BLM_DROME - dbPTM
BLM_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLM_DROME
UniProt AC Q9VGI8
Protein Name Bloom syndrome protein homolog
Gene Name Blm
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1487
Subcellular Localization Nucleus.
Protein Description Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (By similarity).; ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction..
Protein Sequence MSKKPVAQRKQLTLSSFIGLDGNSQSQPKSRAASVRSKPPAVYNPIFLDASSSDDETTEISSQSNNGTIATKKSSRDPRTAKLKKHTYLDLSVSPLAKLSAKKYARDSPKKPTSLDLSVSPLAELLAKKSDRDSPKKPVQNENSYTYRGLSESPVENKSIGDTLRKPPQKERKTSIVWLSDSPEKKVTQNERKILDSPLQRFSFEDFPNKENGNRHHLLTLPDSPPPPQPVKKPEKTMWQNETKTIQDKDSPANPLVSNNLASISTLLDSSRAPNTYKGSSRNLFEDSPEKSGSGEQGYKLGSAKENEIPTKPATASLERNSVTSSPSPAAPLKPRYSVAFDNSLADYLKDLAQNDNFSIDPNKQNTETLKSTLGFFRNTYVELMEKYCSLIDQIPAMHFNEIAGFQPNTFLKLKVMRQKFKARTQLVQNSLDKKESQLKAEQEALEKEEIEMQAEQAQQTVLSSSSPEKSRPIMPLPKVQEIKDEKIPNRNQLIHDLCGEPDNFSPPSSPRDTQLIPKRQQLINDLCGEPDDFSPPSKQNDPHLLRKCEELVHDLCEEPDDYLAQSMMLDGDLEEEQLNGPTQGTTTSGMDDDEDDLEGLLAEIEDEHQKMQGRRSEFNGYSYKELEAVKVKEKHKETPINISLDDDGFPEYDEAMFEQMHSQAAANKSRVSSAGPSTSKSVVPTKQTSALHSQKLSGNFHANVHNDGITGEFDGQKFEHSTRLMHGLSYSFGLKSFRPNQLQVINATLLGNDCFVLMPTGGGKSLCYQLPAILTEGVTIVISPLKSLIFDQINKLASLDICAKSLSGEQKMADVMAIYRDLESQPPMVKLLYVTPEKISSSARFQDTLDTLNSNNYISRFVIDEAHCVSQWGHDFRPDYKKLGVLKKRFPNVPTIALTATATPRVRLDILAQLNLKNCKWFLSSFNRSNLRYRVLPKKGVSTLDDISRYIRSKPQHFSGIIYCLSRKECDETSKKMCKDGVRAVSYHAGLTDTDRESRQKDWLTGKMRVICATVAFGMGIDKPDVRFVLHYSLPKSIEGYYQEAGRAGRDGDVADCILYYNYSDMLRIKKMLDSDKALQYNVKKIHVDNLYRIVGYCENLTDCRRAQQLDYFGEHFTSEQCLENRETACDNCINKRAYKAVDALEHARKAARAVKDLCSGRSRFTLLHIADVLKGSKIKKIIDFNHHKTPHHGVLKDWDKNDVHRLLRKMVIDGFLREDLIFTNDFPQAYLYLGNNISKLMEGTPNFEFAVTKNAKEAKAAVGSVSDGATSSTADGQSGMREIHERCYTDLLDLCRTIASQRNVTMASIMNIQALKSMAETLPITEKDMCSIPHVTKANFDKYGAKLLEITSNYASEKLLMQAVLDEEEEQAAAKQRPSTSGWNNESVDWDMAVASQGNANTSGASGFNSFRAGKRKKIYKSGASKRYKTSTTSPAARKTTSARGRGGRAGAKRAESSASSASGWKSKKTGNSFGFDLMPLPGSK
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
51PhosphorylationNPIFLDASSSDDETT
CCEEEECCCCCCCCC
30.0022817900
52PhosphorylationPIFLDASSSDDETTE
CEEEECCCCCCCCCC
39.2322817900
53PhosphorylationIFLDASSSDDETTEI
EEEECCCCCCCCCCC
46.7322817900
92PhosphorylationKHTYLDLSVSPLAKL
CCEEEECCCHHHHHH
21.8822817900
94PhosphorylationTYLDLSVSPLAKLSA
EEEECCCHHHHHHHH
15.7222817900
108PhosphorylationAKKYARDSPKKPTSL
HHHHCCCCCCCCCCC
32.8222817900
113PhosphorylationRDSPKKPTSLDLSVS
CCCCCCCCCCCCCHH
51.2918327897
118PhosphorylationKPTSLDLSVSPLAEL
CCCCCCCCHHHHHHH
21.8822817900
120PhosphorylationTSLDLSVSPLAELLA
CCCCCCHHHHHHHHH
15.7222817900
130PhosphorylationAELLAKKSDRDSPKK
HHHHHHCCCCCCCCC
36.8522817900
134PhosphorylationAKKSDRDSPKKPVQN
HHCCCCCCCCCCCCC
39.2422817900
151PhosphorylationSYTYRGLSESPVENK
CCCCCCCCCCCCCCC
38.5619429919
153PhosphorylationTYRGLSESPVENKSI
CCCCCCCCCCCCCCH
30.7619429919
175PhosphorylationPQKERKTSIVWLSDS
CCCCCCCEEEEECCC
20.4122817900
180PhosphorylationKTSIVWLSDSPEKKV
CCEEEEECCCCCCCC
21.9622817900
182PhosphorylationSIVWLSDSPEKKVTQ
EEEEECCCCCCCCCH
31.4225749252
197PhosphorylationNERKILDSPLQRFSF
HHHHHCCCCHHHCCC
24.8619429919
203PhosphorylationDSPLQRFSFEDFPNK
CCCHHHCCCCCCCCC
29.8922817900
224PhosphorylationHLLTLPDSPPPPQPV
EEEECCCCCCCCCCC
37.0519429919
245PhosphorylationMWQNETKTIQDKDSP
CCCCCCCCCCCCCCC
31.1528490779
251PhosphorylationKTIQDKDSPANPLVS
CCCCCCCCCCCCCCC
31.4919429919
258PhosphorylationSPANPLVSNNLASIS
CCCCCCCCCCHHHHH
27.9019429919
288PhosphorylationSRNLFEDSPEKSGSG
CCCCCCCCCCCCCCC
27.9719429919
326PhosphorylationERNSVTSSPSPAAPL
HHCCCCCCCCCCCCC
21.7422817900
328PhosphorylationNSVTSSPSPAAPLKP
CCCCCCCCCCCCCCC
29.1722817900
467PhosphorylationQTVLSSSSPEKSRPI
HHHHHCCCCCCCCCC
38.7430478224
506PhosphorylationCGEPDNFSPPSSPRD
CCCCCCCCCCCCHHH
42.0022817900
509PhosphorylationPDNFSPPSSPRDTQL
CCCCCCCCCHHHCCC
57.2522817900
510PhosphorylationDNFSPPSSPRDTQLI
CCCCCCCCHHHCCCC
29.7222817900
535PhosphorylationCGEPDDFSPPSKQND
CCCCCCCCCCHHCCC
42.7822817900
617PhosphorylationQKMQGRRSEFNGYSY
HHHCCCCCCCCCCCH
45.2219429919

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 BLM_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BLM_DROME !!

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_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OTU_DROMEotuphysical
15710747
PANG1_DROMEpanphysical
15710747
PANG2_DROMEpanphysical
15710747
DORS_DROMEdlphysical
15710747
COPG_DROMEgammaCOPphysical
15710747
LIMK1_DROMELIMK1physical
15710747
SPS1_DROMESelDphysical
15710747
RAD54_DROMEokrgenetic
10454573
KU70_DROMEIrbpgenetic
8608940
KU70_DROMEIrbpgenetic
11283371
OTP_DROMEotpphysical
25242320

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-92;SER-94; SER-108; THR-113; SER-118; SER-120; SER-130; SER-151; SER-153;SER-180; SER-182; SER-197; SER-203; SER-328; SER-506; SER-509; SER-510AND SER-535, AND MASS SPECTROMETRY.

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