CNOT3_HUMAN - dbPTM
CNOT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNOT3_HUMAN
UniProt AC O75175
Protein Name CCR4-NOT transcription complex subunit 3
Gene Name CNOT3
Organism Homo sapiens (Human).
Sequence Length 753
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, P-body. NANOS2 promotes its localization to P-body..
Protein Description 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 metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of emryonic stem (ES) cell identity..
Protein Sequence MADKRKLQGEIDRCLKKVSEGVEQFEDIWQKLHNAANANQKEKYEADLKKEIKKLQRLRDQIKTWVASNEIKDKRQLIDNRKLIETQMERFKVVERETKTKAYSKEGLGLAQKVDPAQKEKEEVGQWLTNTIDTLNMQVDQFESEVESLSVQTRKKKGDKDKQDRIEGLKRHIEKHRYHVRMLETILRMLDNDSILVDAIRKIKDDVEYYVDSSQDPDFEENEFLYDDLDLEDIPQALVATSPPSHSHMEDEIFNQSSSTPTSTTSSSPIPPSPANCTTENSEDDKKRGRSTDSEVSQSPAKNGSKPVHSNQHPQSPAVPPTYPSGPPPAASALSTTPGNNGVPAPAAPPSALGPKASPAPSHNSGTPAPYAQAVAPPAPSGPSTTQPRPPSVQPSGGGGGGSGGGGSSSSSNSSAGGGAGKQNGATSYSSVVADSPAEVALSSSGGNNASSQALGPPSGPHNPPPSTSKEPSAAAPTGAGGVAPGSGNNSGGPSLLVPLPVNPPSSPTPSFSDAKAAGALLNGPPQFSTAPEIKAPEPLSSLKSMAERAAISSGIEDPVPTLHLTERDIILSSTSAPPASAQPPLQLSEVNIPLSLGVCPLGPVPLTKEQLYQQAMEEAAWHHMPHPSDSERIRQYLPRNPCPTPPYHHQMPPPHSDTVEFYQRLSTETLFFIFYYLEGTKAQYLAAKALKKQSWRFHTKYMMWFQRHEEPKTITDEFEQGTYIYFDYEKWGQRKKEGFTFEYRYLEDRDLQ
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
41UbiquitinationNAANANQKEKYEADL
HHHHHHHHHHHHHHH		56.85-
82UbiquitinationRQLIDNRKLIETQME
HHHHHHHHHHHHHHH		61.13-
98PhosphorylationFKVVERETKTKAYSK
HCEEECHHCCCCCCC		50.6822210691
100PhosphorylationVVERETKTKAYSKEG
EEECHHCCCCCCCCC		28.4620068231
103PhosphorylationRETKTKAYSKEGLGL
CHHCCCCCCCCCCCH		23.1020068231
104PhosphorylationETKTKAYSKEGLGLA
HHCCCCCCCCCCCHH		29.1420068231
105UbiquitinationTKTKAYSKEGLGLAQ
HCCCCCCCCCCCHHH		43.03-
113AcetylationEGLGLAQKVDPAQKE
CCCCHHHCCCHHHHH		42.8923236377
131PhosphorylationVGQWLTNTIDTLNMQ
HHHHHHHHHHHHHHC		18.2622468782
144PhosphorylationMQVDQFESEVESLSV
HCHHHHHHHHHHCCH		48.5122468782
194PhosphorylationLRMLDNDSILVDAIR
HHHHCCCCHHHHHHH		24.8720230923
241PhosphorylationIPQALVATSPPSHSH
CCHHHHHCCCCCCCC		34.0026074081
242PhosphorylationPQALVATSPPSHSHM
CHHHHHCCCCCCCCC		25.6926074081
245PhosphorylationLVATSPPSHSHMEDE
HHHCCCCCCCCCCCC		40.7926074081
247PhosphorylationATSPPSHSHMEDEIF
HCCCCCCCCCCCCCC		28.9426074081
291PhosphorylationDDKKRGRSTDSEVSQ
HHHHCCCCCCHHHHC		39.1129255136
292PhosphorylationDKKRGRSTDSEVSQS
HHHCCCCCCHHHHCC		42.0329255136
294PhosphorylationKRGRSTDSEVSQSPA
HCCCCCCHHHHCCCC		39.7329255136
297PhosphorylationRSTDSEVSQSPAKNG
CCCCHHHHCCCCCCC		22.3829255136
299PhosphorylationTDSEVSQSPAKNGSK
CCHHHHCCCCCCCCC		21.2229255136
335PhosphorylationPPAASALSTTPGNNG
CCCHHHCCCCCCCCC		29.9226074081
336PhosphorylationPAASALSTTPGNNGV
CCHHHCCCCCCCCCC		37.5526074081
337PhosphorylationAASALSTTPGNNGVP
CHHHCCCCCCCCCCC		26.3126074081
351PhosphorylationPAPAAPPSALGPKAS
CCCCCCHHHCCCCCC		34.7626074081
358PhosphorylationSALGPKASPAPSHNS
HHCCCCCCCCCCCCC		27.9326074081
362PhosphorylationPKASPAPSHNSGTPA
CCCCCCCCCCCCCCC		37.0926074081
365PhosphorylationSPAPSHNSGTPAPYA
CCCCCCCCCCCCCCC		38.3226074081
367PhosphorylationAPSHNSGTPAPYAQA
CCCCCCCCCCCCCCC		18.9926074081
371PhosphorylationNSGTPAPYAQAVAPP
CCCCCCCCCCCCCCC		17.2926074081
403PhosphorylationSGGGGGGSGGGGSSS
CCCCCCCCCCCCCCC		37.2222817900
467PhosphorylationGPHNPPPSTSKEPSA
CCCCCCCCCCCCCCC		51.60-
468PhosphorylationPHNPPPSTSKEPSAA
CCCCCCCCCCCCCCC		49.98-
469PhosphorylationHNPPPSTSKEPSAAA
CCCCCCCCCCCCCCC		39.08-
473PhosphorylationPSTSKEPSAAAPTGA
CCCCCCCCCCCCCCC		31.4727080861
478PhosphorylationEPSAAAPTGAGGVAP
CCCCCCCCCCCCCCC		34.6320873877
487PhosphorylationAGGVAPGSGNNSGGP
CCCCCCCCCCCCCCC		36.9727080861
491PhosphorylationAPGSGNNSGGPSLLV
CCCCCCCCCCCCEEE		49.4827080861
495PhosphorylationGNNSGGPSLLVPLPV
CCCCCCCCEEEECCC		37.3020873877
506PhosphorylationPLPVNPPSSPTPSFS
ECCCCCCCCCCCCHH		50.6530278072
507PhosphorylationLPVNPPSSPTPSFSD
CCCCCCCCCCCCHHH		38.2730278072
509PhosphorylationVNPPSSPTPSFSDAK
CCCCCCCCCCHHHHH		33.2530206219
511PhosphorylationPPSSPTPSFSDAKAA
CCCCCCCCHHHHHHH		39.6030206219
513PhosphorylationSSPTPSFSDAKAAGA
CCCCCCHHHHHHHHH		40.7830278072
529PhosphorylationLNGPPQFSTAPEIKA
HCCCCCCCCCCCCCC		20.5720068231
530PhosphorylationNGPPQFSTAPEIKAP
CCCCCCCCCCCCCCC		47.7420068231
541PhosphorylationIKAPEPLSSLKSMAE
CCCCCCHHHHHHHHH		44.3226657352
542PhosphorylationKAPEPLSSLKSMAER
CCCCCHHHHHHHHHH		47.7225159151
554PhosphorylationAERAAISSGIEDPVP
HHHHHHHCCCCCCCC		37.3628555341
635MethylationPSDSERIRQYLPRNP
CCHHHHHHHHCCCCC		25.8854557691
645PhosphorylationLPRNPCPTPPYHHQM
CCCCCCCCCCCCCCC		43.54-
685PhosphorylationLEGTKAQYLAAKALK
HHCHHHHHHHHHHHH		11.81-
689UbiquitinationKAQYLAAKALKKQSW
HHHHHHHHHHHHCCH		48.95-
714PhosphorylationQRHEEPKTITDEFEQ
HCCCCCCCCCHHHHC		39.5626846344
716PhosphorylationHEEPKTITDEFEQGT
CCCCCCCCHHHHCCE		34.4126846344
723PhosphorylationTDEFEQGTYIYFDYE
CHHHHCCEEEEECHH		13.3626846344
724PhosphorylationDEFEQGTYIYFDYEK
HHHHCCEEEEECHHH		10.6426846344
726PhosphorylationFEQGTYIYFDYEKWG
HHCCEEEEECHHHHC		4.6826846344
729PhosphorylationGTYIYFDYEKWGQRK
CEEEEECHHHHCCCC		14.9826846344
737UbiquitinationEKWGQRKKEGFTFEY
HHHCCCCCCCCEEEE		66.3221890473
737 (in isoform 1)Ubiquitination-66.3221890473
741PhosphorylationQRKKEGFTFEYRYLE
CCCCCCCEEEEEEEC		26.8128509920
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 CNOT3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNOT3_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 CNOT3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAND2_HUMANCAND2physical
12207886
CNOT8_HUMANCNOT8physical
10637334
CNOT9_HUMANRQCD1physical
22939629
HNRLL_HUMANHNRNPLLphysical
22939629
ID3_HUMANID3physical
18255255
CNOT1_HUMANCNOT1physical
26344197
CNOT2_HUMANCNOT2physical
26344197
CNOT7_HUMANCNOT7physical
26344197
CNOT9_HUMANRQCD1physical
26344197
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 CNOT3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, 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-299, 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 THR-292, AND MASSSPECTROMETRY.

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