Domains within Homo sapiens protein DUS11_HUMAN (O75319)

RNA/RNP complex-1-interacting phosphatase

Alternative representations: 1 /

Protein length377 aa
Source databaseUniProt
Identifiers DUS11_HUMAN, O75319, ENSP00000272444.3, ENSP00000272444, B2RCT8, C9JYA6, Q6AI47, Q9BWE3
Source gene ENSG00000144048
Alternative splicing DUS11_HUMAN, O75319-2, H7C0E6_HUMAN

Predicted functional partners

DUS11_HUMAN is shown as DUSP11 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 DUSP11

Protein DUS11_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map03015mRNA surveillance pathway

KEGG orthologous groups

KONameDescription
K13917RNGTTmRNA-capping enzyme [EC:2.7.7.50 3.6.1.74]

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
Ubiquitination2

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein DUSP11.

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.ENSP00000272444 in eggNOG.

OGTaxonomic classDescription
LKOG2386All organisms (root)mRNA-capping enzyme [EC:2.7.7.50 3.6.1.74],atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48],mRNA guanylyltransferase [EC:2.7.7.50]
KOG2386Eukaryota (superkingdom)mRNA-capping enzyme [EC:2.7.7.50 3.6.1.74],atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48],mRNA guanylyltransferase [EC:2.7.7.50]
HWAPDMetazoa (kingdom)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
94PH1Chordata (phylum)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
5QK6YSarcopterygii (superclass)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
8Z00YMammalia (class)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
4RMTYEuarchontoglires (superorder)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
4ZYEPPrimates (order)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
9874GHaplorrhini (suborder)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
BV7HISimiiformes (infraorder)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
9F2AQCatarrhini (parvorder)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
9FNJGVertebrata (clade)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
H6G2SBilateria (clade)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
7GZVSOpisthokonta (clade)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
FXETEHominoidea (superfamily)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
5N04BHominidae (family)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]
5XXVBHomininae (subfamily)atypical dual specificity phosphatase [EC:3.1.3.16 3.1.3.48]

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: