Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

UniProtKB entry Q9H3L0 (MMAD_HUMAN), Cobalamin trafficking protein CblD

Interaction between MMACHC and MMADHC, two human proteins participating in intracellular vitamin B₁₂ metabolism.

Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism.

Subcellular location of MMACHC and MMADHC, two human proteins central to intracellular vitamin B(12) metabolism.

The C-terminal domain of CblD interacts with CblC and influences intracellular cobalamin partitioning.

Characterization of functional domains of the cblD (MMADHC) gene product.

Methionine synthase and methionine synthase reductase interact with MMACHC and with MMADHC.

A reference map of the human binary protein interactome.

An Interprotein Co-S Coordination Complex in the B(12)-Trafficking Pathway.

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

Cobalamin (Cbl) metabolism

MMACHC:cob(II)alamin binds MMADHC

MMADHC targets transport of cytosolic cob(II)alamin to mitochondria

cob(II)alamin is transferred from MMACHC:MMADHC:cob(II)alamin to MTRR:MTR

Defective MMADHC does not bind MMACHC:B12r

Mitochondrial depolarization stabilizes the vitamin B(12) chaperone MMADHC in the cytosol to increase MTR activity.

Afg3l2 couples mitochondrial vitamin B12 trafficking to amino acid metabolism to safeguard hematopoietic stem cell homeostasis.

Gene identification for the cblD defect of vitamin B12 metabolism.

UniProtKB entry P22033 (MUTA_HUMAN), Methylmalonyl-CoA mutase, mitochondrial

Structure of Human B12 Trafficking Protein CblD Reveals Molecular Mimicry and Identifies a New Subfamily of Nitro-FMN Reductases.

OpenScientist focused report on whether the mitochondrial MMADHC pool performs part of the AdoCbl-supply function in the matrix