CAPG_HUMAN - dbPTM
CAPG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAPG_HUMAN
UniProt AC P40121
Protein Name Macrophage-capping protein
Gene Name CAPG
Organism Homo sapiens (Human).
Sequence Length 348
Subcellular Localization Nucleus . Cytoplasm . Secreted . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Redistributes throughout the cytoplasm during mitosis and is excluded from regions containing chromosome
Protein Description Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA..
Protein Sequence MYTAIPQSGSPFPGSVQDPGLHVWRVEKLKPVPVAQENQGVFFSGDSYLVLHNGPEEVSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERPVQHREVQGNESDLFMSYFPRGLKYQEGGVESAFHKTSTGAPAAIKKLYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQVEIVTDGEEPAEMIQVLGPKPALKEGNPEEDLTADKANAQAAALYKVSDATGQMNLTKVADSSPFALELLISDDCFVLDNGLCGKIYIWKGRKANEKERQAALQVAEGFISRMQYAPNTQVEILPQGHESPIFKQFFKDWK
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
1Acetylation-------MYTAIPQS
-------CCCCCCCC		6.3925944712
2Phosphorylation------MYTAIPQSG
------CCCCCCCCC		12.6025106551
3Phosphorylation-----MYTAIPQSGS
-----CCCCCCCCCC		19.4725106551
8PhosphorylationMYTAIPQSGSPFPGS
CCCCCCCCCCCCCCC		35.5628450419
10PhosphorylationTAIPQSGSPFPGSVQ
CCCCCCCCCCCCCCC		28.7225159151
15PhosphorylationSGSPFPGSVQDPGLH
CCCCCCCCCCCCCCE		19.4928450419
103PhosphorylationREVQGNESDLFMSYF
CCCCCCCCHHHHHHC		43.54-
107SulfoxidationGNESDLFMSYFPRGL
CCCCHHHHHHCCCCC		4.0630846556
108PhosphorylationNESDLFMSYFPRGLK
CCCHHHHHHCCCCCC		19.11-
115AcetylationSYFPRGLKYQEGGVE
HHCCCCCCCCCCCHH		47.9525953088
115UbiquitinationSYFPRGLKYQEGGVE
HHCCCCCCCCCCCHH		47.95-
116PhosphorylationYFPRGLKYQEGGVES
HCCCCCCCCCCCHHH		19.4828152594
123PhosphorylationYQEGGVESAFHKTST
CCCCCHHHHCCCCCC		33.5528857561
1272-HydroxyisobutyrylationGVESAFHKTSTGAPA
CHHHHCCCCCCCCCH		37.40-
127UbiquitinationGVESAFHKTSTGAPA
CHHHHCCCCCCCCCH		37.40-
128PhosphorylationVESAFHKTSTGAPAA
HHHHCCCCCCCCCHH		23.9728985074
129PhosphorylationESAFHKTSTGAPAAI
HHHCCCCCCCCCHHH		29.6425159151
130PhosphorylationSAFHKTSTGAPAAIK
HHCCCCCCCCCHHHH		42.4626657352
1372-HydroxyisobutyrylationTGAPAAIKKLYQVKG
CCCCHHHHHHHHCCC		31.81-
137UbiquitinationTGAPAAIKKLYQVKG
CCCCHHHHHHHHCCC		31.81-
137AcetylationTGAPAAIKKLYQVKG
CCCCHHHHHHHHCCC		31.8123749302
143UbiquitinationIKKLYQVKGKKNIRA
HHHHHHCCCCCCCCC		49.87-
143SuccinylationIKKLYQVKGKKNIRA
HHHHHHCCCCCCCCC		49.8723954790
151PhosphorylationGKKNIRATERALNWD
CCCCCCCCHHHHCCC		19.02-
205UbiquitinationRDSERQGKAQVEIVT
HCCCCCCCCEEEEEE		27.57-
212PhosphorylationKAQVEIVTDGEEPAE
CCEEEEEECCCCCHH		43.9028450419
227UbiquitinationMIQVLGPKPALKEGN
HHHHHCCCHHHCCCC		40.92-
231UbiquitinationLGPKPALKEGNPEED
HCCCHHHCCCCCHHC		66.73-
231AcetylationLGPKPALKEGNPEED
HCCCHHHCCCCCHHC		66.7318526033
243AcetylationEEDLTADKANAQAAA
HHCCCCHHHHHHHHH		40.8725953088
243UbiquitinationEEDLTADKANAQAAA
HHCCCCHHHHHHHHH		40.8721906983
253UbiquitinationAQAAALYKVSDATGQ
HHHHHHHHHHCCCCC		35.79-
2532-HydroxyisobutyrylationAQAAALYKVSDATGQ
HHHHHHHHHHCCCCC		35.79-
258PhosphorylationLYKVSDATGQMNLTK
HHHHHCCCCCCCCEE		32.70-
261SulfoxidationVSDATGQMNLTKVAD
HHCCCCCCCCEEECC		4.7321406390
297AcetylationCGKIYIWKGRKANEK
CCEEEEECCCCCCHH		39.0026051181
297UbiquitinationCGKIYIWKGRKANEK
CCEEEEECCCCCCHH		39.00-
318PhosphorylationQVAEGFISRMQYAPN
HHHHHHHHHHCCCCC		21.3121712546
322PhosphorylationGFISRMQYAPNTQVE
HHHHHHCCCCCCCEE		18.0626074081
326PhosphorylationRMQYAPNTQVEILPQ
HHCCCCCCCEEECCC		32.6929507054
337PhosphorylationILPQGHESPIFKQFF
ECCCCCCCHHHHHHH		20.0225159151
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 CAPG_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAPG_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 CAPG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIAH1_HUMANSIAH1physical
25416956
ADK_HUMANADKphysical
26344197
COF1_HUMANCFL1physical
26344197
CRIP1_HUMANCRIP1physical
26344197
DAZP1_HUMANDAZAP1physical
26344197
ETFB_HUMANETFBphysical
26344197
FUBP1_HUMANFUBP1physical
26344197
MIF_HUMANMIFphysical
26344197
PIR_HUMANPIRphysical
26344197
PRDX6_HUMANPRDX6physical
26344197
SNX3_HUMANSNX3physical
26344197
TKT_HUMANTKTphysical
26344197
UFC1_HUMANUFC1physical
26344197
UFM1_HUMANUFM1physical
26344197
KHDR2_HUMANKHDRBS2physical
28514442
HSP7C_HUMANHSPA8physical
28514442
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 CAPG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND MASSSPECTROMETRY.

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