 | - | |
273 | Ubiquitination | RTKIDWNKILSYKIG CCEECHHHHHHHHCH | 40.55 | 21890473 | |
273 | Sumoylation | RTKIDWNKILSYKIG CCEECHHHHHHHHCH | 40.55 | - | |
273 | Acetylation | RTKIDWNKILSYKIG CCEECHHHHHHHHCH | 40.55 | 23954790 | |
277 | Phosphorylation | DWNKILSYKIGKEMQ CHHHHHHHHCHHHHC | 11.81 | - | |
278 | Acetylation | WNKILSYKIGKEMQN HHHHHHHHCHHHHCC | 41.42 | 23749302 | |
278 | Malonylation | WNKILSYKIGKEMQN HHHHHHHHCHHHHCC | 41.42 | 26320211 | |
278 | Ubiquitination | WNKILSYKIGKEMQN HHHHHHHHCHHHHCC | 41.42 | 21890473 | |
278 | 2-Hydroxyisobutyrylation | WNKILSYKIGKEMQN HHHHHHHHCHHHHCC | 41.42 | - | |
278 | Sumoylation | WNKILSYKIGKEMQN HHHHHHHHCHHHHCC | 41.42 | - | |
278 | Sumoylation | WNKILSYKIGKEMQN HHHHHHHHCHHHHCC | 41.42 | - | |
281 | Ubiquitination | ILSYKIGKEMQNA-- HHHHHCHHHHCCC-- | 54.19 | 21890473 |
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_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAZA2_HUMAN !! |
* 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_HUMAN !! |
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. |
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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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY. | |
"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-86; LYS-97 AND LYS-273, ANDMASS SPECTROMETRY. | |
Phosphorylation | |
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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY. |