BLMH_HUMAN - dbPTM
BLMH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLMH_HUMAN
UniProt AC Q13867
Protein Name Bleomycin hydrolase
Gene Name BLMH
Organism Homo sapiens (Human).
Sequence Length 455
Subcellular Localization Cytoplasm.
Protein Description The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity..
Protein Sequence MSSSGLNSEKVAALIQKLNSDPQFVLAQNVGTTHDLLDICLKRATVQRAQHVFQHAVPQEGKPITNQKSSGRCWIFSCLNVMRLPFMKKLNIEEFEFSQSYLFFWDKVERCYFFLSAFVDTAQRKEPEDGRLVQFLLMNPANDGGQWDMLVNIVEKYGVIPKKCFPESYTTEATRRMNDILNHKMREFCIRLRNLVHSGATKGEISATQDVMMEEIFRVVCICLGNPPETFTWEYRDKDKNYQKIGPITPLEFYREHVKPLFNMEDKICLVNDPRPQHKYNKLYTVEYLSNMVGGRKTLYNNQPIDFLKKMVAASIKDGEAVWFGCDVGKHFNSKLGLSDMNLYDHELVFGVSLKNMNKAERLTFGESLMTHAMTFTAVSEKDDQDGAFTKWRVENSWGEDHGHKGYLCMTDEWFSEYVYEVVVDRKHVPEEVLAVLEQEPIILPAWDPMGALAE
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
1Acetylation-------MSSSGLNS
-------CCCCCCCH		8.71-
2Phosphorylation------MSSSGLNSE
------CCCCCCCHH		32.9619651622
3Phosphorylation-----MSSSGLNSEK
-----CCCCCCCHHH		27.4219651622
4Phosphorylation----MSSSGLNSEKV
----CCCCCCCHHHH		39.7418491316
10AcetylationSSGLNSEKVAALIQK
CCCCCHHHHHHHHHH		36.6719608861
10UbiquitinationSSGLNSEKVAALIQK
CCCCCHHHHHHHHHH		36.6723000965
17UbiquitinationKVAALIQKLNSDPQF
HHHHHHHHHCCCCCE		42.5129967540
42UbiquitinationDLLDICLKRATVQRA
HHHHHHHHHHHHHHH		35.2621963094
42AcetylationDLLDICLKRATVQRA
HHHHHHHHHHHHHHH		35.2626051181
45PhosphorylationDICLKRATVQRAQHV
HHHHHHHHHHHHHHH		22.6223532336
58PhosphorylationHVFQHAVPQEGKPIT
HHHHHCCCCCCCCCC		27.5632645325
62UbiquitinationHAVPQEGKPITNQKS
HCCCCCCCCCCCCCC		32.2821906983
68UbiquitinationGKPITNQKSSGRCWI
CCCCCCCCCCCCEEE		48.9724816145
184AcetylationMNDILNHKMREFCIR
HHHHHHHHHHHHHHH		38.2826822725
184UbiquitinationMNDILNHKMREFCIR
HHHHHHHHHHHHHHH		38.2824816145
202UbiquitinationLVHSGATKGEISATQ
HHHCCCCCCCCCCCH		54.7521963094
238UbiquitinationFTWEYRDKDKNYQKI
CEEEEECCCCCCCCC		62.7023503661
240UbiquitinationWEYRDKDKNYQKIGP
EEEECCCCCCCCCCC		64.3923503661
244UbiquitinationDKDKNYQKIGPITPL
CCCCCCCCCCCCCHH		38.9921906983
249PhosphorylationYQKIGPITPLEFYRE
CCCCCCCCHHHHHHH		25.59-
259AcetylationEFYREHVKPLFNMED
HHHHHHCCCCCCCCC		37.6026822725
259UbiquitinationEFYREHVKPLFNMED
HHHHHHCCCCCCCCC		37.6021906983
267UbiquitinationPLFNMEDKICLVNDP
CCCCCCCCEEEECCC		23.2429967540
279UbiquitinationNDPRPQHKYNKLYTV
CCCCCCCCCCCCHHH		45.3229967540
279AcetylationNDPRPQHKYNKLYTV
CCCCCCCCCCCCHHH		45.3223749302
280PhosphorylationDPRPQHKYNKLYTVE
CCCCCCCCCCCHHHH		18.53-
282UbiquitinationRPQHKYNKLYTVEYL
CCCCCCCCCHHHHHH		39.5229967540
282AcetylationRPQHKYNKLYTVEYL
CCCCCCCCCHHHHHH		39.5225953088
284PhosphorylationQHKYNKLYTVEYLSN
CCCCCCCHHHHHHHH		15.45-
288PhosphorylationNKLYTVEYLSNMVGG
CCCHHHHHHHHHCCC		15.87-
297UbiquitinationSNMVGGRKTLYNNQP
HHHCCCCCCCCCCCC		46.2723000965
300PhosphorylationVGGRKTLYNNQPIDF
CCCCCCCCCCCCHHH		19.8030576142
309UbiquitinationNQPIDFLKKMVAASI
CCCHHHHHHHHHHHC		38.5221906983
310UbiquitinationQPIDFLKKMVAASIK
CCHHHHHHHHHHHCC		40.5323503661
317UbiquitinationKMVAASIKDGEAVWF
HHHHHHCCCCCEEEE		58.1329967540
330UbiquitinationWFGCDVGKHFNSKLG
EEEEEEHHHHCCCCC		44.8929967540
330AcetylationWFGCDVGKHFNSKLG
EEEEEEHHHHCCCCC		44.8925953088
353PhosphorylationHELVFGVSLKNMNKA
CEEEEEEECCCCCHH		33.7224719451
391UbiquitinationDQDGAFTKWRVENSW
CCCCCEEEEEEECCC		26.9219608861
391AcetylationDQDGAFTKWRVENSW
CCCCCEEEEEEECCC		26.9219608861
420PhosphorylationEWFSEYVYEVVVDRK
HHHHHHCCEEEECCC		11.3418083107
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 BLMH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BLMH_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 BLMH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
9855622
KBTB7_HUMANKBTBD7physical
16189514
BLMH_HUMANBLMHphysical
16189514
TRIO_HUMANTRIOphysical
16169070
A4_HUMANAPPphysical
10973933
RL11_HUMANRPL11physical
10353821
RL29_HUMANRPL29physical
10353821
BLMH_HUMANBLMHphysical
21163940
TF2AA_HUMANGTF2A1physical
22863883
LZTL1_HUMANLZTFL1physical
22863883
PESC_HUMANPES1physical
22863883
SHLB2_HUMANSH3GLB2physical
22863883
BLMH_HUMANBLMHphysical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
NUD12_HUMANNUDT12physical
25416956
G6PD_HUMANG6PDphysical
26344197
NUD12_HUMANNUDT12physical
28514442
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
DB00290Bleomycin
Regulatory Network of BLMH_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-391, AND MASS SPECTROMETRY.

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