O35465 · FKBP8_MOUSE

  • Protein
    Peptidyl-prolyl cis-trans isomerase FKBP8
  • Gene
    Fkbp8
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity).
Required for normal embryonic development

Miscellaneous

Binds the immunosuppressant FK506 only in its calmodulin/calcium activated form.

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentendomembrane system
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmembrane
Cellular Componentmitochondrial envelope
Cellular Componentmitochondrial membrane
Cellular Componentmitochondrion
Cellular Componentprotein-containing complex
Molecular Functioncalmodulin binding
Molecular Functiondisordered domain specific binding
Molecular Functionidentical protein binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functionprotein folding chaperone
Biological Processapoptotic process
Biological ProcessBMP signaling pathway
Biological Processcamera-type eye development
Biological Processcell fate specification
Biological Processdorsal/ventral neural tube patterning
Biological Processdorsal/ventral pattern formation
Biological Processmulticellular organism growth
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of protein phosphorylation
Biological Processneural tube development
Biological Processneuron fate specification
Biological Processpositive regulation of BMP signaling pathway
Biological Processprotein folding
Biological Processprotein localization to mitochondrion
Biological Processregulation of BMP signaling pathway
Biological Processregulation of gene expression
Biological Processregulation of mitophagy
Biological Processsmoothened signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase FKBP8
  • EC number
  • Short names
    PPIase FKBP8
  • Alternative names
    • 38 kDa FK506-binding protein (38 kDa FKBP; FKBP-38; mFKBP38)
    • FK506-binding protein 8 (FKBP-8)
    • FKBPR38
    • Rotamase

Gene names

    • Name
      Fkbp8
    • Synonyms
      Fkbp38, Sam11

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
    • NOD
    • FVB/N
    • C57BL/6 X DBA/2
    • 129/SvJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O35465
  • Secondary accessions
    • Q3UK86
    • Q6GTX9
    • Q811M7
    • Q811R4
    • Q8C2F0
    • Q99L93

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane380-400Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Mice die shortly after birth. They display neural tube and skeletal defects. The neuroepithelium is disorganized and the formation of dorsal root ganglia is defective, likely as a result of an increased frequency of apoptosis and aberrant migration of neuronal cells. The extension of nerve fibers in the spinal cord is also abnormal.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000753321-402Peptidyl-prolyl cis-trans isomerase FKBP8
Cross-link239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue286Phosphoserine
Cross-link297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link338Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link341Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link342Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected throughout the embryonic body, in caudal neural tube, limbs and head. Detected in adult retina, brain, heart, kidney, liver, pancreas, lung, testis and urinary bladder (at protein level). Detected in adult brain, kidney, liver, testis and trigeminal nerve, and in embryo. Detected at lower levels in lung, spleen, heart and ovary. Widely expressed in forebrain. Detected in the Purkinje cell layer in the cerebellum and in hippocampus neurons.

Gene expression databases

Interaction

Subunit

Homomultimers or heteromultimers (Potential). Forms heterodimer with calmodulin. When activated by calmodulin and calcium, interacts with the BH4 domain of BCL2 and weakly with BCLX isoform Bcl-X(L). Does not bind and inhibit calcineurin (By similarity).
Interacts with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, repeat.

TypeIDPosition(s)Description
Compositional bias28-42Acidic residues
Region28-54Disordered
Domain110-194PPIase FKBP-type
Repeat211-244TPR 1
Repeat262-295TPR 2
Repeat296-329TPR 3

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

O35465-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    402
  • Mass (Da)
    43,529
  • Last updated
    2008-07-01 v2
  • Checksum
    609A954FAD3A76F8
MASWAEPSEPAALRLPGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRMKTLVPGPKGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNTKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKRAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN

O35465-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3Z597D3Z597_MOUSEFkbp856
F6WP10F6WP10_MOUSEFkbp836

Sequence caution

The sequence AAB86422.1 differs from that shown. Reason: Erroneous initiation
The sequence AAH03739.1 differs from that shown. Reason: Erroneous initiation
The sequence AAH27808.1 differs from that shown. Reason: Erroneous initiation
The sequence AAO27795.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence BAC40541.1 differs from that shown. Reason: Erroneous initiation
The sequence BAE26916.1 differs from that shown. Reason: Erroneous initiation
The sequence BAE31027.1 differs from that shown. Reason: Erroneous initiation
The sequence BAE38118.1 differs from that shown. Reason: Erroneous initiation
The sequence BAE39713.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias28-42Acidic residues
Sequence conflict100in Ref. 1; AAO39021, 2; AAQ84562, 4; AAH03739 and 5; AAB86422
Sequence conflict163in Ref. 3; BAE26916
Sequence conflict170in Ref. 3; BAC40541
Alternative sequenceVSP_034487173in isoform 2
Sequence conflict400in Ref. 1; AAO39021, 2; AAQ84562, 4; AAH03739 and 5; AAB86422

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY225340
EMBL· GenBank· DDBJ
AAO39021.1
EMBL· GenBank· DDBJ
mRNA
AY278608
EMBL· GenBank· DDBJ
AAQ84562.1
EMBL· GenBank· DDBJ
mRNA
AK088739
EMBL· GenBank· DDBJ
BAC40541.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK146122
EMBL· GenBank· DDBJ
BAE26916.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK152198
EMBL· GenBank· DDBJ
BAE31027.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK165281
EMBL· GenBank· DDBJ
BAE38118.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK167663
EMBL· GenBank· DDBJ
BAE39713.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC003739
EMBL· GenBank· DDBJ
AAH03739.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC027808
EMBL· GenBank· DDBJ
AAH27808.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AF030635
EMBL· GenBank· DDBJ
AAB86422.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AY187231
EMBL· GenBank· DDBJ
AAO27795.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp