BLM_HUMAN - dbPTM
BLM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLM_HUMAN
UniProt AC P54132
Protein Name Bloom syndrome protein
Gene Name BLM
Organism Homo sapiens (Human).
Sequence Length 1417
Subcellular Localization Nucleus . Together with SPIDR, is redistributed in discrete nuclear DNA damage-induced foci following hydroxyurea (HU) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a RMI complex- and SPIDR-dependent manner.
Protein Description ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. [PubMed: 9388193]
Protein Sequence MAAVPQNNLQEQLERHSARTLNNKLSLSKPKFSGFTFKKKTSSDNNVSVTNVSVAKTPVLRNKDVNVTEDFSFSEPLPNTTNQQRVKDFFKNAPAGQETQRGGSKSLLPDFLQTPKEVVCTTQNTPTVKKSRDTALKKLEFSSSPDSLSTINDWDDMDDFDTSETSKSFVTPPQSHFVRVSTAQKSKKGKRNFFKAQLYTTNTVKTDLPPPSSESEQIDLTEEQKDDSEWLSSDVICIDDGPIAEVHINEDAQESDSLKTHLEDERDNSEKKKNLEEAELHSTEKVPCIEFDDDDYDTDFVPPSPEEIISASSSSSKCLSTLKDLDTSDRKEDVLSTSKDLLSKPEKMSMQELNPETSTDCDARQISLQQQLIHVMEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLTEVDFNKSDASLLGSLWRYRPDSLDGPMEGDSCPTGNSMKELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSFVSSNWAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPSYDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAYQPIKEGRPIKSVSERLSSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSLSFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLYSMVHYCENITECRRIQLLAYFGENGFNPDFCKKHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNIKHVGPSGRFTMNMLVDIFLGSKSAKIQSGIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGNKAQTVLNGNLKVDFMETENSSSVKKQKALVAKVSQREEMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPAEDSSPGISLSSSRGPGRSAAEELDEEIPVSSHYFASKTRNERKRKKMPASQRSKRRKTASSGSKAKGGSATCRKISSKTKSSSIIGSSSASHTSQATSGANSKLGIMAPPKPINRPFLKPSYAFS
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
17PhosphorylationQEQLERHSARTLNNK
HHHHHHHHHHHHHHH
26.1825159151
20PhosphorylationLERHSARTLNNKLSL
HHHHHHHHHHHHHCC
33.29-
24SumoylationSARTLNNKLSLSKPK
HHHHHHHHHCCCCCC
38.08-
24SumoylationSARTLNNKLSLSKPK
HHHHHHHHHCCCCCC
38.0828112733
24UbiquitinationSARTLNNKLSLSKPK
HHHHHHHHHCCCCCC
38.08-
26PhosphorylationRTLNNKLSLSKPKFS
HHHHHHHCCCCCCCC
32.0025159151
28PhosphorylationLNNKLSLSKPKFSGF
HHHHHCCCCCCCCCE
43.4621712546
29AcetylationNNKLSLSKPKFSGFT
HHHHCCCCCCCCCEE
58.4825953088
31SumoylationKLSLSKPKFSGFTFK
HHCCCCCCCCCEEEE
56.76-
31AcetylationKLSLSKPKFSGFTFK
HHCCCCCCCCCEEEE
56.7625953088
31SumoylationKLSLSKPKFSGFTFK
HHCCCCCCCCCEEEE
56.7628112733
33PhosphorylationSLSKPKFSGFTFKKK
CCCCCCCCCEEEEEE
38.8425159151
36PhosphorylationKPKFSGFTFKKKTSS
CCCCCCEEEEEECCC
37.7623186163
38MethylationKFSGFTFKKKTSSDN
CCCCEEEEEECCCCC
50.75-
38SumoylationKFSGFTFKKKTSSDN
CCCCEEEEEECCCCC
50.7528112733
39MethylationFSGFTFKKKTSSDNN
CCCEEEEEECCCCCC
58.03-
40SumoylationSGFTFKKKTSSDNNV
CCEEEEEECCCCCCE
54.98-
40SumoylationSGFTFKKKTSSDNNV
CCEEEEEECCCCCCE
54.98-
41PhosphorylationGFTFKKKTSSDNNVS
CEEEEEECCCCCCEE
42.2030177828
42PhosphorylationFTFKKKTSSDNNVSV
EEEEEECCCCCCEEE
44.5730177828
43PhosphorylationTFKKKTSSDNNVSVT
EEEEECCCCCCEEEE
49.9822199227
48PhosphorylationTSSDNNVSVTNVSVA
CCCCCCEEEEEEEEE
25.9125159151
50PhosphorylationSDNNVSVTNVSVAKT
CCCCEEEEEEEEEEC
23.5419691289
53PhosphorylationNVSVTNVSVAKTPVL
CEEEEEEEEEECCCC
20.5825159151
56SumoylationVTNVSVAKTPVLRNK
EEEEEEEECCCCCCC
51.73-
56SumoylationVTNVSVAKTPVLRNK
EEEEEEEECCCCCCC
51.7328112733
57PhosphorylationTNVSVAKTPVLRNKD
EEEEEEECCCCCCCC
14.6426055452
63SumoylationKTPVLRNKDVNVTED
ECCCCCCCCCCCCCC
57.5328112733
68PhosphorylationRNKDVNVTEDFSFSE
CCCCCCCCCCCCCCC
25.3221712546
72PhosphorylationVNVTEDFSFSEPLPN
CCCCCCCCCCCCCCC
39.9430576142
74PhosphorylationVTEDFSFSEPLPNTT
CCCCCCCCCCCCCCC
36.7925159151
87SumoylationTTNQQRVKDFFKNAP
CCCHHHHHHHHHCCC
51.5128112733
91SumoylationQRVKDFFKNAPAGQE
HHHHHHHHCCCCCCC
52.79-
91SumoylationQRVKDFFKNAPAGQE
HHHHHHHHCCCCCCC
52.7928112733
91UbiquitinationQRVKDFFKNAPAGQE
HHHHHHHHCCCCCCC
52.79-
99PhosphorylationNAPAGQETQRGGSKS
CCCCCCCCCCCCCCC
18.7116199871
104PhosphorylationQETQRGGSKSLLPDF
CCCCCCCCCCCCHHH
23.1521712546
105SumoylationETQRGGSKSLLPDFL
CCCCCCCCCCCHHHH
48.69-
105SumoylationETQRGGSKSLLPDFL
CCCCCCCCCCCHHHH
48.6928112733
105UbiquitinationETQRGGSKSLLPDFL
CCCCCCCCCCCHHHH
48.69-
106PhosphorylationTQRGGSKSLLPDFLQ
CCCCCCCCCCHHHHC
36.5121712546
114PhosphorylationLLPDFLQTPKEVVCT
CCHHHHCCCCEEEEE
38.1829255136
116SumoylationPDFLQTPKEVVCTTQ
HHHHCCCCEEEEECC
67.5428112733
121PhosphorylationTPKEVVCTTQNTPTV
CCCEEEEECCCCCCC
21.5824732914
122PhosphorylationPKEVVCTTQNTPTVK
CCEEEEECCCCCCCC
18.0729255136
125PhosphorylationVVCTTQNTPTVKKSR
EEEECCCCCCCCCCH
15.5429255136
127PhosphorylationCTTQNTPTVKKSRDT
EECCCCCCCCCCHHH
42.8129255136
129SumoylationTQNTPTVKKSRDTAL
CCCCCCCCCCHHHHH
47.73-
129AcetylationTQNTPTVKKSRDTAL
CCCCCCCCCCHHHHH
47.7325953088
129SumoylationTQNTPTVKKSRDTAL
CCCCCCCCCCHHHHH
47.7328112733
129UbiquitinationTQNTPTVKKSRDTAL
CCCCCCCCCCHHHHH
47.73-
131PhosphorylationNTPTVKKSRDTALKK
CCCCCCCCHHHHHHH
29.6621712546
142PhosphorylationALKKLEFSSSPDSLS
HHHHCCCCCCCCCCC
22.1128176443
143PhosphorylationLKKLEFSSSPDSLST
HHHCCCCCCCCCCCC
51.7328176443
144PhosphorylationKKLEFSSSPDSLSTI
HHCCCCCCCCCCCCC
31.3728176443
147PhosphorylationEFSSSPDSLSTINDW
CCCCCCCCCCCCCCC
27.8328176443
149PhosphorylationSSSPDSLSTINDWDD
CCCCCCCCCCCCCCC
31.0628450419
150PhosphorylationSSPDSLSTINDWDDM
CCCCCCCCCCCCCCC
29.1528464451
162PhosphorylationDDMDDFDTSETSKSF
CCCCCCCCCCCHHCC
28.5828176443
163PhosphorylationDMDDFDTSETSKSFV
CCCCCCCCCCHHCCC
40.5028176443
165PhosphorylationDDFDTSETSKSFVTP
CCCCCCCCHHCCCCC
41.0228176443
166PhosphorylationDFDTSETSKSFVTPP
CCCCCCCHHCCCCCC
23.4228176443
167UbiquitinationFDTSETSKSFVTPPQ
CCCCCCHHCCCCCCC
56.16-
168PhosphorylationDTSETSKSFVTPPQS
CCCCCHHCCCCCCCC
25.3930266825
171PhosphorylationETSKSFVTPPQSHFV
CCHHCCCCCCCCCEE
27.5230266825
175PhosphorylationSFVTPPQSHFVRVST
CCCCCCCCCEEECCC
25.3528450419
181PhosphorylationQSHFVRVSTAQKSKK
CCCEEECCCCCCCCC
13.8827282143
182PhosphorylationSHFVRVSTAQKSKKG
CCEEECCCCCCCCCC
30.19-
195SumoylationKGKRNFFKAQLYTTN
CCCCCEEEEEEEECC
30.96-
195MethylationKGKRNFFKAQLYTTN
CCCCCEEEEEEEECC
30.96-
195SumoylationKGKRNFFKAQLYTTN
CCCCCEEEEEEEECC
30.9628112733
199PhosphorylationNFFKAQLYTTNTVKT
CEEEEEEEECCCCCC
10.23-
201PhosphorylationFKAQLYTTNTVKTDL
EEEEEEECCCCCCCC
18.4828555341
205SumoylationLYTTNTVKTDLPPPS
EEECCCCCCCCCCCC
33.9928112733
225UbiquitinationIDLTEEQKDDSEWLS
CCCCHHHCCCCCHHC
67.78-
259UbiquitinationAQESDSLKTHLEDER
CHHCCHHHHHHHHCC
37.54-
269PhosphorylationLEDERDNSEKKKNLE
HHHCCCCHHHHHCHH
55.9030576142
282PhosphorylationLEEAELHSTEKVPCI
HHHHHHHCCCCCCCE
51.3825159151
283PhosphorylationEEAELHSTEKVPCIE
HHHHHHCCCCCCCEE
29.1325849741
296PhosphorylationIEFDDDDYDTDFVPP
EECCCCCCCCCCCCC
27.9528102081
298PhosphorylationFDDDDYDTDFVPPSP
CCCCCCCCCCCCCCH
25.7129116813
304PhosphorylationDTDFVPPSPEEIISA
CCCCCCCCHHHHHCC
38.5825159151
312PhosphorylationPEEIISASSSSSKCL
HHHHHCCCCCCHHHH
24.7825852190
313PhosphorylationEEIISASSSSSKCLS
HHHHCCCCCCHHHHH
33.6825852190
314PhosphorylationEIISASSSSSKCLST
HHHCCCCCCHHHHHH
35.8125852190
315PhosphorylationIISASSSSSKCLSTL
HHCCCCCCHHHHHHH
35.4525852190
316PhosphorylationISASSSSSKCLSTLK
HCCCCCCHHHHHHHH
29.3625852190
317SumoylationSASSSSSKCLSTLKD
CCCCCCHHHHHHHHC
40.94-
317SumoylationSASSSSSKCLSTLKD
CCCCCCHHHHHHHHC
40.94-
323UbiquitinationSKCLSTLKDLDTSDR
HHHHHHHHCCCCCCC
57.23-
327PhosphorylationSTLKDLDTSDRKEDV
HHHHCCCCCCCHHHH
39.5625159151
328PhosphorylationTLKDLDTSDRKEDVL
HHHCCCCCCCHHHHH
34.7823401153
331SumoylationDLDTSDRKEDVLSTS
CCCCCCCHHHHHHHC
64.36-
331SumoylationDLDTSDRKEDVLSTS
CCCCCCCHHHHHHHC
64.3628112733
331UbiquitinationDLDTSDRKEDVLSTS
CCCCCCCHHHHHHHC
64.36-
336PhosphorylationDRKEDVLSTSKDLLS
CCHHHHHHHCHHHHC
30.4025159151
337PhosphorylationRKEDVLSTSKDLLSK
CHHHHHHHCHHHHCC
35.3225159151
338PhosphorylationKEDVLSTSKDLLSKP
HHHHHHHCHHHHCCH
22.3125159151
339UbiquitinationEDVLSTSKDLLSKPE
HHHHHHCHHHHCCHH
53.11-
343PhosphorylationSTSKDLLSKPEKMSM
HHCHHHHCCHHHCCH
54.1627259358
344SumoylationTSKDLLSKPEKMSMQ
HCHHHHCCHHHCCHH
58.11-
344SumoylationTSKDLLSKPEKMSMQ
HCHHHHCCHHHCCHH
58.1128112733
344UbiquitinationTSKDLLSKPEKMSMQ
HCHHHHCCHHHCCHH
58.11-
347SumoylationDLLSKPEKMSMQELN
HHHCCHHHCCHHHHC
44.81-
347SumoylationDLLSKPEKMSMQELN
HHHCCHHHCCHHHHC
44.8128112733
349PhosphorylationLSKPEKMSMQELNPE
HCCHHHCCHHHHCCC
28.5125159151
357PhosphorylationMQELNPETSTDCDAR
HHHHCCCCCCCHHHH
37.8825159151
358PhosphorylationQELNPETSTDCDARQ
HHHCCCCCCCHHHHH
22.1625159151
359PhosphorylationELNPETSTDCDARQI
HHCCCCCCCHHHHHH
48.3325159151
367PhosphorylationDCDARQISLQQQLIH
CHHHHHHHHHHHHHH
16.2825159151
390AcetylationIDTIPDDKLKLLDCG
HHHCCCCCCCHHHHC
55.7026051181
390UbiquitinationIDTIPDDKLKLLDCG
HHHCCCCCCCHHHHC
55.70-
392SumoylationTIPDDKLKLLDCGNE
HCCCCCCCHHHHCHH
53.39-
392SumoylationTIPDDKLKLLDCGNE
HCCCCCCCHHHHCHH
53.39-
392UbiquitinationTIPDDKLKLLDCGNE
HCCCCCCCHHHHCHH
53.39-
409SumoylationQQRNIRRKLLTEVDF
HHHHHHHHHHHHCCC
37.69-
409SumoylationQQRNIRRKLLTEVDF
HHHHHHHHHHHHCCC
37.69-
409UbiquitinationQQRNIRRKLLTEVDF
HHHHHHHHHHHHCCC
37.69-
412PhosphorylationNIRRKLLTEVDFNKS
HHHHHHHHHCCCCHH
44.3828450419
418SumoylationLTEVDFNKSDASLLG
HHHCCCCHHHHHHHH
50.10-
418SumoylationLTEVDFNKSDASLLG
HHHCCCCHHHHHHHH
50.10-
418UbiquitinationLTEVDFNKSDASLLG
HHHCCCCHHHHHHHH
50.10-
419PhosphorylationTEVDFNKSDASLLGS
HHCCCCHHHHHHHHH
39.2425159151
422PhosphorylationDFNKSDASLLGSLWR
CCCHHHHHHHHHHHC
29.1725159151
426PhosphorylationSDASLLGSLWRYRPD
HHHHHHHHHHCCCCC
25.4025159151
430PhosphorylationLLGSLWRYRPDSLDG
HHHHHHCCCCCCCCC
18.2129396449
434PhosphorylationLWRYRPDSLDGPMEG
HHCCCCCCCCCCCCC
30.9225159151
443PhosphorylationDGPMEGDSCPTGNSM
CCCCCCCCCCCCCCC
32.6221712546
449PhosphorylationDSCPTGNSMKELNFS
CCCCCCCCCCCCCCC
32.3525159151
451SumoylationCPTGNSMKELNFSHL
CCCCCCCCCCCCCCC
59.8928112733
456PhosphorylationSMKELNFSHLPSNSV
CCCCCCCCCCCCCCC
24.0424732914
460PhosphorylationLNFSHLPSNSVSPGD
CCCCCCCCCCCCCCC
48.3624732914
462PhosphorylationFSHLPSNSVSPGDCL
CCCCCCCCCCCCCEE
28.4525159151
464PhosphorylationHLPSNSVSPGDCLLT
CCCCCCCCCCCEEEE
24.0025159151
471PhosphorylationSPGDCLLTTTLGKTG
CCCCEEEECCCCCCC
12.5624732914
472PhosphorylationPGDCLLTTTLGKTGF
CCCEEEECCCCCCCC
21.7224732914
473PhosphorylationGDCLLTTTLGKTGFS
CCEEEECCCCCCCCC
28.4224732914
476AcetylationLLTTTLGKTGFSATR
EEECCCCCCCCCCHH
48.8926051181
476SumoylationLLTTTLGKTGFSATR
EEECCCCCCCCCCHH
48.8928112733
476UbiquitinationLLTTTLGKTGFSATR
EEECCCCCCCCCCHH
48.89-
480PhosphorylationTLGKTGFSATRKNLF
CCCCCCCCCHHCCHH
30.0321815630
482PhosphorylationGKTGFSATRKNLFER
CCCCCCCHHCCHHCC
40.7629396449
484SumoylationTGFSATRKNLFERPL
CCCCCHHCCHHCCCC
54.36-
484SumoylationTGFSATRKNLFERPL
CCCCCHHCCHHCCCC
54.3628112733
484UbiquitinationTGFSATRKNLFERPL
CCCCCHHCCHHCCCC
54.36-
494PhosphorylationFERPLFNTHLQKSFV
HCCCCCCHHHHHHHH
19.3428555341
498SumoylationLFNTHLQKSFVSSNW
CCCHHHHHHHHCCCC
52.82-
498SumoylationLFNTHLQKSFVSSNW
CCCHHHHHHHHCCCC
52.8228112733
499PhosphorylationFNTHLQKSFVSSNWA
CCHHHHHHHHCCCCC
20.2325159151
502PhosphorylationHLQKSFVSSNWAETP
HHHHHHHCCCCCCCC
18.8829396449
503PhosphorylationLQKSFVSSNWAETPR
HHHHHHCCCCCCCCC
30.9626074081
508PhosphorylationVSSNWAETPRLGKKN
HCCCCCCCCCCCCCC
13.1325159151
513SumoylationAETPRLGKKNESSYF
CCCCCCCCCCCCCCC
57.9528112733
514SumoylationETPRLGKKNESSYFP
CCCCCCCCCCCCCCC
65.24-
514SumoylationETPRLGKKNESSYFP
CCCCCCCCCCCCCCC
65.2428112733
514UbiquitinationETPRLGKKNESSYFP
CCCCCCCCCCCCCCC
65.24-
517PhosphorylationRLGKKNESSYFPGNV
CCCCCCCCCCCCCCC
39.4728555341
518PhosphorylationLGKKNESSYFPGNVL
CCCCCCCCCCCCCCE
25.3128555341
519PhosphorylationGKKNESSYFPGNVLT
CCCCCCCCCCCCCEE
24.0728555341
526PhosphorylationYFPGNVLTSTAVKDQ
CCCCCCEEHHEEECC
21.5425627689
527PhosphorylationFPGNVLTSTAVKDQN
CCCCCEEHHEEECCC
15.3725627689
528PhosphorylationPGNVLTSTAVKDQNK
CCCCEEHHEEECCCC
30.1825159151
531SumoylationVLTSTAVKDQNKHTA
CEEHHEEECCCCCCC
51.6528112733
531UbiquitinationVLTSTAVKDQNKHTA
CEEHHEEECCCCCCC
51.65-
535SumoylationTAVKDQNKHTASIND
HEEECCCCCCCCHHH
36.3828112733
535UbiquitinationTAVKDQNKHTASIND
HEEECCCCCCCCHHH
36.38-
537PhosphorylationVKDQNKHTASINDLE
EECCCCCCCCHHHHH
24.5726055452
539PhosphorylationDQNKHTASINDLERE
CCCCCCCCHHHHHHH
24.0725159151
550PhosphorylationLERETQPSYDIDNFD
HHHHCCCCCCCCCCC
26.1418669648
551PhosphorylationERETQPSYDIDNFDI
HHHCCCCCCCCCCCC
24.4918669648
578UbiquitinationMHNLAASKSSTAAYQ
HHHHHHCCCCCCCCC
43.64-
579PhosphorylationHNLAASKSSTAAYQP
HHHHHCCCCCCCCCC
30.3525159151
580PhosphorylationNLAASKSSTAAYQPI
HHHHCCCCCCCCCCC
26.2925159151
581PhosphorylationLAASKSSTAAYQPIK
HHHCCCCCCCCCCCC
23.5422199227
588SumoylationTAAYQPIKEGRPIKS
CCCCCCCCCCCCCCC
61.88-
588SumoylationTAAYQPIKEGRPIKS
CCCCCCCCCCCCCCC
61.8828112733
588UbiquitinationTAAYQPIKEGRPIKS
CCCCCCCCCCCCCCC
61.88-
594SumoylationIKEGRPIKSVSERLS
CCCCCCCCCHHHHHH
47.70-
594SumoylationIKEGRPIKSVSERLS
CCCCCCCCCHHHHHH
47.7028112733
594UbiquitinationIKEGRPIKSVSERLS
CCCCCCCCCHHHHHH
47.70-
597PhosphorylationGRPIKSVSERLSSAK
CCCCCCHHHHHHCCC
24.8829396449
601PhosphorylationKSVSERLSSAKTDCL
CCHHHHHHCCCCCCE
34.1819691289
602PhosphorylationSVSERLSSAKTDCLP
CHHHHHHCCCCCCEE
38.0719691289
604SumoylationSERLSSAKTDCLPVS
HHHHHCCCCCCEECC
47.0128112733
604UbiquitinationSERLSSAKTDCLPVS
HHHHHCCCCCCEECC
47.01-
629UbiquitinationSIQNYTDKSAQNLAS
HHHHCCCHHHHHHHH
39.63-
646PhosphorylationLKHERFQSLSFPHTK
CCHHHHHHCCCCCHH
24.2225159151
652PhosphorylationQSLSFPHTKEMMKIF
HHCCCCCHHHHHHHH
29.0128509920
653UbiquitinationSLSFPHTKEMMKIFH
HCCCCCHHHHHHHHH
40.35-
657AcetylationPHTKEMMKIFHKKFG
CCHHHHHHHHHHHHC
40.6919816819
661AcetylationEMMKIFHKKFGLHNF
HHHHHHHHHHCCCCC
38.7619816827
662SumoylationMMKIFHKKFGLHNFR
HHHHHHHHHCCCCCC
35.77-
662AcetylationMMKIFHKKFGLHNFR
HHHHHHHHHCCCCCC
35.7719816835
662SumoylationMMKIFHKKFGLHNFR
HHHHHHHHHCCCCCC
35.77-
662UbiquitinationMMKIFHKKFGLHNFR
HHHHHHHHHCCCCCC
35.77-
695SumoylationLMPTGGGKSLCYQLP
EEECCCCCCHHHCCC
43.46-
695SumoylationLMPTGGGKSLCYQLP
EEECCCCCCHHHCCC
43.4611500040
696PhosphorylationMPTGGGKSLCYQLPA
EECCCCCCHHHCCCC
27.2620068231
699PhosphorylationGGGKSLCYQLPACVS
CCCCCHHHCCCCCCC
20.5520068231
706PhosphorylationYQLPACVSPGVTVVI
HCCCCCCCCCEEEEE
18.8020068231
714PhosphorylationPGVTVVISPLRSLIV
CCEEEEECCCHHHHH
13.2816880735
729PhosphorylationDQVQKLTSLDIPATY
HHHHHHHHCCCCCEE
34.1828787133
736PhosphorylationSLDIPATYLTGDKTD
HCCCCCEEECCCCCC
12.36-
741UbiquitinationATYLTGDKTDSEATN
CEEECCCCCCHHHHH
56.42-
742PhosphorylationTYLTGDKTDSEATNI
EEECCCCCCHHHHHH
49.8830576142
750PhosphorylationDSEATNIYLQLSKKD
CHHHHHHHHHHCCCC
7.1730576142
755AcetylationNIYLQLSKKDPIIKL
HHHHHHCCCCCCEEE
70.5519608861
755UbiquitinationNIYLQLSKKDPIIKL
HHHHHHCCCCCCEEE
70.5519608861
764PhosphorylationDPIIKLLYVTPEKIC
CCCEEEEEECHHHHH
16.8327251275
766PhosphorylationIIKLLYVTPEKICAS
CEEEEEECHHHHHHC
16.5130266825
769UbiquitinationLLYVTPEKICASNRL
EEEECHHHHHHCCCH
44.27-
773PhosphorylationTPEKICASNRLISTL
CHHHHHHCCCHHHHH
20.33-
820SumoylationRMNMLRQKFPSVPVM
HHHHHHHHCCCCCEE
53.46-
820SumoylationRMNMLRQKFPSVPVM
HHHHHHHHCCCCCEE
53.46-
820UbiquitinationRMNMLRQKFPSVPVM
HHHHHHHHCCCCCEE
53.46-
823PhosphorylationMLRQKFPSVPVMALT
HHHHHCCCCCEEEEE
42.0326503514
830PhosphorylationSVPVMALTATANPRV
CCCEEEEECCCCHHH
16.66-
832PhosphorylationPVMALTATANPRVQK
CEEEEECCCCHHHHH
23.02-
839SumoylationTANPRVQKDILTQLK
CCCHHHHHHHHHHHH
43.83-
839SumoylationTANPRVQKDILTQLK
CCCHHHHHHHHHHHH
43.83-
839UbiquitinationTANPRVQKDILTQLK
CCCHHHHHHHHHHHH
43.83-
863AcetylationSFNRHNLKYYVLPKK
EECCCCCEEEECCCC
39.5919608861
863UbiquitinationSFNRHNLKYYVLPKK
EECCCCCEEEECCCC
39.5919608861
873SumoylationVLPKKPKKVAFDCLE
ECCCCCCCCHHHHHH
47.53-
873SumoylationVLPKKPKKVAFDCLE
ECCCCCCCCHHHHHH
47.53-
873UbiquitinationVLPKKPKKVAFDCLE
ECCCCCCCCHHHHHH
47.53-
888PhosphorylationWIRKHHPYDSGIIYC
HHHHHCCCCCCCEEE
20.5526552605
890PhosphorylationRKHHPYDSGIIYCLS
HHHCCCCCCCEEECC
26.5026552605
894PhosphorylationPYDSGIIYCLSRREC
CCCCCCEEECCHHCC
5.8526552605
897PhosphorylationSGIIYCLSRRECDTM
CCCEEECCHHCCCCH
26.2326552605
903PhosphorylationLSRRECDTMADTLQR
CCHHCCCCHHHHHHH
26.39-
907PhosphorylationECDTMADTLQRDGLA
CCCCHHHHHHHHHHH
18.43-
968AcetylationVIHASLPKSVEGYYQ
EEEECCCCCCCEEHH
72.8726051181
1057UbiquitinationFNPDFCKKHPDVSCD
CCHHHHHHCCCCCCC
62.64-
1082SumoylationRDVTDDVKSIVRFVQ
CCCCHHHHHHHHHHH
41.27-
1082SumoylationRDVTDDVKSIVRFVQ
CCCCHHHHHHHHHHH
41.27-
1082UbiquitinationRDVTDDVKSIVRFVQ
CCCCHHHHHHHHHHH
41.27-
1083PhosphorylationDVTDDVKSIVRFVQE
CCCHHHHHHHHHHHH
26.6020860994
1125SumoylationFLGSKSAKIQSGIFG
HHCCCCCEEECCCCC
48.66-
1125AcetylationFLGSKSAKIQSGIFG
HHCCCCCEEECCCCC
48.6625953088
1125SumoylationFLGSKSAKIQSGIFG
HHCCCCCEEECCCCC
48.6628112733
1125UbiquitinationFLGSKSAKIQSGIFG
HHCCCCCEEECCCCC
48.66-
1128PhosphorylationSKSAKIQSGIFGKGS
CCCCEEECCCCCCCC
37.0129523821
1133AcetylationIQSGIFGKGSAYSRH
EECCCCCCCCCCCHH
38.6526051181
1133UbiquitinationIQSGIFGKGSAYSRH
EECCCCCCCCCCCHH
38.65-
1135PhosphorylationSGIFGKGSAYSRHNA
CCCCCCCCCCCHHCH
27.7629523821
1137PhosphorylationIFGKGSAYSRHNAER
CCCCCCCCCHHCHHH
14.1329523821
1138PhosphorylationFGKGSAYSRHNAERL
CCCCCCCCHHCHHHH
27.1229523821
1195PhosphorylationDFMETENSSSVKKQK
EEEECCCCCCHHHHH
20.1225159151
1196PhosphorylationFMETENSSSVKKQKA
EEECCCCCCHHHHHH
51.2121815630
1197PhosphorylationMETENSSSVKKQKAL
EECCCCCCHHHHHHH
37.4621815630
1199SumoylationTENSSSVKKQKALVA
CCCCCCHHHHHHHHH
51.97-
1199SumoylationTENSSSVKKQKALVA
CCCCCCHHHHHHHHH
51.9728112733
1199UbiquitinationTENSSSVKKQKALVA
CCCCCCHHHHHHHHH
51.97-
1200UbiquitinationENSSSVKKQKALVAK
CCCCCHHHHHHHHHH
55.67-
1207SumoylationKQKALVAKVSQREEM
HHHHHHHHHHHHHHH
34.6328112733
1207UbiquitinationKQKALVAKVSQREEM
HHHHHHHHHHHHHHH
34.63-
1217UbiquitinationQREEMVKKCLGELTE
HHHHHHHHHHHHHHH
24.23-
1237PhosphorylationGKVFGVHYFNIFNTV
HHHHCEEEEECCCCC
8.9125219547
1243PhosphorylationHYFNIFNTVTLKKLA
EEEECCCCCCHHHHH
12.2425219547
1245PhosphorylationFNIFNTVTLKKLAES
EECCCCCCHHHHHHH
30.7125219547
1252PhosphorylationTLKKLAESLSSDPEV
CHHHHHHHHCCCCCC
28.1322210691
1254PhosphorylationKKLAESLSSDPEVLL
HHHHHHHCCCCCCEE
41.8122210691
1267PhosphorylationLLQIDGVTEDKLEKY
EEEECCCCHHHHHHH
43.9522210691
1273SumoylationVTEDKLEKYGAEVIS
CCHHHHHHHCHHHHH
60.46-
1273SumoylationVTEDKLEKYGAEVIS
CCHHHHHHHCHHHHH
60.46-
1273UbiquitinationVTEDKLEKYGAEVIS
CCHHHHHHHCHHHHH
60.46-
1280PhosphorylationKYGAEVISVLQKYSE
HHCHHHHHHHHHHHC
23.1925159151
1285PhosphorylationVISVLQKYSEWTSPA
HHHHHHHHHCCCCCC
10.0026074081
1286PhosphorylationISVLQKYSEWTSPAE
HHHHHHHHCCCCCCC
33.4226074081
1289PhosphorylationLQKYSEWTSPAEDSS
HHHHHCCCCCCCCCC
22.3026074081
1290PhosphorylationQKYSEWTSPAEDSSP
HHHHCCCCCCCCCCC
24.1625159151
1295PhosphorylationWTSPAEDSSPGISLS
CCCCCCCCCCCEECC
29.9123401153
1296PhosphorylationTSPAEDSSPGISLSS
CCCCCCCCCCEECCC
39.1925159151
1300PhosphorylationEDSSPGISLSSSRGP
CCCCCCEECCCCCCC
28.2825262027
1302PhosphorylationSSPGISLSSSRGPGR
CCCCEECCCCCCCCC
21.3429978859
1303PhosphorylationSPGISLSSSRGPGRS
CCCEECCCCCCCCCH
29.3725159151
1304PhosphorylationPGISLSSSRGPGRSA
CCEECCCCCCCCCHH
37.5725159151
1310PhosphorylationSSRGPGRSAAEELDE
CCCCCCCHHHHHHCC
37.4330266825
1325PhosphorylationEIPVSSHYFASKTRN
CCCCCHHHHHCCCCC
11.6427642862
1329AcetylationSSHYFASKTRNERKR
CHHHHHCCCCCHHHH
48.3425953088
1329SumoylationSSHYFASKTRNERKR
CHHHHHCCCCCHHHH
48.3428112733
1329UbiquitinationSSHYFASKTRNERKR
CHHHHHCCCCCHHHH
48.34-
1372SumoylationRKISSKTKSSSIIGS
HHCCCCCCCCCEECC
52.67-
1372SumoylationRKISSKTKSSSIIGS
HHCCCCCCCCCEECC
52.6728112733
1372UbiquitinationRKISSKTKSSSIIGS
HHCCCCCCCCCEECC
52.67-
1374PhosphorylationISSKTKSSSIIGSSS
CCCCCCCCCEECCCC
27.4120860994
1375PhosphorylationSSKTKSSSIIGSSSA
CCCCCCCCEECCCCC
25.8928985074
1379PhosphorylationKSSSIIGSSSASHTS
CCCCEECCCCCCCCC
15.6520860994
1380PhosphorylationSSSIIGSSSASHTSQ
CCCEECCCCCCCCCC
25.3920860994
1381PhosphorylationSSIIGSSSASHTSQA
CCEECCCCCCCCCCC
35.1725159151
1383PhosphorylationIIGSSSASHTSQATS
EECCCCCCCCCCCCC
29.2821712546
1390PhosphorylationSHTSQATSGANSKLG
CCCCCCCCCCCCCCC
38.6320860994
1394PhosphorylationQATSGANSKLGIMAP
CCCCCCCCCCCCCCC
28.8220860994
1395SumoylationATSGANSKLGIMAPP
CCCCCCCCCCCCCCC
51.0128112733
1403AcetylationLGIMAPPKPINRPFL
CCCCCCCCCCCCCCC
58.4326051181
1411AcetylationPINRPFLKPSYAFS-
CCCCCCCCCCCCCC-
32.0919608861
1417PhosphorylationLKPSYAFS-------
CCCCCCCC-------
31.0125159151

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
99TPhosphorylationKinaseATRQ13535
PSP
99TPhosphorylationKinaseATMQ13315
PSP
122TPhosphorylationKinaseATMQ13315
PSP
122TPhosphorylationKinaseATRQ13535
PSP
144SPhosphorylationKinaseTTKP33981
PSP
171TPhosphorylationKinaseGSK3BP49841
PSP
175SPhosphorylationKinaseCDK2P24941
PSP
182TPhosphorylationKinaseCHEK1O14757
GPS
182TPhosphorylationKinaseCHEK2O96017
GPS
338SPhosphorylationKinaseNEK11Q8NG66
PSP
502SPhosphorylationKinaseCHK1O14757
PSP
539SPhosphorylationKinaseCHEK1O14757
GPS
646SPhosphorylationKinaseCHEK1O14757
GPS
714SPhosphorylationKinaseCDK1P06493
PSP
766TPhosphorylationKinaseCDK1P06493
PSP
1290SPhosphorylationKinaseTTKP33981
PSP
1296SPhosphorylationKinaseTTKP33981
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF8O76064
PMID:23708797
-KUbiquitinationE3 ubiquitin ligaseTRIM49P0CI25
PMID:23708797
-KUbiquitinationE3 ubiquitin ligaseMIB1Q86YT6
PMID:24239288

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
259Kubiquitylation

-

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 BLM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOP3A_HUMANTOP3Aphysical
10734115
H2AX_HUMANH2AFXphysical
15364958
P53_HUMANTP53physical
15364958
TP53B_HUMANTP53BP1physical
15364958
FEN1_HUMANFEN1physical
14688284
MLH1_HUMANMLH1physical
11325959
CAF1A_HUMANCHAF1Aphysical
15143166
P53_HUMANTP53physical
11399766
P53_HUMANTP53physical
11781842
XRCC2_HUMANXRCC2physical
12975363
ATM_HUMANATMphysical
12034743
RAD51_HUMANRAD51physical
11278509
RFA1_HUMANRPA1physical
10825162
TERF2_HUMANTERF2physical
12181313
WRN_HUMANWRNphysical
11919194
MLH1_HUMANMLH1physical
11470874
RFC1_HUMANRFC1physical
10783165
RFA1_HUMANRPA1physical
12181313
TOP3A_HUMANTOP3Aphysical
10825162
P53_HUMANTP53physical
12080066
TOP3A_HUMANTOP3Aphysical
11406610
MLH1_HUMANMLH1physical
11691925
EXO1_HUMANEXO1physical
18971343
UBC9_HUMANUBE2Iphysical
15829507
SYN1_HUMANSYN1physical
15829507
MCRS1_HUMANMCRS1physical
15829507
PSMD3_HUMANPSMD3physical
15829507
FANCJ_HUMANBRIP1physical
21240188
ATR_HUMANATRphysical
14729972
FACD2_HUMANFANCD2physical
15257300
FANCA_HUMANFANCAphysical
12724401
TOP3A_HUMANTOP3Aphysical
12724401
MLH1_HUMANMLH1physical
12724401
RFA1_HUMANRPA1physical
12724401
RFA2_HUMANRPA2physical
12724401
RFA3_HUMANRPA3physical
12724401
MSH2_HUMANMSH2physical
15064730
MSH6_HUMANMSH6physical
15064730
ATRX_HUMANATRXphysical
19671661
RAD51_HUMANRAD51physical
19671661
TEP1_HUMANTEP1physical
19329795
BLM_HUMANBLMphysical
19329795
HS90A_HUMANHSP90AA1physical
19329795
TOP2A_HUMANTOP2Aphysical
19329795
SF3B2_HUMANSF3B2physical
19329795
RAD51_HUMANRAD51physical
18562274
TERF2_HUMANTERF2physical
15229185
TERF1_HUMANTERF1physical
15229185
UIMC1_HUMANUIMC1physical
23708797
BLM_HUMANBLMphysical
24239288
TOP3A_HUMANTOP3Aphysical
24239288
TOPB1_HUMANTOPBP1physical
24239288
RMI1_HUMANRMI1physical
24239288
RFA1_HUMANRPA1physical
24239288
PARP1_HUMANPARP1physical
24239288
MIB1_HUMANMIB1physical
24239288
P53_HUMANTP53physical
24239288
PWP1_HUMANPWP1physical
24239288
FAN1_HUMANFAN1physical
25135477
FACD2_HUMANFANCD2physical
25135477
RFA1_HUMANRPA1physical
25135477
RAD50_HUMANRAD50physical
25084169
AQR_HUMANAQRgenetic
24104479
TERA_HUMANVCPgenetic
24104479
MMS22_HUMANMMS22Lgenetic
24104479
ELK4_HUMANELK4genetic
24104479
RS14_HUMANRPS14genetic
24104479
ICK_HUMANICKgenetic
24104479
XIAP_HUMANXIAPgenetic
24104479
U520_HUMANSNRNP200genetic
24104479
PO3F3_HUMANPOU3F3genetic
24104479
SPT5H_HUMANSUPT5Hgenetic
24104479
RS27A_HUMANRPS27Agenetic
24104479
ARP5_HUMANACTR5genetic
24104479
RL37_HUMANRPL37genetic
24104479
RD23B_HUMANRAD23Bgenetic
24104479
TRI15_HUMANTRIM15genetic
24104479
TRIM8_HUMANTRIM8genetic
24104479
RAD51_HUMANRAD51genetic
24104479
TREX2_HUMANTREX2genetic
24104479
RL14_HUMANRPL14genetic
24104479
RREB1_HUMANRREB1genetic
24104479
RL7_HUMANRPL7genetic
24104479
AL3B1_HUMANALDH3B1genetic
24104479
RS19_HUMANRPS19genetic
24104479
MO4L2_HUMANMORF4L2genetic
24104479
H2A1_HUMANHIST1H2AIgenetic
24104479
NDUAD_HUMANNDUFA13genetic
24104479
KLF16_HUMANKLF16genetic
24104479
CSK2B_HUMANCSNK2Bgenetic
24104479
SYCM_HUMANCARS2genetic
24104479
ALDR_HUMANAKR1B1genetic
24104479
RAMP1_HUMANRAMP1genetic
24104479
PSMD1_HUMANPSMD1genetic
24104479
HES5_HUMANHES5genetic
24104479
RL23A_HUMANRPL23Agenetic
24104479
RMP_HUMANURI1genetic
24104479
CEBPD_HUMANCEBPDgenetic
24104479
CASP8_HUMANCASP8physical
26496610
TOP3A_HUMANTOP3Aphysical
26496610
GANP_HUMANMCM3APphysical
26496610
HPS5_HUMANHPS5physical
26496610
CORO7_HUMANCORO7physical
26496610
RMI1_HUMANRMI1physical
26496610
F192A_HUMANFAM192Aphysical
26496610
APBB1_HUMANAPBB1physical
23572515
FANCJ_HUMANBRIP1physical
24895130
AIPL1_HUMANAIPL1physical
27173435
PDE5A_HUMANPDE5Aphysical
27173435
NEK4_HUMANNEK4physical
27173435
MYC_HUMANMYCphysical
23750012
JUN_HUMANJUNphysical
23750012
FBXW7_HUMANFBXW7physical
23750012

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
210900Bloom syndrome (BLM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BLM_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-863 AND LYS-1411, AND MASSSPECTROMETRY.
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, AND MASSSPECTROMETRY.
"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-48; SER-53; THR-57;THR-114; SER-358; SER-419; SER-422; SER-1295; SER-1296; SER-1303 ANDSER-1310, AND MASS SPECTROMETRY.
"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 SER-48; SER-282; SER-480 ANDSER-579, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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-419 AND SER-422, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND THR-508, 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-1296, 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-125, AND MASSSPECTROMETRY.

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