CNOT1_HUMAN - dbPTM
CNOT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNOT1_HUMAN
UniProt AC A5YKK6
Protein Name CCR4-NOT transcription complex subunit 1
Gene Name CNOT1
Organism Homo sapiens (Human).
Sequence Length 2376
Subcellular Localization Cytoplasm, P-body . Nucleus . NANOS2 promotes its localization to P-body..
Protein Description Scaffolding 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. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of emryonic stem (ES) cell identity..
Protein Sequence MNLDSLSLALSQISYLVDNLTKKNYRASQQEIQHIVNRHGPEADRHLLRCLFSHVDFSGDGKSSGKDFHQTQFLIQECALLITKPNFISTLSYAIDNPLHYQKSLKPAPHLFAQLSKVLKLSKVQEVIFGLALLNSSSSDLRGFAAQFIKQKLPDLLRSYIDADVSGNQEGGFQDIAIEVLHLLLSHLLFGQKGAFGVGQEQIDAFLKTLRRDFPQERCPVVLAPLLYPEKRDILMDRILPDSGGVAKTMMESSLADFMQEVGYGFCASIEECRNIIVQFGVREVTAAQVARVLGMMARTHSGLTDGIPLQSISAPGSGIWSDGKDKSDGAQAHTWNVEVLIDVLKELNPSLNFKEVTYELDHPGFQIRDSKGLHNVVYGIQRGLGMEVFPVDLIYRPWKHAEGQLSFIQHSLINPEIFCFADYPCHTVATDILKAPPEDDNREIATWKSLDLIESLLRLAEVGQYEQVKQLFSFPIKHCPDMLVLALLQINTSWHTLRHELISTLMPIFLGNHPNSAIILHYAWHGQGQSPSIRQLIMHAMAEWYMRGEQYDQAKLSRILDVAQDLKALSMLLNGTPFAFVIDLAALASRREYLKLDKWLTDKIREHGEPFIQACMTFLKRRCPSILGGLAPEKDQPKSAQLPPETLATMLACLQACAGSVSQELSETILTMVANCSNVMNKARQPPPGVMPKGRPPSASSLDAISPVQIDPLAGMTSLSIGGSAAPHTQSMQGFPPNLGSAFSTPQSPAKAFPPLSTPNQTTAFSGIGGLSSQLPVGGLGTGSLTGIGTGALGLPAVNNDPFVQRKLGTSGLNQPTFQQSKMKPSDLSQVWPEANQHFSKEIDDEANSYFQRIYNHPPHPTMSVDEVLEMLQRFKDSTIKREREVFNCMLRNLFEEYRFFPQYPDKELHITACLFGGIIEKGLVTYMALGLALRYVLEALRKPFGSKMYYFGIAALDRFKNRLKDYPQYCQHLASISHFMQFPHHLQEYIEYGQQSRDPPVKMQGSITTPGSIALAQAQAQAQVPAKAPLAGQVSTMVTTSTTTTVAKTVTVTRPTGVSFKKDVPPSINTTNIDTLLVATDQTERIVEPPENIQEKIAFIFNNLSQSNMTQKVEELKETVKEEFMPWVSQYLVMKRVSIEPNFHSLYSNFLDTLKNPEFNKMVLNETYRNIKVLLTSDKAAANFSDRSLLKNLGHWLGMITLAKNKPILHTDLDVKSLLLEAYVKGQQELLYVVPFVAKVLESSIRSVVFRPPNPWTMAIMNVLAELHQEHDLKLNLKFEIEVLCKNLALDINELKPGNLLKDKDRLKNLDEQLSAPKKDVKQPEELPPITTTTTSTTPATNTTCTATVPPQPQYSYHDINVYSLAGLAPHITLNPTIPLFQAHPQLKQCVRQAIERAVQELVHPVVDRSIKIAMTTCEQIVRKDFALDSEESRMRIAAHHMMRNLTAGMAMITCREPLLMSISTNLKNSFASALRTASPQQREMMDQAAAQLAQDNCELACCFIQKTAVEKAGPEMDKRLATEFELRKHARQEGRRYCDPVVLTYQAERMPEQIRLKVGGVDPKQLAVYEEFARNVPGFLPTNDLSQPTGFLAQPMKQAWATDDVAQIYDKCITELEQHLHAIPPTLAMNPQAQALRSLLEVVVLSRNSRDAIAALGLLQKAVEGLLDATSGADADLLLRYRECHLLVLKALQDGRAYGSPWCNKQITRCLIECRDEYKYNVEAVELLIRNHLVNMQQYDLHLAQSMENGLNYMAVAFAMQLVKILLVDERSVAHVTEADLFHTIETLMRINAHSRGNAPEGLPQLMEVVRSNYEAMIDRAHGGPNFMMHSGISQASEYDDPPGLREKAEYLLREWVNLYHSAAAGRDSTKAFSAFVGQMHQQGILKTDDLITRFFRLCTEMCVEISYRAQAEQQHNPAANPTMIRAKCYHNLDAFVRLIALLVKHSGEATNTVTKINLLNKVLGIVVGVLLQDHDVRQSEFQQLPYHRIFIMLLLELNAPEHVLETINFQTLTAFCNTFHILRPTKAPGFVYAWLELISHRIFIARMLAHTPQQKGWPMYAQLLIDLFKYLAPFLRNVELTKPMQILYKGTLRVLLVLLHDFPEFLCDYHYGFCDVIPPNCIQLRNLILSAFPRNMRLPDPFTPNLKVDMLSEINIAPRILTNFTGVMPPQFKKDLDSYLKTRSPVTFLSDLRSNLQVSNEPGNRYNLQLINALVLYVGTQAIAHIHNKGSTPSMSTITHSAHMDIFQNLAVDLDTEGRYLFLNAIANQLRYPNSHTHYFSCTMLYLFAEANTEAIQEQITRVLLERLIVNRPHPWGLLITFIELIKNPAFKFWNHEFVHCAPEIEKLFQSVAQCCMGQKQAQQVMEGTGAS
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
5Phosphorylation---MNLDSLSLALSQ
---CCHHHHHHHHHH
24.0323401153
7Phosphorylation-MNLDSLSLALSQIS
-CCHHHHHHHHHHHH
18.6223401153
11PhosphorylationDSLSLALSQISYLVD
HHHHHHHHHHHHHHH
21.6227762562
14PhosphorylationSLALSQISYLVDNLT
HHHHHHHHHHHHHHC
12.5523401153
21PhosphorylationSYLVDNLTKKNYRAS
HHHHHHHCHHCHHHH
46.3427762562
45MethylationRHGPEADRHLLRCLF
HHCHHHHHHHHHHHH
29.42115485447
231UbiquitinationAPLLYPEKRDILMDR
CCCCCHHHHCHHHHH
51.3629967540
238MethylationKRDILMDRILPDSGG
HHCHHHHHCCCCCCC
20.55115485453
243PhosphorylationMDRILPDSGGVAKTM
HHHCCCCCCCHHHHH
35.1925599653
253PhosphorylationVAKTMMESSLADFMQ
HHHHHHHHHHHHHHH
16.8625332170
286PhosphorylationQFGVREVTAAQVARV
HHCCCHHHHHHHHHH
16.1223403867
318PhosphorylationQSISAPGSGIWSDGK
CCCCCCCCCCCCCCC
26.5030576142
322PhosphorylationAPGSGIWSDGKDKSD
CCCCCCCCCCCCCCC
34.2722067460
355UbiquitinationLNPSLNFKEVTYELD
HCCCCCCEEEEEECC
50.6432015554
358PhosphorylationSLNFKEVTYELDHPG
CCCCEEEEEECCCCC
16.6328152594
359PhosphorylationLNFKEVTYELDHPGF
CCCEEEEEECCCCCE
21.4828152594
372UbiquitinationGFQIRDSKGLHNVVY
CEEEECCCCHHHHHH
70.5429967540
379PhosphorylationKGLHNVVYGIQRGLG
CCHHHHHHHHHCCCC
12.2929496907
435UbiquitinationTVATDILKAPPEDDN
CHHHHHHCCCCCCCC
60.2129967540
449UbiquitinationNREIATWKSLDLIES
CCHHCHHHHHHHHHH
36.4629967540
466PhosphorylationRLAEVGQYEQVKQLF
HHHHHCCHHHHHHHH
11.4728152594
5562-HydroxyisobutyrylationGEQYDQAKLSRILDV
CHHHCHHHHHHHHHH
41.17-
556UbiquitinationGEQYDQAKLSRILDV
CHHHCHHHHHHHHHH
41.1724816145
556 (in isoform 2)Ubiquitination-41.17-
599UbiquitinationREYLKLDKWLTDKIR
HHHHHHHHHHHHHHH
55.3129967540
626PhosphorylationFLKRRCPSILGGLAP
HHHHHCHHHHCCCCC
33.7924719451
635AcetylationLGGLAPEKDQPKSAQ
HCCCCCCCCCCCCCC
61.6826051181
635UbiquitinationLGGLAPEKDQPKSAQ
HCCCCCCCCCCCCCC
61.6829967540
640PhosphorylationPEKDQPKSAQLPPET
CCCCCCCCCCCCHHH
28.1224043423
647PhosphorylationSAQLPPETLATMLAC
CCCCCHHHHHHHHHH
27.7124043423
650PhosphorylationLPPETLATMLACLQA
CCHHHHHHHHHHHHH
18.8124043423
661PhosphorylationCLQACAGSVSQELSE
HHHHHCCCCCHHHHH
10.4824043423
663PhosphorylationQACAGSVSQELSETI
HHHCCCCCHHHHHHH
21.4524043423
667PhosphorylationGSVSQELSETILTMV
CCCCHHHHHHHHHHH
31.7624043423
669PhosphorylationVSQELSETILTMVAN
CCHHHHHHHHHHHHH
20.2224043423
672PhosphorylationELSETILTMVANCSN
HHHHHHHHHHHHHHH
13.0224043423
678PhosphorylationLTMVANCSNVMNKAR
HHHHHHHHHHHHHHC
32.0624043423
699PhosphorylationMPKGRPPSASSLDAI
CCCCCCCCCHHCCCC
43.3926074081
701PhosphorylationKGRPPSASSLDAISP
CCCCCCCHHCCCCCC
35.4526074081
702PhosphorylationGRPPSASSLDAISPV
CCCCCCHHCCCCCCC
29.9526074081
707PhosphorylationASSLDAISPVQIDPL
CHHCCCCCCCCCCCC
22.2726074081
725PhosphorylationTSLSIGGSAAPHTQS
CEEEECCCCCCCCCC
18.95-
730PhosphorylationGGSAAPHTQSMQGFP
CCCCCCCCCCCCCCC
22.68-
745PhosphorylationPNLGSAFSTPQSPAK
CCCCCCCCCCCCCCC
38.6026074081
746PhosphorylationNLGSAFSTPQSPAKA
CCCCCCCCCCCCCCC
20.9226074081
749PhosphorylationSAFSTPQSPAKAFPP
CCCCCCCCCCCCCCC
28.2026074081
808UbiquitinationNDPFVQRKLGTSGLN
CCHHHHHHHCCCCCC
33.8921906983
808 (in isoform 1)Ubiquitination-33.8921890473
808 (in isoform 4)Ubiquitination-33.8921890473
811PhosphorylationFVQRKLGTSGLNQPT
HHHHHHCCCCCCCCC
30.0228555341
812PhosphorylationVQRKLGTSGLNQPTF
HHHHHCCCCCCCCCC
39.2128555341
822PhosphorylationNQPTFQQSKMKPSDL
CCCCCCCCCCCHHHH
24.7628857561
823UbiquitinationQPTFQQSKMKPSDLS
CCCCCCCCCCHHHHH
46.7529967540
851PhosphorylationIDDEANSYFQRIYNH
CCHHHHHHHHHHHCC
11.98-
872UbiquitinationSVDEVLEMLQRFKDS
CHHHHHHHHHHHHHH
3.1924816145
877AcetylationLEMLQRFKDSTIKRE
HHHHHHHHHHHHHHH
53.6219818057
877UbiquitinationLEMLQRFKDSTIKRE
HHHHHHHHHHHHHHH
53.6224816145
879PhosphorylationMLQRFKDSTIKRERE
HHHHHHHHHHHHHHH
32.4020068231
882AcetylationRFKDSTIKREREVFN
HHHHHHHHHHHHHHH
48.5825953088
927PhosphorylationIIEKGLVTYMALGLA
HHHHHHHHHHHHHHH
16.7820068231
928PhosphorylationIEKGLVTYMALGLAL
HHHHHHHHHHHHHHH
3.4920068231
937PhosphorylationALGLALRYVLEALRK
HHHHHHHHHHHHHHC
15.38-
948PhosphorylationALRKPFGSKMYYFGI
HHHCCCCCCCHHHHH
18.0320068231
951PhosphorylationKPFGSKMYYFGIAAL
CCCCCCCHHHHHHHH
10.2020068231
952PhosphorylationPFGSKMYYFGIAALD
CCCCCCHHHHHHHHH
7.5720068231
1008PhosphorylationPPVKMQGSITTPGSI
CCCCCCCCCCCCHHH
10.4025159151
1010PhosphorylationVKMQGSITTPGSIAL
CCCCCCCCCCHHHHH
28.7425159151
1011PhosphorylationKMQGSITTPGSIALA
CCCCCCCCCHHHHHH
24.7925159151
1038PhosphorylationPLAGQVSTMVTTSTT
CCCCCEEEEEEECCC
19.4630576142
1043PhosphorylationVSTMVTTSTTTTVAK
EEEEEEECCCCEEEE
17.8730576142
1045PhosphorylationTMVTTSTTTTVAKTV
EEEEECCCCEEEEEE
21.9030576142
1051PhosphorylationTTTTVAKTVTVTRPT
CCCEEEEEEEEECCC
16.2123403867
1053PhosphorylationTTVAKTVTVTRPTGV
CEEEEEEEEECCCCC
22.7623403867
1055PhosphorylationVAKTVTVTRPTGVSF
EEEEEEEECCCCCCC
22.8923403867
1058PhosphorylationTVTVTRPTGVSFKKD
EEEEECCCCCCCCCC
47.1023401153
1058UbiquitinationTVTVTRPTGVSFKKD
EEEEECCCCCCCCCC
47.1027667366
1059UbiquitinationVTVTRPTGVSFKKDV
EEEECCCCCCCCCCC
18.7629967540
1061PhosphorylationVTRPTGVSFKKDVPP
EECCCCCCCCCCCCC
32.4725159151
1063AcetylationRPTGVSFKKDVPPSI
CCCCCCCCCCCCCCC
40.3225953088
1063UbiquitinationRPTGVSFKKDVPPSI
CCCCCCCCCCCCCCC
40.3227667366
1064UbiquitinationPTGVSFKKDVPPSIN
CCCCCCCCCCCCCCC
63.0529967540
1073PhosphorylationVPPSINTTNIDTLLV
CCCCCCCCCCCEEEE
26.20-
1109UbiquitinationIFNNLSQSNMTQKVE
HHHCCCCCCCHHHHH
25.7829967540
1114UbiquitinationSQSNMTQKVEELKET
CCCCCHHHHHHHHHH
42.3129967540
1158UbiquitinationNFLDTLKNPEFNKMV
HHHHHHCCHHHHHHH
44.4321890473
1158 (in isoform 2)Ubiquitination-44.4321890473
1158 (in isoform 3)Ubiquitination-44.4321890473
1163UbiquitinationLKNPEFNKMVLNETY
HCCHHHHHHHHCHHH
35.3922817900
1163 (in isoform 1)Ubiquitination-35.3921890473
1163 (in isoform 4)Ubiquitination-35.3921890473
11812-HydroxyisobutyrylationKVLLTSDKAAANFSD
EEEECCCHHHCCCCC
39.43-
1189MethylationAAANFSDRSLLKNLG
HHCCCCCHHHHHHHH
28.18115485441
1190PhosphorylationAANFSDRSLLKNLGH
HCCCCCHHHHHHHHH
42.9424719451
1203UbiquitinationGHWLGMITLAKNKPI
HHHHHHHHHHCCCCC
16.2729967540
1208UbiquitinationMITLAKNKPILHTDL
HHHHHCCCCCCCCCC
32.5029967540
1234PhosphorylationKGQQELLYVVPFVAK
HCCCHHHHHHHHHHH
16.42-
1305UbiquitinationKPGNLLKDKDRLKNL
CCCCCCCCHHHHCCH
59.0429967540
1310UbiquitinationLKDKDRLKNLDEQLS
CCCHHHHCCHHHHHC
57.2529967540
1315UbiquitinationRLKNLDEQLSAPKKD
HHCCHHHHHCCCCCC
40.1429967540
1320UbiquitinationDEQLSAPKKDVKQPE
HHHHCCCCCCCCCCH
62.4129967540
1321UbiquitinationEQLSAPKKDVKQPEE
HHHCCCCCCCCCCHH
67.69-
1418PhosphorylationRSIKIAMTTCEQIVR
CHHHHHHHCHHHHHH
21.19-
1419PhosphorylationSIKIAMTTCEQIVRK
HHHHHHHCHHHHHHH
10.85-
1421UbiquitinationKIAMTTCEQIVRKDF
HHHHHCHHHHHHHCC
41.0522817900
1421 (in isoform 2)Ubiquitination-41.0521890473
1421 (in isoform 3)Ubiquitination-41.0521890473
1426UbiquitinationTCEQIVRKDFALDSE
CHHHHHHHCCCCCCH
46.4321906983
1426 (in isoform 1)Ubiquitination-46.4321890473
1426 (in isoform 4)Ubiquitination-46.4321890473
1432PhosphorylationRKDFALDSEESRMRI
HHCCCCCCHHHHHHH
44.08-
1479PhosphorylationSFASALRTASPQQRE
HHHHHHHCCCHHHHH
32.1329052541
1481PhosphorylationASALRTASPQQREMM
HHHHHCCCHHHHHHH
23.7229052541
1491 (in isoform 4)Phosphorylation-10.66-
1503 (in isoform 4)Phosphorylation-2.58-
1514AcetylationIQKTAVEKAGPEMDK
HHHHHHHHHCHHHHH
52.6323749302
1514UbiquitinationIQKTAVEKAGPEMDK
HHHHHHHHHCHHHHH
52.63-
1525PhosphorylationEMDKRLATEFELRKH
HHHHHHHHHHHHHHH
45.88-
1541GlutathionylationRQEGRRYCDPVVLTY
HHHCHHCCCCEEEEE
4.5222555962
1547PhosphorylationYCDPVVLTYQAERMP
CCCCEEEEEEHHCCC
11.2820068231
1548PhosphorylationCDPVVLTYQAERMPE
CCCEEEEEEHHCCCC
11.1020068231
1555UbiquitinationYQAERMPEQIRLKVG
EEHHCCCCCEEEEEC
49.6629967540
1560UbiquitinationMPEQIRLKVGGVDPK
CCCCEEEEECCCCHH
29.0529967540
1562UbiquitinationEQIRLKVGGVDPKQL
CCEEEEECCCCHHHH
28.9022817900
1562 (in isoform 2)Ubiquitination-28.9021890473
1562 (in isoform 3)Ubiquitination-28.9021890473
1567UbiquitinationKVGGVDPKQLAVYEE
EECCCCHHHHHHHHH
54.1821906983
1567 (in isoform 1)Ubiquitination-54.1821890473
1572PhosphorylationDPKQLAVYEEFARNV
CHHHHHHHHHHHHHC
12.2527642862
1595UbiquitinationLSQPTGFLAQPMKQA
CCCCCCCCCCCHHHH
4.5922817900
1595 (in isoform 2)Ubiquitination-4.5921890473
1595 (in isoform 3)Ubiquitination-4.5921890473
1600UbiquitinationGFLAQPMKQAWATDD
CCCCCCHHHHHCCHH
43.4722817900
1600 (in isoform 1)Ubiquitination-43.4721890473
1612PhosphorylationTDDVAQIYDKCITEL
CHHHHHHHHHHHHHH
9.4027642862
1649PhosphorylationLLEVVVLSRNSRDAI
HHHHHHHCCCCHHHH
20.1520860994
1703PhosphorylationQDGRAYGSPWCNKQI
HCCCCCCCHHHCHHH
11.5320873877
1703UbiquitinationQDGRAYGSPWCNKQI
HCCCCCCCHHHCHHH
11.5323000965
1708AcetylationYGSPWCNKQITRCLI
CCCHHHCHHHHHHHH
39.6826051181
1708MalonylationYGSPWCNKQITRCLI
CCCHHHCHHHHHHHH
39.6826320211
1708UbiquitinationYGSPWCNKQITRCLI
CCCHHHCHHHHHHHH
39.6823000965
1775PhosphorylationILLVDERSVAHVTEA
HHCCCCCHHCCCCHH
22.9320860994
1780PhosphorylationERSVAHVTEADLFHT
CCHHCCCCHHHHHHH
18.6520860994
1787PhosphorylationTEADLFHTIETLMRI
CHHHHHHHHHHHHHH
17.1120860994
1790PhosphorylationDLFHTIETLMRINAH
HHHHHHHHHHHHCCC
23.2320860994
1817PhosphorylationMEVVRSNYEAMIDRA
HHHHHHCHHHHHHHH
13.3028796482
1834PhosphorylationGPNFMMHSGISQASE
CCCCCCCCCCCCCCC
21.6728555341
1837PhosphorylationFMMHSGISQASEYDD
CCCCCCCCCCCCCCC
24.1828555341
1842PhosphorylationGISQASEYDDPPGLR
CCCCCCCCCCCCCHH
24.1327642862
1846UbiquitinationASEYDDPPGLREKAE
CCCCCCCCCHHHHHH
62.5427667366
1851UbiquitinationDPPGLREKAEYLLRE
CCCCHHHHHHHHHHH
39.8327667366
1863PhosphorylationLREWVNLYHSAAAGR
HHHHHHHHHHHHCCC
6.6321406692
1865PhosphorylationEWVNLYHSAAAGRDS
HHHHHHHHHHCCCCC
13.1721406692
1927SulfoxidationNPAANPTMIRAKCYH
CCCCCCHHHHHHHHC
1.7421406390
1933PhosphorylationTMIRAKCYHNLDAFV
HHHHHHHHCCHHHHH
7.9519060867
1959UbiquitinationEATNTVTKINLLNKV
CCCCHHHHHHHHHHH
25.84-
2074PhosphorylationLLIDLFKYLAPFLRN
HHHHHHHHHHHHHHC
10.7620068231
2081UbiquitinationYLAPFLRNVELTKPM
HHHHHHHCCCCCCCC
33.4921890473
2081 (in isoform 2)Ubiquitination-33.4921890473
2081 (in isoform 3)Ubiquitination-33.4921890473
2086UbiquitinationLRNVELTKPMQILYK
HHCCCCCCCCHHHHH
51.6327667366
2086 (in isoform 1)Ubiquitination-51.6321890473
2146UbiquitinationNMRLPDPFTPNLKVD
CCCCCCCCCCCCCCC
26.7521963094
2146 (in isoform 2)Ubiquitination-26.7521890473
2151UbiquitinationDPFTPNLKVDMLSEI
CCCCCCCCCCHHHHC
42.7121906983
2151 (in isoform 1)Ubiquitination-42.7121890473
2154SulfoxidationTPNLKVDMLSEINIA
CCCCCCCHHHHCCCC
5.0621406390
2172UbiquitinationLTNFTGVMPPQFKKD
HHCCCCCCCCHHHHH
4.1929967540
2173UbiquitinationTNFTGVMPPQFKKDL
HCCCCCCCCHHHHHH
19.6829967540
2177UbiquitinationGVMPPQFKKDLDSYL
CCCCCHHHHHHHHHH
39.8829967540
2178UbiquitinationVMPPQFKKDLDSYLK
CCCCHHHHHHHHHHH
65.8929967540
2180UbiquitinationPPQFKKDLDSYLKTR
CCHHHHHHHHHHHCC
6.9133845483
2180 (in isoform 2)Ubiquitination-6.9121890473
2185AcetylationKDLDSYLKTRSPVTF
HHHHHHHHCCCCCCH
33.3925953088
2185UbiquitinationKDLDSYLKTRSPVTF
HHHHHHHHCCCCCCH
33.3927667366
2185 (in isoform 1)Ubiquitination-33.3921890473
2186PhosphorylationDLDSYLKTRSPVTFL
HHHHHHHCCCCCCHH
33.5128450419
2188PhosphorylationDSYLKTRSPVTFLSD
HHHHHCCCCCCHHHH
29.0228450419
2191PhosphorylationLKTRSPVTFLSDLRS
HHCCCCCCHHHHHHH
23.4228450419
2194PhosphorylationRSPVTFLSDLRSNLQ
CCCCCHHHHHHHCCC
30.3326091039
2264PhosphorylationDLDTEGRYLFLNAIA
CCCCCCCHHHHHHHH
16.80-
2359UbiquitinationLFQSVAQCCMGQKQA
HHHHHHHHHCCHHHH
0.9329967540
2361SulfoxidationQSVAQCCMGQKQAQQ
HHHHHHHCCHHHHHH
9.3021406390
2364UbiquitinationAQCCMGQKQAQQVME
HHHHCCHHHHHHHHH
41.7029967540

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 CNOT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNOT1_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 CNOT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNOT2_HUMANCNOT2physical
10637334
CNOT4_HUMANCNOT4physical
10637334
CNOT8_HUMANCNOT8physical
10637334
CNOT4_HUMANCNOT4physical
11823428
NOT4_YEASTMOT2physical
11823428
CNOT3_HUMANCNOT3physical
22939629
CNOT9_HUMANRQCD1physical
22939629
RPAC1_HUMANPOLR1Cphysical
22863883
CNOT2_HUMANCNOT2physical
16778766
CNOT3_HUMANCNOT3physical
16778766
CNOT8_HUMANCNOT8physical
16778766
RXRA_HUMANRXRAphysical
16778766
ESR1_MOUSEEsr1physical
16778766
TNR6C_HUMANTNRC6Cphysical
21981923
TNR6A_HUMANTNRC6Aphysical
23172285
CNOT7_HUMANCNOT7physical
26344197
ABCF1_HUMANABCF1physical
26496610
ATRX_HUMANATRXphysical
26496610
CAZA1_HUMANCAPZA1physical
26496610
CAZA2_HUMANCAPZA2physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
FHL2_HUMANFHL2physical
26496610
CNOT2_HUMANCNOT2physical
26496610
CNOT3_HUMANCNOT3physical
26496610
RS27_HUMANRPS27physical
26496610
SDCB1_HUMANSDCBPphysical
26496610
UBF1_HUMANUBTFphysical
26496610
CNOT9_HUMANRQCD1physical
26496610
CNOT8_HUMANCNOT8physical
26496610
TOB1_HUMANTOB1physical
26496610
TOB2_HUMANTOB2physical
26496610
BTG3_HUMANBTG3physical
26496610
NUPL2_HUMANNUPL2physical
26496610
CNO10_HUMANCNOT10physical
26496610
IBTK_HUMANIBTKphysical
26496610
SND1_HUMANSND1physical
26496610
AFF4_HUMANAFF4physical
26496610
CNOT7_HUMANCNOT7physical
26496610
AKIP_HUMANAURKAIP1physical
26496610
P4K2A_HUMANPI4K2Aphysical
26496610
CNO11_HUMANCNOT11physical
26496610
CNOT6_HUMANCNOT6physical
26496610
GPBL1_HUMANGPBP1L1physical
26496610
RN219_HUMANRNF219physical
26496610
INT5_HUMANINTS5physical
26496610
TB182_HUMANTNKS1BP1physical
26496610
RAVR1_HUMANRAVER1physical
26496610
CNO6L_HUMANCNOT6Lphysical
26496610
CNOT9_HUMANRQCD1physical
24768540
DDX6_HUMANDDX6physical
24768540
TNR6A_HUMANTNRC6Aphysical
24768540
CNOT6_HUMANCNOT6physical
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 CNOT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1933, AND MASSSPECTROMETRY.

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