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UniProtKB/Swiss-Prot entry Q07866


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KLC1_HUMAN
Primary accession number Q07866
Secondary accession numbers Q7RTM2 Q7RTM3 Q7RTM5 Q7RTP9 Q7RTQ5 Q7RTQ6 Q86SF5 Q86TF5 Q86V74 Q86V75 Q86V76 Q86V77 Q86V78 Q86V79 Q96H62
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 1, 1994 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 86)
Name and origin of the protein
Protein name Kinesin light chain 1
Synonym KLC 1
Gene name
Name: KLC1
Synonyms: KLC, KNS2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=8274221 [NCBI, ExPASy, EBI, Israel, Japan]
Cabeza-Arvelaiz Y., Shih L.-C.N., Hardman N., Asselbergs F., Bilbe G., Schmitz A., White B., Siciliano M.J., Lachman L.B.;
"Cloning and genetic characterization of the human kinesin light-chain (KLC) gene.";
DNA Cell Biol. 12:881-892(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Gerber S., Rozet J.-M., Perrault I., Ducroq D., Souied E., Munnich A., Kaplan J.;
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C; G; I; J; K; N; P AND S).
TISSUE=Brain, Foreskin, and Liver;
PubMed=12839500 [NCBI, ExPASy, EBI, Israel, Japan]
McCart A.E., Mahony D., Rothnagel J.A.;
"Alternatively spliced products of the human kinesin light chain 1 (KNS2) gene.";
Traffic 4:576-580(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596 (ISOFORM I), AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627 (ISOFORM J), AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., 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 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-517 AND SER-520, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L04733; AAA16576.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267530; AAF72543.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267518; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267519; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267520; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267521; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267522; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267523; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267524; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267525; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267526; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267527; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267528; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF267529; AAF72543.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180163; AAO62548.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180164; AAO62549.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180165; AAO62550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180166; AAO62551.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180168; AAO62553.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180167; AAO62552.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180169; AAO62554.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY180170; AAO62555.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY244715; AAO64641.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK000681; DAA01265.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK000682; DAA01266.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK000684; DAA01268.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK001165; DAA01291.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK001166; DAA01292.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK001169; DAA01295.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK001170; DAA01296.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BK001171; DAA01297.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008881; AAH08881.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I53013; I53013.
RefSeq NP_005543.2; -.
NP_891553.2; -.
UniGene Hs.20107
3D structure databases
ModBase Q07866.
Protein-protein interaction databases
IntAct Q07866; 5.
Organism-specific databases
GeneCards GC14P103167; -.
H-InvDB HIX0012004; -.
HGNC HGNC:6387; KLC1.
GenAtlas KLC1.
HPA CAB009798; -.
MIM 600025; gene. [NCBI / EBI]
GeneCards Q07866.
Gene expression databases
ArrayExpress Q07866; -.
GermOnline ENSG00000126214; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from sequence or structural similarity from HGNC).
GO:0005871; Cellular component: kinesin complex (inferred from sequence or structural similarity from HGNC).
GO:0005874; Cellular component: microtubule (inferred from electronic annotation from UniProtKB-KW).
GO:0003777; Molecular function: microtubule motor activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002151; Kinesin_light.
IPR015792; Kinesin_light_repeat.
IPR015390; Rabaptin_Rab5-bd.
IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 1.
Pfam PF09311; Rab5-bind; 1.
PF00515; TPR_1; 5.
Pfam graphical view of domain structure.
PRINTS PR00381; KINESINLIGHT.
SMART SM00028; TPR; 5.
SMART graphical view of domain structure.
PROSITE PS01160; KINESIN_LIGHT; 4.
PS50005; TPR; 6.
PS50293; TPR_REGION; 2.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q07866; -.
Genome annotation databases
Ensembl ENSG00000126214; Homo sapiens. [Contig view]
GeneID 3831; -.
KEGG hsa:3831; -.
Phylogenomic databases
HOVERGEN Q07866; -.
Other
NextBio 15055; -.
SOURCE KLC1; Homo sapiens.
ProtoNet Q07866.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Coiled coil; Microtubule; Motor protein; Phosphoprotein; Repeat; TPR repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   569  569     Kinesin light chain 1. PRO_0000215092
REPEAT   209   242  34     TPR 1. 
REPEAT   251   284  34     TPR 2. 
REPEAT   293   326  34     TPR 3. 
REPEAT   335   368  34     TPR 4. 
REPEAT   377   410  34     TPR 5. 
REPEAT   460   493  34     TPR 6. 
COILED   23   152  130      
MOD_RES   445   445        Phosphotyrosine (By similarity). 
MOD_RES   456   456        Phosphoserine. 
MOD_RES   517   517        Phosphoserine. 
MOD_RES   520   520        Phosphoserine. 
VAR_SEQ   538   569        VSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR -> MKRASSLNVLNVGGKAAEDRFQERNNCLADSRALSASH TDLAH (in isoform P). VSP_008021
VAR_SEQ   538   546        Missing (in isoform G, isoform N and isoform S). VSP_008017
VAR_SEQ   546   546        G -> GDGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESE PKNPGMKRASSLNVLNVGGKAAEDRFQ (in isoform I). VSP_023323
VAR_SEQ   547   569        GVSGRASFCGKRQQQQWPGRRHR -> MRKMKLGLVN (in isoform C and isoform S). VSP_008018
VAR_SEQ   547   547        G -> DGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESE PKNPG (in isoform J, isoform K and isoform N). VSP_008019
VAR_SEQ   548   569        VSGRASFCGKRQQQQWPGRRHR -> MKRASSLNVLNVGGKAAEDRFQERNNCLADSRALSASH TDLAH (in isoform J and isoform N). VSP_008020
Sequence information
Length: 569 AA [This is the length of the unprocessed precursor] Molecular weight: 64786 Da [This is the MW of the unprocessed precursor] CRC64: 5D9376C3EEDD00FE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTMVYIKED KLEKLTQDEI ISKTKQVIQG LEALKNEHNS ILQSLLETLK CLKKDDESNL 

        70         80         90        100        110        120 
VEEKSNMIRK SLEMLELGLS EAQVMMALSN HLNAVESEKQ KLRAQVRRLC QENQWLRDEL 

       130        140        150        160        170        180 
ANTQQKLQKS EQSVAQLEEE KKHLEFMNQL KKYDDDISPS EDKDTDSTKE PLDDLFPNDE 

       190        200        210        220        230        240 
DDPGQGIQQQ HSSAAAAAQQ GGYEIPARLR TLHNLVIQYA SQGRYEVAVP LCKQALEDLE 

       250        260        270        280        290        300 
KTSGHDHPDV ATMLNILALV YRDQNKYKDA ANLLNDALAI REKTLGKDHP AVAATLNNLA 

       310        320        330        340        350        360 
VLYGKRGKYK EAEPLCKRAL EIREKVLGKD HPDVAKQLNN LALLCQNQGK YEEVEYYYQR 

       370        380        390        400        410        420 
ALEIYQTKLG PDDPNVAKTK NNLASCYLKQ GKFKQAETLY KEILTRAHER EFGSVDDENK 

       430        440        450        460        470        480 
PIWMHAEERE ECKGKQKDGT SFGEYGGWYK ACKVDSPTVT TTLKNLGALY RRQGKFEAAE 

       490        500        510        520        530        540 
TLEEAAMRSR KQGLDNVHKQ RVAEVLNDPE NMEKRRSRES LNVDVVKYES GPDGGEEVSM 

       550        560 
SVEWNGGVSG RASFCGKRQQ QQWPGRRHR 

Q07866 in FASTA format

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