Q9NSK0 (KLC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 99.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Kinesin light chain 4 Short name=KLC 4 Alternative name(s): Kinesin-like protein 8 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 619 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity By similarity. |
| Subunit structure | Oligomeric complex composed of two heavy chains and two light chains By similarity. |
| Subcellular location | Cytoplasm › cytoskeleton Probable. |
| Sequence similarities | Belongs to the kinesin light chain family. Contains 7 TPR repeats. |
| Sequence caution | The sequence BAC86788.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton Microtubule |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil Repeat TPR repeat |
| Molecular function | Motor protein |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW kinesin complexInferred from electronic annotation. Source: InterPro microtubuleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro microtubule motor activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9NSK0-1) 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. | ||||||
| Isoform 2 (identifier: Q9NSK0-2) The sequence of this isoform differs from the canonical sequence as follows: 87-131: VMLALASHLS...ELAGTQQRLQ → NLELRGCAHL...AMPGEPVAAG 132-619: Missing. | ||||||
| Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q9NSK0-3) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MEVTGFGVTRPGKVPQARM |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 619 | 619 | Kinesin light chain 4 | PRO_0000215097 | |||||
Regions | |||||||||
| Repeat | 55 – 88 | 34 | TPR 1 | ||||||
| Repeat | 211 – 244 | 34 | TPR 2 | ||||||
| Repeat | 253 – 286 | 34 | TPR 3 | ||||||
| Repeat | 295 – 328 | 34 | TPR 4 | ||||||
| Repeat | 337 – 370 | 34 | TPR 5 | ||||||
| Repeat | 379 – 412 | 34 | TPR 6 | ||||||
| Repeat | 464 – 497 | 34 | TPR 7 | ||||||
| Coiled coil | 32 – 150 | 119 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 74 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 83 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 93 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 100 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 174 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 391 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 460 | 1 | Phosphoserine Ref.5 Ref.8 Ref.9 Ref.11 | ||||||
| Modified residue | 566 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 590 | 1 | Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 | ||||||
| Modified residue | 593 | 1 | Phosphotyrosine Ref.10 | ||||||
| Modified residue | 612 | 1 | Phosphothreonine Ref.10 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 | 1 | M → MEVTGFGVTRPGKVPQARM in isoform 3. | VSP_038083 | |||||
| Alternative sequence | 87 – 131 | 45 | VMLAL…QQRLQ → NLELRGCAHLGDAGSSQPPE HSGVGETEAAGSGAAAMPGE PVAAG in isoform 2. | VSP_037875 | |||||
| Alternative sequence | 132 – 619 | 488 | Missing in isoform 2. | VSP_037876 | |||||
| Natural variant | 72 | 1 | R → H. Ref.1 Corresponds to variant rs11558979 [ dbSNP | Ensembl ]. | VAR_049708 | |||||
Experimental info | |||||||||
| Sequence conflict | 54 | 1 | L → LQTIECL in BAC87179. Ref.1 | ||||||
| Sequence conflict | 286 | 1 | T → S in BAG51695. Ref.1 | ||||||
| Sequence conflict | 366 | 1 | I → T in BAG51695. Ref.1 | ||||||
| Sequence conflict | 434 | 1 | M → L in BAG52815. Ref.1 | ||||||
Sequences
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References
| [1] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT HIS-72. Tissue: Adrenal gland, Brain and Small intestine. |
| [2] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Amygdala and Oesophageal carcinoma. |
| [3] | "The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Prostate and Skin. |
| [5] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [6] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-83; SER-93 AND SER-100, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [7] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [8] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590; TYR-593 AND THR-612, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [11] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [12] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, MASS SPECTROMETRY. |
| [13] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK055293 mRNA. Translation: BAG51496.1. AK056393 mRNA. Translation: BAG51695.1. AK094102 mRNA. Translation: BAG52815.1. AK127018 mRNA. Translation: BAC86788.1. Sequence problems. AK127894 mRNA. Translation: BAC87179.1. AL162078 mRNA. Translation: CAB82411.1. AL355385 Genomic DNA. Translation: CAI13781.1. BC080637 mRNA. Translation: AAH80637.1. BC103727 mRNA. Translation: AAI03728.1. BX640717 mRNA. Translation: CAE45836.1. |
| IPI | IPI00398812. IPI00743879. IPI00788630. |
| PIR | T47147. |
| RefSeq | NP_612352.1. NM_138343.2. NP_958929.1. NM_201521.1. NP_958930.1. NM_201522.1. NP_958931.1. NM_201523.1. |
| UniGene | Hs.655123. |
3D structure databases | |
| ProteinModelPortal | Q9NSK0. |
| SMR | Q9NSK0. Positions 65-90, 118-561. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9NSK0. 3 interactions. |
| MINT | MINT-4999921. |
PTM databases | |
| PhosphoSite | Q9NSK0. |
Polymorphism databases | |
| DMDM | 116242607. |
Proteomic databases | |
| PRIDE | Q9NSK0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000259708; ENSP00000259708; ENSG00000137171. ENST00000347162; ENSP00000340221; ENSG00000137171. ENST00000394056; ENSP00000377620; ENSG00000137171. ENST00000394058; ENSP00000377622; ENSG00000137171. ENST00000479388; ENSP00000418031; ENSG00000137171. |
| GeneID | 89953. |
| KEGG | hsa:89953. |
| UCSC | uc003otv.1. human. |
Organism-specific databases | |
| CTD | 89953. |
| GeneCards | GC06P043008. |
| H-InvDB | HIX0005895. |
| HGNC | HGNC:21624. KLC4. |
| HPA | HPA030168. HPA030169. |
| neXtProt | NX_Q9NSK0. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG19638. |
| GeneTree | ENSGT00390000006393. |
| HOVERGEN | HBG006217. |
| InParanoid | Q9NSK0. |
| OMA | MSKSRHR. |
| OrthoDB | EOG4NZTT0. |
| PhylomeDB | Q9NSK0. |
Enzyme and pathway databases | |
| Reactome | REACT_604. Hemostasis. |
Gene expression databases | |
| ArrayExpress | Q9NSK0. |
| Bgee | Q9NSK0. |
| CleanEx | HS_KLC4. |
| Genevestigator | Q9NSK0. |
| GermOnline | ENSG00000137171. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR002151. Kinesin_light. IPR015792. Kinesin_light_repeat. IPR015390. Rabaptin_Rab5-bd. IPR001440. TPR-1. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view] |
| Gene3D | G3DSA:1.25.40.10. TPR-like_helical. 2 hits. |
| KO | K10407. |
| Pfam | PF09311. Rab5-bind. 1 hit. PF00515. TPR_1. 3 hits. [Graphical view] |
| PRINTS | PR00381. KINESINLIGHT. |
| SMART | SM00028. TPR. 4 hits. [Graphical view] |
| PROSITE | PS01160. KINESIN_LIGHT. 3 hits. PS50005. TPR. 6 hits. PS50293. TPR_REGION. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 76452. |
Entry information
| Entry name | KLC4_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9NSK0 Secondary accession number(s): B3KNY4 Q66K28 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| SIMILARITY comments Index of protein domains and families |

Clusters with