BPL1_HUMAN - dbPTM
BPL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BPL1_HUMAN
UniProt AC P50747
Protein Name Biotin--protein ligase
Gene Name HLCS
Organism Homo sapiens (Human).
Sequence Length 726
Subcellular Localization Cytoplasm. Mitochondrion.
Protein Description Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase..
Protein Sequence MEDRLHMDNGLVPQKIVSVHLQDSTLKEVKDQVSNKQAQILEPKPEPSLEIKPEQDGMEHVGRDDPKALGEEPKQRRGSASGSEPAGDSDRGGGPVEHYHLHLSSCHECLELENSTIESVKFASAENIPDLPYDYSSSLESVADETSPEREGRRVNLTGKAPNILLYVGSDSQEALGRFHEVRSVLADCVDIDSYILYHLLEDSALRDPWTDNCLLLVIATRESIPEDLYQKFMAYLSQGGKVLGLSSSFTFGGFQVTSKGALHKTVQNLVFSKADQSEVKLSVLSSGCRYQEGPVRLSPGRLQGHLENEDKDRMIVHVPFGTRGGEAVLCQVHLELPPSSNIVQTPEDFNLLKSSNFRRYEVLREILTTLGLSCDMKQVPALTPLYLLSAAEEIRDPLMQWLGKHVDSEGEIKSGQLSLRFVSSYVSEVEITPSCIPVVTNMEAFSSEHFNLEIYRQNLQTKQLGKVILFAEVTPTTMRLLDGLMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGCGFNVTNSNPTICINDLITEYNKQHKAELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIVGLDDSGFLQVHQEGGEVVTVHPDGNSFDMLRNLILPKRR
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
79PhosphorylationEPKQRRGSASGSEPA
CCCCCCCCCCCCCCC
19.9029255136
81PhosphorylationKQRRGSASGSEPAGD
CCCCCCCCCCCCCCC
44.5423927012
83PhosphorylationRRGSASGSEPAGDSD
CCCCCCCCCCCCCCC
37.6023927012
89PhosphorylationGSEPAGDSDRGGGPV
CCCCCCCCCCCCCCC
28.4323927012
119PhosphorylationLENSTIESVKFASAE
HCCCCEEEEEECCCC
27.1026074081
124PhosphorylationIESVKFASAENIPDL
EEEEEECCCCCCCCC
38.9728176443
133PhosphorylationENIPDLPYDYSSSLE
CCCCCCCCCCCCCHH
34.5128450419
135PhosphorylationIPDLPYDYSSSLESV
CCCCCCCCCCCHHHH
12.4728450419
136PhosphorylationPDLPYDYSSSLESVA
CCCCCCCCCCHHHHC
15.5628450419
137PhosphorylationDLPYDYSSSLESVAD
CCCCCCCCCHHHHCC
32.4828450419
138PhosphorylationLPYDYSSSLESVADE
CCCCCCCCHHHHCCC
30.1630576142
141PhosphorylationDYSSSLESVADETSP
CCCCCHHHHCCCCCC
28.0928450419
146PhosphorylationLESVADETSPEREGR
HHHHCCCCCCCCCCC
50.5625159151
147PhosphorylationESVADETSPEREGRR
HHHCCCCCCCCCCCC
23.7925159151
236PhosphorylationLYQKFMAYLSQGGKV
HHHHHHHHHHCCCEE
8.63-
238PhosphorylationQKFMAYLSQGGKVLG
HHHHHHHHCCCEEEE
17.69-
259PhosphorylationFGGFQVTSKGALHKT
ECCEEEECCCHHHHH
30.18-
274UbiquitinationVQNLVFSKADQSEVK
HHHHHHCCCCCCHHH
44.5129967540
299PhosphorylationQEGPVRLSPGRLQGH
CCCCCEECCCCEECC
18.109396568
312UbiquitinationGHLENEDKDRMIVHV
CCCCCCCCCCEEEEE
40.8424816145
355PhosphorylationEDFNLLKSSNFRRYE
HHHCCHHCCCCCHHH
30.4028634120
356PhosphorylationDFNLLKSSNFRRYEV
HHCCHHCCCCCHHHH
38.1028634120
419PhosphorylationEIKSGQLSLRFVSSY
CCCCCEEEEEEHHHC
15.0424719451
459UbiquitinationNLEIYRQNLQTKQLG
CHHHHHHHCCCCCCC
25.7224816145
527PhosphorylationALSTLLISIPLRSQL
HHHHHHHHHHHHHHH
20.3724719451
567UbiquitinationQDINLRVKWPNDIYY
CCCCEEECCCCCCCH
50.96-
635PhosphorylationLKPLRADYLIARVVT
CCHHCHHHHHHHHHH
10.06-
642PhosphorylationYLIARVVTVLEKLIK
HHHHHHHHHHHHHHH
19.27-

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 BPL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BPL1_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 BPL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACACB_HUMANACACBphysical
20085763
BPL1_HUMANHLCSphysical
20085763
SNX27_HUMANSNX27physical
21988832
TBC20_HUMANTBC1D20physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
253270Holocarboxylase synthetase deficiency (HLCS deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00121Biotin
Regulatory Network of BPL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-147, AND MASSSPECTROMETRY.

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