SMC4_HUMAN - dbPTM
SMC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMC4_HUMAN
UniProt AC Q9NTJ3
Protein Name Structural maintenance of chromosomes protein 4
Gene Name SMC4
Organism Homo sapiens (Human).
Sequence Length 1288
Subcellular Localization Nucleus . Cytoplasm . Chromosome . In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chro
Protein Description Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases..
Protein Sequence MPRKGTQPSTARRREEGPPPPSPDGASSDAEPEPPSGRTESPATAAETASEELDNRSLEEILNSIPPPPPPAMTNEAGAPRLMITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVEVHFQKIIDKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKGQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLPQTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDVAISSCCHALDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFDLVKVKDEKIRQAFYFALRDTLVADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNITKSVAVNPKEIASKGLC
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
4Methylation----MPRKGTQPSTA
----CCCCCCCCCCC
76.63116253841
6Phosphorylation--MPRKGTQPSTARR
--CCCCCCCCCCCCC
40.1025137130
22PhosphorylationEEGPPPPSPDGASSD
CCCCCCCCCCCCCCC
41.2029255136
27PhosphorylationPPSPDGASSDAEPEP
CCCCCCCCCCCCCCC
33.9929255136
28PhosphorylationPSPDGASSDAEPEPP
CCCCCCCCCCCCCCC
40.0629255136
36PhosphorylationDAEPEPPSGRTESPA
CCCCCCCCCCCCCCC
52.1830266825
39PhosphorylationPEPPSGRTESPATAA
CCCCCCCCCCCCHHH
44.3222167270
41PhosphorylationPPSGRTESPATAAET
CCCCCCCCCCHHHHH
21.1519664994
44PhosphorylationGRTESPATAAETASE
CCCCCCCHHHHHHCH
29.7719664994
48PhosphorylationSPATAAETASEELDN
CCCHHHHHHCHHHCC
30.6623927012
50PhosphorylationATAAETASEELDNRS
CHHHHHHCHHHCCCC
38.7430266825
57PhosphorylationSEELDNRSLEEILNS
CHHHCCCCHHHHHHC
46.5220873877
85PhosphorylationGAPRLMITHIVNQNF
CCCCEEEEHHHCCCH
7.50-
93MethylationHIVNQNFKSYAGEKI
HHHCCCHHHHCCCCC
50.54100328913
93UbiquitinationHIVNQNFKSYAGEKI
HHHCCCHHHHCCCCC
50.54-
99UbiquitinationFKSYAGEKILGPFHK
HHHHCCCCCCCCCCC
42.17-
106AcetylationKILGPFHKRFSCIIG
CCCCCCCCCEEEEEC
56.3625953088
106UbiquitinationKILGPFHKRFSCIIG
CCCCCCCCCEEEEEC
56.36-
109PhosphorylationGPFHKRFSCIIGPNG
CCCCCCEEEEECCCC
14.40-
119MethylationIGPNGSGKSNVIDSM
ECCCCCCCCCHHHHH
40.32115980899
120PhosphorylationGPNGSGKSNVIDSML
CCCCCCCCCHHHHHH
39.5921406692
125PhosphorylationGKSNVIDSMLFVFGY
CCCCHHHHHHHHHHH
13.2721406692
132PhosphorylationSMLFVFGYRAQKIRS
HHHHHHHHHHHHHHH
7.4221406692
141UbiquitinationAQKIRSKKLSVLIHN
HHHHHHCCEEEEEEC
47.44-
143PhosphorylationKIRSKKLSVLIHNSD
HHHHCCEEEEEECCC
24.6125159151
149PhosphorylationLSVLIHNSDEHKDIQ
EEEEEECCCCCCCHH
30.1625159151
153UbiquitinationIHNSDEHKDIQSCTV
EECCCCCCCHHHCEE
55.25-
170UbiquitinationHFQKIIDKEGDDYEV
EEEEHHHCCCCCCEE
53.86-
175PhosphorylationIDKEGDDYEVIPNSN
HHCCCCCCEECCCCC
19.4825147952
184PhosphorylationVIPNSNFYVSRTACR
ECCCCCEEEEEEEEC
11.1929496907
188PhosphorylationSNFYVSRTACRDNTS
CCEEEEEEEECCCCE
23.70-
194PhosphorylationRTACRDNTSVYHISG
EEEECCCCEEEEEEC
24.6928152594
195PhosphorylationTACRDNTSVYHISGK
EEECCCCEEEEEECC
27.2528152594
197PhosphorylationCRDNTSVYHISGKKK
ECCCCEEEEEECCCC
8.0028152594
200PhosphorylationNTSVYHISGKKKTFK
CCEEEEEECCCCCHH
31.1128152594
2022-HydroxyisobutyrylationSVYHISGKKKTFKDV
EEEEEECCCCCHHHH
44.28-
202AcetylationSVYHISGKKKTFKDV
EEEEEECCCCCHHHH
44.2825953088
202UbiquitinationSVYHISGKKKTFKDV
EEEEEECCCCCHHHH
44.2821890473
202 (in isoform 1)Ubiquitination-44.2821890473
202 (in isoform 2)Ubiquitination-44.2821890473
203UbiquitinationVYHISGKKKTFKDVG
EEEEECCCCCHHHHH
61.65-
204UbiquitinationYHISGKKKTFKDVGN
EEEECCCCCHHHHHH
63.78-
207AcetylationSGKKKTFKDVGNLLR
ECCCCCHHHHHHHHH
57.6525953088
207UbiquitinationSGKKKTFKDVGNLLR
ECCCCCHHHHHHHHH
57.6521890473
207 (in isoform 1)Ubiquitination-57.6521890473
207 (in isoform 2)Ubiquitination-57.6521890473
214MethylationKDVGNLLRSHGIDLD
HHHHHHHHHCCCCCC
29.76115917257
239UbiquitinationVEQIAMMKPKGQTEH
EEEEEECCCCCCCCC
30.41-
241UbiquitinationQIAMMKPKGQTEHDE
EEEECCCCCCCCCCH
59.12-
250SulfoxidationQTEHDEGMLEYLEDI
CCCCCHHHHHHHHHH
2.1230846556
268AcetylationGRLNEPIKVLCRRVE
CCCCHHHHHHHHHHH
39.6123749302
268UbiquitinationGRLNEPIKVLCRRVE
CCCCHHHHHHHHHHH
39.61-
281MethylationVEILNEHRGEKLNRV
HHHHHHCCCCCCCCC
49.11115917261
284AcetylationLNEHRGEKLNRVKMV
HHHCCCCCCCCCEEE
54.6126051181
2892-HydroxyisobutyrylationGEKLNRVKMVEKEKD
CCCCCCCEEEHHHHH
33.71-
293UbiquitinationNRVKMVEKEKDALEG
CCCEEEHHHHHHHHC
59.67-
3192-HydroxyisobutyrylationENEIFRKKNHVCQYY
CHHHHHCCCCHHHHH
48.29-
332UbiquitinationYYIYELQKRIAEMET
HHHHHHHHHHHHHHH
59.40-
341UbiquitinationIAEMETQKEKIHEDT
HHHHHHHHHHHHHHH
69.28-
343UbiquitinationEMETQKEKIHEDTKE
HHHHHHHHHHHHHHH
57.30-
348PhosphorylationKEKIHEDTKEINEKS
HHHHHHHHHHHHHHH
27.8220860994
349AcetylationEKIHEDTKEINEKSN
HHHHHHHHHHHHHHC
69.7623749302
349UbiquitinationEKIHEDTKEINEKSN
HHHHHHHHHHHHHHC
69.76-
3542-HydroxyisobutyrylationDTKEINEKSNILSNE
HHHHHHHHHCCCCHH
44.29-
354AcetylationDTKEINEKSNILSNE
HHHHHHHHHCCCCHH
44.2919827019
354UbiquitinationDTKEINEKSNILSNE
HHHHHHHHHCCCCHH
44.29-
355PhosphorylationTKEINEKSNILSNEM
HHHHHHHHCCCCHHH
23.9519691289
363AcetylationNILSNEMKAKNKDVK
CCCCHHHHHCCCCHH
50.4525953088
363UbiquitinationNILSNEMKAKNKDVK
CCCCHHHHHCCCCHH
50.45-
381AcetylationKKLNKITKFIEENKE
HHHHHHHHHHHHCHH
48.0619608861
381UbiquitinationKKLNKITKFIEENKE
HHHHHHHHHHHHCHH
48.0619608861
387AcetylationTKFIEENKEKFTQLD
HHHHHHCHHHHHCCC
66.6125953088
389UbiquitinationFIEENKEKFTQLDLE
HHHHCHHHHHCCCHH
56.1521890473
389 (in isoform 1)Ubiquitination-56.1521890473
389 (in isoform 2)Ubiquitination-56.1521890473
409PhosphorylationEKLKHATSKAKKLEK
HHHHHHHHHHHHHHH
31.2525367160
413UbiquitinationHATSKAKKLEKQLQK
HHHHHHHHHHHHHHH
67.7321890473
413 (in isoform 1)Ubiquitination-67.7321890473
413 (in isoform 2)Ubiquitination-67.7321890473
416AcetylationSKAKKLEKQLQKDKE
HHHHHHHHHHHHHHH
67.7423749302
416UbiquitinationSKAKKLEKQLQKDKE
HHHHHHHHHHHHHHH
67.74-
434UbiquitinationEFKSIPAKSNNIINE
HHHCCCCCCCCCCCC
48.65-
444PhosphorylationNIINETTTRNNALEK
CCCCCCCHHCHHHHH
38.5321601212
464SulfoxidationEKKLKEVMDSLKQET
HHHHHHHHHHHHHHH
2.8021406390
466PhosphorylationKLKEVMDSLKQETQG
HHHHHHHHHHHHHHH
21.2628985074
483AcetylationKEKESREKELMGFSK
HHHHHHHHHHHHHHH
55.8525953088
489PhosphorylationEKELMGFSKSVNEAR
HHHHHHHHHHHHHHH
20.49-
490AcetylationKELMGFSKSVNEARS
HHHHHHHHHHHHHHH
57.0425953088
511PhosphorylationSELDIYLSRHNTAVS
HHHHHHHHCCCHHHH
17.9630257219
515PhosphorylationIYLSRHNTAVSQLTK
HHHHCCCHHHHHHHH
23.4721406692
518PhosphorylationSRHNTAVSQLTKAKE
HCCCHHHHHHHHHHH
19.6021406692
521PhosphorylationNTAVSQLTKAKEALI
CHHHHHHHHHHHHHH
22.7121406692
5222-HydroxyisobutyrylationTAVSQLTKAKEALIA
HHHHHHHHHHHHHHH
67.08-
522UbiquitinationTAVSQLTKAKEALIA
HHHHHHHHHHHHHHH
67.08-
5242-HydroxyisobutyrylationVSQLTKAKEALIAAS
HHHHHHHHHHHHHCH
45.11-
531PhosphorylationKEALIAASETLKERK
HHHHHHCHHHHHHHH
23.30-
533PhosphorylationALIAASETLKERKAA
HHHHCHHHHHHHHHH
40.40-
547UbiquitinationAIRDIEGKLPQTEQE
HHHHHCCCCCHHHHH
44.17-
551PhosphorylationIEGKLPQTEQELKEK
HCCCCCHHHHHHHHH
37.3825003641
564AcetylationEKEKELQKLTQEETN
HHHHHHHHHHHHHHH
67.1523236377
564UbiquitinationEKEKELQKLTQEETN
HHHHHHHHHHHHHHH
67.15-
5732-HydroxyisobutyrylationTQEETNFKSLVHDLF
HHHHHHHHHHHHHHH
44.97-
573AcetylationTQEETNFKSLVHDLF
HHHHHHHHHHHHHHH
44.9723954790
573UbiquitinationTQEETNFKSLVHDLF
HHHHHHHHHHHHHHH
44.97-
574PhosphorylationQEETNFKSLVHDLFQ
HHHHHHHHHHHHHHH
31.3321712546
582AcetylationLVHDLFQKVEEAKSS
HHHHHHHHHHHHHHH
44.2625953088
582UbiquitinationLVHDLFQKVEEAKSS
HHHHHHHHHHHHHHH
44.26-
5872-HydroxyisobutyrylationFQKVEEAKSSLAMNR
HHHHHHHHHHHHCCC
43.80-
587UbiquitinationFQKVEEAKSSLAMNR
HHHHHHHHHHHHCCC
43.80-
588PhosphorylationQKVEEAKSSLAMNRS
HHHHHHHHHHHCCCC
37.3220044836
589PhosphorylationKVEEAKSSLAMNRSR
HHHHHHHHHHCCCCH
21.3120044836
595PhosphorylationSSLAMNRSRGKVLDA
HHHHCCCCHHHHHHH
40.1420044836
5982-HydroxyisobutyrylationAMNRSRGKVLDAIIQ
HCCCCHHHHHHHHHH
38.22-
598AcetylationAMNRSRGKVLDAIIQ
HCCCCHHHHHHHHHH
38.2230592473
598UbiquitinationAMNRSRGKVLDAIIQ
HCCCCHHHHHHHHHH
38.22-
6072-HydroxyisobutyrylationLDAIIQEKKSGRIPG
HHHHHHHHHCCCCCC
35.54-
607AcetylationLDAIIQEKKSGRIPG
HHHHHHHHHCCCCCC
35.5423954790
607UbiquitinationLDAIIQEKKSGRIPG
HHHHHHHHHCCCCCC
35.5421906983
607 (in isoform 1)Ubiquitination-35.5421890473
607 (in isoform 2)Ubiquitination-35.5421890473
608AcetylationDAIIQEKKSGRIPGI
HHHHHHHHCCCCCCC
58.3430592485
616PhosphorylationSGRIPGIYGRLGDLG
CCCCCCCCCCCCCCC
11.3420068231
6792-HydroxyisobutyrylationDKMAVWAKKMTEIQT
HHHHHHHHHHCCCCC
27.62-
679AcetylationDKMAVWAKKMTEIQT
HHHHHHHHHHCCCCC
27.6219608861
6802-HydroxyisobutyrylationKMAVWAKKMTEIQTP
HHHHHHHHHCCCCCC
43.22-
680MalonylationKMAVWAKKMTEIQTP
HHHHHHHHHCCCCCC
43.2226320211
681SulfoxidationMAVWAKKMTEIQTPE
HHHHHHHHCCCCCCC
3.9121406390
682PhosphorylationAVWAKKMTEIQTPEN
HHHHHHHCCCCCCCC
38.5222817900
686PhosphorylationKKMTEIQTPENTPRL
HHHCCCCCCCCCCCC
37.9322817900
690PhosphorylationEIQTPENTPRLFDLV
CCCCCCCCCCCCHHE
14.2329083192
698UbiquitinationPRLFDLVKVKDEKIR
CCCCHHEEECCHHHH
51.36-
709PhosphorylationEKIRQAFYFALRDTL
HHHHHHHHHHHHHHH
7.3122817900
739PhosphorylationDRRWRVVTLQGQIIE
CCCEEEEEEECEEEE
15.5424043423
748PhosphorylationQGQIIEQSGTMTGGG
ECEEEEECCCCCCCC
24.3624043423
750PhosphorylationQIIEQSGTMTGGGSK
EEEEECCCCCCCCCC
19.4624043423
752PhosphorylationIEQSGTMTGGGSKVM
EEECCCCCCCCCCCC
32.2924043423
756PhosphorylationGTMTGGGSKVMKGRM
CCCCCCCCCCCCCCC
25.9224043423
760UbiquitinationGGGSKVMKGRMGSSL
CCCCCCCCCCCCCCE
46.48-
765PhosphorylationVMKGRMGSSLVIEIS
CCCCCCCCCEEEEEC
15.9128450419
766PhosphorylationMKGRMGSSLVIEISE
CCCCCCCCEEEEECH
22.4128450419
787PhosphorylationESQLQNDSKKAMQIQ
HHHHHHHHHHHHHHH
43.5428842319
789UbiquitinationQLQNDSKKAMQIQEQ
HHHHHHHHHHHHHHH
53.71-
797UbiquitinationAMQIQEQKVQLEERV
HHHHHHHHHHHHHHH
31.06-
820UbiquitinationEMRNTLEKFTASIQR
HHHHHHHHHHHHHHH
51.64-
822PhosphorylationRNTLEKFTASIQRLI
HHHHHHHHHHHHHHH
30.4823403867
8532-HydroxyisobutyrylationVLATAPDKKKQKLLE
HHCCCCCHHHHHHHH
61.89-
853AcetylationVLATAPDKKKQKLLE
HHCCCCCHHHHHHHH
61.8925953088
853UbiquitinationVLATAPDKKKQKLLE
HHCCCCCHHHHHHHH
61.89-
855UbiquitinationATAPDKKKQKLLEEN
CCCCCHHHHHHHHHH
59.41-
857AcetylationAPDKKKQKLLEENVS
CCCHHHHHHHHHHHH
65.0125953088
857UbiquitinationAPDKKKQKLLEENVS
CCCHHHHHHHHHHHH
65.01-
867UbiquitinationEENVSAFKTEYDAVA
HHHHHHHHHHHHHHH
39.91-
876AcetylationEYDAVAEKAGKVEAE
HHHHHHHHHCCHHHH
53.3425953088
876UbiquitinationEYDAVAEKAGKVEAE
HHHHHHHHHCCHHHH
53.34-
8852-HydroxyisobutyrylationGKVEAEVKRLHNTIV
CCHHHHHHHHHHHHH
40.52-
898AcetylationIVEINNHKLKAQQDK
HHHCCHHHHHHHHHH
54.5325953088
898UbiquitinationIVEINNHKLKAQQDK
HHHCCHHHHHHHHHH
54.53-
905UbiquitinationKLKAQQDKLDKINKQ
HHHHHHHHHHHHHHH
55.00-
908AcetylationAQQDKLDKINKQLDE
HHHHHHHHHHHHHHH
59.6325953088
922UbiquitinationECASAITKAQVAIKT
HHHHHHHHHHHHHHH
30.61-
9282-HydroxyisobutyrylationTKAQVAIKTADRNLQ
HHHHHHHHHHCHHHH
28.11-
928AcetylationTKAQVAIKTADRNLQ
HHHHHHHHHHCHHHH
28.1125953088
928UbiquitinationTKAQVAIKTADRNLQ
HHHHHHHHHHCHHHH
28.11-
929PhosphorylationKAQVAIKTADRNLQK
HHHHHHHHHCHHHHH
27.9027174698
936UbiquitinationTADRNLQKAQDSVLR
HHCHHHHHHHHHHHH
51.70-
940PhosphorylationNLQKAQDSVLRTEKE
HHHHHHHHHHHHHHH
15.8030576142
944PhosphorylationAQDSVLRTEKEIKDT
HHHHHHHHHHHHHHH
47.4530576142
953UbiquitinationKEIKDTEKEVDDLTA
HHHHHHHHHHHHHHH
66.19-
963UbiquitinationDDLTAELKSLEDKAA
HHHHHHHHHHHHHHH
44.49-
9682-HydroxyisobutyrylationELKSLEDKAAEVVKN
HHHHHHHHHHHHHHC
39.87-
968AcetylationELKSLEDKAAEVVKN
HHHHHHHHHHHHHHC
39.8725953088
968UbiquitinationELKSLEDKAAEVVKN
HHHHHHHHHHHHHHC
39.87-
974UbiquitinationDKAAEVVKNTNAAEE
HHHHHHHHCCCHHHH
64.33-
976PhosphorylationAAEVVKNTNAAEESL
HHHHHHCCCHHHHCH
22.1023312004
982PhosphorylationNTNAAEESLPEIQKE
CCCHHHHCHHHHHHH
40.5025159151
988AcetylationESLPEIQKEHRNLLQ
HCHHHHHHHHHHHHH
62.2426051181
988UbiquitinationESLPEIQKEHRNLLQ
HCHHHHHHHHHHHHH
62.24-
998AcetylationRNLLQELKVIQENEH
HHHHHHHHHHHHCHH
36.2225953088
998UbiquitinationRNLLQELKVIQENEH
HHHHHHHHHHHHCHH
36.22-
1009AcetylationENEHALQKDALSIKL
HCHHHHHHHHHHHHH
45.9023954790
1009UbiquitinationENEHALQKDALSIKL
HCHHHHHHHHHHHHH
45.90-
1013PhosphorylationALQKDALSIKLKLEQ
HHHHHHHHHHHHHHH
21.28-
1015UbiquitinationQKDALSIKLKLEQID
HHHHHHHHHHHHHHC
35.87-
1030PhosphorylationGHIAEHNSKIKYWHK
CHHHHCCCCCCHHHH
37.3525159151
1031AcetylationHIAEHNSKIKYWHKE
HHHHCCCCCCHHHHH
48.8425953088
1031UbiquitinationHIAEHNSKIKYWHKE
HHHHCCCCCCHHHHH
48.84-
1033UbiquitinationAEHNSKIKYWHKEIS
HHCCCCCCHHHHHHC
46.13-
1037AcetylationSKIKYWHKEISKISL
CCCCHHHHHHCCCCC
42.4719608861
1037UbiquitinationSKIKYWHKEISKISL
CCCCHHHHHHCCCCC
42.4719608861
1041UbiquitinationYWHKEISKISLHPIE
HHHHHHCCCCCCCCC
41.81-
1043PhosphorylationHKEISKISLHPIEDN
HHHHCCCCCCCCCCC
25.1024732914
1054 (in isoform 2)Ubiquitination-41.0821890473
1056PhosphorylationDNPIEEISVLSPEDL
CCCCCEEEECCHHHH
21.9325159151
1059PhosphorylationIEEISVLSPEDLEAI
CCEEEECCHHHHHHH
24.8825159151
1067UbiquitinationPEDLEAIKNPDSITN
HHHHHHHCCCCHHHH
70.27-
1071PhosphorylationEAIKNPDSITNQIAL
HHHCCCCHHHHHHHH
32.3524732914
1073PhosphorylationIKNPDSITNQIALLE
HCCCCHHHHHHHHHH
25.6424732914
1087AcetylationEARCHEMKPNLGAIA
HHHHHHCCCCHHHHH
27.9826051181
1087UbiquitinationEARCHEMKPNLGAIA
HHHHHHCCCCHHHHH
27.98-
1097UbiquitinationLGAIAEYKKKEELYL
HHHHHHHHCHHHHHH
49.20-
1098UbiquitinationGAIAEYKKKEELYLQ
HHHHHHHCHHHHHHH
65.60-
1099UbiquitinationAIAEYKKKEELYLQR
HHHHHHCHHHHHHHH
52.87-
1112UbiquitinationQRVAELDKITYERDS
HHHHHHHHHHCCHHH
49.9621890473
1112 (in isoform 1)Ubiquitination-49.9621890473
1115PhosphorylationAELDKITYERDSFRQ
HHHHHHHCCHHHHHH
16.67-
1129UbiquitinationQAYEDLRKQRLNEFM
HHHHHHHHHHHHHHH
47.25-
1129 (in isoform 2)Ubiquitination-47.2521890473
1145UbiquitinationGFYIITNKLKENYQM
HHHHHHHHHHHCCEE
52.89-
1187UbiquitinationPPKKSWKKIFNLSGG
CCCCCHHHHHCCCCC
46.3921890473
1187 (in isoform 1)Ubiquitination-46.3921890473
1192PhosphorylationWKKIFNLSGGEKTLS
HHHHHCCCCCCHHHH
45.9525367160
1209 (in isoform 2)Ubiquitination-32.9121890473
1213PhosphorylationALHHYKPTPLYFMDE
HHHHCCCCCEEEHHH
23.0528787133
1215 (in isoform 2)Ubiquitination-5.9121890473
1222 (in isoform 2)Ubiquitination-24.6021890473
1227 (in isoform 2)Ubiquitination-6.8821890473
1266PhosphorylationSDRLIGIYKTYNITK
HHHHHEEEECCCCCC
7.65-
1267UbiquitinationDRLIGIYKTYNITKS
HHHHEEEECCCCCCC
42.4821890473
1267 (in isoform 1)Ubiquitination-42.4821890473
1273UbiquitinationYKTYNITKSVAVNPK
EECCCCCCCEECCHH
38.8521906983
1273 (in isoform 1)Ubiquitination-38.8521890473
1280UbiquitinationKSVAVNPKEIASKGL
CCEECCHHHHHHCCC
57.452190698
1280 (in isoform 1)Ubiquitination-57.4521890473
1284PhosphorylationVNPKEIASKGLC---
CCHHHHHHCCCC---
32.6828122231
1285AcetylationNPKEIASKGLC----
CHHHHHHCCCC----
47.0525953088
1285UbiquitinationNPKEIASKGLC----
CHHHHHHCCCC----
47.05-
1285 (in isoform 1)Ubiquitination-47.0521890473

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 SMC4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMC4_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 SMC4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMC2_HUMANSMC2physical
9789013
CND2_HUMANNCAPHphysical
17268547
CNDH2_HUMANNCAPH2physical
17268547
AP3S1_HUMANAP3S1physical
22863883
CCAR2_HUMANCCAR2physical
22863883
CND2_HUMANNCAPHphysical
22863883
RABL6_HUMANRABL6physical
22863883
PLEC_HUMANPLECphysical
22863883
TBCD4_HUMANTBC1D4physical
22863883
KIF2C_HUMANKIF2Cphysical
26344197
CND2_HUMANNCAPHphysical
26344197
SMC1A_HUMANSMC1Aphysical
26344197
SMC2_HUMANSMC2physical
26344197
HECD1_HUMANHECTD1physical
26166704

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 SMC4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-381; LYS-679 AND LYS-1037,AND MASS SPECTROMETRY.
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-22; SER-28; THR-39;SER-41 AND SER-50, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND THR-39, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39; SER-41 AND SER-50,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 SER-22 AND SER-27, 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 THR-39 AND SER-982, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-1056, ANDMASS SPECTROMETRY.
"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-22; SER-28 AND SER-41,AND MASS SPECTROMETRY.

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