Kinesin light chain 1

NameKinesin light chain 1
SynonymsKLC KLC 1 KNS2
Gene NameKLC1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0009171|Kinesin light chain 1
MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDD
ESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWL
RDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLF
PNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQAL
EDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATL
NNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEY
YYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVD
DENKPIWMHAEEREECKGKQKDGTSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKF
EAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPENMEKRRSRESLNVDVVKYESGPDGGE
EVSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR
Number of residues573
Molecular Weight65309.09
Theoretical pINone
GO Classification
Functions
    motor activity
microtubule motor activity
Processes
    axon cargo transport
antigen processing and presentation of exogenous peptide antigen via MHC class II
microtubule-based movement
viral process
blood coagulation
small GTPase mediated signal transduction
stress granule disassembly
Components
    cytosol
cytoplasmic membrane-bounded vesicle
growth cone
membrane
axon
microtubule
ciliary rootlet
kinesin complex
General FunctionMotor activity
Specific FunctionKinesin 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDQ07866
UniProtKB Entry NameKLC1_HUMAN
Cellular LocationCell projection
Gene sequence
>lcl|BSEQ0013650|Kinesin light chain 1 (KLC1)
ATGTATGACAACATGTCCACAATGGTGTACATAAAGGAAGACAAGTTGGAGAAGCTTACA
CAGGATGAAATTATTTCTAAGACAAAGCAAGTAATTCAGGGGCTGGAAGCTTTGAAGAAT
GAGCACAATTCCATTTTACAAAGTTTGCTGGAGACACTGAAGTGTTTGAAGAAAGATGAT
GAAAGTAATTTGGTGGAGGAGAAATCAAACATGATCCGGAAGTCACTGGAGATGTTGGAG
CTCGGCCTGAGTGAGGCACAGGTTATGATGGCTTTGTCAAATCACCTGAATGCTGTGGAG
TCCGAGAAGCAGAAACTGCGTGCGCAGGTTCGTCGTCTGTGCCAGGAGAATCAGTGGCTA
CGGGATGAACTGGCCAACACGCAGCAGAAACTGCAGAAGAGTGAGCAGTCTGTGGCTCAA
CTGGAGGAGGAGAAGAAGCATCTGGAGTTTATGAATCAGCTAAAAAAATATGATGACGAC
ATTTCCCCATCCGAGGACAAAGACACTGATTCTACCAAAGAGCCTCTGGATGACCTTTTC
CCCAATGATGAAGACGACCCAGGGCAAGGAATCCAGCAGCAGCACAGCAGTGCAGCCGCG
GCTGCCCAGCAGGGCGGCTACGAGATCCCCGCGCGGCTGCGGACGCTCCACAACCTGGTG
ATCCAGTACGCCTCGCAGGGGCGCTACGAGGTAGCTGTGCCCCTCTGCAAGCAGGCCCTG
GAGGACCTGGAGAAGACTTCAGGACACGACCACCCGGACGTGGCCACCATGCTCAACATC
CTGGCCTTGGTGTACAGGGATCAGAATAAATACAAAGATGCAGCTAACCTACTGAATGAT
GCCTTGGCTATTCGTGAGAAAACTTTGGGCAAAGATCATCCTGCGGTGGCGGCGACTTTG
AATAACCTTGCAGTCCTTTATGGTAAAAGAGGGAAGTACAAAGAAGCAGAGCCGTTGTGT
AAAAGAGCTCTGGAAATCCGAGAAAAGGTTTTGGGGAAGGATCACCCCGATGTTGCCAAG
CAGTTAAATAACTTGGCCTTACTGTGCCAGAACCAGGGCAAGTATGAAGAAGTAGAATAT
TATTATCAAAGAGCCCTCGAGATCTACCAGACAAAACTGGGACCTGATGACCCCAACGTG
GCTAAGACGAAAAATAACCTGGCATCCTGCTATTTGAAACAAGGAAAGTTCAAGCAAGCA
GAAACACTGTACAAAGAGATTCTCACTCGTGCACATGAAAGGGAGTTTGGTTCTGTAGAT
GATGAAAATAAACCCATCTGGATGCATGCTGAAGAAAGAGAAGAATGCAAAGGAAAGCAA
AAGGATGGGACATCTTTTGGAGAGTATGGCGGCTGGTACAAAGCCTGCAAAGTTGATAGT
CCAACTGTTACAACCACTCTAAAAAACCTTGGGGCACTTTACAGACGTCAAGGCAAATTT
GAAGCTGCAGAAACGTTAGAAGAAGCTGCTATGAGGTCTCGTAAACAGGGTCTTGACAAT
GTTCACAAACAGAGGGTGGCAGAAGTGCTCAATGACCCTGAGAACATGGAGAAGCGCAGG
AGCCGTGAGAGCCTCAACGTGGACGTGGTCAAGTACGAGAGTGGCCCTGACGGAGGGGAG
GAAGTGAGTATGAGCGTAGAGTGGAACGGGGATGGCACTGGATCTTTAAAACGCAGTGGT
TCCTTTAGCAAACTCCGGGCTTCCATTAGACGCAGCAGTGAGAAGCTGGTTAGGAAGCTG
AAGGGAGGAAGTTCACGAGAGAGTGAGCCAAAGAACCCCGGGGCGTCTCTGGCCGAGCCT
CTTTTTGTGGAAAACGACAGCAGCAGCAGTGGCCTGGAAGACGCCACCGCTAACTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:6387
Chromosome Location14
LocusNone
References
  1. Cabeza-Arvelaiz Y, Shih LC, Hardman N, Asselbergs F, Bilbe G, Schmitz A, White B, Siciliano MJ, Lachman LB: Cloning and genetic characterization of the human kinesin light-chain (KLC) gene. DNA Cell Biol. 1993 Dec;12(10):881-92.[8274221 ]
  2. McCart AE, Mahony D, Rothnagel JA: Alternatively spliced products of the human kinesin light chain 1 (KNS2) gene. Traffic. 2003 Aug;4(8):576-80.[12839500 ]
  3. Kamm C, Boston H, Hewett J, Wilbur J, Corey DP, Hanson PI, Ramesh V, Breakefield XO: The early onset dystonia protein torsinA interacts with kinesin light chain 1. J Biol Chem. 2004 May 7;279(19):19882-92. Epub 2004 Feb 17.[14970196 ]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48.[17081983 ]
  5. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26.[18220336 ]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007.[18691976 ]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31.[18669648 ]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007.[19690332 ]
  9. McDonald A, Fogarty S, Leclerc I, Hill EV, Hardie DG, Rutter GA: Cell-wide analysis of secretory granule dynamics in three dimensions in living pancreatic beta-cells: evidence against a role for AMPK-dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose-stimulated insulin granule movement. Biochem Soc Trans. 2010 Feb;38(Pt 1):205-8. doi: 10.1042/BST0380205.[20074060 ]
  10. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475.[20068231 ]
  11. Strunze S, Engelke MF, Wang IH, Puntener D, Boucke K, Schleich S, Way M, Schoenenberger P, Burckhardt CJ, Greber UF: Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection. Cell Host Microbe. 2011 Sep 15;10(3):210-23. doi: 10.1016/j.chom.2011.08.010.[21925109 ]
  12. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570.[21406692 ]
  13. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22.[24275569 ]
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