Q9H0B6 · KLC2_HUMAN
- ProteinKinesin light chain 2
- GeneKLC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids622 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends (PubMed:22172677).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | kinesin complex | |
Cellular Component | kinesin I complex | |
Cellular Component | lysosomal membrane | |
Cellular Component | membrane | |
Cellular Component | microtubule | |
Cellular Component | mitochondrion | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | cadherin binding | |
Molecular Function | kinesin binding | |
Biological Process | lysosome localization | |
Biological Process | microtubule-based movement |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKinesin light chain 2
- Short namesKLC 2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H0B6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Lysosome membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Spastic paraplegia, optic atrophy, and neuropathy (SPOAN)
- Note
- DescriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPOAN is characterized by spastic paraplegia with progressive joint contractures and spine deformities, loss of independent ambulation by age 10 years, sub-normal vision secondary to congenital optic atrophy, and neuropathy. Inheritance is autosomal recessive.
- See alsoMIM:609541
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_020379 | 517 | in dbSNP:rs2276036 | |||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 712 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000215095 | 1-622 | UniProt | Kinesin light chain 2 | |||
Sequence: MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGDNKPIWMHAEEREESKDKRRDSAPYGEYGSWYKACKVDSPTVNTTLRSLGALYRRQGKLEAAHTLEDCASRNRKQGLDPASQTKVVELLKDGSGRRGDRRSSRDMAGGAGPRSESDLEDVGPTAEWNGDGSGSLRRSGSFGKLRDALRRSSEMLVKKLQGGTPQEPPNPRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG | |||||||
Modified residue | 151 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 175 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 179 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 428 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 434 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 445 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 445 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 487 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 508 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 508 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 521 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 537 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 545 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 556 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 581 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 581 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 582 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 582 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 589 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 604 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 608 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 608 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 609 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 610 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 610 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 611 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 615 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 615 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 619 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Oligomeric complex composed of two heavy chains and two light chains (Probable). Interacts (via TPR repeats) with PLEKHM2 (Probable).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H0B6 | FYCO1 Q9BQS8 | 2 | EBI-726994, EBI-2869338 | |
XENO | Q9H0B6 | N P0DTC9 | 4 | EBI-726994, EBI-25475856 | |
BINARY | Q9H0B6 | SFN P31947 | 5 | EBI-726994, EBI-476295 | |
BINARY | Q9H0B6 | YWHAE P62258 | 6 | EBI-726994, EBI-356498 | |
BINARY | Q9H0B6 | YWHAZ P63104 | 6 | EBI-726994, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 78-143 | |||||
Sequence: ILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQI | ||||||
Compositional bias | 145-168 | Basic and acidic residues | ||||
Sequence: KLDEDASPNEEKGDVPKDTLDDLF | ||||||
Region | 145-191 | Disordered | ||||
Sequence: KLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGG | ||||||
Repeat | 198-231 | TPR 1 | ||||
Sequence: LRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKT | ||||||
Repeat | 240-273 | TPR 2 | ||||
Sequence: ATMLNILALVYRDQNKYKEAAHLLNDALAIREKT | ||||||
Repeat | 282-315 | TPR 3 | ||||
Sequence: AATLNNLAVLYGKRGKYKEAEPLCKRALEIREKV | ||||||
Repeat | 324-357 | TPR 4 | ||||
Sequence: AKQLSNLALLCQNQGKAEEVEYYYRRALEIYATR | ||||||
Repeat | 366-399 | TPR 5 | ||||
Sequence: AKTKNNLASCYLKQGKYQDAETLYKEILTRAHEK | ||||||
Repeat | 449-482 | TPR 6 | ||||
Sequence: NTTLRSLGALYRRQGKLEAAHTLEDCASRNRKQG | ||||||
Region | 476-548 | Disordered | ||||
Sequence: SRNRKQGLDPASQTKVVELLKDGSGRRGDRRSSRDMAGGAGPRSESDLEDVGPTAEWNGDGSGSLRRSGSFGK | ||||||
Compositional bias | 495-511 | Basic and acidic residues | ||||
Sequence: LKDGSGRRGDRRSSRDM | ||||||
Region | 563-622 | Disordered | ||||
Sequence: KLQGGTPQEPPNPRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG | ||||||
Compositional bias | 575-622 | Polar residues | ||||
Sequence: PRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG |
Sequence similarities
Belongs to the kinesin light chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9H0B6-1
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.
- Name1
- Length622
- Mass (Da)68,935
- Last updated2001-03-01 v1
- Checksum5B57ABE4DF6E396E
Q9H0B6-2
- Name2
- Differences from canonical
- 77-153: Missing
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 6 | in Ref. 2; BAB14302 | ||||
Sequence: F → Y | ||||||
Alternative sequence | VSP_043486 | 77-153 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 145-168 | Basic and acidic residues | ||||
Sequence: KLDEDASPNEEKGDVPKDTLDDLF | ||||||
Sequence conflict | 306 | in Ref. 2; BAB14039 | ||||
Sequence: K → R | ||||||
Compositional bias | 495-511 | Basic and acidic residues | ||||
Sequence: LKDGSGRRGDRRSSRDM | ||||||
Compositional bias | 575-622 | Polar residues | ||||
Sequence: PRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL136864 EMBL· GenBank· DDBJ | CAB66798.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022449 EMBL· GenBank· DDBJ | BAB14039.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022907 EMBL· GenBank· DDBJ | BAB14302.1 EMBL· GenBank· DDBJ | mRNA | ||
AK094593 EMBL· GenBank· DDBJ | BAG52895.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315725 EMBL· GenBank· DDBJ | BAG38081.1 EMBL· GenBank· DDBJ | mRNA | ||
AP000759 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP001107 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC034373 EMBL· GenBank· DDBJ | AAH34373.1 EMBL· GenBank· DDBJ | mRNA |