TONSL_HUMAN - dbPTM
TONSL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TONSL_HUMAN
UniProt AC Q96HA7
Protein Name Tonsoku-like protein
Gene Name TONSL
Organism Homo sapiens (Human).
Sequence Length 1378
Subcellular Localization Cytoplasm. Nucleus. Mainly nuclear. Localizes to DNA damage sites, accumulates at stressed replication forks.
Protein Description Component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork-associated double-strand breaks. It may act by mediating the assembly of RAD51 filaments on ssDNA. Within the complex, may act as a scaffold..
Protein Sequence MSLERELRQLSKAKAKAQRAGQRREEAALCHQLGELLAGHGRYAEALEQHWQELQLRERADDPLGCAVAHRKIGERLAEMEDYPAALQHQHQYLELAHSLRNHTELQRAWATIGRTHLDIYDHCQSRDALLQAQAAFEKSLAIVDEELEGTLAQGELNEMRTRLYLNLGLTFESLQQTALCNDYFRKSIFLAEQNHLYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARECAHTMRKRFMESECCVVIAQVLQDLGDFLAAKRALKKAYRLGSQKPVQRAAICQNLQHVLAVVRLQQQLEEAEGRDPQGAMVICEQLGDLFSKAGDFPRAAEAYQKQLRFAELLDRPGAERAIIHVSLATTLGDMKDHHGAVRHYEEELRLRSGNVLEEAKTWLNIALSREEAGDAYELLAPCFQKALSCAQQAQRPQLQRQVLQHLHTVQLRLQPQEAPETETRLRELSVAEDEDEEEEAEEAAATAESEALEAGEVELSEGEDDTDGLTPQLEEDEELQGHLGRRKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLETLQQWVKLYRRDLDLETRQKARAMEMLLQAAASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPGQAAPAMARPRRSRHGPASSSSSSEGEDSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPEEECLAGDWLELDMPLTRSRRPRPRGTGDNRRPSSTSGSDSEESRPRARAKQVRLTCMQSCSAPVNAGPSSLASEPPGSPSTPRVSEPSGDSSAAGQPLGPAPPPPIRVRVQVQDHLFLIPVPHSSDTHSVAWLAEQAAQRYYQTCGLLPRLTLRKEGALLAPQDLIPDVLQSNDEVLAEVTSWDLPPLTDRYRRACQSLGQGEHQQVLQAVELQGLGLSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPGQATLQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFLSHQTALGSAFQDAEHLKTLSLSYNALGAPALARTLQSLPAGTLLHLELSSVAAGKGDSDLMEPVFRYLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLISLDLSANPEISCASLEELLSTLQKRPQGLSFLGLSGCAVQGPLGLGLWDKIAAQLRELQLCSRRLCAEDRDALRQLQPSRPGPGECTLDHGSKLFFRRL
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
2Acetylation------MSLERELRQ
------CCHHHHHHH		50.6819413330
2Phosphorylation------MSLERELRQ
------CCHHHHHHH		50.6827067055
2O-linked_Glycosylation------MSLERELRQ
------CCHHHHHHH		50.6830379171
187UbiquitinationLCNDYFRKSIFLAEQ
HCCHHHHHHHHHHHC		37.70-
275UbiquitinationAYRLGSQKPVQRAAI
HHHHCCCCHHHHHHH		49.1822817900
275 (in isoform 2)Ubiquitination-49.1821906983
275 (in isoform 1)Ubiquitination-49.1821906983
322PhosphorylationEQLGDLFSKAGDFPR
HHHHHHHHHCCCCHH		28.9724719451
323UbiquitinationQLGDLFSKAGDFPRA
HHHHHHHHCCCCHHH		49.4021963094
334PhosphorylationFPRAAEAYQKQLRFA
CHHHHHHHHHHHHHH		14.03-
336UbiquitinationRAAEAYQKQLRFAEL
HHHHHHHHHHHHHHH		38.3329967540
399PhosphorylationTWLNIALSREEAGDA
HHHHHHHCHHHHCCH		28.7324719451
407PhosphorylationREEAGDAYELLAPCF
HHHHCCHHHHHHHHH		16.3227642862
416UbiquitinationLLAPCFQKALSCAQQ
HHHHHHHHHHHHHHH		30.92-
623PhosphorylationLLLERGASVTLRTRK
HHHHCCCCEEEECCC		20.6129449344
625PhosphorylationLERGASVTLRTRKGL
HHCCCCEEEECCCCC		14.1824719451
628PhosphorylationGASVTLRTRKGLSPL
CCCEEEECCCCCCHH		39.58-
643UbiquitinationETLQQWVKLYRRDLD
HHHHHHHHHHHCCCC		36.5229967540
669PhosphorylationMLLQAAASGQDPHSS
HHHHHHHCCCCCCCC		32.0628348404
675PhosphorylationASGQDPHSSQAFHTP
HCCCCCCCCCCCCCC		29.5428348404
676PhosphorylationSGQDPHSSQAFHTPS
CCCCCCCCCCCCCCH		23.6128348404
683PhosphorylationSQAFHTPSSLLFDPE
CCCCCCCHHHCCCCC		34.4728348404
684PhosphorylationQAFHTPSSLLFDPET
CCCCCCHHHCCCCCC		30.2328348404
691PhosphorylationSLLFDPETSPPLSPC
HHCCCCCCCCCCCCC		52.5028348404
692PhosphorylationLLFDPETSPPLSPCP
HCCCCCCCCCCCCCC		23.9028464451
696PhosphorylationPETSPPLSPCPEPPS
CCCCCCCCCCCCCCC		30.1725137130
712PhosphorylationSTRLPEASQAHVRVS
CCCCCHHHHCCEECC		26.6622210691
719PhosphorylationSQAHVRVSPGQAAPA
HHCCEECCCCCCCCC		16.8523401153
727SulfoxidationPGQAAPAMARPRRSR
CCCCCCCCCCCCCCC		2.9421406390
733PhosphorylationAMARPRRSRHGPASS
CCCCCCCCCCCCCCC		29.8824719451
739PhosphorylationRSRHGPASSSSSSEG
CCCCCCCCCCCCCCC		33.6120363803
740PhosphorylationSRHGPASSSSSSEGE
CCCCCCCCCCCCCCC		36.0220363803
741PhosphorylationRHGPASSSSSSEGED
CCCCCCCCCCCCCCC		31.5720363803
742PhosphorylationHGPASSSSSSEGEDS
CCCCCCCCCCCCCCC		39.5720363803
743PhosphorylationGPASSSSSSEGEDSA
CCCCCCCCCCCCCCC		34.0620363803
744PhosphorylationPASSSSSSEGEDSAG
CCCCCCCCCCCCCCC		52.1220363803
749PhosphorylationSSSEGEDSAGPARPS
CCCCCCCCCCCCCCC		30.7230177828
756PhosphorylationSAGPARPSQKRPRCS
CCCCCCCCCCCCCCC		42.6630177828
773PhosphorylationAQRVAAWTPGPASNR
HHHHHHCCCCCCCHH		17.4021815630
778PhosphorylationAWTPGPASNREAATA
HCCCCCCCHHHHHHH		39.2824532841
784PhosphorylationASNREAATASTSRAA
CCHHHHHHHHHHHHH		28.3422210691
788PhosphorylationEAATASTSRAAYQAA
HHHHHHHHHHHHHHH		19.8924532841
792PhosphorylationASTSRAAYQAAIRGV
HHHHHHHHHHHHHCC		9.5622210691
797MethylationAAYQAAIRGVGSAQS
HHHHHHHHCCCCCHH		29.0830988645
801PhosphorylationAAIRGVGSAQSRLGP
HHHHCCCCCHHHCCC		22.2622210691
804PhosphorylationRGVGSAQSRLGPGPP
HCCCCCHHHCCCCCC		29.2322210691
812MethylationRLGPGPPRGHSKALA
HCCCCCCCCCCCCCC		59.60115484915
860PhosphorylationTGDNRRPSSTSGSDS
CCCCCCCCCCCCCCC		44.4223663014
861PhosphorylationGDNRRPSSTSGSDSE
CCCCCCCCCCCCCCH		29.3123663014
862PhosphorylationDNRRPSSTSGSDSEE
CCCCCCCCCCCCCHH		41.2523663014
863PhosphorylationNRRPSSTSGSDSEES
CCCCCCCCCCCCHHC		37.9423663014
865PhosphorylationRPSSTSGSDSEESRP
CCCCCCCCCCHHCCH		37.4223663014
867PhosphorylationSSTSGSDSEESRPRA
CCCCCCCCHHCCHHH		44.9823663014
870PhosphorylationSGSDSEESRPRARAK
CCCCCHHCCHHHHHH		43.4623663014
882PhosphorylationRAKQVRLTCMQSCSA
HHHHHHHHHHHHCCC		8.7228450419
886PhosphorylationVRLTCMQSCSAPVNA
HHHHHHHHCCCCCCC		5.3328450419
888PhosphorylationLTCMQSCSAPVNAGP
HHHHHHCCCCCCCCC		40.6328450419
896PhosphorylationAPVNAGPSSLASEPP
CCCCCCCHHHCCCCC		36.7530266825
897PhosphorylationPVNAGPSSLASEPPG
CCCCCCHHHCCCCCC		30.9630266825
900PhosphorylationAGPSSLASEPPGSPS
CCCHHHCCCCCCCCC		56.8030266825
905PhosphorylationLASEPPGSPSTPRVS
HCCCCCCCCCCCCCC		22.8130266825
907PhosphorylationSEPPGSPSTPRVSEP
CCCCCCCCCCCCCCC		53.3830266825
908PhosphorylationEPPGSPSTPRVSEPS
CCCCCCCCCCCCCCC		20.6430266825
909UbiquitinationPPGSPSTPRVSEPSG
CCCCCCCCCCCCCCC		38.7321963094
912PhosphorylationSPSTPRVSEPSGDSS
CCCCCCCCCCCCCCC		45.1026714015
912O-linked_GlycosylationSPSTPRVSEPSGDSS
CCCCCCCCCCCCCCC		45.1030379171
915PhosphorylationTPRVSEPSGDSSAAG
CCCCCCCCCCCCCCC		51.7026714015
918PhosphorylationVSEPSGDSSAAGQPL
CCCCCCCCCCCCCCC		25.9626714015
919PhosphorylationSEPSGDSSAAGQPLG
CCCCCCCCCCCCCCC		27.2128555341
921UbiquitinationPSGDSSAAGQPLGPA
CCCCCCCCCCCCCCC		21.0721963094
1070PhosphorylationLRALKLHTALRELRL
HHHHHHHHHHHHHHH		37.5124719451
1198PhosphorylationLKTLSLSYNALGAPA
HHHHCCCHHCCCHHH		15.1120068231
1245UbiquitinationPVFRYLAKEGCALAH
HHHHHHHHHCCHHHH		52.6321963094
1263UbiquitinationSANHLGDKAVRDLCR
CCCHHCHHHHHHHHH		47.1629967540
1273PhosphorylationRDLCRCLSLCPSLIS
HHHHHHHHHCCHHHC		31.3922468782
1277PhosphorylationRCLSLCPSLISLDLS
HHHHHCCHHHCCCCC		37.0222468782
1293PhosphorylationNPEISCASLEELLST
CCCCCHHHHHHHHHH		40.4122468782
1329AcetylationLGLGLWDKIAAQLRE
CCCCHHHHHHHHHHH		23.74156183
1341PhosphorylationLRELQLCSRRLCAED
HHHHHHHHHHHCCCC		29.0930576142
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 TONSL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TONSL_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 TONSL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TONSL_HUMANTONSLphysical
21055985
MMS22_HUMANMMS22Lphysical
21055985
SP16H_HUMANSUPT16Hphysical
21055985
SSRP1_HUMANSSRP1physical
21055985
MCM2_HUMANMCM2physical
21055985
MCM3_HUMANMCM3physical
21055985
MCM4_HUMANMCM4physical
21055985
MCM5_HUMANMCM5physical
21055985
MCM6_HUMANMCM6physical
21055985
MCM7_HUMANMCM7physical
21055985
TONSL_HUMANTONSLphysical
21113133
MMS22_HUMANMMS22Lphysical
21113133
XRCC6_HUMANXRCC6physical
21113133
MCM2_HUMANMCM2physical
21113133
H2B1L_HUMANHIST1H2BLphysical
21113133
SGT1_HUMANSUGT1physical
21113133
XRCC5_HUMANXRCC5physical
21113133
MPCP_HUMANSLC25A3physical
21113133
H12_HUMANHIST1H1Cphysical
21113133
H2A1B_HUMANHIST1H2AEphysical
21113133
ASF1A_HUMANASF1Aphysical
21113133
ADT2_HUMANSLC25A5physical
21113133
MCM6_HUMANMCM6physical
21113133
SSRP1_HUMANSSRP1physical
21113133
MCM4_HUMANMCM4physical
21113133
ASF1B_HUMANASF1Bphysical
21113133
SP16H_HUMANSUPT16Hphysical
21113133
AIFM1_HUMANAIFM1physical
21113133
H15_HUMANHIST1H1Bphysical
21113133
SCC4_HUMANMAU2physical
22939629
MMS22_HUMANMMS22Lphysical
21055984
ASF1A_HUMANASF1Aphysical
21055984
ASF1B_HUMANASF1Bphysical
21055984
MCM2_HUMANMCM2physical
21055984
MCM6_HUMANMCM6physical
21055984
H31T_HUMANHIST3H3physical
21055984
BRCA1_HUMANBRCA1genetic
25184681
BRCA1_HUMANBRCA1physical
25184681
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 TONSL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-719, AND MASSSPECTROMETRY.

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