SLF1_HUMAN - dbPTM
SLF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLF1_HUMAN
UniProt AC Q9BQI6
Protein Name SMC5-SMC6 complex localization factor protein 1 {ECO:0000312|HGNC:HGNC:25408}
Gene Name SLF1 {ECO:0000303|PubMed:25931565, ECO:0000312|HGNC:HGNC:25408}
Organism Homo sapiens (Human).
Sequence Length 1058
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Relocalizes with RAD18 to nuclear foci in response to DNA damage. Colocalizes with RAD18 in the nucleus and to centrosomes (By similarity). Associates with chr
Protein Description Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. [PubMed: 25931565 The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks]
Protein Sequence MEDGTPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETTYEWGYKIEKDSRYSPQMQSAPKRWREELKRTGAPGAFHRWKVVLLVRTDKRSDSLIRVLEAGKANVILPKSSPSGITHVIASNARIKAEKEKDNFKAPFYPIQYLGDFLLEKEIQNDEDSQTNSVWTEHSNEETNKDFRKDAGFLEMKGALRETMYRTQKEMQNHEDVNVGSILIQHHKKEKFSGSSKDLKFVKMRNTFGSHTYENQKEIKKKDEDIQRSYTLRRKRKKGKESNCKKGVEHEKIKSTLRRHIYNRDQKEMKNSIFAEYAKESKAMAIKTDVDVVEIKNTLRKHIYRAQAVRYNCIRIDKQPVYNVEVKNAEFPRGVLNLIESLIEGHFFKEAIEELSTLQAHYIPPVCVLHALLENVLQDNIDTFSGRYFHILSALLHLHPPWKSPAMSRYYLELFQCPTCMKGAWSLVEVLIRSCLFNESFCHQISENIGSKVLHLTLLKFFFNLIESEVQHLSQKLYDWSDSQNLKITGKAMLLEIFWSGSETSGLLTKPVNMLLEWTIYSHKEKFKSNDVFKHELAYLLAGILGAAIDYWIFLGLKMGRNVMRHMSDDLGSYVSLSCDDFSSQELEIFICSFSSSWLQMFVAEAVFKKLCLQSSGSVSSEPLSLQKMVYSYLPALGKTGVLGSGKIQVSKKIGQRPCFDSQRTLLMLNGTKQKQVEGLPELLDLNLAKCSSSLKKLKKKSEGELSCSKENCPSVVKKMNFHKTNLKGETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQHGGPVLLQQRNAKGELPLDYVVSPQIKEELFAITKIEDTVENFHAQAEKHFHYQQLEFGSFLLSRMLLNFCSIFDLSSEFILASKGLTHLNELLMACKSHKETTSVHTDWLLDLYAGNIKTLQKLPHILKELPENLKVCPGVHTEALMITLEMMCRSVMEFS
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
7Ubiquitination-MEDGTPKHIIQMTG
-CCCCCCCHHEEECC
-
7Ubiquitination-MEDGTPKHIIQMTG
-CCCCCCCHHEEECC
-
16AcetylationIIQMTGFKMEEKEAL
HEEECCCCHHHHHHH
7369645
25UbiquitinationEEKEALVKLLLKLDC
HHHHHHHHHHHHCCC
-
25AcetylationEEKEALVKLLLKLDC
HHHHHHHHHHHHCCC
7369655
36UbiquitinationKLDCTFIKSEKYKNC
HCCCCEECCHHHCCC
-
36UbiquitinationKLDCTFIKSEKYKNC
HCCCCEECCHHHCCC
-
41UbiquitinationFIKSEKYKNCTHLIA
EECCHHHCCCHHHHH
-
44PhosphorylationSEKYKNCTHLIAERL
CHHHCCCHHHHHHHH
17192257
56UbiquitinationERLCKSEKFLAACAA
HHHHCCHHHHHHHHC
-
78SumoylationDYIIHSAKSGRWLDE
CEEEEECCCCCCCCC
-
78UbiquitinationDYIIHSAKSGRWLDE
CEEEEECCCCCCCCC
-
78SumoylationDYIIHSAKSGRWLDE
CEEEEECCCCCCCCC
-
78UbiquitinationDYIIHSAKSGRWLDE
CEEEEECCCCCCCCC
-
101PhosphorylationIEKDSRYSPQMQSAP
CCCCCCCCCCCCCCC
28985074
106PhosphorylationRYSPQMQSAPKRWRE
CCCCCCCCCCHHHHH
28985074
109UbiquitinationPQMQSAPKRWREELK
CCCCCCCHHHHHHHH
-
109UbiquitinationPQMQSAPKRWREELK
CCCCCCCHHHHHHHH
-
141PhosphorylationRTDKRSDSLIRVLEA
EECCCCHHHHHHHHC
24719451
150UbiquitinationIRVLEAGKANVILPK
HHHHHCCCCCEEECC
-
157UbiquitinationKANVILPKSSPSGIT
CCCEEECCCCCCCCC
-
158PhosphorylationANVILPKSSPSGITH
CCEEECCCCCCCCCH
25159151
159PhosphorylationNVILPKSSPSGITHV
CEEECCCCCCCCCHH
25159151
161PhosphorylationILPKSSPSGITHVIA
EECCCCCCCCCHHHH
23911959
164PhosphorylationKSSPSGITHVIASNA
CCCCCCCCHHHHCCC
23663014
183SumoylationEKEKDNFKAPFYPIQ
HHHHCCCCCCCCCHH
-
183SumoylationEKEKDNFKAPFYPIQ
HHHHCCCCCCCCCHH
-
223UbiquitinationHSNEETNKDFRKDAG
CCCCCCCHHHHHHHH
-
227UbiquitinationETNKDFRKDAGFLEM
CCCHHHHHHHHHHHH
-
235SumoylationDAGFLEMKGALRETM
HHHHHHHHHHHHHHH
-
235UbiquitinationDAGFLEMKGALRETM
HHHHHHHHHHHHHHH
-
235SumoylationDAGFLEMKGALRETM
HHHHHHHHHHHHHHH
-
235MethylationDAGFLEMKGALRETM
HHHHHHHHHHHHHHH
-
241PhosphorylationMKGALRETMYRTQKE
HHHHHHHHHHHHHHH
25954137
247UbiquitinationETMYRTQKEMQNHED
HHHHHHHHHHCCCCC
-
275UbiquitinationEKFSGSSKDLKFVKM
CCCCCCCCCCEEEEE
-
278SumoylationSGSSKDLKFVKMRNT
CCCCCCCEEEEECCC
-
278SumoylationSGSSKDLKFVKMRNT
CCCCCCCEEEEECCC
-
285PhosphorylationKFVKMRNTFGSHTYE
EEEEECCCCCCCCCC
29083192
288PhosphorylationKMRNTFGSHTYENQK
EECCCCCCCCCCCHH
29083192
290PhosphorylationRNTFGSHTYENQKEI
CCCCCCCCCCCHHHH
29083192
291PhosphorylationNTFGSHTYENQKEIK
CCCCCCCCCCHHHHH
29083192
295UbiquitinationSHTYENQKEIKKKDE
CCCCCCHHHHHHCCH
-
309PhosphorylationEDIQRSYTLRRKRKK
HHHHHHHHHHHHHHC
24719451
348SumoylationNRDQKEMKNSIFAEY
CCCHHHHHHHHHHHH
-
348SumoylationNRDQKEMKNSIFAEY
CCCHHHHHHHHHHHH
-
348UbiquitinationNRDQKEMKNSIFAEY
CCCHHHHHHHHHHHH
-
357UbiquitinationSIFAEYAKESKAMAI
HHHHHHHHHHHCCEE
-
365SumoylationESKAMAIKTDVDVVE
HHHCCEECCCCCHHH
-
365SumoylationESKAMAIKTDVDVVE
HHHCCEECCCCCHHH
-
374UbiquitinationDVDVVEIKNTLRKHI
CCCHHHHHHHHHHHH
-
379UbiquitinationEIKNTLRKHIYRAQA
HHHHHHHHHHHHHHH
-
396UbiquitinationYNCIRIDKQPVYNVE
ECEEEECCCCEEEEE
-
405UbiquitinationPVYNVEVKNAEFPRG
CEEEEEECCCCCCHH
-
482PhosphorylationHLHPPWKSPAMSRYY
HHCCCCCCHHHHHHH
26437602
489PhosphorylationSPAMSRYYLELFQCP
CHHHHHHHHHHCCCC
30576142
565UbiquitinationWSDSQNLKITGKAML
CCCCCCCEECCEEEE
-
646PhosphorylationRNVMRHMSDDLGSYV
HHHHHHCCCCHHHCE
22468782
654PhosphorylationDDLGSYVSLSCDDFS
CCHHHCEEEECCCCC
46164229
661PhosphorylationSLSCDDFSSQELEIF
EEECCCCCCCCEEEE
22468782
703PhosphorylationSVSSEPLSLQKMVYS
CCCCCCCCHHHHHHH
24719451
717UbiquitinationSYLPALGKTGVLGSG
HHHHHCCCCCCCCCC
-
725UbiquitinationTGVLGSGKIQVSKKI
CCCCCCCCEEEEEEC
-
731UbiquitinationGKIQVSKKIGQRPCF
CCEEEEEECCCCCCC
-
750O-linked_GlycosylationTLLMLNGTKQKQVEG
EEEECCCCCHHHCCC
30379171
753UbiquitinationMLNGTKQKQVEGLPE
ECCCCCHHHCCCCHH
-
768UbiquitinationLLDLNLAKCSSSLKK
HHHHHHHHCHHHHHH
-
780PhosphorylationLKKLKKKSEGELSCS
HHHHHHCCCCCCCCC
28270605
785PhosphorylationKKSEGELSCSKENCP
HCCCCCCCCCCCCCH
28270605
787PhosphorylationSEGELSCSKENCPSV
CCCCCCCCCCCCHHH
28270605
788AcetylationEGELSCSKENCPSVV
CCCCCCCCCCCHHHH
20167786
788UbiquitinationEGELSCSKENCPSVV
CCCCCCCCCCCHHHH
-
797UbiquitinationNCPSVVKKMNFHKTN
CCHHHHHHCCCCCCC
21906983
802UbiquitinationVKKMNFHKTNLKGET
HHHCCCCCCCCCCCH
2190698
806SumoylationNFHKTNLKGETALHR
CCCCCCCCCCHHHHH
-
806UbiquitinationNFHKTNLKGETALHR
CCCCCCCCCCHHHHH
-
806SumoylationNFHKTNLKGETALHR
CCCCCCCCCCHHHHH
-
909UbiquitinationLLQQRNAKGELPLDY
EEEECCCCCCCCCCE
-
916PhosphorylationKGELPLDYVVSPQIK
CCCCCCCEEECHHHH
22817900
919PhosphorylationLPLDYVVSPQIKEEL
CCCCEEECHHHHHHH
25159151
923UbiquitinationYVVSPQIKEELFAIT
EEECHHHHHHHHHHE
-
931SumoylationEELFAITKIEDTVEN
HHHHHHEEEHHHHHH
28112733
931UbiquitinationEELFAITKIEDTVEN
HHHHHHEEEHHHHHH
-
1017PhosphorylationLYAGNIKTLQKLPHI
HHCCCHHHHHHHHHH
-
1020UbiquitinationGNIKTLQKLPHILKE
CCHHHHHHHHHHHHH
-
1026UbiquitinationQKLPHILKELPENLK
HHHHHHHHHCCCCCC
-

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 SLF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLF1_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 SLF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD18_HUMANRAD18physical
22036607

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLF1_HUMAN

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Related Literatures of Post-Translational Modification

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