CAPZB_HUMAN - dbPTM
CAPZB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAPZB_HUMAN
UniProt AC P47756
Protein Name F-actin-capping protein subunit beta
Gene Name CAPZB
Organism Homo sapiens (Human).
Sequence Length 277
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere.
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. Plays a role in the regulation of cell morphology and cytoskeletal organization..
Protein Sequence MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSIDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN
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------MSDQQLDCA
------CCHHHHHHH		44.0925159151
2Acetylation------MSDQQLDCA
------CCHHHHHHH		44.0918491316
14MethylationDCALDLMRRLPPQQI
HHHHHHHHHCCHHHH		44.26-
23UbiquitinationLPPQQIEKNLSDLID
CCHHHHHHHHHHHHH		65.89-
34PhosphorylationDLIDLVPSLCEDLLS
HHHHHHHHHHHHHHH		37.8726434776
41PhosphorylationSLCEDLLSSVDQPLK
HHHHHHHHCCCCCHH		35.3026434776
42PhosphorylationLCEDLLSSVDQPLKI
HHHHHHHCCCCCHHH		29.6826434776
53UbiquitinationPLKIARDKVVGKDYL
CHHHHHHCCCCCCEE		33.01-
572-HydroxyisobutyrylationARDKVVGKDYLLCDY
HHHCCCCCCEEECCC		31.43-
57UbiquitinationARDKVVGKDYLLCDY
HHHCCCCCCEEECCC		31.43-
57AcetylationARDKVVGKDYLLCDY
HHHCCCCCCEEECCC		31.4326822725
59PhosphorylationDKVVGKDYLLCDYNR
HCCCCCCEEECCCCC		12.6928152594
64PhosphorylationKDYLLCDYNRDGDSY
CCEEECCCCCCCCCC		15.8828152594
73PhosphorylationRDGDSYRSPWSNKYD
CCCCCCCCCCCCCCC		23.6125159151
76PhosphorylationDSYRSPWSNKYDPPL
CCCCCCCCCCCCCCC		27.1623532336
78UbiquitinationYRSPWSNKYDPPLED
CCCCCCCCCCCCCCC		45.5821890473
78AcetylationYRSPWSNKYDPPLED
CCCCCCCCCCCCCCC		45.5823749302
78UbiquitinationYRSPWSNKYDPPLED
CCCCCCCCCCCCCCC		45.5821890473
78 (in isoform 1)Ubiquitination-45.5821890473
78 (in isoform 2)Ubiquitination-45.5821890473
88SulfoxidationPPLEDGAMPSARLRK
CCCCCCCCCCHHHHH		3.0921406390
90PhosphorylationLEDGAMPSARLRKLE
CCCCCCCCHHHHHHH		16.9723532336
95AcetylationMPSARLRKLEVEANN
CCCHHHHHHHHHHCC		54.3026051181
95UbiquitinationMPSARLRKLEVEANN
CCCHHHHHHHHHHCC		54.30-
95UbiquitinationMPSARLRKLEVEANN
CCCHHHHHHHHHHCC		54.3021890473
95 (in isoform 2)Ubiquitination-54.3021890473
95 (in isoform 1)Ubiquitination-54.3021890473
95MalonylationMPSARLRKLEVEANN
CCCHHHHHHHHHHCC		54.3026320211
107PhosphorylationANNAFDQYRDLYFEG
HCCHHHHHHHHHEEC		14.13-
135AcetylationFAGVILIKKAGDGSK
EEEEEEEEECCCCCC		32.8830587443
136AcetylationAGVILIKKAGDGSKK
EEEEEEEECCCCCCC		51.0826051181
142AcetylationKKAGDGSKKIKGCWD
EECCCCCCCCCCCCC		65.1426051181
145MalonylationGDGSKKIKGCWDSIH
CCCCCCCCCCCCEEE		57.8226320211
159AcetylationHVVEVQEKSSGRTAH
EEEEEEECCCCCCEE		32.6023236377
1592-HydroxyisobutyrylationHVVEVQEKSSGRTAH
EEEEEEECCCCCCEE		32.60-
159UbiquitinationHVVEVQEKSSGRTAH
EEEEEEECCCCCCEE		32.60-
160PhosphorylationVVEVQEKSSGRTAHY
EEEEEECCCCCCEEE		36.9526437602
164PhosphorylationQEKSSGRTAHYKLTS
EECCCCCCEEEEEEE		22.7026437602
170PhosphorylationRTAHYKLTSTVMLWL
CCEEEEEEEEEEEEE		20.4223403867
171PhosphorylationTAHYKLTSTVMLWLQ
CEEEEEEEEEEEEEE		29.4620068231
172PhosphorylationAHYKLTSTVMLWLQT
EEEEEEEEEEEEEEE		12.5223403867
179PhosphorylationTVMLWLQTNKSGSGT
EEEEEEEECCCCCCE		42.3020068231
182PhosphorylationLWLQTNKSGSGTMNL
EEEEECCCCCCEEEC		40.0225159151
184PhosphorylationLQTNKSGSGTMNLGG
EEECCCCCCEEECCC		37.8825159151
186PhosphorylationTNKSGSGTMNLGGSL
ECCCCCCEEECCCCC		12.4625159151
187SulfoxidationNKSGSGTMNLGGSLT
CCCCCCEEECCCCCE		4.4321406390
192PhosphorylationGTMNLGGSLTRQMEK
CEEECCCCCEEHHHC		25.4325159151
194PhosphorylationMNLGGSLTRQMEKDE
EECCCCCEEHHHCCC		22.13-
197SulfoxidationGGSLTRQMEKDETVS
CCCCEEHHHCCCCHH		6.6128465586
199UbiquitinationSLTRQMEKDETVSDC
CCEEHHHCCCCHHHC		56.36-
199MalonylationSLTRQMEKDETVSDC
CCEEHHHCCCCHHHC		56.3626320211
199AcetylationSLTRQMEKDETVSDC
CCEEHHHCCCCHHHC		56.3623749302
202PhosphorylationRQMEKDETVSDCSPH
EHHHCCCCHHHCCHH		35.1326126808
204PhosphorylationMEKDETVSDCSPHIA
HHCCCCHHHCCHHHH		40.0826126808
207PhosphorylationDETVSDCSPHIANIG
CCCHHHCCHHHHHHH		25.2227050516
223MalonylationLVEDMENKIRSTLNE
HHHHHHHHHHHHHHH		26.6226320211
223AcetylationLVEDMENKIRSTLNE
HHHHHHHHHHHHHHH		26.6223954790
223UbiquitinationLVEDMENKIRSTLNE
HHHHHHHHHHHHHHH		26.62-
2232-HydroxyisobutyrylationLVEDMENKIRSTLNE
HHHHHHHHHHHHHHH		26.62-
226PhosphorylationDMENKIRSTLNEIYF
HHHHHHHHHHHHHHC		40.4923312004
227PhosphorylationMENKIRSTLNEIYFG
HHHHHHHHHHHHHCC		24.6129083192
232 (in isoform 2)Phosphorylation-10.4928064214
232PhosphorylationRSTLNEIYFGKTKDI
HHHHHHHHCCCHHHH		10.4918180459
235 (in isoform 1)Ubiquitination-42.3721890473
2352-HydroxyisobutyrylationLNEIYFGKTKDIVNG
HHHHHCCCHHHHHHC		42.37-
235AcetylationLNEIYFGKTKDIVNG
HHHHHCCCHHHHHHC		42.3719608861
235 (in isoform 2)Ubiquitination-42.3721890473
235UbiquitinationLNEIYFGKTKDIVNG
HHHHHCCCHHHHHHC		42.3719608861
235UbiquitinationLNEIYFGKTKDIVNG
HHHHHCCCHHHHHHC		42.3721890473
236PhosphorylationNEIYFGKTKDIVNGL
HHHHCCCHHHHHHCH		34.0429083192
237UbiquitinationEIYFGKTKDIVNGLR
HHHCCCHHHHHHCHH		49.28-
245 (in isoform 2)Phosphorylation-29.8420068231
245PhosphorylationDIVNGLRSIDAIPDN
HHHHCHHCCCCCCCC		29.8426437602
248 (in isoform 2)Phosphorylation-17.3420068231
252 (in isoform 2)Ubiquitination-41.4021890473
252UbiquitinationSIDAIPDNQKFKQLQ
CCCCCCCCHHHHHHH		41.4021890473
253 (in isoform 2)Phosphorylation-61.0020068231
256UbiquitinationIPDNQKFKQLQRELS
CCCCHHHHHHHHHHH		58.07-
263PhosphorylationKQLQRELSQVLTQRQ
HHHHHHHHHHHHHCC		17.3123911959
267 (in isoform 2)Ubiquitination-23.89-
267PhosphorylationRELSQVLTQRQIYIQ
HHHHHHHHHCCEEEC		23.8928060719
272PhosphorylationVLTQRQIYIQPDN--
HHHHCCEEECCCC--		5.7927642862
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 CAPZB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAPZB_HUMAN !!
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 CAPZB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RM20_HUMANMRPL20physical
16169070
PTN_HUMANPTNphysical
16169070
BCCIP_HUMANBCCIPphysical
16169070
HSP7C_HUMANHSPA8physical
20884878
CAZA1_HUMANCAPZA1physical
22939629
PAPS1_HUMANPAPSS1physical
22863883
ARPC2_HUMANARPC2physical
26344197
ARPC3_HUMANARPC3physical
26344197
CNOT2_HUMANCNOT2physical
26344197
DCTN1_HUMANDCTN1physical
26344197
DCTN6_HUMANDCTN6physical
26344197
DDX53_HUMANDDX53physical
26344197
MYO5B_HUMANMYO5Bphysical
26344197
SNAA_HUMANNAPAphysical
26344197
RPAP3_HUMANRPAP3physical
26344197
TMOD3_HUMANTMOD3physical
26344197
TOM40_HUMANTOMM40physical
26344197
TPM2_HUMANTPM2physical
26344197
UBL7_HUMANUBL7physical
26344197
DCTN2_HUMANDCTN2physical
27173435
DCTN1_HUMANDCTN1physical
27173435
Drug and Disease Associations
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.
Regulatory Network of CAPZB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT SER-2.
"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-235, AND MASS SPECTROMETRY.

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