CAPZB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAPZB_MOUSE
• UniProt AC: P47757
• Protein Name: F-actin-capping protein subunit beta
• Gene Name: Capzb
• Organism: Mus musculus (Mouse).
• Sequence Length: 277
• Subcellular Localization: Cytoplasm, cytoskeleton.; Isoform 1: Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere. In cardiac muscle, isoform 1 is located at Z-disks of sarcomeres while isoform 2 is enriched at intercalated disks..; Isoform 3: Cytoplasm,
• 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. Isoform 3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity)..
• Protein Sequence: MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSLDAIPDNHKFKQLQRELSQVLTQRQVYIQPDN

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
2	Phosphorylation	------MSDQQLDCA ------CCHHHHHHH	44.09	27566939
2	Acetylation	------MSDQQLDCA ------CCHHHHHHH	44.09	-
31 (in isoform 4)	Phosphorylation	-	4.90	25266776
53	Acetylation	PLKIARDKVVGKDYL CHHHHHHCCCCCCEE	33.01	22826441
57	Acetylation	ARDKVVGKDYLLCDY HHHCCCCCCEEECCC	31.43	22826441
62	S-palmitoylation	VGKDYLLCDYNRDGD CCCCEEECCCCCCCC	4.88	28526873
62	Glutathionylation	VGKDYLLCDYNRDGD CCCCEEECCCCCCCC	4.88	24333276
78	Acetylation	YRSPWSNKYDPPLED CCCCCCCCCCCCCCC	45.58	22826441
78	Ubiquitination	YRSPWSNKYDPPLED CCCCCCCCCCCCCCC	45.58	22790023
78	Ubiquitination	YRSPWSNKYDPPLED CCCCCCCCCCCCCCC	45.58	22790023
95	Ubiquitination	MPSARLRKLEVEANN CCCHHHHHHHHHHCC	54.30	22790023
95	Malonylation	MPSARLRKLEVEANN CCCHHHHHHHHHHCC	54.30	26320211
95	Acetylation	MPSARLRKLEVEANN CCCHHHHHHHHHHCC	54.30	23806337
95	Ubiquitination	MPSARLRKLEVEANN CCCHHHHHHHHHHCC	54.30	-
145	Acetylation	GDGSKKIKGCWDSIH CCCCCCCCCCCCEEE	57.82	22826441
147	Glutathionylation	GSKKIKGCWDSIHVV CCCCCCCCCCEEEEE	2.87	24333276
159	Ubiquitination	HVVEVQEKSSGRTAH EEEEEEECCCCCCEE	32.60	-
159	Acetylation	HVVEVQEKSSGRTAH EEEEEEECCCCCCEE	32.60	23236377
159	Ubiquitination	HVVEVQEKSSGRTAH EEEEEEECCCCCCEE	32.60	22790023
159	Malonylation	HVVEVQEKSSGRTAH EEEEEEECCCCCCEE	32.60	26320211
182	Phosphorylation	LWLQTNKSGSGTMNL EEEEECCCCCCEEEC	40.02	25521595
184	Phosphorylation	LQTNKSGSGTMNLGG EEECCCCCCEEECCC	37.88	25266776
186	Phosphorylation	TNKSGSGTMNLGGSL ECCCCCCEEECCCCC	12.46	26643407
199	Acetylation	SLTRQMEKDETVSDC CCCHHHHCCCCHHHC	56.36	23806337
204	Phosphorylation	MEKDETVSDCSPHIA HHCCCCHHHCCHHHH	40.08	26525534
206	Glutathionylation	KDETVSDCSPHIANI CCCCHHHCCHHHHHH	5.48	24333276
206	S-nitrosylation	KDETVSDCSPHIANI CCCCHHHCCHHHHHH	5.48	21278135
206	S-nitrosocysteine	KDETVSDCSPHIANI CCCCHHHCCHHHHHH	5.48	-
223	Ubiquitination	LVEDMENKIRSTLNE HHHHHHHHHHHHHHH	26.62	22790023
223	Acetylation	LVEDMENKIRSTLNE HHHHHHHHHHHHHHH	26.62	23236377
223	Malonylation	LVEDMENKIRSTLNE HHHHHHHHHHHHHHH	26.62	26320211
223	Ubiquitination	LVEDMENKIRSTLNE HHHHHHHHHHHHHHH	26.62	-
226	Phosphorylation	DMENKIRSTLNEIYF HHHHHHHHHHHHHHC	40.49	29899451
232	Phosphorylation	RSTLNEIYFGKTKDI HHHHHHHHCCCHHHH	10.49	-
235	Ubiquitination	LNEIYFGKTKDIVNG HHHHHCCCHHHHHHH	42.37	-
235	Ubiquitination	LNEIYFGKTKDIVNG HHHHHCCCHHHHHHH	42.37	22790023
235	Acetylation	LNEIYFGKTKDIVNG HHHHHCCCHHHHHHH	42.37	23806337
235	Succinylation	LNEIYFGKTKDIVNG HHHHHCCCHHHHHHH	42.37	23806337
237	Ubiquitination	EIYFGKTKDIVNGLR HHHCCCHHHHHHHHH	49.28	22790023
237	Ubiquitination	EIYFGKTKDIVNGLR HHHCCCHHHHHHHHH	49.28	22790023
245 (in isoform 2)	Phosphorylation	-	35.33	25521595
245	Phosphorylation	DIVNGLRSLDAIPDN HHHHHHHHCCCCCCC	35.33	28464351
252 (in isoform 2)	Ubiquitination	-	34.59	-
254 (in isoform 2)	Ubiquitination	-	61.58	-
254	Ubiquitination	DAIPDNHKFKQLQRE CCCCCCHHHHHHHHH	61.58	-
259 (in isoform 2)	Ubiquitination	-	34.02	-
263	Phosphorylation	KQLQRELSQVLTQRQ HHHHHHHHHHHHHCC	17.31	25521595
274 (in isoform 4)	Phosphorylation	-	22.93	25521595

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CAPZB_MOUSE !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CAPZB_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CAPZB_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.
PubMed: 17242355