Kinesin-1 heavy chain (KIF5B)
The protein contains 963 amino acids for an estimated molecular weight of 109685 Da.
Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner (By similarity). Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes (PubMed:20386726). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). Through binding with PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus ends (Probable). Involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells (PubMed:24088571). (updated: June 2, 2021)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Anterograde axonal protein transport
Anterograde dendritic transport of neurotransmitter receptor complex
Anterograde neuronal dense core vesicle transport
Axon guidance
Cellular protein metabolic process
Cellular response to interferon-gamma
Centrosome localization
Cytoplasm organization
Cytoskeleton-dependent intracellular transport
Hippocampus development
Lysosome localization
Microtubule-based movement
Natural killer cell mediated cytotoxicity
Plus-end-directed vesicle transport along microtubule
Positive regulation of establishment of protein localization to plasma membrane
Positive regulation of insulin secretion involved in cellular response to glucose stimulus
Positive regulation of intracellular protein transport
Positive regulation of potassium ion transport
Positive regulation of protein localization to plasma membrane
Positive regulation of synaptic transmission, GABAergic
Positive regulation of vesicle fusion
Positive regulation of voltage-gated sodium channel activity
Regulation of membrane potential
Retrograde neuronal dense core vesicle transport
Stress granule disassembly
Synaptic vesicle transport
Vesicle transport along microtubule
Cellular Component
Axon cytoplasm
Axonal growth cone
Centriolar satellite
Ciliary rootlet
Cytoplasm
Cytosol
Dendrite cytoplasm
Endocytic vesicle
Kinesin complex
Membrane
Microtubule
Microtubule organizing center
Neuron projection
Obsolete cell
Perinuclear region of cytoplasm
Phagocytic vesicle
Vesicle
The reference OMIM entry for this protein is 602809
Kinesin family member 5b; kif5b
Kinesin 1 heavy chain; kns1
Kinesin, heavy chain, ubiquitous; ukhc
Kinh
DESCRIPTION
Kinesins are microtubule-based motor proteins involved in the transport of organelles in eukaryotic cells. They typically consist of 2 identical, approximately 110- to 120-kD heavy chains, such as KIF5B, and 2 identical, approximately 60- to 70-kD light chains. The heavy chain contains 3 domains: a globular N-terminal motor domain, which converts the chemical energy of ATP into a motile force along microtubules in 1 fixed direction; a central alpha-helical rod domain, which enables the 2 heavy chains to dimerize; and a globular C-terminal domain, which interacts with light chains and possibly an organelle receptor (summary by Navone et al., 1992 and Niclas et al., 1994).CLONING
By screening a human placenta cDNA library with a probe based on a conserved region of the Drosophila and squid kinesin heavy chains (KHCs), Navone et al. (1992) isolated cDNAs encoding KNS1. The predicted 963-amino acid protein has 63% sequence identity to the Drosophila KHC. Immunoblot analysis using antibodies against squid KHC detected a 120-kD protein in CV-1 monkey kidney epithelial cells. Immunofluorescence studies showed that KNS1 expressed in CV-1 cells had both a diffuse distribution and a filamentous staining pattern that coaligned with microtubules but not vimentin (VIM; 193060) intermediate filaments; the KNS1 N- and C-terminal domains, but not the alpha-helical rod domain, also colocalized with microtubules. By Northern blot analysis, Niclas et al. (1994) demonstrated that Ukhc was expressed as multiple transcripts in all rat tissues examined. Immunoblot analysis of rat tissue extracts using antibodies specific for UKHC detected a 120-kD protein in all examined tissues. Niclas et al. (1994) found that UKHC is distributed uniformly between the cell body and processes of cultured hippocampal neurons.MAPPING
Niclas et al. (1994) stated that the placenta UKHC cDNA isolated by Navone et al. (1992) hybridizes to a region on mouse chromosome 18 that shows homology of synteny with human 18q. However, Gross (2013) mapped the human KIF5B gene to chromosome 10p11.22 based on an alignment of the KIF5B sequence (GenBank GENBANK BC126279) with the genomic sequence (GRCh37).NOMENCLATURE
Lawrence et al. (2004) presented a standardized kinesin nomenclature based on 14 family designations. Under this system, KIF5B belongs to the kinesin-1 family.GENE FUNCTION
Kamal et al. (2000) demonstrated that the axonal transport of APP in neurons is mediated by the direct binding of APP to the kinesin light chain (600025) subunit of kinesin-I. Kamal et al. (2001) identified an axonal membrane compartment that contains APP, beta-secretase (604252), and presenilin-1 (104311). The fast anterograde axonal transport of this compartment is mediated by APP and kinesin-I. Proteolytic processing of APP can occur in the compartment in vitro and in vivo in axons. This proteolysis generates amyloid-beta and a carboxy-terminal fragment of APP, and liberates kinesin-I from the membrane. Kamal et al. (2001) concluded that APP functions as a kinesin-I membrane receptor, mediating the axonal transport of beta-secretase and presenilin-1, and that processing of APP to amyloid-beta by secretases can occur in an axonal membrane compartment transported by kinesin-I. Kanai et al. (2004) found that the hinge and C-terminal tail regions of Kif5a (602821), Kif5b, and Kif5c (604593) bound a large detergent-resistant RNase-sensitive gra ... More on the omim web site
July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 2, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602809 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed