CCNL1_HUMAN - dbPTM
CCNL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCNL1_HUMAN
UniProt AC Q9UK58
Protein Name Cyclin-L1
Gene Name CCNL1
Organism Homo sapiens (Human).
Sequence Length 526
Subcellular Localization Nucleus speckle . Nucleus, nucleoplasm . Found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing..
Protein Description Involved in pre-mRNA splicing. Functions in association with cyclin-dependent kinases (CDKs). [PubMed: 18216018 Inhibited by the CDK-specific inhibitor CDKN1A/p21]
Protein Sequence MASGPHSTATAAAAASSAAPSAGGSSSGTTTTTTTTTGGILIGDRLYSEVSLTIDHSLIPEERLSPTPSMQDGLDLPSETDLRILGCELIQAAGILLRLPQVAMATGQVLFHRFFYSKSFVKHSFEIVAMACINLASKIEEAPRRIRDVINVFHHLRQLRGKRTPSPLILDQNYINTKNQVIKAERRVLKELGFCVHVKHPHKIIVMYLQVLECERNQTLVQTAWNYMNDSLRTNVFVRFQPETIACACIYLAARALQIPLPTRPHWFLLFGTTEEEIQEICIETLRLYTRKKPNYELLEKEVEKRKVALQEAKLKAKGLNPDGTPALSTLGGFSPASKPSSPREVKAEEKSPISINVKTVKKEPEDRQQASKSPYNGVRKDSKRSRNSRSASRSRSRTRSRSRSHTPRRHYNNRRSRSGTYSSRSRSRSRSHSESPRRHHNHGSPHLKAKHTRDDLKSSNRHGHKRKKSRSRSQSKSRDHSDAAKKHRHERGHHRDRRERSRSFERSHKSKHHGGSRSGHGRHRR
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
30PhosphorylationGGSSSGTTTTTTTTT
CCCCCCCEEEEEEEC		26.18-
32PhosphorylationSSSGTTTTTTTTTGG
CCCCCEEEEEEECCC		21.76-
33PhosphorylationSSGTTTTTTTTTGGI
CCCCEEEEEEECCCE		21.76-
37PhosphorylationTTTTTTTTGGILIGD
EEEEEEECCCEEECC		31.17-
47PhosphorylationILIGDRLYSEVSLTI
EEECCCCEEEEEEEE		12.0428122231
48PhosphorylationLIGDRLYSEVSLTID
EECCCCEEEEEEEEC		35.7928122231
51PhosphorylationDRLYSEVSLTIDHSL
CCCEEEEEEEECCCC		18.7528122231
53PhosphorylationLYSEVSLTIDHSLIP
CEEEEEEEECCCCCC		19.4928122231
57PhosphorylationVSLTIDHSLIPEERL
EEEEECCCCCCHHHC		25.0128122231
65PhosphorylationLIPEERLSPTPSMQD
CCCHHHCCCCCCCCC		32.7129255136
67PhosphorylationPEERLSPTPSMQDGL
CHHHCCCCCCCCCCC		25.3129255136
69PhosphorylationERLSPTPSMQDGLDL
HHCCCCCCCCCCCCC		31.3929255136
164PhosphorylationRQLRGKRTPSPLILD
HHHCCCCCCCCEEEC		31.4428450419
166PhosphorylationLRGKRTPSPLILDQN
HCCCCCCCCEEECCC		31.5528464451
178UbiquitinationDQNYINTKNQVIKAE
CCCCCCCHHHHHHHH		40.6829967540
183AcetylationNTKNQVIKAERRVLK
CCHHHHHHHHHHHHH		45.3925953088
289PhosphorylationCIETLRLYTRKKPNY
HHHHHHHHCCCCCCH		9.69-
314AcetylationKVALQEAKLKAKGLN
HHHHHHHHHHHCCCC		50.1725953088
325PhosphorylationKGLNPDGTPALSTLG
CCCCCCCCCCHHHCC		16.8729255136
329PhosphorylationPDGTPALSTLGGFSP
CCCCCCHHHCCCCCC		24.5629255136
330PhosphorylationDGTPALSTLGGFSPA
CCCCCHHHCCCCCCC		30.2129255136
335PhosphorylationLSTLGGFSPASKPSS
HHHCCCCCCCCCCCC		23.8829255136
338PhosphorylationLGGFSPASKPSSPRE
CCCCCCCCCCCCCCC		48.7829255136
339SumoylationGGFSPASKPSSPREV
CCCCCCCCCCCCCCC		51.5328112733
341PhosphorylationFSPASKPSSPREVKA
CCCCCCCCCCCCCCC		57.6322167270
342PhosphorylationSPASKPSSPREVKAE
CCCCCCCCCCCCCCC		36.1822167270
347SumoylationPSSPREVKAEEKSPI
CCCCCCCCCCCCCCC		45.3828112733
352PhosphorylationEVKAEEKSPISINVK
CCCCCCCCCCEEEEE		30.6429255136
355PhosphorylationAEEKSPISINVKTVK
CCCCCCCEEEEEEEC		16.1122167270
359AcetylationSPISINVKTVKKEPE
CCCEEEEEEECCCHH		43.0125953088
362SumoylationSINVKTVKKEPEDRQ
EEEEEEECCCHHHHH		57.5625755297
372PhosphorylationPEDRQQASKSPYNGV
HHHHHHHCCCCCCCC		29.3623401153
374PhosphorylationDRQQASKSPYNGVRK
HHHHHCCCCCCCCCC		30.0723401153
376PhosphorylationQQASKSPYNGVRKDS
HHHCCCCCCCCCCCC		31.4730266825
401PhosphorylationRSRSRTRSRSRSHTP
HHHHHHHHHCCCCCC		33.7119651622
403PhosphorylationRSRTRSRSRSHTPRR
HHHHHHHCCCCCCCC		39.1119651622
405PhosphorylationRTRSRSRSHTPRRHY
HHHHHCCCCCCCCCC		32.7219651622
407PhosphorylationRSRSRSHTPRRHYNN
HHHCCCCCCCCCCCC		21.5325599653
417PhosphorylationRHYNNRRSRSGTYSS
CCCCCCCCCCCCCCC		27.79-
419PhosphorylationYNNRRSRSGTYSSRS
CCCCCCCCCCCCCCC		36.41-
421PhosphorylationNRRSRSGTYSSRSRS
CCCCCCCCCCCCCCC		22.83-
422PhosphorylationRRSRSGTYSSRSRSR
CCCCCCCCCCCCCCC		14.2621406692
423PhosphorylationRSRSGTYSSRSRSRS
CCCCCCCCCCCCCCC		21.0721406692
424PhosphorylationSRSGTYSSRSRSRSR
CCCCCCCCCCCCCCC		24.7021406692
426PhosphorylationSGTYSSRSRSRSRSH
CCCCCCCCCCCCCCC		36.2321406692
430PhosphorylationSSRSRSRSRSHSESP
CCCCCCCCCCCCCCC		39.1124719451
432PhosphorylationRSRSRSRSHSESPRR
CCCCCCCCCCCCCCC		32.3930177828
434PhosphorylationRSRSRSHSESPRRHH
CCCCCCCCCCCCCCC		40.8030177828
436PhosphorylationRSRSHSESPRRHHNH
CCCCCCCCCCCCCCC		27.0724719451
445PhosphorylationRRHHNHGSPHLKAKH
CCCCCCCCCCHHCCC		11.1227362937
449AcetylationNHGSPHLKAKHTRDD
CCCCCCHHCCCCHHH		52.977427899
451AcetylationGSPHLKAKHTRDDLK
CCCCHHCCCCHHHHH		43.877427909
470PhosphorylationHGHKRKKSRSRSQSK
HHCCHHHHHCHHHHH		38.22-
471MethylationGHKRKKSRSRSQSKS
HCCHHHHHCHHHHHC		44.99-
473MethylationKRKKSRSRSQSKSRD
CHHHHHCHHHHHCCC		37.29-
486UbiquitinationRDHSDAAKKHRHERG
CCCHHHHHHHHHHHH		51.32-
487UbiquitinationDHSDAAKKHRHERGH
CCHHHHHHHHHHHHC		40.94-
502PhosphorylationHRDRRERSRSFERSH
HHHHHHHHHHHHHHH		27.7628355574
504PhosphorylationDRRERSRSFERSHKS
HHHHHHHHHHHHHCC		32.4828355574
512MethylationFERSHKSKHHGGSRS
HHHHHCCCCCCCCCC		44.41-
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 CCNL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCNL1_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 CCNL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD11A_HUMANCDK11Aphysical
11980906
CD11A_HUMANCDK11Aphysical
11683997
A4_HUMANAPPphysical
21832049
JMJD6_HUMANJMJD6physical
23455924
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 CCNL1_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-335; SER-338; SER-352AND SER-355, AND MASS SPECTROMETRY.
"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-325; SER-329; SER-335;SER-338; SER-341 AND SER-342, 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-325; SER-335; SER-338;SER-342; SER-352 AND SER-355, AND MASS SPECTROMETRY.
"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-65, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, 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 SER-65 AND SER-355, AND MASSSPECTROMETRY.

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