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MKKS MKKS centrosomal shuttling protein [ Ficedula albicollis (Collared flycatcher) ]

Gene ID: 101807131, updated on 3-Aug-2024

Summary

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Gene symbol
MKKS
Gene description
MKKS centrosomal shuttling protein
See related
Ensembl:ENSFALG00000011040
Gene type
protein coding
RefSeq status
MODEL
Organism
Ficedula albicollis
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves; Passeriformes; Muscicapidae; Ficedula
Orthologs
human mouse all
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Genomic context

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See MKKS in Genome Data Viewer
Location:
chromosome: 3
Exon count:
9
Annotation release Status Assembly Chr Location
101 current FicAlb1.5 (GCF_000247815.1) 3 NC_021674.1 (4788953..4798916, complement)

Chromosome 3 - NC_021674.1Genomic Context describing neighboring genes Neighboring gene tubulin monoglycylase TTLL3-like Neighboring gene synaptosome associated protein 25 Neighboring gene SLX4 interacting protein Neighboring gene jagged canonical Notch ligand 1

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_021674.1 Chromosome 3 Reference FicAlb1.5 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

General gene information

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Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in chaperone-mediated protein complex assembly IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in cilium assembly IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in developmental process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in intracellular transport IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in kinociliary basal body IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin
Names
McKusick-Kaufman syndrome

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Ficedula albicollis Annotation Release 101 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference FicAlb1.5 Primary Assembly

Genomic

  1. NC_021674.1 Reference FicAlb1.5 Primary Assembly

    Range
    4788953..4798916 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005042756.2 → XP_005042813.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042813.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  2. XM_016297123.1 → XP_016152609.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    UniProtKB/TrEMBL
    U3K919
    Related
    ENSFALP00000011523.1, ENSFALT00000011570.2
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  3. XM_005042751.2 → XP_005042808.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042808.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  4. XM_005042757.2 → XP_005042814.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042814.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  5. XM_005042752.2 → XP_005042809.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042809.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  6. XM_005042750.2 → XP_005042807.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042807.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  7. XM_005042755.2 → XP_005042812.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042812.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  8. XM_005042749.2 → XP_005042806.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042806.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  9. XM_005042747.2 → XP_005042804.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042804.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  10. XM_005042754.2 → XP_005042811.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042811.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  11. XM_005042746.2 → XP_005042803.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042803.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  12. XM_005042744.2 → XP_005042801.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042801.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  13. XM_005042753.2 → XP_005042810.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042810.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  14. XM_005042743.2 → XP_005042800.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042800.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  15. XM_005042741.2 → XP_005042798.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042798.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  16. XM_005042745.2 → XP_005042802.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042802.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  17. XM_005042742.2 → XP_005042799.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042799.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  18. XM_005042748.2 → XP_005042805.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    See identical proteins and their annotated locations for XP_005042805.1

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...

  19. XM_016297124.1 → XP_016152610.1  McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin

    UniProtKB/TrEMBL
    U3K919
    Conserved Domains (2) summary
    pfam00118
    Location:29 → 570
    Cpn60_TCP1; TCP-1/cpn60 chaperonin family
    cl02777
    Location:29 → 478
    chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...
Nucleotide Protein
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