Domains within Homo sapiens protein BCS1_HUMAN (Q9Y276)

Mitochondrial chaperone BCS1

Alternative representations: 1 /

Protein length419 aa
Source databaseUniProt
Identifiers BCS1_HUMAN, Q9Y276, ENSP00000352219.3, ENSP00000352219, ENSP00000375957.1, ENSP00000375957, ENSP00000375958.2, ENSP00000375958, ENSP00000375959.2, ENSP00000375959, ENSP00000406494.1, ENSP00000406494, ENSP00000404999.1, ENSP00000404999, ENSP00000413908.1, ENSP00000413908, B3KTW9, Q7Z2V7, A0A024R467_HUMAN, A0A024R467, H2R1H7_PANTR, H2R1H7, K7ANP6, G3QHN5_GORGO, G3QHN5, C9J8G3_HUMAN, C9J8G3, A0A2J8NGH6_PANTR, A0A2J8NGH6, C9J1S9_HUMAN, C9J1S9, A0A2J8TU31_PONAB, A0A2J8TU31, A0A2J8NGH2_PANTR, A0A2J8NGH2, C9JAS4_HUMAN, C9JAS4, A0A2J8NGH7_PANTR, A0A2J8NGH7, C9J4Q9_HUMAN, C9J4Q9, A0A2J8NGJ0_PANTR, A0A2J8NGJ0, Q53RT4_HUMAN, Q53RT4
Source gene ENSG00000074582
Alternative splicing ENSP00000398957.1, ENSP00000412729.1, BCS1_HUMAN, ENSP00000397293.1, ENSP00000496514.1, H7C492_HUMAN, H7BZF6_HUMAN, ENSP00000391007.1

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

Predicted functional partners

BCS1_HUMAN is shown as BCS1L in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for BCS1L

Protein BCS1_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map05017Spinocerebellar ataxia
map05010Alzheimer disease

KEGG orthologous groups

KONameDescription
K03798ftsH, hflBcell division protease FtsH [EC:3.4.24.-]
K08900BCS1mitochondrial chaperone BCS1

Post-translational modifications

PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 6 PTMs annotated in this protein:

PTMCount
Phosphorylation3
Ubiquitination3

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein BCS1L.

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 9606.ENSP00000413908 in eggNOG.

OGTaxonomic classDescription
LCOG0465All organisms (root)cell division protease FtsH [EC:3.4.24.-],mitochondrial chaperone BCS1,AFG3 family protein [EC:3.4.24.-]
KOG0743Eukaryota (superkingdom)mitochondrial chaperone BCS1,solute carrier family 39 (zinc transporter), member 7
HU5ICMetazoa (kingdom)mitochondrial chaperone BCS1,solute carrier family 39 (zinc transporter), member 7
949I7Chordata (phylum)mitochondrial chaperone BCS1
5R3ZDSarcopterygii (superclass)mitochondrial chaperone BCS1
8Z5NCMammalia (class)mitochondrial chaperone BCS1
4R8W1Euarchontoglires (superorder)mitochondrial chaperone BCS1
4ZXGMPrimates (order)mitochondrial chaperone BCS1
98CZHHaplorrhini (suborder)mitochondrial chaperone BCS1
BVJ3YSimiiformes (infraorder)mitochondrial chaperone BCS1
9EWYYCatarrhini (parvorder)mitochondrial chaperone BCS1
9GRRIVertebrata (clade)mitochondrial chaperone BCS1
7IMV1Opisthokonta (clade)mitochondrial chaperone BCS1,solute carrier family 39 (zinc transporter), member 7
H5DFWBilateria (clade)mitochondrial chaperone BCS1,solute carrier family 39 (zinc transporter), member 7
FXFE0Hominoidea (superfamily)mitochondrial chaperone BCS1
5N3Q9Hominidae (family)mitochondrial chaperone BCS1
5XVF7Homininae (subfamily)mitochondrial chaperone BCS1

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: