CCYL1_HUMAN - dbPTM
CCYL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCYL1_HUMAN
UniProt AC Q8N7R7
Protein Name Cyclin-Y-like protein 1
Gene Name CCNYL1
Organism Homo sapiens (Human).
Sequence Length 359
Subcellular Localization
Protein Description
Protein Sequence MGNTLTCCVSPNASPKLGRRAGSAELYCASDIYEAVSGDAVAVAPAVVEPAELDFGEGEGHHLQHISDREMPEDLALESNPSDHPRASTIFLSKSQTDVREKRKSNHLNHVSPGQLTKKYSSCSTIFLDDSTVSQPNLRTTVKCVTLAIYYHIKNRDANRSLDIFDERSHPLTREKVPEEYFKHDPEHKFIYRFVRTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPTNWKRIVLGAILLASKVWDDQAVWNVDYCQILKDITVEDMNEMERHFLELLQFNINVPASVYAKYYFDLRSLADDNNLNFLFAPLSKERAQNLEAISRLCEDKDLCRAAMRRSFSADNFIGIQRSKAILS
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
10PhosphorylationNTLTCCVSPNASPKL
CEEEEEECCCCCCCC		9.8729978859
14PhosphorylationCCVSPNASPKLGRRA
EEECCCCCCCCCCCC		29.2524275569
18PhosphorylationPNASPKLGRRAGSAE
CCCCCCCCCCCCCCE		24.1332142685
23PhosphorylationKLGRRAGSAELYCAS
CCCCCCCCCEEEECH		20.0028348404
24UbiquitinationLGRRAGSAELYCASD
CCCCCCCCEEEECHH		15.1921890473
33PhosphorylationLYCASDIYEAVSGDA
EEECHHHHHHHCCCC		11.65-
35PhosphorylationCASDIYEAVSGDAVA
ECHHHHHHHCCCCEE		5.4732142685
35 (in isoform 3)Phosphorylation-5.4724719451
42 (in isoform 3)Phosphorylation-8.0924719451
47 (in isoform 3)Phosphorylation-4.95-
48UbiquitinationVAVAPAVVEPAELDF
EEEECEEECCEECCC		8.7229967540
52PhosphorylationPAVVEPAELDFGEGE
CEEECCEECCCCCCC		60.6333259812
52 (in isoform 3)Phosphorylation-60.63-
54 (in isoform 3)Phosphorylation-40.8024719451
55PhosphorylationVEPAELDFGEGEGHH
ECCEECCCCCCCCCC		17.5232645325
67PhosphorylationGHHLQHISDREMPED
CCCCCCCCCCCCCHH		28.6124275569
79PhosphorylationPEDLALESNPSDHPR
CHHHHCCCCCCCCCC		55.6928122231
82PhosphorylationLALESNPSDHPRAST
HHCCCCCCCCCCCCE		53.4528122231
88PhosphorylationPSDHPRASTIFLSKS
CCCCCCCCEEEEECC		24.2630266825
89PhosphorylationSDHPRASTIFLSKSQ
CCCCCCCEEEEECCH		18.1130266825
93PhosphorylationRASTIFLSKSQTDVR
CCCEEEEECCHHHHH		21.3623401153
94 (in isoform 2)Ubiquitination-49.0521890473
94 (in isoform 1)Ubiquitination-49.0521890473
94UbiquitinationASTIFLSKSQTDVRE
CCEEEEECCHHHHHH		49.0521890473
95PhosphorylationSTIFLSKSQTDVREK
CEEEEECCHHHHHHH		34.6323401153
97PhosphorylationIFLSKSQTDVREKRK
EEEECCHHHHHHHHH		43.4826846344
105PhosphorylationDVREKRKSNHLNHVS
HHHHHHHHCCCCCCC		33.2530266825
106UbiquitinationVREKRKSNHLNHVSP
HHHHHHHCCCCCCCC		46.8529967540
112PhosphorylationSNHLNHVSPGQLTKK
HCCCCCCCCCHHCCC		18.7623401153
117PhosphorylationHVSPGQLTKKYSSCS
CCCCCHHCCCCCCCC		20.0123927012
118UbiquitinationVSPGQLTKKYSSCST
CCCCHHCCCCCCCCE		59.3029967540
120PhosphorylationPGQLTKKYSSCSTIF
CCHHCCCCCCCCEEE		13.8422167270
121PhosphorylationGQLTKKYSSCSTIFL
CHHCCCCCCCCEEEE		33.4723401153
122PhosphorylationQLTKKYSSCSTIFLD
HHCCCCCCCCEEEEC		14.7030266825
124PhosphorylationTKKYSSCSTIFLDDS
CCCCCCCCEEEECCC		26.8730266825
125PhosphorylationKKYSSCSTIFLDDST
CCCCCCCEEEECCCC		21.7830266825
131PhosphorylationSTIFLDDSTVSQPNL
CEEEECCCCCCCCCH		30.3023663014
132PhosphorylationTIFLDDSTVSQPNLR
EEEECCCCCCCCCHH		31.0423663014
150PhosphorylationKCVTLAIYYHIKNRD
HHHHHHHHHHHHCCC		5.3828152594
151PhosphorylationCVTLAIYYHIKNRDA
HHHHHHHHHHHCCCC		7.3128152594
176UbiquitinationSHPLTREKVPEEYFK
CCCCCHHCCCHHHHC		60.8529967540
192PhosphorylationDPEHKFIYRFVRTLF
CCCHHHHHHHHHHHH		10.9228152594
246 (in isoform 3)Ubiquitination-6.6721890473
246UbiquitinationAILLASKVWDDQAVW
HHHHHHCCCCCCCCC		6.6722505724
257PhosphorylationQAVWNVDYCQILKDI
CCCCCCCHHHHHCCC		5.0828796482
265 (in isoform 2)Ubiquitination-28.1621890473
265UbiquitinationCQILKDITVEDMNEM
HHHHCCCCHHHHHHH		28.1622505724
272PhosphorylationTVEDMNEMERHFLEL
CHHHHHHHHHHHHHH		4.6932142685
272 (in isoform 3)Phosphorylation-4.69-
274 (in isoform 3)Phosphorylation-25.2524719451
274PhosphorylationEDMNEMERHFLELLQ
HHHHHHHHHHHHHHH		25.2532142685
281UbiquitinationRHFLELLQFNINVPA
HHHHHHHHCCCCCCH		41.80-
291PhosphorylationINVPASVYAKYYFDL
CCCCHHHHHEEEEEH		8.5532142685
291 (in isoform 2)Phosphorylation-8.5527251275
293PhosphorylationVPASVYAKYYFDLRS
CCHHHHHEEEEEHHH		23.8532142685
293 (in isoform 2)Phosphorylation-23.8527251275
300PhosphorylationKYYFDLRSLADDNNL
EEEEEHHHHCCCCCC		34.9020873877
316 (in isoform 1)Ubiquitination-59.9221890473
316UbiquitinationFLFAPLSKERAQNLE
EEEECCCHHHHHHHH		59.922190698
332UbiquitinationISRLCEDKDLCRAAM
HHHHHCCHHHHHHHH		30.24-
332AcetylationISRLCEDKDLCRAAM
HHHHHCCHHHHHHHH		30.2427452117
342PhosphorylationCRAAMRRSFSADNFI
HHHHHHHHCCCCCCC		17.1222167270
344PhosphorylationAAMRRSFSADNFIGI
HHHHHHCCCCCCCEE		35.6419664994
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 CCYL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCYL1_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 CCYL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNY_HUMANCCNYphysical
28514442
S1A7A_HUMANS100A7Aphysical
28514442
INVO_HUMANIVLphysical
28514442
TREX2_HUMANTREX2physical
28514442
PEPL_HUMANPPLphysical
28514442
EVPL_HUMANEVPLphysical
28514442
FIBB_HUMANFGBphysical
28514442
SPB4_HUMANSERPINB4physical
28514442
SPB5_HUMANSERPINB5physical
28514442
TRI29_HUMANTRIM29physical
28514442
PAI2_HUMANSERPINB2physical
28514442
FIBG_HUMANFGGphysical
28514442
PKP3_HUMANPKP3physical
28514442
SPP2B_HUMANSPPL2Bphysical
28514442
SBSN_HUMANSBSNphysical
28514442
POF1B_HUMANPOF1Bphysical
28514442
CAPG_HUMANCAPGphysical
28514442
CALL5_HUMANCALML5physical
28514442
S10A8_HUMANS100A8physical
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 CCYL1_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-344, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.
"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 SER-344, AND MASSSPECTROMETRY.
"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 SER-344, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.

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