COIL_HUMAN - dbPTM
COIL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COIL_HUMAN
UniProt AC P38432
Protein Name Coilin
Gene Name COIL
Organism Homo sapiens (Human).
Sequence Length 576
Subcellular Localization Nucleus . Nucleus, Cajal body .
Protein Description Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs..
Protein Sequence MAASETVRLRLQFDYPPPATPHCTAFWLLVDLNRCRVVTDLISLIRQRFGFSSGAFLGLYLEGGLLPPAESARLVRDNDCLRVKLEERGVAENSVVISNGDINLSLRKAKKRAFQLEEGEETEPDCKYSKKHWKSRENNNNNEKVLDLEPKAVTDQTVSKKNKRKNKATCGTVGDDNEEAKRKSPKKKEKCEYKKKAKNPKSPKVQAVKDWANQRCSSPKGSARNSLVKAKRKGSVSVCSKESPSSSSESESCDESISDGPSKVTLEARNSSEKLPTELSKEEPSTKNTTADKLAIKLGFSLTPSKGKTSGTTSSSSDSSAESDDQCLMSSSTPECAAGFLKTVGLFAGRGRPGPGLSSQTAGAAGWRRSGSNGGGQAPGASPSVSLPASLGRGWGREENLFSWKGAKGRGMRGRGRGRGHPVSCVVNRSTDNQRQQQLNDVVKNSSTIIQNPVETPKKDYSLLPLLAAAPQVGEKIAFKLLELTSSYSPDVSDYKEGRILSHNPETQQVDIEILSSLPALREPGKFDLVYHNENGAEVVEYAVTQESKITVFWKELIDPRLIIESPSNTSSTEPA
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
39PhosphorylationLNRCRVVTDLISLIR
HHCHHHHHHHHHHHH		23.41-
43PhosphorylationRVVTDLISLIRQRFG
HHHHHHHHHHHHHHC		25.66-
94PhosphorylationERGVAENSVVISNGD
HCCCCCCEEEEECCC		14.8530266825
98PhosphorylationAENSVVISNGDINLS
CCCEEEEECCCCCCH		24.1330266825
105PhosphorylationSNGDINLSLRKAKKR
ECCCCCCHHHHHHHH		22.9530266825
122PhosphorylationQLEEGEETEPDCKYS
ECCCCCCCCCCCHHC		48.8219664994
127SumoylationEETEPDCKYSKKHWK
CCCCCCCHHCHHHHH		61.0028112733
127UbiquitinationEETEPDCKYSKKHWK
CCCCCCCHHCHHHHH		61.0032015554
128PhosphorylationETEPDCKYSKKHWKS
CCCCCCHHCHHHHHC		31.8624732914
129PhosphorylationTEPDCKYSKKHWKSR
CCCCCHHCHHHHHCC		22.2624732914
151SumoylationKVLDLEPKAVTDQTV
CEECCCCHHHCCCCC		46.22-
151SumoylationKVLDLEPKAVTDQTV
CEECCCCHHHCCCCC		46.2228112733
151UbiquitinationKVLDLEPKAVTDQTV
CEECCCCHHHCCCCC		46.2229967540
160SumoylationVTDQTVSKKNKRKNK
HCCCCCCHHCCCCCC		56.9028112733
160UbiquitinationVTDQTVSKKNKRKNK
HCCCCCCHHCCCCCC		56.9029967540
169PhosphorylationNKRKNKATCGTVGDD
CCCCCCCCCCCCCCC		17.05-
172PhosphorylationKNKATCGTVGDDNEE
CCCCCCCCCCCCCHH		24.3824732914
184PhosphorylationNEEAKRKSPKKKEKC
CHHHHHHCHHHHHHH		46.0811102515
202PhosphorylationKKAKNPKSPKVQAVK
HHHCCCCCHHHHHHH		31.079013710
204AcetylationAKNPKSPKVQAVKDW
HCCCCCHHHHHHHHH		54.817428741
204SumoylationAKNPKSPKVQAVKDW
HCCCCCHHHHHHHHH		54.8128112733
209SumoylationSPKVQAVKDWANQRC
CHHHHHHHHHHHHCC		51.04-
209SumoylationSPKVQAVKDWANQRC
CHHHHHHHHHHHHCC		51.0428112733
209UbiquitinationSPKVQAVKDWANQRC
CHHHHHHHHHHHHCC		51.0432015554
217PhosphorylationDWANQRCSSPKGSAR
HHHHHCCCCCCCCHH		52.4425159151
218PhosphorylationWANQRCSSPKGSARN
HHHHCCCCCCCCHHH		33.9725849741
222PhosphorylationRCSSPKGSARNSLVK
CCCCCCCCHHHHHHH		30.1326074081
226PhosphorylationPKGSARNSLVKAKRK
CCCCHHHHHHHHHHC		29.0521406692
235PhosphorylationVKAKRKGSVSVCSKE
HHHHHCCCEEEEECC		17.7925849741
237PhosphorylationAKRKGSVSVCSKESP
HHHCCCEEEEECCCC		21.0727732954
240PhosphorylationKGSVSVCSKESPSSS
CCCEEEEECCCCCCC		36.9823312004
247PhosphorylationSKESPSSSSESESCD
ECCCCCCCCCCCCCC		42.32-
248PhosphorylationKESPSSSSESESCDE
CCCCCCCCCCCCCCC		47.2730576142
250PhosphorylationSPSSSSESESCDESI
CCCCCCCCCCCCCCC		36.44-
252PhosphorylationSSSSESESCDESISD
CCCCCCCCCCCCCCC		35.8330576142
256PhosphorylationESESCDESISDGPSK
CCCCCCCCCCCCCCC		17.72-
265PhosphorylationSDGPSKVTLEARNSS
CCCCCCEEEEECCCC		23.7123403867
271PhosphorylationVTLEARNSSEKLPTE
EEEEECCCCCCCCCC		34.0323927012
272PhosphorylationTLEARNSSEKLPTEL
EEEECCCCCCCCCCH		42.1523927012
274AcetylationEARNSSEKLPTELSK
EECCCCCCCCCCHHC		62.8126051181
274SumoylationEARNSSEKLPTELSK
EECCCCCCCCCCHHC		62.8128112733
274UbiquitinationEARNSSEKLPTELSK
EECCCCCCCCCCHHC		62.8129967540
277PhosphorylationNSSEKLPTELSKEEP
CCCCCCCCCHHCCCC		61.0523927012
280PhosphorylationEKLPTELSKEEPSTK
CCCCCCHHCCCCCCC		31.6123927012
281AcetylationKLPTELSKEEPSTKN
CCCCCHHCCCCCCCC		77.9126051181
281SumoylationKLPTELSKEEPSTKN
CCCCCHHCCCCCCCC		77.9128112733
281UbiquitinationKLPTELSKEEPSTKN
CCCCCHHCCCCCCCC		77.9129967540
285PhosphorylationELSKEEPSTKNTTAD
CHHCCCCCCCCCCHH		56.1224732914
286PhosphorylationLSKEEPSTKNTTADK
HHCCCCCCCCCCHHH		38.7424732914
289PhosphorylationEEPSTKNTTADKLAI
CCCCCCCCCHHHHHH		25.5624732914
290PhosphorylationEPSTKNTTADKLAIK
CCCCCCCCHHHHHHH		42.1026055452
293AcetylationTKNTTADKLAIKLGF
CCCCCHHHHHHHHCE		37.0425953088
293SumoylationTKNTTADKLAIKLGF
CCCCCHHHHHHHHCE		37.0428112733
293UbiquitinationTKNTTADKLAIKLGF
CCCCCHHHHHHHHCE		37.0429967540
297SumoylationTADKLAIKLGFSLTP
CHHHHHHHHCEEECC		36.6328112733
301PhosphorylationLAIKLGFSLTPSKGK
HHHHHCEEECCCCCC		29.5430266825
303PhosphorylationIKLGFSLTPSKGKTS
HHHCEEECCCCCCCC		25.0719664994
305PhosphorylationLGFSLTPSKGKTSGT
HCEEECCCCCCCCCC		49.1330266825
316PhosphorylationTSGTTSSSSDSSAES
CCCCCCCCCCCCCCC		37.6230576142
317PhosphorylationSGTTSSSSDSSAESD
CCCCCCCCCCCCCCC		43.3830576142
320PhosphorylationTSSSSDSSAESDDQC
CCCCCCCCCCCCCCE		40.8330576142
330PhosphorylationSDDQCLMSSSTPECA
CCCCEECCCCCHHHH		14.2730576142
333PhosphorylationQCLMSSSTPECAAGF
CEECCCCCHHHHHHH		25.6730576142
350DimethylationTVGLFAGRGRPGPGL
HHHHHCCCCCCCCCC		34.22-
350MethylationTVGLFAGRGRPGPGL
HHHHHCCCCCCCCCC		34.22-
352MethylationGLFAGRGRPGPGLSS
HHHCCCCCCCCCCCC		31.47-
358PhosphorylationGRPGPGLSSQTAGAA
CCCCCCCCCCCCCCC		26.7330576142
361PhosphorylationGPGLSSQTAGAAGWR
CCCCCCCCCCCCCCC		29.0730576142
370PhosphorylationGAAGWRRSGSNGGGQ
CCCCCCCCCCCCCCC		37.6923186163
372PhosphorylationAGWRRSGSNGGGQAP
CCCCCCCCCCCCCCC		33.2823186163
393DimethylationSLPASLGRGWGREEN
CCCCCCCCCCCCCCC		42.88-
393MethylationSLPASLGRGWGREEN
CCCCCCCCCCCCCCC		42.88-
397DimethylationSLGRGWGREENLFSW
CCCCCCCCCCCCCCC		41.36-
397MethylationSLGRGWGREENLFSW
CCCCCCCCCCCCCCC		41.36-
403PhosphorylationGREENLFSWKGAKGR
CCCCCCCCCCCCCCC		30.9221815630
405AcetylationEENLFSWKGAKGRGM
CCCCCCCCCCCCCCC		48.0323236377
405MethylationEENLFSWKGAKGRGM
CCCCCCCCCCCCCCC		48.03-
405UbiquitinationEENLFSWKGAKGRGM
CCCCCCCCCCCCCCC		48.0329967540
419MethylationMRGRGRGRGHPVSCV
CCCCCCCCCCCEEEE		38.60-
444SumoylationQQLNDVVKNSSTIIQ
HHHHHHHHHCCHHHC		51.4628112733
446PhosphorylationLNDVVKNSSTIIQNP
HHHHHHHCCHHHCCC		24.1224732914
447PhosphorylationNDVVKNSSTIIQNPV
HHHHHHCCHHHCCCC		32.7829255136
448PhosphorylationDVVKNSSTIIQNPVE
HHHHHCCHHHCCCCC		23.1728464451
456PhosphorylationIIQNPVETPKKDYSL
HHCCCCCCCCCCCCH		40.4130266825
459UbiquitinationNPVETPKKDYSLLPL
CCCCCCCCCCCHHHH		64.2029967540
461PhosphorylationVETPKKDYSLLPLLA
CCCCCCCCCHHHHHH		15.3124732914
462PhosphorylationETPKKDYSLLPLLAA
CCCCCCCCHHHHHHH		33.3028464451
476UbiquitinationAAPQVGEKIAFKLLE
HCCCCCHHHHHHHHH		33.15-
485PhosphorylationAFKLLELTSSYSPDV
HHHHHHHHHCCCCCH		13.2725159151
486PhosphorylationFKLLELTSSYSPDVS
HHHHHHHHCCCCCHH		39.6425159151
487PhosphorylationKLLELTSSYSPDVSD
HHHHHHHCCCCCHHH		25.1325159151
488PhosphorylationLLELTSSYSPDVSDY
HHHHHHCCCCCHHHC		24.8030278072
489PhosphorylationLELTSSYSPDVSDYK
HHHHHCCCCCHHHCC		19.3025159151
493PhosphorylationSSYSPDVSDYKEGRI
HCCCCCHHHCCCCCC		42.4722115753
495PhosphorylationYSPDVSDYKEGRILS
CCCCHHHCCCCCCCC		11.9324732914
496AcetylationSPDVSDYKEGRILSH
CCCHHHCCCCCCCCC		59.7026051181
496SumoylationSPDVSDYKEGRILSH
CCCHHHCCCCCCCCC		59.7028112733
496UbiquitinationSPDVSDYKEGRILSH
CCCHHHCCCCCCCCC		59.7021906983
502PhosphorylationYKEGRILSHNPETQQ
CCCCCCCCCCCCCCE		20.88-
517PhosphorylationVDIEILSSLPALREP
ECHHHHHCCHHHCCC		34.6224719451
555UbiquitinationSKITVFWKELIDPRL
CEEEEEEHHHCCCEE		31.0421906983
566PhosphorylationDPRLIIESPSNTSST
CCEEEEECCCCCCCC		24.1825159151
568PhosphorylationRLIIESPSNTSSTEP
EEEEECCCCCCCCCC		63.1230266825
570PhosphorylationIIESPSNTSSTEPA-
EEECCCCCCCCCCC-		28.5230278072
571PhosphorylationIESPSNTSSTEPA--
EECCCCCCCCCCC--		39.2425159151
572PhosphorylationESPSNTSSTEPA---
ECCCCCCCCCCC---		34.4525159151
573PhosphorylationSPSNTSSTEPA----
CCCCCCCCCCC----		45.8425159151
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
184SPhosphorylationKinaseCDK2P24941
PhosphoELM
184SPhosphorylationKinaseVRK1Q99986
Uniprot
184SPhosphorylationKinaseVRK1Q80X41
PSP
184SPhosphorylationKinaseVRK2Q86Y07
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COIL_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 COIL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATX1_HUMANATXN1physical
12757932
NOLC1_HUMANNOLC1physical
9679133
COIL_HUMANCOILphysical
11102515
SMN_HUMANSMN1physical
12361597
SMN_HUMANSMN1physical
11641277
RSMB_HUMANSNRPBphysical
11641277
ATX1_HUMANATXN1physical
18439907
XRCC5_HUMANXRCC5physical
21070772
XRCC6_HUMANXRCC6physical
21070772
BYST_HUMANBYSLphysical
16713569
CEP76_HUMANCEP76physical
16713569
CEP70_HUMANCEP70physical
16713569
COIL_HUMANCOILphysical
16713569
NB5R2_HUMANCYB5R2physical
16713569
DHX16_HUMANDHX16physical
16713569
DNJA3_HUMANDNAJA3physical
16713569
FHL5_HUMANFHL5physical
16713569
NTAQ1_HUMANWDYHV1physical
16713569
NUD18_HUMANNUDT18physical
16713569
FXR2_HUMANFXR2physical
16713569
GCC1_HUMANGCC1physical
16713569
TCAF1_HUMANFAM115Aphysical
16713569
KLH42_HUMANKLHL42physical
16713569
IMA4_HUMANKPNA3physical
16713569
LNX1_HUMANLNX1physical
16713569
MD1L1_HUMANMAD1L1physical
16713569
NIF3L_HUMANNIF3L1physical
16713569
PSA1_HUMANPSMA1physical
16713569
PSME3_HUMANPSME3physical
16713569
TAF9_HUMANTAF9physical
16713569
ELOA2_HUMANTCEB3Bphysical
16713569
ZBT25_HUMANZBTB25physical
16713569
ACTN1_HUMANACTN1physical
16713569
ACTN2_HUMANACTN2physical
16713569
ACTN4_HUMANACTN4physical
16713569
C1QBP_HUMANC1QBPphysical
16713569
CSK2B_HUMANCSNK2Bphysical
16713569
KALRN_HUMANKALRNphysical
16713569
KAZRN_HUMANKAZNphysical
16713569
KLHL8_HUMANKLHL8physical
16713569
CC159_HUMANCCDC159physical
16713569
MYO5B_HUMANMYO5Bphysical
16713569
CC136_HUMANCCDC136physical
16713569
TGS1_HUMANTGS1physical
16713569
PKHG4_HUMANPLEKHG4physical
16713569
PICK1_HUMANPICK1physical
16713569
SART3_HUMANSART3physical
16713569
SCYL1_HUMANSCYL1physical
16713569
SNX6_HUMANSNX6physical
16713569
TFCP2_HUMANTFCP2physical
16713569
TSYL2_HUMANTSPYL2physical
16713569
ZN277_HUMANZNF277physical
16713569
ANM1_HUMANPRMT1physical
16713569
ANM8_HUMANPRMT8physical
16713569
KLC2_HUMANKLC2physical
16713569
KLC4_HUMANKLC4physical
16713569
PPCEL_HUMANPREPLphysical
16713569
A4_HUMANAPPphysical
21832049
T2FA_HUMANGTF2F1physical
22939629
SMN_HUMANSMN1physical
22939629
CDC23_HUMANCDC23physical
25416956
PDLI5_HUMANPDLIM5physical
25416956
ZN277_HUMANZNF277physical
25416956
ARMX1_HUMANARMCX1physical
25416956
ZCH10_HUMANZCCHC10physical
25416956
WDR34_HUMANWDR34physical
25416956
VRK1_HUMANVRK1physical
26068304
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 COIL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Substrate profiling of human vaccinia-related kinases identifiescoilin, a Cajal body nuclear protein, as a phosphorylation target withneurological implications.";
Sanz-Garcia M., Vazquez-Cedeira M., Kellerman E., Renbaum P.,Levy-Lahad E., Lazo P.A.;
J. Proteomics 75:548-560(2011).
Cited for: PHOSPHORYLATION AT SER-184 BY VRK1 AND VRK2.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-271; THR-303;THR-456; SER-487; SER-489; SER-566 AND SER-568, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-271; THR-290;SER-301; THR-303 AND SER-489, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 AND SER-489, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, AND MASSSPECTROMETRY.

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