Domains within Homo sapiens protein CALB2_HUMAN (P22676)

Calretinin

Alternative representations: 1 /

Protein length271 aa
Source databaseUniProt
Identifiers CALB2_HUMAN, P22676, ENSP00000307508.4, ENSP00000307508, ENSP00000488916.1, ENSP00000488916, A8K4Y1, Q53HD2, Q96BK4, A0A140VK08_HUMAN, A0A140VK08
Source gene ENSG00000172137
Alternative splicing CALB2_HUMAN, H3BN14_HUMAN, H3BMN5_HUMAN, A6NER6_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 cellular organisms

Predicted functional partners

CALB2_HUMAN is shown as CALB2 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 CALB2

Protein CALB2_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map00760Nicotinate and nicotinamide metabolism iPath3
map04961Endocrine and other factor-regulated calcium reabsorption
map04626Plant-pathogen interaction
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K13448CMLcalcium-binding protein CML
K23908CALB2calretinin

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 11 PTMs annotated in this protein:

PTMCount
Phosphorylation11

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein CALB2.

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.ENSP00000307508 in eggNOG.

OGTaxonomic classDescription
LCOG5126All organisms (root)calcium-binding protein CML,calmodulin,serine/threonine-protein phosphatase 2B regulatory subunit
KOG0027Eukaryota (superkingdom)calcium-binding protein CML,calmodulin,calcium-binding protein 1/2/4/5
HVH7JMetazoa (kingdom)calretinin,calbindin,secretagogin
94FMMChordata (phylum)calretinin,calbindin,secretagogin
5QT9HSarcopterygii (superclass)calretinin,purine-nucleoside phosphorylase [EC:2.4.2.1]
8Z4TJMammalia (class)calretinin
4RDQWEuarchontoglires (superorder)calretinin
4ZTRBPrimates (order)calretinin
98CMHHaplorrhini (suborder)calretinin
BVJT3Simiiformes (infraorder)calretinin
9EVSPCatarrhini (parvorder)calretinin
7J97ROpisthokonta (clade)calretinin,calbindin,secretagogin
H3QH8Bilateria (clade)calretinin,calbindin,secretagogin
9FGC5Vertebrata (clade)calbindin,calretinin,purine-nucleoside phosphorylase [EC:2.4.2.1]
FWZ9THominoidea (superfamily)calretinin
5MXC8Hominidae (family)calretinin
5Y13CHomininae (subfamily)calretinin

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: