Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cyclin-L2  

UniProtKB / Swiss-Prot ID :  CCNL2_HUMAN

Gene Name (Synonyms) : 
CCNL2 SB138  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus speckle. 

Protein Function :  Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Also modulates the expression of critical apoptotic factor, leading to cell apoptosis. 

Protein Sequence MAAAAAAAGAAGSAAPAAAAGAPGSGGAPSGSQGVLIGDRLYSGVLITLENCLLPDDKLRFTPSMSSGLD...
Predicted Secondary Structure CCCCCCCCCCCCCHHHHCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAA
---CCCCCC
13.05UniProtKB
Link-
101PhosphothreonineVAMATGQVL
HHHHHHHHH
18.30HPRD
Link-
101PhosphothreonineVAMATGQVL
HHHHHHHHH
18.30Phosphositeplus
Link-
326PhosphothreonineVLDGTSGFS
CCCCCCCCC
25.91HPRD
Link-
326PhosphothreonineVLDGTSGFS
CCCCCCCCC
25.91Phosphositeplus
Link-
330PhosphoserineTSGFSPAPK
CCCCCCCCC
24.55HPRD
Link-
330PhosphoserineTSGFSPAPK
CCCCCCCCC
24.55HPRD
Link-
330PhosphoserineTSGFSPAPK
CCCCCCCCC
24.55Phosphositeplus
Link-
330PhosphoserineTSGFSPAPK
CCCCCCCCC
24.55SysPTM
Link-
330Phosphoserine (DYRK1A)TSGFSPAPK
CCCCCCCCC
24.55HPRD
Link-
330Phosphoserine.TSGFSPAPK
CCCCCCCCC
24.55UniProtKB
Link-
338PhosphoserineKLVESPKEG
CCCCCCCCC
33.52Phosphositeplus
Link-
338Phosphoserine (DYRK1A)KLVESPKEG
CCCCCCCCC
33.52HPRD
Link-
345PhosphoserineEGKGSKPSP
CCCCCCCCC
44.90HPRD
Link-
345PhosphoserineEGKGSKPSP
CCCCCCCCC
44.90PhosphoELM
Link-
345Phosphoserine.EGKGSKPSP
CCCCCCCCC
44.90UniProtKB
Link-
348PhosphoserineGSKPSPLSV
CCCCCCCCC
42.06Phosphositeplus
Link-
351PhosphoserinePSPLSVKNT
CCCCCCCCC
34.13HPRD
Link-
351PhosphoserinePSPLSVKNT
CCCCCCCCC
34.13PhosphoELM
Link-
351PhosphoserinePSPLSVKNT
CCCCCCCCC
34.13Phosphositeplus
Link-
351Phosphoserine.PSPLSVKNT
CCCCCCCCC
34.13UniProtKB
Link-
369PhosphoserineAKADSPVNG
CCCCCCCCC
35.29HPRD
Link-
369PhosphoserineAKADSPVNG
CCCCCCCCC
35.29PhosphoELM
Link-
369PhosphoserineAKADSPVNG
CCCCCCCCC
35.29Phosphositeplus
Link-
369PhosphoserineAKADSPVNG
CCCCCCCCC
35.29SysPTM
Link-
369Phosphoserine (DYRK1A)AKADSPVNG
CCCCCCCCC
35.29HPRD
Link-
369Phosphoserine.AKADSPVNG
CCCCCCCCC
35.29UniProtKB
Link-
406PhosphoserineKRRKSDSGS
HHHCCCCCC
34.89HPRD
Link-
408PhosphoserineRKSDSGSTS
HCCCCCCCC
41.56HPRD
Link-
410PhosphoserineSDSGSTSGG
CCCCCCCCC
24.29HPRD
Link-
411PhosphothreonineDSGSTSGGS
CCCCCCCCC
34.61HPRD
Link-
419PhosphoserineSKSQSRSRS
CCCCCCCCC
39.04HPRD
Link-
423PhosphoserineSRSRSRSDS
CCCCCCCCC
37.07Phosphositeplus
Link-
425PhosphoserineSRSRSDSPP
CCCCCCCCC
43.62Phosphositeplus
Link-
427PhosphoserineSRSDSPPRQ
CCCCCCCCC
37.74Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SFRS2_HUMANin vivoHPRD:10815HPRD14684736
CD2L1_HUMANin vivoHPRD:10815HPRD14623875
14684736
RPB1_HUMANin vivoHPRD:10815HPRD14684736
SFRS7_HUMANin vivoHPRD:10815HPRD14684736
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-330 AND SER-369, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-369, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-330 AND SER-369, AND MASS SPECTROMETRY.
"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-330 AND SER-369, ANDMASS SPECTROMETRY.
"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 SER-345; SER-351 ANDSER-369, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures