SCML2_HUMAN - dbPTM
SCML2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCML2_HUMAN
UniProt AC Q9UQR0
Protein Name Sex comb on midleg-like protein 2
Gene Name SCML2
Organism Homo sapiens (Human).
Sequence Length 700
Subcellular Localization Nucleus .
Protein Description Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity)..
Protein Sequence MGQTVNEDSMDVKKENQEKTPQSSTSSVQRDDFHWEEYLKETGSISAPSECFRQSQIPPVNDFKVGMKLEARDPRNATSVCIATVIGITGARLRLRLDGSDNRNDFWRLVDSPDIQPVGTCEKEGDLLQPPLGYQMNTSSWPMFLLKTLNGSEMASATLFKKEPPKPPLNNFKVGMKLEAIDKKNPYLICPATIGDVKGDEVHITFDGWSGAFDYWCKYDSRDIFPAGWCRLTGDVLQPPGTSVPIVKNIAKTESSPSEASQHSMQSPQKTTLILPTQQVRRSSRIKPPGPTAVPKRSSSVKNITPRKKGPNSGKKEKPLPVICSTSAASLKSLTRDRGMLYKDVASGPCKIVMSTVCVYVNKHGNFGPHLDPKRIQQLPDHFGPGPVNVVLRRIVQACVDCALETKTVFGYLKPDNRGGEVITASFDGETHSIQLPPVNSASFALRFLENFCHSLQCDNLLSSQPFSSSRGHTHSSAEHDKNQSAKEDVTERQSTKRSPQQTVPYVVPLSPKLPKTKEYASEGEPLFAGGSAIPKEENLSEDSKSSSLNSGNYLNPACRNPMYIHTSVSQDFSRSVPGTTSSPLVGDISPKSSPHEVKFQMQRKSEAPSYIAVPDPSVLKQGFSKDPSTWSVDEVIQFMKHTDPQISGPLADLFRQHEIDGKALFLLKSDVMMKYMGLKLGPALKLCYYIEKLKEGKYS
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
9PhosphorylationGQTVNEDSMDVKKEN
CCCCCCCCCCCHHHH
15.6521815630
10SulfoxidationQTVNEDSMDVKKENQ
CCCCCCCCCCHHHHH
12.1221406390
13SumoylationNEDSMDVKKENQEKT
CCCCCCCHHHHHCCC
50.54-
13SumoylationNEDSMDVKKENQEKT
CCCCCCCHHHHHCCC
50.54-
13UbiquitinationNEDSMDVKKENQEKT
CCCCCCCHHHHHCCC
50.5432015554
19UbiquitinationVKKENQEKTPQSSTS
CHHHHHCCCCCCCCC
56.6029967540
20PhosphorylationKKENQEKTPQSSTSS
HHHHHCCCCCCCCCC
26.3021815630
23PhosphorylationNQEKTPQSSTSSVQR
HHCCCCCCCCCCHHH
36.4729449344
32UbiquitinationTSSVQRDDFHWEEYL
CCCHHHCCCCHHHHH
39.2324816145
40UbiquitinationFHWEEYLKETGSISA
CCHHHHHHHHCCCCC
52.9429967540
64UbiquitinationIPPVNDFKVGMKLEA
CCCCCCCCCCEEEEE
40.5229967540
68UbiquitinationNDFKVGMKLEARDPR
CCCCCCEEEEECCCC
36.93-
123MethylationQPVGTCEKEGDLLQP
CCCCCCCCCCCCCCC
69.9723583077
148PhosphorylationWPMFLLKTLNGSEMA
CCEEEEHHCCCCCCC
25.9822210691
152PhosphorylationLLKTLNGSEMASATL
EEHHCCCCCCCCCCC
24.1122210691
161SumoylationMASATLFKKEPPKPP
CCCCCCCCCCCCCCC
60.38-
161SumoylationMASATLFKKEPPKPP
CCCCCCCCCCCCCCC
60.38-
162UbiquitinationASATLFKKEPPKPPL
CCCCCCCCCCCCCCC
69.0329967540
166UbiquitinationLFKKEPPKPPLNNFK
CCCCCCCCCCCCCCC
70.7229967540
173UbiquitinationKPPLNNFKVGMKLEA
CCCCCCCCCEEEEEE
39.7529967540
177SumoylationNNFKVGMKLEAIDKK
CCCCCEEEEEECCCC
36.93-
177SumoylationNNFKVGMKLEAIDKK
CCCCCEEEEEECCCC
36.93-
177UbiquitinationNNFKVGMKLEAIDKK
CCCCCEEEEEECCCC
36.9329967540
184SumoylationKLEAIDKKNPYLICP
EEEECCCCCCEEECC
60.45-
184SumoylationKLEAIDKKNPYLICP
EEEECCCCCCEEECC
60.45-
184UbiquitinationKLEAIDKKNPYLICP
EEEECCCCCCEEECC
60.4529967540
248UbiquitinationGTSVPIVKNIAKTES
CCCCCEEEEEECCCC
43.2729967540
252SumoylationPIVKNIAKTESSPSE
CEEEEEECCCCCHHH
49.37-
252SumoylationPIVKNIAKTESSPSE
CEEEEEECCCCCHHH
49.37-
253PhosphorylationIVKNIAKTESSPSEA
EEEEEECCCCCHHHH
31.8821712546
255PhosphorylationKNIAKTESSPSEASQ
EEEECCCCCHHHHHH
53.4325159151
256PhosphorylationNIAKTESSPSEASQH
EEECCCCCHHHHHHH
26.6423401153
258PhosphorylationAKTESSPSEASQHSM
ECCCCCHHHHHHHCC
47.9823401153
261PhosphorylationESSPSEASQHSMQSP
CCCHHHHHHHCCCCC
25.1125159151
264PhosphorylationPSEASQHSMQSPQKT
HHHHHHHCCCCCCCE
15.7523401153
267PhosphorylationASQHSMQSPQKTTLI
HHHHCCCCCCCEEEE
22.2125159151
271PhosphorylationSMQSPQKTTLILPTQ
CCCCCCCEEEEEECH
22.9127174698
272PhosphorylationMQSPQKTTLILPTQQ
CCCCCCEEEEEECHH
20.8827174698
277PhosphorylationKTTLILPTQQVRRSS
CEEEEEECHHHHHHC
28.3427174698
283PhosphorylationPTQQVRRSSRIKPPG
ECHHHHHHCCCCCCC
17.2629396449
284PhosphorylationTQQVRRSSRIKPPGP
CHHHHHHCCCCCCCC
35.8929396449
292PhosphorylationRIKPPGPTAVPKRSS
CCCCCCCCCCCCCCC
46.3229396449
296AcetylationPGPTAVPKRSSSVKN
CCCCCCCCCCCCCCC
59.317707299
296UbiquitinationPGPTAVPKRSSSVKN
CCCCCCCCCCCCCCC
59.3124816145
298PhosphorylationPTAVPKRSSSVKNIT
CCCCCCCCCCCCCCC
32.8426434776
299PhosphorylationTAVPKRSSSVKNITP
CCCCCCCCCCCCCCC
43.0918669648
300PhosphorylationAVPKRSSSVKNITPR
CCCCCCCCCCCCCCC
38.0523401153
302UbiquitinationPKRSSSVKNITPRKK
CCCCCCCCCCCCCCC
44.5829967540
305PhosphorylationSSSVKNITPRKKGPN
CCCCCCCCCCCCCCC
26.8323401153
318SumoylationPNSGKKEKPLPVICS
CCCCCCCCCCCEEEC
61.81-
318AcetylationPNSGKKEKPLPVICS
CCCCCCCCCCCEEEC
61.8125953088
318SumoylationPNSGKKEKPLPVICS
CCCCCCCCCCCEEEC
61.81-
326PhosphorylationPLPVICSTSAASLKS
CCCEEECCCCHHHHH
20.2719413330
332AcetylationSTSAASLKSLTRDRG
CCCCHHHHHHHCCCC
40.7125953088
332UbiquitinationSTSAASLKSLTRDRG
CCCCHHHHHHHCCCC
40.7132015554
333PhosphorylationTSAASLKSLTRDRGM
CCCHHHHHHHCCCCC
40.0220068231
335PhosphorylationAASLKSLTRDRGMLY
CHHHHHHHCCCCCCH
37.3020068231
343UbiquitinationRDRGMLYKDVASGPC
CCCCCCHHHHCCCCC
41.5929967540
374UbiquitinationFGPHLDPKRIQQLPD
CCCCCCHHHHHHCCC
62.9029967540
407AcetylationVDCALETKTVFGYLK
HHHHHHCCEEEEEEC
33.067987909
482AcetylationHSSAEHDKNQSAKED
CCCHHHCCCCCHHHH
59.8118526221
487SumoylationHDKNQSAKEDVTERQ
HCCCCCHHHHHHHHH
60.74-
487SumoylationHDKNQSAKEDVTERQ
HCCCCCHHHHHHHHH
60.74-
495PhosphorylationEDVTERQSTKRSPQQ
HHHHHHHHCCCCCCC
41.9623927012
496PhosphorylationDVTERQSTKRSPQQT
HHHHHHHCCCCCCCC
23.3423927012
499PhosphorylationERQSTKRSPQQTVPY
HHHHCCCCCCCCCCE
28.7222167270
503PhosphorylationTKRSPQQTVPYVVPL
CCCCCCCCCCEEEEC
20.4322167270
506PhosphorylationSPQQTVPYVVPLSPK
CCCCCCCEEEECCCC
15.1130266825
511PhosphorylationVPYVVPLSPKLPKTK
CCEEEECCCCCCCCH
17.5825159151
517PhosphorylationLSPKLPKTKEYASEG
CCCCCCCCHHHHCCC
27.4626074081
518SumoylationSPKLPKTKEYASEGE
CCCCCCCHHHHCCCC
55.6528112733
518UbiquitinationSPKLPKTKEYASEGE
CCCCCCCHHHHCCCC
55.6529967540
520PhosphorylationKLPKTKEYASEGEPL
CCCCCHHHHCCCCCC
19.5826074081
522PhosphorylationPKTKEYASEGEPLFA
CCCHHHHCCCCCCCC
45.2821815630
536SumoylationAGGSAIPKEENLSED
CCCCCCCCCCCCCCC
72.11-
536SumoylationAGGSAIPKEENLSED
CCCCCCCCCCCCCCC
72.1128112733
536UbiquitinationAGGSAIPKEENLSED
CCCCCCCCCCCCCCC
72.1129967540
544PhosphorylationEENLSEDSKSSSLNS
CCCCCCCCCCCCCCC
30.3120068231
545SumoylationENLSEDSKSSSLNSG
CCCCCCCCCCCCCCC
67.68-
545SumoylationENLSEDSKSSSLNSG
CCCCCCCCCCCCCCC
67.68-
545UbiquitinationENLSEDSKSSSLNSG
CCCCCCCCCCCCCCC
67.6832015554
546PhosphorylationNLSEDSKSSSLNSGN
CCCCCCCCCCCCCCC
29.1625627689
547PhosphorylationLSEDSKSSSLNSGNY
CCCCCCCCCCCCCCC
42.4525627689
548PhosphorylationSEDSKSSSLNSGNYL
CCCCCCCCCCCCCCC
38.3725627689
551PhosphorylationSKSSSLNSGNYLNPA
CCCCCCCCCCCCCHH
33.4428555341
564PhosphorylationPACRNPMYIHTSVSQ
HHHCCCEEEEEECCC
7.2729978859
567PhosphorylationRNPMYIHTSVSQDFS
CCCEEEEEECCCCCC
22.6729978859
568O-linked_GlycosylationNPMYIHTSVSQDFSR
CCEEEEEECCCCCCC
12.9530059200
568PhosphorylationNPMYIHTSVSQDFSR
CCEEEEEECCCCCCC
12.9528450419
570O-linked_GlycosylationMYIHTSVSQDFSRSV
EEEEEECCCCCCCCC
24.6530059200
570PhosphorylationMYIHTSVSQDFSRSV
EEEEEECCCCCCCCC
24.6517525332
574PhosphorylationTSVSQDFSRSVPGTT
EECCCCCCCCCCCCC
31.7528450419
576PhosphorylationVSQDFSRSVPGTTSS
CCCCCCCCCCCCCCC
31.3121712546
580PhosphorylationFSRSVPGTTSSPLVG
CCCCCCCCCCCCCCC
19.8921712546
581PhosphorylationSRSVPGTTSSPLVGD
CCCCCCCCCCCCCCC
32.8721712546
582PhosphorylationRSVPGTTSSPLVGDI
CCCCCCCCCCCCCCC
29.7825159151
583PhosphorylationSVPGTTSSPLVGDIS
CCCCCCCCCCCCCCC
21.8423401153
590PhosphorylationSPLVGDISPKSSPHE
CCCCCCCCCCCCCCC
30.8929255136
593PhosphorylationVGDISPKSSPHEVKF
CCCCCCCCCCCCCEE
53.1127362937
594PhosphorylationGDISPKSSPHEVKFQ
CCCCCCCCCCCCEEE
36.0827362937
599SumoylationKSSPHEVKFQMQRKS
CCCCCCCEEEEECCC
27.22-
599AcetylationKSSPHEVKFQMQRKS
CCCCCCCEEEEECCC
27.2226051181
599SumoylationKSSPHEVKFQMQRKS
CCCCCCCEEEEECCC
27.2228112733
599UbiquitinationKSSPHEVKFQMQRKS
CCCCCCCEEEEECCC
27.2232015554
605SumoylationVKFQMQRKSEAPSYI
CEEEEECCCCCCCEE
35.44-
605SumoylationVKFQMQRKSEAPSYI
CEEEEECCCCCCCEE
35.4428112733
605UbiquitinationVKFQMQRKSEAPSYI
CEEEEECCCCCCCEE
35.4429967540
606PhosphorylationKFQMQRKSEAPSYIA
EEEEECCCCCCCEEE
40.9725159151
610PhosphorylationQRKSEAPSYIAVPDP
ECCCCCCCEEECCCH
35.9029449344
611PhosphorylationRKSEAPSYIAVPDPS
CCCCCCCEEECCCHH
7.5827642862
621SumoylationVPDPSVLKQGFSKDP
CCCHHHHHCCCCCCC
46.34-
621UbiquitinationVPDPSVLKQGFSKDP
CCCHHHHHCCCCCCC
46.3429967540
663UbiquitinationRQHEIDGKALFLLKS
HHCCCCCEEEEEECH
37.8629967540
670PhosphorylationKALFLLKSDVMMKYM
EEEEEECHHHHHHHC
35.0921406692
680SumoylationMMKYMGLKLGPALKL
HHHHCCCCHHHHHHH
45.74-
680SumoylationMMKYMGLKLGPALKL
HHHHCCCCHHHHHHH
45.74-
693AcetylationKLCYYIEKLKEGKYS
HHHHHHHHHHCCCCC
56.1326051181

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
267SPhosphorylationKinaseCDK1P06493
PSP
267SPhosphorylationKinaseCDK2P24941
PSP
305TPhosphorylationKinaseCDK1P06493
PSP
305TPhosphorylationKinaseCDK2P24941
PSP
511SPhosphorylationKinaseCDK1P06493
PSP
511SPhosphorylationKinaseCDK2P24941
PSP
590SPhosphorylationKinaseCDK1P06493
PSP
590SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCML2_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 SCML2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG1_HUMANBAG1physical
26344197
UBP7_HUMANUSP7physical
25605328

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 SCML2_HUMAN

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Related Literatures of Post-Translational Modification
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-499; TYR-506; SER-511AND SER-590, AND MASS SPECTROMETRY.
"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-253; SER-255; SER-267;SER-499; THR-503; TYR-506; SER-511; SER-582; SER-583 AND SER-590, ANDMASS 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-256; SER-258; SER-267;SER-299; SER-300; THR-305; SER-499; THR-503; SER-511; SER-576;SER-583; SER-590 AND SER-594, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASSSPECTROMETRY.

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