BCS1_HUMAN - dbPTM
BCS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCS1_HUMAN
UniProt AC Q9Y276
Protein Name Mitochondrial chaperone BCS1
Gene Name BCS1L
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization Mitochondrion inner membrane
Single-pass membrane protein .
Protein Description Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex..
Protein Sequence MPLSDFILALKDNPYFGAGFGLVGVGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRHSTRTQHLSVETSYLQHESGRISTKFEFVPSPGNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFGYPRRRRPLNSVVLQQGLADRIVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYVGYCSHWQLTQMFQRFYPGQAPSLAENFAEHVLRATNQISPAQVQGYFMLYKNDPVGAIHNAESLRR
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
4Phosphorylation----MPLSDFILALK
----CCHHHHHHHHC
25.30-
145UbiquitinationTALGTDRKVFFNILE
EEECCCHHHHHHHHH
46.3221890473
169PhosphorylationEEGKTVMYTAVGSEW
HCCCEEEEEEECCCC
6.2928152594
170PhosphorylationEGKTVMYTAVGSEWR
CCCEEEEEEECCCCC
9.2128152594
174PhosphorylationVMYTAVGSEWRPFGY
EEEEEECCCCCCCCC
27.6428152594
181PhosphorylationSEWRPFGYPRRRRPL
CCCCCCCCCCCCCCC
8.2412910490
213UbiquitinationQEFIDNPKWYTDRGI
HHHHHCCCCCCCCCC
60.1221890473
241PhosphorylationCGKSSFITALAGELE
CCHHHHHHHHHHHHC
17.3822210691
262PhosphorylationSLTDSSLSDDRLNHL
ECCCCCCCHHHHHHH
39.1422210691
271PhosphorylationDRLNHLLSVAPQQSL
HHHHHHHHHCCCCEE
23.6924719451
277PhosphorylationLSVAPQQSLVLLEDV
HHHCCCCEEEEEECC
18.3924719451
290PhosphorylationDVDAAFLSRDLAVEN
CCCHHHHCCCCCCCC
19.7924719451
300UbiquitinationLAVENPVKYQGLGRL
CCCCCCCCCCCCCCC
32.8721890473
330PhosphorylationEARIVFMTTNHVDRL
CEEEEEEECCCHHCC
17.0020068231
331PhosphorylationARIVFMTTNHVDRLD
EEEEEEECCCHHCCC
16.1320068231

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 BCS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCS1_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 BCS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNJA1_HUMANDNAJA1physical
21900206
UCRI_HUMANUQCRFS1physical
22939629
RM10_HUMANMRPL10physical
22939629
AIFM1_HUMANAIFM1physical
26344197
VAPA_HUMANVAPAphysical
26344197

Drug and Disease Associations
Kegg Disease
H00473 Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency (
H00820 Bjornstad syndrome
OMIM Disease
603358GRACILE syndrome (GRACILE)
124000Mitochondrial complex III deficiency, nuclear 1 (MC3DN1)
262000Bjoernstad syndrome (BJS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BCS1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181, AND MASSSPECTROMETRY.

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