Domains within Homo sapiens protein TILB_HUMAN (Q86X45)

Protein tilB homolog

Alternative representations: 1 /

Protein length466 aa
Source databaseUniProt
Identifiers TILB_HUMAN, Q86X45, ENSP00000429791.1, ENSP00000429791, ENSP00000484634.1, ENSP00000484634, Q13648, Q4G183
Source gene ENSG00000129295
Alternative splicing TILB_HUMAN, H0YAS5_HUMAN, G5EA20_HUMAN, H0YBC4_HUMAN, E5RHF9_HUMAN, A0A087X298_HUMAN

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.

This domain architecture was probably invented with the emergence of Eukaryota

Predicted functional partners

TILB_HUMAN is shown as LRRC6 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 LRRC6

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

KEGG pathways

PathwayDescription
map04921Oxytocin signaling pathway
map04514Cell adhesion molecules

KEGG orthologous groups

KONameDescription
K22038LRRC8volume-regulated anion channel
K17550PPP1R7, SDS22protein phosphatase 1 regulatory subunit 7

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 2 PTMs annotated in this protein:

PTMCount
Phosphorylation2

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein LRRC6.

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.ENSP00000484634 in eggNOG.

OGTaxonomic classDescription
LCOG1552All organisms (root)volume-regulated anion channel,leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein,protein phosphatase 1 regulatory subunit 7
KOG0531Eukaryota (superkingdom)protein phosphatase 1 regulatory subunit 7,dynein axonemal light chain 1,dynein axonemal assembly factor 11
HU7J4Metazoa (kingdom)dynein axonemal assembly factor 11
9449XChordata (phylum)dynein axonemal assembly factor 11
5RCWBSarcopterygii (superclass)dynein axonemal assembly factor 11
8ZA88Mammalia (class)dynein axonemal assembly factor 11
4RFR7Euarchontoglires (superorder)dynein axonemal assembly factor 11
4ZX8PPrimates (order)dynein axonemal assembly factor 11
986Z0Haplorrhini (suborder)dynein axonemal assembly factor 11
BVF33Simiiformes (infraorder)dynein axonemal assembly factor 11
9ERNKCatarrhini (parvorder)dynein axonemal assembly factor 11
9FNZYVertebrata (clade)dynein axonemal assembly factor 11
H5BJSBilateria (clade)dynein axonemal assembly factor 11
7K6A5Opisthokonta (clade)dynein axonemal assembly factor 11
FX6SHHominoidea (superfamily)dynein axonemal assembly factor 11
5MZIAHominidae (family)dynein axonemal assembly factor 11
5Y11YHomininae (subfamily)dynein axonemal assembly factor 11

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: