CNO6L_HUMAN - dbPTM
CNO6L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNO6L_HUMAN
UniProt AC Q96LI5
Protein Name CCR4-NOT transcription complex subunit 6-like
Gene Name CNOT6L
Organism Homo sapiens (Human).
Sequence Length 555
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in the deadenylation-dependent degradation of mRNAs through the 3'-UTR AU-rich element-mediated mechanism. Involved in deadenylation-dependent degradation of CDKN1B mRNA. Its mRNA deadenylase activity can be inhibited by TOB1. Mediates cell proliferation and cell survival and prevents cellular senescence..
Protein Sequence MRLIGMPKEKYDPPDPRRIYTIMSAEEVANGKKSHWAELEISGRVRSLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRVLPYELGRLFQLQTLGLKGNPLSQDILNLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKERDQILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAKIMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAADKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSLLTQLELHPPLLPLVNGVHLPNRR
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
11PhosphorylationIGMPKEKYDPPDPRR
CCCCHHHCCCCCHHH		34.4718083107
24PhosphorylationRRIYTIMSAEEVANG
HHEEEEEEHHHHHCC		28.7824719451
90AcetylationYLDLSSNKLRSLPAE
EEECCCCCHHCCCHH		47.4225953088
90UbiquitinationYLDLSSNKLRSLPAE
EEECCCCCHHCCCHH		47.42-
133UbiquitinationQLQTLGLKGNPLSQD
HHHHCCCCCCCCCHH		55.64-
186PhosphorylationERDQILPSASFTVMC
HCCCCCCCCCEEEEH		32.8524043423
188PhosphorylationDQILPSASFTVMCYN
CCCCCCCCEEEEHHH		26.2824043423
190PhosphorylationILPSASFTVMCYNVL
CCCCCCEEEEHHHHH		12.5824043423
201PhosphorylationYNVLCDKYATRQLYG
HHHHHHHHHHHHHHC		10.4324043423
203PhosphorylationVLCDKYATRQLYGYC
HHHHHHHHHHHHCCC		18.8324043423
212PhosphorylationQLYGYCPSWALNWEY
HHHCCCHHHHHCHHH		22.78-
259PhosphorylationPALKERGYDGFFSPK
HHHHHCCCCCCCCHH		21.0818083107
264PhosphorylationRGYDGFFSPKSRAKI
CCCCCCCCHHHHHHH		29.2024719451
266UbiquitinationYDGFFSPKSRAKIMS
CCCCCCHHHHHHHCC		51.91-
270UbiquitinationFSPKSRAKIMSEQER
CCHHHHHHHCCHHHH		37.52-
273PhosphorylationKSRAKIMSEQERKHV
HHHHHHCCHHHHHCC		39.3329457462
278UbiquitinationIMSEQERKHVDGCAI
HCCHHHHHCCCCEEE		47.42-
289PhosphorylationGCAIFFKTEKFTLVQ
CEEEEEECCEEEEEE		38.97-
291UbiquitinationAIFFKTEKFTLVQKH
EEEEECCEEEEEEEE		49.21-
322PhosphorylationAMLNRVMTKDNIGVA
HHHHHHCCCCCCEEE		32.1822210691
344SumoylationELFGAGMKPIHAADK
HHHCCCCCCCCCCCC		39.64-
344SumoylationELFGAGMKPIHAADK
HHHCCCCCCCCCCCC		39.64-
380PhosphorylationIQTMMFVSEVKNILE
HHHHHHHHHHHHHHH		25.9625404012
388UbiquitinationEVKNILEKASSRPGS
HHHHHHHHHHCCCCC		50.56-
390PhosphorylationKNILEKASSRPGSPT
HHHHHHHHCCCCCCC		37.6427080861
391PhosphorylationNILEKASSRPGSPTA
HHHHHHHCCCCCCCC		47.5627080861
395PhosphorylationKASSRPGSPTADPNS
HHHCCCCCCCCCCCC		23.0427080861
397PhosphorylationSSRPGSPTADPNSIP
HCCCCCCCCCCCCCC		45.4424247654
402PhosphorylationSPTADPNSIPLVLCA
CCCCCCCCCCEEEEE		30.8527080861
452UbiquitinationMNFSCNGKNGSSEGR
EEEEECCCCCCCCCC		44.11-
468O-linked_GlycosylationTHGFQLKSAYENNLM
CCCEECCCHHHCCCC		44.6829351928
468PhosphorylationTHGFQLKSAYENNLM
CCCEECCCHHHCCCC		44.6829978859
470PhosphorylationGFQLKSAYENNLMPY
CEECCCHHHCCCCCC		26.7029978859
477PhosphorylationYENNLMPYTNYTFDF
HHCCCCCCCCEEECC		8.1429978859
478PhosphorylationENNLMPYTNYTFDFK
HCCCCCCCCEEECCC		18.8429978859
480PhosphorylationNLMPYTNYTFDFKGV
CCCCCCCEEECCCCC		10.8629978859
481PhosphorylationLMPYTNYTFDFKGVI
CCCCCCEEECCCCCC		20.8529978859
490PhosphorylationDFKGVIDYIFYSKTH
CCCCCCEEEEEECCC		5.04-
493PhosphorylationGVIDYIFYSKTHMNV
CCCEEEEEECCCCEE		10.33-
494PhosphorylationVIDYIFYSKTHMNVL
CCEEEEEECCCCEEC		21.96-
531PhosphorylationHIPSDHFSLLTQLEL
CCCCCHHHHHHHHCC		21.0324719451
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 CNO6L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNO6L_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 CNO6L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZSCA1_HUMANZSCAN1physical
20211142
CNOT1_HUMANCNOT1physical
17452450
CNOT2_HUMANCNOT2physical
17452450
CNOT3_HUMANCNOT3physical
17452450
CAF1A_HUMANCHAF1Aphysical
17452450
CNOT9_HUMANRQCD1physical
17452450
TB182_HUMANTNKS1BP1physical
17452450
CNO10_HUMANCNOT10physical
17452450
CAF1B_HUMANCHAF1Bphysical
17452450
TTP_HUMANZFP36physical
21078877
CNOT6_HUMANCNOT6physical
27173435
CNOT2_HUMANCNOT2physical
27173435
CNOT7_HUMANCNOT7physical
27173435
TB182_HUMANTNKS1BP1physical
27173435
CNO11_HUMANCNOT11physical
27173435
CNO10_HUMANCNOT10physical
27173435
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 CNO6L_HUMAN

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Related Literatures of Post-Translational Modification

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