Domains within Homo sapiens protein CRIM1_HUMAN (Q9NZV1)

Cysteine-rich motor neuron 1 protein

Alternative representations: 1 /

Protein length1036 aa
Source databaseUniProt
Identifiers CRIM1_HUMAN, Q9NZV1, ENSP00000280527.2, ENSP00000280527, Q2M2G4, Q59GH0, Q7LCQ5, Q9H318
Source gene ENSG00000150938
Alternative splicing CRIM1_HUMAN, H7C2T6_HUMAN, H7C458_HUMAN, ENSP00000403120.1

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.

This domain architecture was probably invented with the emergence of Chordata

Predicted functional partners

CRIM1_HUMAN is shown as CRIM1 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 CRIM1

Protein CRIM1_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map05165Human papillomavirus infection
map04610Complement and coagulation cascades

KEGG orthologous groups

KONameDescription
K24518CRIM1cysteine-rich motor neuron 1 protein
K01051E3.1.1.11pectinesterase [EC:3.1.1.11] iPath3
Some of these orthologous groups are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

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 10 PTMs annotated in this protein:

PTMCount
Phosphorylation8
Ubiquitination2

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein CRIM1.

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.ENSP00000280527 in eggNOG.

OGTaxonomic classDescription
7553KAll organisms (root)pectinesterase [EC:3.1.1.11],Rho family-interacting cell polarization regulator,calcineurin-binding protein cabin-1
KOG1216Eukaryota (superkingdom)pectinesterase [EC:3.1.1.11],Rho family-interacting cell polarization regulator,calcineurin-binding protein cabin-1
HSRX8Metazoa (kingdom)cysteine-rich motor neuron 1 protein,otogelin,von Willebrand factor
948N4Chordata (phylum)cysteine-rich motor neuron 1 protein
5R62ZSarcopterygii (superclass)cysteine-rich motor neuron 1 protein
8ZFJVMammalia (class)cysteine-rich motor neuron 1 protein
4RQM3Euarchontoglires (superorder)cysteine-rich motor neuron 1 protein
502BYPrimates (order)cysteine-rich motor neuron 1 protein
98RDHHaplorrhini (suborder)cysteine-rich motor neuron 1 protein
BVJKSSimiiformes (infraorder)cysteine-rich motor neuron 1 protein
9EN9RCatarrhini (parvorder)cysteine-rich motor neuron 1 protein
H3BVNBilateria (clade)cysteine-rich motor neuron 1 protein,reduction in cnn dots 2
7I09ZOpisthokonta (clade)cysteine-rich motor neuron 1 protein,otogelin,von Willebrand factor
9GKY8Vertebrata (clade)cysteine-rich motor neuron 1 protein
FX7DAHominoidea (superfamily)cysteine-rich motor neuron 1 protein
5N1XYHominidae (family)cysteine-rich motor neuron 1 protein
5Y0XFHomininae (subfamily)cysteine-rich motor neuron 1 protein

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: