BTD_HUMAN - dbPTM
BTD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BTD_HUMAN
UniProt AC P43251
Protein Name Biotinidase
Gene Name BTD
Organism Homo sapiens (Human).
Sequence Length 543
Subcellular Localization Secreted, extracellular space.
Protein Description Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation..
Protein Sequence MAHAHIQGGRRAKSRFVVCIMSGARSKLALFLCGCYVVALGAHTGEESVADHHEAEYYVAAVYEHPSILSLNPLALISRQEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPSPQVVRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYFEAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAANVHHPVLGMTGSGIHTPLESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETDPSHSKFLKILSGDPYCEKDAQEVHCDEATKWNVNAPPTFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYERPTLSKELYALGVFDGLHTVHGTYYIQVCALVRCGGLGFDTCGQEITEATGIFEFHLWGNFSTSYIFPLFLTSGMTLEVPDQLGWENDHYFLRKSRLSSGLVTAALYGRLYERD
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
4Ubiquitination----MAHAHIQGGRR
----CCCCCCCCCCC
7.61-
24 (in isoform 2)Phosphorylation-12.7926434776
119N-linked_GlycosylationEDGIHGFNFTRTSIY
CCCCCCCCCCCCCCE
41.8117623646
121N-linked_GlycosylationGIHGFNFTRTSIYPF
CCCCCCCCCCCCEEC
33.8616335952
121N-linked_GlycosylationGIHGFNFTRTSIYPF
CCCCCCCCCCCCEEC
33.8616335952
150N-linked_GlycosylationCLEPHRFNDTEVLQR
CCCCCCCCCHHHHHH
56.0819139490
152N-linked_GlycosylationEPHRFNDTEVLQRLS
CCCCCCCHHHHHHHH
29.1516335952
152N-linked_GlycosylationEPHRFNDTEVLQRLS
CCCCCCCHHHHHHHH
29.1516335952
159PhosphorylationTEVLQRLSCMAIRGD
HHHHHHHHHHHHCCC
12.2022210691
175PhosphorylationFLVANLGTKEPCHSS
EEEEECCCCCCCCCC
35.0922210691
203N-linked_GlycosylationTNVVFSNNGTLVDRY
CEEEECCCCCEEEHH
43.5616335952
205N-linked_GlycosylationVVFSNNGTLVDRYRK
EEECCCCCEEEHHHH
26.2316335952
340UbiquitinationIIAQVAKNPVGLIGA
EEEEECCCCCCEECC
27.1029967540
349N-linked_GlycosylationVGLIGAENATGETDP
CCEECCCCCCCCCCC
42.1219159218
351N-linked_GlycosylationLIGAENATGETDPSH
EECCCCCCCCCCCCH
47.3216335952
351N-linked_GlycosylationLIGAENATGETDPSH
EECCCCCCCCCCCCH
47.3216335952
353UbiquitinationGAENATGETDPSHSK
CCCCCCCCCCCCHHH
45.7629967540
362UbiquitinationDPSHSKFLKILSGDP
CCCHHHHHHHHCCCC
3.76-
370PhosphorylationKILSGDPYCEKDAQE
HHHCCCCCCCCCCCE
20.2730576142
375UbiquitinationDPYCEKDAQEVHCDE
CCCCCCCCCEECCCH
20.64-
402N-linked_GlycosylationHSEMMYDNFTLVPVW
CCHHCCCCEEEEEEC
17.8316335952
404N-linked_GlycosylationEMMYDNFTLVPVWGK
HHCCCCEEEEEECCC
32.8516335952
489N-linked_GlycosylationFEFHLWGNFSTSYIF
EEEEEECCCCCCCEE
19.00UniProtKB CARBOHYD
524PhosphorylationDHYFLRKSRLSSGLV
CCEEEHHHHHHHHHH
31.83-
527PhosphorylationFLRKSRLSSGLVTAA
EEHHHHHHHHHHHHH
22.6529449344
528PhosphorylationLRKSRLSSGLVTAAL
EHHHHHHHHHHHHHH
40.5129449344
532PhosphorylationRLSSGLVTAALYGRL
HHHHHHHHHHHHHHH
15.9729449344
536PhosphorylationGLVTAALYGRLYERD
HHHHHHHHHHHHCCC
8.7529449344

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 BTD_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BTD_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 BTD_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO1D_HUMANMYO1Dphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
253260Biotinidase deficiency (BTD deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BTD_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-349 ANDASN-402, AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-203;ASN-349 AND ASN-402, AND MASS SPECTROMETRY.

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