Domains within Homo sapiens protein ZFR_HUMAN (Q96KR1)

Zinc finger RNA-binding protein

Alternative representations: 1 /

Protein length1074 aa
Source databaseUniProt
Identifiers ZFR_HUMAN, Q96KR1, ENSP00000265069.8, ENSP00000265069, B2RNR5, Q05C08, Q3B7X5, Q6P5A3, Q86UA0, Q9H6V4, Q9NTI1, Q9Y687
Source gene ENSG00000056097
Alternative splicing ZFR_HUMAN, H0Y8W1_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 Coelomata

Predicted functional partners

ZFR_HUMAN is shown as ZFR 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 ZFR

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

KEGG pathways

PathwayDescription
map04722Neurotrophin signaling pathway

KEGG orthologous groups

KONameDescription
K13203ZFRzinc finger RNA-binding protein

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 32 PTMs annotated in this protein:

PTMCount
Phosphorylation18
Ubiquitination5
Acetylation5
O-linked glycosylation4

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

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.ENSP00000265069 in eggNOG.

OGTaxonomic classDescription
LKOG3792All organisms (root)zinc finger RNA-binding protein,interleukin enhancer-binding factor 3,spermatid perinuclear RNA-binding protein
KOG3792Eukaryota (superkingdom)zinc finger RNA-binding protein,interleukin enhancer-binding factor 3,spermatid perinuclear RNA-binding protein
HTIM6Metazoa (kingdom)zinc finger RNA-binding protein,megakaryocyte-associated tyrosine kinase [EC:2.7.10.2],spermatid perinuclear RNA-binding protein
93EEZChordata (phylum)zinc finger RNA-binding protein,megakaryocyte-associated tyrosine kinase [EC:2.7.10.2]
5QSK8Sarcopterygii (superclass)zinc finger RNA-binding protein,megakaryocyte-associated tyrosine kinase [EC:2.7.10.2]
8Z3SGMammalia (class)zinc finger RNA-binding protein,megakaryocyte-associated tyrosine kinase [EC:2.7.10.2]
4RNQ4Euarchontoglires (superorder)zinc finger RNA-binding protein
504IDPrimates (order)zinc finger RNA-binding protein
98FKTHaplorrhini (suborder)zinc finger RNA-binding protein
BVC94Simiiformes (infraorder)zinc finger RNA-binding protein
9EY8XCatarrhini (parvorder)zinc finger RNA-binding protein
7IRFVOpisthokonta (clade)zinc finger RNA-binding protein,megakaryocyte-associated tyrosine kinase [EC:2.7.10.2],spermatid perinuclear RNA-binding protein
H6F6GBilateria (clade)zinc finger RNA-binding protein,megakaryocyte-associated tyrosine kinase [EC:2.7.10.2],spermatid perinuclear RNA-binding protein
9FZA4Vertebrata (clade)zinc finger RNA-binding protein,megakaryocyte-associated tyrosine kinase [EC:2.7.10.2]
FX0A8Hominoidea (superfamily)zinc finger RNA-binding protein
5NC0KHominidae (family)zinc finger RNA-binding protein
5Y6SDHomininae (subfamily)zinc finger RNA-binding 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: