COR1A_HUMAN - dbPTM
COR1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COR1A_HUMAN
UniProt AC P31146
Protein Name Coronin-1A
Gene Name CORO1A
Organism Homo sapiens (Human).
Sequence Length 461
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cytoplasmic vesicle, phagosome membrane. In non-infected macrophages, associated with the cortical microtubule network. In mycobacteria-infected macrophages, becomes progressively relocalized and retai
Protein Description May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes..
Protein Sequence MSRQVVRSSKFRHVFGQPAKADQCYEDVRVSQTTWDSGFCAVNPKFVALICEASGGGAFLVLPLGKTGRVDKNAPTVCGHTAPVLDIAWCPHNDNVIASGSEDCTVMVWEIPDGGLMLPLREPVVTLEGHTKRVGIVAWHTTAQNVLLSAGCDNVIMVWDVGTGAAMLTLGPEVHPDTIYSVDWSRDGGLICTSCRDKRVRIIEPRKGTVVAEKDRPHEGTRPVRAVFVSEGKILTTGFSRMSERQVALWDTKHLEEPLSLQELDTSSGVLLPFFDPDTNIVYLCGKGDSSIRYFEITSEAPFLHYLSMFSSKESQRGMGYMPKRGLEVNKCEIARFYKLHERRCEPIAMTVPRKSDLFQEDLYPPTAGPDPALTAEEWLGGRDAGPLLISLKDGYVPPKSRELRVNRGLDTGRRRAAPEASGTPSSDAVSRLEEEMRKLQATVQELQKRLDRLEETVQAK
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------MSRQVVRSS
------CCCHHHHHH		31.2723100250
2Acetylation------MSRQVVRSS
------CCCHHHHHH		31.2723100250
8PhosphorylationMSRQVVRSSKFRHVF
CCCHHHHHHHHHHHH		26.6924719451
9PhosphorylationSRQVVRSSKFRHVFG
CCHHHHHHHHHHHHC		25.8321406692
20AcetylationHVFGQPAKADQCYED
HHHCCCCCCCHHCCC		60.2123749302
20UbiquitinationHVFGQPAKADQCYED
HHHCCCCCCCHHCCC		60.2121890473
25PhosphorylationPAKADQCYEDVRVSQ
CCCCCHHCCCCCCCC		14.9927155012
33PhosphorylationEDVRVSQTTWDSGFC
CCCCCCCCCCCCCEE		23.50-
34PhosphorylationDVRVSQTTWDSGFCA
CCCCCCCCCCCCEEE		21.45-
54PhosphorylationVALICEASGGGAFLV
EEEEEECCCCCEEEE		18.7130301811
66UbiquitinationFLVLPLGKTGRVDKN
EEEEECCCCCCCCCC		56.33-
132AcetylationVTLEGHTKRVGIVAW
EEEECCCCEEEEEEE		39.1425953088
178PhosphorylationGPEVHPDTIYSVDWS
CCCCCCCCEEEEEEC		26.68-
180PhosphorylationEVHPDTIYSVDWSRD
CCCCCCEEEEEECCC		12.53-
181PhosphorylationVHPDTIYSVDWSRDG
CCCCCEEEEEECCCC		15.11-
193PhosphorylationRDGGLICTSCRDKRV
CCCCEEEECCCCCCE		24.7028450419
194PhosphorylationDGGLICTSCRDKRVR
CCCEEEECCCCCCEE		11.6228450419
207UbiquitinationVRIIEPRKGTVVAEK
EEEECCCCCEEEEEC		70.42-
214UbiquitinationKGTVVAEKDRPHEGT
CCEEEEECCCCCCCC		49.66-
230PhosphorylationPVRAVFVSEGKILTT
CEEEEEEECCCEEEE		29.2128348404
233AcetylationAVFVSEGKILTTGFS
EEEEECCCEEEECCC		30.4123749302
233UbiquitinationAVFVSEGKILTTGFS
EEEEECCCEEEECCC		30.4121890473
236PhosphorylationVSEGKILTTGFSRMS
EECCCEEEECCCCCC		28.4821406692
237PhosphorylationSEGKILTTGFSRMSE
ECCCEEEECCCCCCC		32.5521406692
240PhosphorylationKILTTGFSRMSERQV
CEEEECCCCCCCCCE		28.5521406692
253UbiquitinationQVALWDTKHLEEPLS
CEEEECCCCCCCCCC		43.66-
268PhosphorylationLQELDTSSGVLLPFF
HHEECCCCCCEEEEE		34.7128464451
290O-linked_GlycosylationYLCGKGDSSIRYFEI
EEECCCCCEEEEEEE		36.0129351928
291O-linked_GlycosylationLCGKGDSSIRYFEIT
EECCCCCEEEEEEEC		18.8029351928
294PhosphorylationKGDSSIRYFEITSEA
CCCCEEEEEEECCCC		12.1430576142
299PhosphorylationIRYFEITSEAPFLHY
EEEEEECCCCCHHHH		37.11-
306PhosphorylationSEAPFLHYLSMFSSK
CCCCHHHHHHHHCCC		11.5630576142
311PhosphorylationLHYLSMFSSKESQRG
HHHHHHHCCCCHHCC		31.6830576142
313UbiquitinationYLSMFSSKESQRGMG
HHHHHCCCCHHCCCC		61.2521890473
313AcetylationYLSMFSSKESQRGMG
HHHHHCCCCHHCCCC		61.25156829
324UbiquitinationRGMGYMPKRGLEVNK
CCCCCCCCCCCCCCH		42.44-
331AcetylationKRGLEVNKCEIARFY
CCCCCCCHHHHHHHH		38.1223749302
331UbiquitinationKRGLEVNKCEIARFY
CCCCCCCHHHHHHHH		38.12-
339UbiquitinationCEIARFYKLHERRCE
HHHHHHHHHHHCCCE		40.4319608861
339AcetylationCEIARFYKLHERRCE
HHHHHHHHHHHCCCE		40.4319608861
350SulfoxidationRRCEPIAMTVPRKSD
CCCEECEEECCCHHH		3.9321406390
355UbiquitinationIAMTVPRKSDLFQED
CEEECCCHHHCCCCC		42.10-
356PhosphorylationAMTVPRKSDLFQEDL
EEECCCHHHCCCCCC		40.6022817900
364PhosphorylationDLFQEDLYPPTAGPD
HCCCCCCCCCCCCCC		21.3527642862
367PhosphorylationQEDLYPPTAGPDPAL
CCCCCCCCCCCCCCC		39.4828122231
391PhosphorylationDAGPLLISLKDGYVP
CCCCEEEEECCCCCC		29.3627067055
393UbiquitinationGPLLISLKDGYVPPK
CCEEEEECCCCCCCC		42.17-
396PhosphorylationLISLKDGYVPPKSRE
EEEECCCCCCCCCCC		21.6627642862
400UbiquitinationKDGYVPPKSRELRVN
CCCCCCCCCCCCCCC		56.95-
412PhosphorylationRVNRGLDTGRRRAAP
CCCCCCCCCCCCCCC		37.3226074081
422PhosphorylationRRAAPEASGTPSSDA
CCCCCCCCCCCCHHH		41.3528387310
424PhosphorylationAAPEASGTPSSDAVS
CCCCCCCCCCHHHHH		19.9423401153
424O-linked_GlycosylationAAPEASGTPSSDAVS
CCCCCCCCCCHHHHH		19.94OGP
426PhosphorylationPEASGTPSSDAVSRL
CCCCCCCCHHHHHHH		40.4629255136
427PhosphorylationEASGTPSSDAVSRLE
CCCCCCCHHHHHHHH		30.6929255136
431PhosphorylationTPSSDAVSRLEEEMR
CCCHHHHHHHHHHHH		32.6329255136
439AcetylationRLEEEMRKLQATVQE
HHHHHHHHHHHHHHH		43.5725953088
439UbiquitinationRLEEEMRKLQATVQE
HHHHHHHHHHHHHHH		43.57-
449AcetylationATVQELQKRLDRLEE
HHHHHHHHHHHHHHH		68.5019608861
449UbiquitinationATVQELQKRLDRLEE
HHHHHHHHHHHHHHH		68.5019608861
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
2SPhosphorylationKinasePKC-Uniprot
412TPhosphorylationKinasePKC-Uniprot
-KUbiquitinationE3 ubiquitin ligaseRNF128Q8TEB7
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
412TPhosphorylation

23100250
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 COR1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAT3_HUMANSTAT3physical
21988832
MGN_HUMANMAGOHphysical
21988832
TAB1_HUMANTAB1physical
21988832
RPAC1_HUMANPOLR1Cphysical
21988832
FHL3_HUMANFHL3physical
21988832
RBTN2_HUMANLMO2physical
21988832
SMAD3_HUMANSMAD3physical
21988832
SMRD1_HUMANSMARCD1physical
21988832
GIT2_HUMANGIT2physical
21988832
POTE1_HUMANPOT1physical
21988832
SPT20_HUMANSPATA20physical
21988832
YTDC1_HUMANYTHDC1physical
21988832
FSD2_HUMANFSD2physical
25416956
POC1B_HUMANPOC1Bphysical
26186194
CORO6_HUMANCORO6physical
26186194
COR1B_HUMANCORO1Bphysical
26186194
BICD2_HUMANBICD2physical
26186194
IF172_HUMANIFT172physical
26186194
SYVC_HUMANVARSphysical
26186194
RBG10_HUMANRABGAP1Lphysical
26186194
RBG1L_HUMANRABGAP1Lphysical
26186194
RBGP1_HUMANRABGAP1physical
26186194
IFT20_HUMANIFT20physical
26186194
TRAF7_HUMANTRAF7physical
26186194
TJAP1_HUMANTJAP1physical
26186194
IFT80_HUMANIFT80physical
26186194
TASOR_HUMANFAM208Aphysical
26186194
CEP44_HUMANCEP44physical
26186194
COR2A_HUMANCORO2Aphysical
26186194
ARP2_HUMANACTR2physical
26344197
ARP3_HUMANACTR3physical
26344197
POC1B_HUMANPOC1Bphysical
28514442
TJAP1_HUMANTJAP1physical
28514442
RBGP1_HUMANRABGAP1physical
28514442
IFT80_HUMANIFT80physical
28514442
RBG10_HUMANRABGAP1Lphysical
28514442
RBG1L_HUMANRABGAP1Lphysical
28514442
COR1C_HUMANCORO1Cphysical
28514442
COR1B_HUMANCORO1Bphysical
28514442
TRAF7_HUMANTRAF7physical
28514442
IFT20_HUMANIFT20physical
28514442
IF172_HUMANIFT172physical
28514442
CEP44_HUMANCEP44physical
28514442
BICD2_HUMANBICD2physical
28514442
SYVC_HUMANVARSphysical
28514442
TASOR_HUMANFAM208Aphysical
28514442
IFT57_HUMANIFT57physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615401Immunodeficiency 8 (IMD8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COR1A_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-449, AND MASS SPECTROMETRY.
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-356, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory