COR1C_HUMAN - dbPTM
COR1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COR1C_HUMAN
UniProt AC Q9ULV4
Protein Name Coronin-1C
Gene Name CORO1C
Organism Homo sapiens (Human).
Sequence Length 474
Subcellular Localization Cell membrane . Cell projection, lamellipodium . Cytoplasm, cytoskeleton . All isoforms localize in a diffuse and punctate pattern in the cytosol and are highly enriched in F-actin-rich areas. Isoform 3 colocalizes with the thin filaments of the sarc
Protein Description May be involved in cytokinesis, motility, and signal transduction.; Isoform 3: Involved in myogenic differentiation..
Protein Sequence MRRVVRQSKFRHVFGQAVKNDQCYDDIRVSRVTWDSSFCAVNPRFVAIIIEASGGGAFLVLPLHKTGRIDKSYPTVCGHTGPVLDIDWCPHNDQVIASGSEDCTVMVWQIPENGLTLSLTEPVVILEGHSKRVGIVAWHPTARNVLLSAGCDNAIIIWNVGTGEALINLDDMHSDMIYNVSWNRNGSLICTASKDKKVRVIDPRKQEIVAEKEKAHEGARPMRAIFLADGNVFTTGFSRMSERQLALWNPKNMQEPIALHEMDTSNGVLLPFYDPDTSIIYLCGKGDSSIRYFEITDESPYVHYLNTFSSKEPQRGMGYMPKRGLDVNKCEIARFFKLHERKCEPIIMTVPRKSDLFQDDLYPDTAGPEAALEAEEWFEGKNADPILISLKHGYIPGKNRDLKVVKKNILDSKPTANKKCDLISIPKKTTDTASVQNEAKLDEILKEIKSIKDTICNQDERISKLEQQMAKIAA
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
19MalonylationHVFGQAVKNDQCYDD
HHHCHHHCCCCCCCC		58.8026320211
19AcetylationHVFGQAVKNDQCYDD
HHHCHHHCCCCCCCC		58.8025953088
25UbiquitinationVKNDQCYDDIRVSRV
HCCCCCCCCEEEEEE		53.11-
28MethylationDQCYDDIRVSRVTWD
CCCCCCEEEEEEEEC		27.61-
187PhosphorylationVSWNRNGSLICTASK
EEECCCCCEEEEECC		20.3626657352
194MalonylationSLICTASKDKKVRVI
CEEEEECCCCCEEEE		71.7226320211
194AcetylationSLICTASKDKKVRVI
CEEEEECCCCCEEEE		71.7225953088
203UbiquitinationKKVRVIDPRKQEIVA
CCEEEECHHHHHHHH		33.95-
240PhosphorylationFTTGFSRMSERQLAL
ECCCCCCCCHHHHHH		4.7727251275
291MethylationGKGDSSIRYFEITDE
CCCCCEEEEEEECCC		31.84-
292PhosphorylationKGDSSIRYFEITDES
CCCCEEEEEEECCCC		12.1428331001
296PhosphorylationSIRYFEITDESPYVH
EEEEEEECCCCCCEE		26.9028152594
299PhosphorylationYFEITDESPYVHYLN
EEEECCCCCCEEEEE		25.0828152594
301PhosphorylationEITDESPYVHYLNTF
EECCCCCCEEEEEEC		14.7822115753
304PhosphorylationDESPYVHYLNTFSSK
CCCCCEEEEEECCCC		7.5128152594
307PhosphorylationPYVHYLNTFSSKEPQ
CCEEEEEECCCCCCC		23.4628152594
309PhosphorylationVHYLNTFSSKEPQRG
EEEEEECCCCCCCCC		38.1628152594
310PhosphorylationHYLNTFSSKEPQRGM
EEEEECCCCCCCCCC		36.5328152594
311UbiquitinationYLNTFSSKEPQRGMG
EEEECCCCCCCCCCC		72.6921906983
317UbiquitinationSKEPQRGMGYMPKRG
CCCCCCCCCCCCCCC		3.66-
317SulfoxidationSKEPQRGMGYMPKRG
CCCCCCCCCCCCCCC		3.6630846556
320SulfoxidationPQRGMGYMPKRGLDV
CCCCCCCCCCCCCCC		2.3330846556
322UbiquitinationRGMGYMPKRGLDVNK
CCCCCCCCCCCCCCH		42.44-
328UbiquitinationPKRGLDVNKCEIARF
CCCCCCCCHHHHHHH		42.82-
329AcetylationKRGLDVNKCEIARFF
CCCCCCCHHHHHHHH		32.8526051181
329UbiquitinationKRGLDVNKCEIARFF
CCCCCCCHHHHHHHH		32.85-
329MalonylationKRGLDVNKCEIARFF
CCCCCCCHHHHHHHH		32.8526320211
335UbiquitinationNKCEIARFFKLHERK
CHHHHHHHHHHCCCC		4.71-
337AcetylationCEIARFFKLHERKCE
HHHHHHHHHCCCCCE		46.3425825284
343GlutathionylationFKLHERKCEPIIMTV
HHHCCCCCEEEEEEC		10.6122555962
348SulfoxidationRKCEPIIMTVPRKSD
CCCEEEEEECCCHHH		2.9830846556
353UbiquitinationIIMTVPRKSDLFQDD
EEEECCCHHHCCCCC		42.10-
354PhosphorylationIMTVPRKSDLFQDDL
EEECCCHHHCCCCCC		40.6027251275
364UbiquitinationFQDDLYPDTAGPEAA
CCCCCCCCCCCHHHH		35.3121890473
389PhosphorylationNADPILISLKHGYIP
CCCCEEEEEECCCCC		28.1121712546
390AcetylationADPILISLKHGYIPG
CCCEEEEEECCCCCC		3.6319608861
391UbiquitinationDPILISLKHGYIPGK
CCEEEEEECCCCCCC		28.3521890473
391AcetylationDPILISLKHGYIPGK
CCEEEEEECCCCCCC		28.3525953088
394PhosphorylationLISLKHGYIPGKNRD
EEEEECCCCCCCCCC		12.0328152594
397UbiquitinationLKHGYIPGKNRDLKV
EECCCCCCCCCCCHH		30.25-
398UbiquitinationKHGYIPGKNRDLKVV
ECCCCCCCCCCCHHH		43.38-
398MalonylationKHGYIPGKNRDLKVV
ECCCCCCCCCCCHHH		43.3826320211
407UbiquitinationRDLKVVKKNILDSKP
CCCHHHHHHHCCCCC		37.30-
412PhosphorylationVKKNILDSKPTANKK
HHHHHCCCCCCCCCC		36.7720068231
413UbiquitinationKKNILDSKPTANKKC
HHHHCCCCCCCCCCC		46.16-
413AcetylationKKNILDSKPTANKKC
HHHHCCCCCCCCCCC		46.1623954790
413MalonylationKKNILDSKPTANKKC
HHHHCCCCCCCCCCC		46.1626320211
415PhosphorylationNILDSKPTANKKCDL
HHCCCCCCCCCCCCE		46.7420068231
418AcetylationDSKPTANKKCDLISI
CCCCCCCCCCCEEEC		52.9225953088
420GlutathionylationKPTANKKCDLISIPK
CCCCCCCCCEEECCC		5.7022555962
424PhosphorylationNKKCDLISIPKKTTD
CCCCCEEECCCCCCC		39.8928348404
430PhosphorylationISIPKKTTDTASVQN
EECCCCCCCCHHHHC		39.9925159151
434PhosphorylationKKTTDTASVQNEAKL
CCCCCCHHHHCHHHH		26.7425159151
440AcetylationASVQNEAKLDEILKE
HHHHCHHHHHHHHHH		50.7420167786
440MalonylationASVQNEAKLDEILKE
HHHHCHHHHHHHHHH		50.7426320211
444UbiquitinationNEAKLDEILKEIKSI
CHHHHHHHHHHHHHH		7.1321890473
444UbiquitinationNEAKLDEILKEIKSI
CHHHHHHHHHHHHHH		7.1321890473
446MalonylationAKLDEILKEIKSIKD
HHHHHHHHHHHHHHH		64.1526320211
446UbiquitinationAKLDEILKEIKSIKD
HHHHHHHHHHHHHHH		64.1519608861
446AcetylationAKLDEILKEIKSIKD
HHHHHHHHHHHHHHH		64.1519608861
447PhosphorylationKLDEILKEIKSIKDT
HHHHHHHHHHHHHHH		52.8027642862
449MalonylationDEILKEIKSIKDTIC
HHHHHHHHHHHHHHC		47.4126320211
452AcetylationLKEIKSIKDTICNQD
HHHHHHHHHHHCCHH		56.7826051181
452AcetylationLKEIKSIKDTICNQD
HHHHHHHHHHHCCHH		56.78-
452MalonylationLKEIKSIKDTICNQD
HHHHHHHHHHHCCHH		56.7826320211
456GlutathionylationKSIKDTICNQDERIS
HHHHHHHCCHHHHHH		3.9822555962
463PhosphorylationCNQDERISKLEQQMA
CCHHHHHHHHHHHHH		37.0922355754
464AcetylationNQDERISKLEQQMAK
CHHHHHHHHHHHHHH		54.3826051181
464UbiquitinationNQDERISKLEQQMAK
CHHHHHHHHHHHHHH		54.38-
471UbiquitinationKLEQQMAKIAA----
HHHHHHHHHHC----		27.7721890473
477UbiquitinationAKIAA----------
HHHHC----------		-
477PhosphorylationAKIAA----------
HHHHC----------		27251275
499Acetylation--------------------------------
--------------------------------		19608861
499Ubiquitination--------------------------------
--------------------------------		-
517Ubiquitination--------------------------------------------------
--------------------------------------------------		-
524Ubiquitination---------------------------------------------------------
---------------------------------------------------------		-
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
463SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COR1C_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 COR1C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT05_HUMANMRPS5physical
22939629
STT3B_HUMANSTT3Bphysical
22939629
GNAI2_HUMANGNAI2physical
22939629
RAB7A_HUMANRAB7Aphysical
22939629
CYB5B_HUMANCYB5Bphysical
22939629
MMGT1_HUMANMMGT1physical
22939629
RHOB_HUMANRHOBphysical
22939629
TPM4_HUMANTPM4physical
22939629
PREB_HUMANPREBphysical
22939629
RBTN2_HUMANLMO2physical
21988832
COR1B_HUMANCORO1Bphysical
22863883
ERF1_HUMANETF1physical
22863883
NIBL1_HUMANFAM129Bphysical
22863883
GARS_HUMANGARSphysical
22863883
H33_HUMANH3F3Aphysical
22863883
NUDC_HUMANNUDCphysical
22863883
PAPOA_HUMANPAPOLAphysical
22863883
SMOC1_HUMANSMOC1physical
22863883
SYTC_HUMANTARSphysical
22863883
ACTB_HUMANACTBphysical
26344197
ACTG_HUMANACTG1physical
26344197
ARP2_HUMANACTR2physical
26344197
ARP3_HUMANACTR3physical
26344197
AIMP1_HUMANAIMP1physical
26344197
VATF_HUMANATP6V1Fphysical
26344197
ERF1_HUMANETF1physical
26344197
RM01_HUMANMRPL1physical
26344197
MYCBP_HUMANMYCBPphysical
26344197
PDIA3_HUMANPDIA3physical
26344197
RFA1_HUMANRPA1physical
26344197
SKP1_HUMANSKP1physical
26344197
TIPRL_HUMANTIPRLphysical
26344197
RCC2_HUMANRCC2physical
25074804
RAC1_HUMANRAC1physical
25074804
COR1B_HUMANCORO1Bphysical
28514442
GTPB1_HUMANGTPBP1physical
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 COR1C_HUMAN

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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-337 AND LYS-446, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASSSPECTROMETRY.

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