SMC6_HUMAN - dbPTM
SMC6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMC6_HUMAN
UniProt AC Q96SB8
Protein Name Structural maintenance of chromosomes protein 6
Gene Name SMC6
Organism Homo sapiens (Human).
Sequence Length 1091
Subcellular Localization Nucleus . Nucleus speckle . Chromosome . Nucleus, PML body . Chromosome, telomere . Colocalizes with SMC5 on the X-Y chromosome pair within the sex vesicle during late pachytene/diplotene (By similarity). Localizes to PML nuclear bodies in ALT cell l
Protein Description Core component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome. [PubMed: 26983541]
Protein Sequence MAKRKEENFSSPKNAKRPRQEELEDFDKDGDEDECKGTTLTAAEVGIIESIHLKNFMCHSMLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFVKDGQNSADISITLRNRGDDAFKASVYGNSILIQQHISIDGSRSYKLKSATGSVVSTRKEELIAILDHFNIQVDNPVSVLTQEMSKQFLQSKNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAWAVVNEIEKQLNAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRSLNEYKALKKDDEQLCKRIEELKKSTDQSLEPERLERQKKISWLKERVKAFQNQENSVNQEIEQFQQAIEKDKEEHGKIKREELDVKHALSYNQRQLKELKDSKTDRLKRFGPNVPALLEAIDDAYRQGHFTYKPVGPLGACIHLRDPELALAIESCLKGLLQAYCCHNHADERVLQALMKRFYLPGTSRPPIIVSEFRNEIYDVRHRAAYHPDFPTVLTALEIDNAVVANSLIDMRGIETVLLIKNNSVARAVMQSQKPPKNCREAFTADGDQVFAGRYYSSENTRPKFLSRDVDSEISDLENEVENKTAQILNLQQHLSALEKDIKHNEELLKRCQLHYKELKMKIRKNISEIRELENIEEHQSVDIATLEDEAQENKSKMKMVEEHMEQQKENMEHLKSLKIEAENKYDAIKFKINQLSELADPLKDELNLADSEVDNQKRGKRHYEEKQKEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMRQYQEARETYLDLDSKVRTLKKFIKLLGEIMEHRFKTYQQFRRCLTLRCKLYFDNLLSQRAYCGKMNFDHKNETLSISVQPGEGNKAAFNDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLILKMADSQRFRQFILLTPQSMSSLPSSKLIRILRMSDPERGQTTLPFRPVTQEEDDDQR
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
10PhosphorylationKRKEENFSSPKNAKR
CCCCCCCCCCCCCCC		58.2626462736
11PhosphorylationRKEENFSSPKNAKRP
CCCCCCCCCCCCCCC		35.4425159151
107UbiquitinationTNRGSSLKGFVKDGQ
CCCCCCCCCEEECCC		52.85-
111UbiquitinationSSLKGFVKDGQNSAD
CCCCCEEECCCCCCE		54.6121906983
111 (in isoform 1)Ubiquitination-54.6121890473
122PhosphorylationNSADISITLRNRGDD
CCCEEEEEEEECCCC		16.9324719451
137 (in isoform 2)Ubiquitination-21.1821890473
153PhosphorylationISIDGSRSYKLKSAT
EECCCCCCEEECCCC		28.4628634120
154PhosphorylationSIDGSRSYKLKSATG
ECCCCCCEEECCCCC		21.16-
157UbiquitinationGSRSYKLKSATGSVV
CCCCEEECCCCCCEE		33.61-
158PhosphorylationSRSYKLKSATGSVVS
CCCEEECCCCCCEEE		41.31-
160PhosphorylationSYKLKSATGSVVSTR
CEEECCCCCCEEECC		36.7628634120
162PhosphorylationKLKSATGSVVSTRKE
EECCCCCCEEECCHH		18.2628634120
165O-linked_GlycosylationSATGSVVSTRKEELI
CCCCCEEECCHHHHH		21.9730379171
165PhosphorylationSATGSVVSTRKEELI
CCCCCEEECCHHHHH		21.9728634120
166PhosphorylationATGSVVSTRKEELIA
CCCCEEECCHHHHHH		33.8628634120
201UbiquitinationSKQFLQSKNEGDKYK
HHHHHHCCCCCHHHH		46.16-
206AcetylationQSKNEGDKYKFFMKA
HCCCCCHHHHHHHHH		62.2819826953
208AcetylationKNEGDKYKFFMKATQ
CCCCHHHHHHHHHHH		37.5519826963
212AcetylationDKYKFFMKATQLEQM
HHHHHHHHHHHHHHH		43.0319826973
220UbiquitinationATQLEQMKEDYSYIM
HHHHHHHHHHHCHHH		47.3221906983
220 (in isoform 1)Ubiquitination-47.3221890473
223PhosphorylationLEQMKEDYSYIMETK
HHHHHHHHCHHHHCH		12.40-
225PhosphorylationQMKEDYSYIMETKER
HHHHHHCHHHHCHHH		9.69-
230UbiquitinationYSYIMETKERTKEQI
HCHHHHCHHHHHHHH		31.7121890473
230 (in isoform 1)Ubiquitination-31.7121890473
246 (in isoform 2)Ubiquitination-57.8121890473
248UbiquitinationEERLTELKRQCVEKE
HHHHHHHHHHHHHHH		33.90-
254AcetylationLKRQCVEKEERFQSI
HHHHHHHHHHHHHHH		44.4725953088
256 (in isoform 2)Ubiquitination-70.6221890473
260PhosphorylationEKEERFQSIAGLSTM
HHHHHHHHHHHHHHH		16.2221406692
265PhosphorylationFQSIAGLSTMKTNLE
HHHHHHHHHHCHHHH		26.0725159151
266PhosphorylationQSIAGLSTMKTNLES
HHHHHHHHHCHHHHH		27.9426270265
268AcetylationIAGLSTMKTNLESLK
HHHHHHHCHHHHHHH		34.0625953088
268SumoylationIAGLSTMKTNLESLK
HHHHHHHCHHHHHHH		34.0628112733
268UbiquitinationIAGLSTMKTNLESLK
HHHHHHHCHHHHHHH		34.0621890473
268 (in isoform 1)Ubiquitination-34.0621890473
275UbiquitinationKTNLESLKHEMAWAV
CHHHHHHHHHHHHHH		46.96-
286 (in isoform 2)Phosphorylation-7.2721406692
291PhosphorylationNEIEKQLNAIRDNIK
HHHHHHHHHHHHHCC		30.7222067460
294 (in isoform 2)Ubiquitination-28.6321890473
350AcetylationAPECMALKADVVAKK
CHHHHHHCCHHHHHC		32.7625953088
375UbiquitinationNRSLNEYKALKKDDE
HCCHHHHHHHCCCHH		40.85-
386 (in isoform 2)Phosphorylation-66.0727642862
393AcetylationKRIEELKKSTDQSLE
HHHHHHHHHCCCCCC		71.8125038526
393 (in isoform 2)Phosphorylation-71.8127642862
418UbiquitinationSWLKERVKAFQNQEN
HHHHHHHHHHHCCCH		50.10-
456UbiquitinationKREELDVKHALSYNQ
CHHHHHHHHHHCCCH		23.87-
658AcetylationSSENTRPKFLSRDVD
CCCCCCCCCCCCCCH		56.5025953088
658UbiquitinationSSENTRPKFLSRDVD
CCCCCCCCCCCCCCH		56.5021890473
658 (in isoform 1)Ubiquitination-56.5021890473
661PhosphorylationNTRPKFLSRDVDSEI
CCCCCCCCCCCHHHH		29.5723090842
666PhosphorylationFLSRDVDSEISDLEN
CCCCCCHHHHHHHHH		36.3630175587
669PhosphorylationRDVDSEISDLENEVE
CCCHHHHHHHHHHHH		31.9025159151
684 (in isoform 2)Ubiquitination-37.1221890473
694UbiquitinationQHLSALEKDIKHNEE
HHHHHHHHHHHCHHH		66.65-
695PhosphorylationHLSALEKDIKHNEEL
HHHHHHHHHHCHHHH		45.8822067460
722PhosphorylationMKIRKNISEIRELEN
HHHHHCHHHHHHHCC		36.0424719451
773SumoylationMEHLKSLKIEAENKY
HHHHHHCHHHHHCHH		45.66-
773AcetylationMEHLKSLKIEAENKY
HHHHHHCHHHHHCHH		45.6625953088
773SumoylationMEHLKSLKIEAENKY
HHHHHHCHHHHHCHH		45.6628112733
780PhosphorylationKIEAENKYDAIKFKI
HHHHHCHHHHHHHHH		23.3725839225
784AcetylationENKYDAIKFKINQLS
HCHHHHHHHHHHHHH		42.1823749302
784UbiquitinationENKYDAIKFKINQLS
HCHHHHHHHHHHHHH		42.18-
786UbiquitinationKYDAIKFKINQLSEL
HHHHHHHHHHHHHHH		35.4321890473
786 (in isoform 1)Ubiquitination-35.4321890473
798UbiquitinationSELADPLKDELNLAD
HHHCHHHHHHHCCCC		55.32-
806 (in isoform 2)Phosphorylation-33.6327642862
812UbiquitinationDSEVDNQKRGKRHYE
CHHHHHHHHCHHHHH		70.17-
812 (in isoform 2)Ubiquitination-70.1721890473
828PhosphorylationKQKEHLDTLNKKKRE
HHHHHHHHHHHHHHH		38.29-
831UbiquitinationEHLDTLNKKKRELDM
HHHHHHHHHHHHHHH		63.89-
862UbiquitinationPERIEVEKSASILDK
HHHHHHHHHHHHHHH		57.4021890473
862 (in isoform 1)Ubiquitination-57.4021890473
863PhosphorylationERIEVEKSASILDKE
HHHHHHHHHHHHHHH		17.4730108239
865PhosphorylationIEVEKSASILDKEIN
HHHHHHHHHHHHHHH		30.6730108239
869UbiquitinationKSASILDKEINRLRQ
HHHHHHHHHHHHHHH		57.98-
888 (in isoform 2)Ubiquitination-48.3021890473
902PhosphorylationYQEARETYLDLDSKV
HHHHHHHHCCCHHHH		8.08-
907PhosphorylationETYLDLDSKVRTLKK
HHHCCCHHHHHHHHH		40.11-
908UbiquitinationTYLDLDSKVRTLKKF
HHCCCHHHHHHHHHH		35.09-
917AcetylationRTLKKFIKLLGEIME
HHHHHHHHHHHHHHH		40.5725953088
917UbiquitinationRTLKKFIKLLGEIME
HHHHHHHHHHHHHHH		40.5721890473
917 (in isoform 1)Ubiquitination-40.5721890473
928UbiquitinationEIMEHRFKTYQQFRR
HHHHHHHHHHHHHHH		46.4021890473
928 (in isoform 1)Ubiquitination-46.4021890473
938PhosphorylationQQFRRCLTLRCKLYF
HHHHHHHHHHHHHHH		18.7830177828
943 (in isoform 2)Ubiquitination-6.2021890473
944PhosphorylationLTLRCKLYFDNLLSQ
HHHHHHHHHHCHHHC		8.3830177828
950PhosphorylationLYFDNLLSQRAYCGK
HHHHCHHHCCEEECC		22.3024719451
954 (in isoform 2)Ubiquitination-12.1521890473
978UbiquitinationVQPGEGNKAAFNDMR
ECCCCCCCHHHHCCC		52.5321906983
978 (in isoform 1)Ubiquitination-52.5321890473
1004 (in isoform 2)Ubiquitination-5.5921890473
1035UbiquitinationIAMDLILKMADSQRF
HHHHHHHHHHCCHHH		25.66-
1039PhosphorylationLILKMADSQRFRQFI
HHHHHHCCHHHHHHH		17.4520068231
1049PhosphorylationFRQFILLTPQSMSSL
HHHHHHHCCCCHHCC		18.8121406692
1052PhosphorylationFILLTPQSMSSLPSS
HHHHCCCCHHCCCHH		23.1021406692
1054PhosphorylationLLTPQSMSSLPSSKL
HHCCCCHHCCCHHHH		33.6921406692
1055PhosphorylationLTPQSMSSLPSSKLI
HCCCCHHCCCHHHHH		35.3421406692
1058PhosphorylationQSMSSLPSSKLIRIL
CCHHCCCHHHHHHHH		45.4521406692
1059PhosphorylationSMSSLPSSKLIRILR
CHHCCCHHHHHHHHC		29.5521406692
1060AcetylationMSSLPSSKLIRILRM
HHCCCHHHHHHHHCC		52.8825953088
1060UbiquitinationMSSLPSSKLIRILRM
HHCCCHHHHHHHHCC		52.8821890473
1060 (in isoform 1)Ubiquitination-52.8821890473
1068PhosphorylationLIRILRMSDPERGQT
HHHHHCCCCCCCCCC		43.5123186163
1075PhosphorylationSDPERGQTTLPFRPV
CCCCCCCCCCCCCCC		32.8823186163
1076PhosphorylationDPERGQTTLPFRPVT
CCCCCCCCCCCCCCC		25.2523186163
1083PhosphorylationTLPFRPVTQEEDDDQ
CCCCCCCCCCCCCCC		32.7122817901
1086 (in isoform 2)Ubiquitination-57.8521890473
1091MethylationQEEDDDQR-------
CCCCCCCC-------		56.3429161005
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
-KUbiquitinationE3 ubiquitin ligaseXP03165
PMID:32235678
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMC6_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 SMC6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMC5_HUMANSMC5physical
11408570
NSE1_HUMANNSMCE1physical
18086888
NSE2_HUMANNSMCE2physical
18086888
SMC5_HUMANSMC5physical
18086888
SMC6_HUMANSMC6physical
18086888
NSE4A_HUMANNSMCE4Aphysical
18086888
NSE3_HUMANNDNL2physical
18086888
SMC5_HUMANSMC5physical
26344197
TISD_HUMANZFP36L2physical
26496610
BTF3_HUMANBTF3physical
26496610
SCRB2_HUMANSCARB2physical
26496610
HEXB_HUMANHEXBphysical
26496610
SMBP2_HUMANIGHMBP2physical
26496610
LAMA2_HUMANLAMA2physical
26496610
KI67_HUMANMKI67physical
26496610
TP53B_HUMANTP53BP1physical
26496610
TTC3_HUMANTTC3physical
26496610
IFT88_HUMANIFT88physical
26496610
CEPT1_HUMANCEPT1physical
26496610
PRDX3_HUMANPRDX3physical
26496610
HPS5_HUMANHPS5physical
26496610
KIF1B_HUMANKIF1Bphysical
26496610
SMC5_HUMANSMC5physical
26496610
ASCC1_HUMANASCC1physical
26496610
GPN3_HUMANGPN3physical
26496610
CC174_HUMANCCDC174physical
26496610
SPN90_HUMANNCKIPSDphysical
26496610
DGCR8_HUMANDGCR8physical
26496610
NSE4A_HUMANNSMCE4Aphysical
26496610
TTC19_HUMANTTC19physical
26496610
HEAT1_HUMANHEATR1physical
26496610
ELP3_HUMANELP3physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
SLF2_HUMANFAM178Aphysical
26496610
TM165_HUMANTMEM165physical
26496610
NSE3_HUMANNDNL2physical
26496610
RAD18_HUMANRAD18physical
26496610
KLC2_HUMANKLC2physical
26496610
T126A_HUMANTMEM126Aphysical
26496610
SLF1_HUMANANKRD32physical
26496610
MAK16_HUMANMAK16physical
26496610
MUM1_HUMANMUM1physical
26496610
ESCO1_HUMANESCO1physical
26496610
B3GLT_HUMANB3GALTLphysical
26496610
NSE1_HUMANNSMCE1physical
26496610
NSE2_HUMANNSMCE2physical
26496610
ZBED6_HUMANZBED6physical
26496610
IFT25_HUMANHSPB11physical
27173435
IFT27_HUMANIFT27physical
27173435
HSF1_HUMANHSF1physical
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 SMC6_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-666 AND SER-669, ANDMASS SPECTROMETRY.

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