Full text data of KLC1
KLC1
(KLC, KNS2)
[Confidence: low (only semi-automatic identification from reviews)]
Kinesin light chain 1; KLC 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Kinesin light chain 1; KLC 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q07866
ID KLC1_HUMAN Reviewed; 573 AA.
AC Q07866; A6NF62; F8VTM4; Q7RTM2; Q7RTM3; Q7RTM5; Q7RTP9; Q7RTQ3;
read moreAC Q7RTQ5; Q7RTQ6; Q86SF5; Q86TF5; Q86V74; Q86V75; Q86V76; Q86V77;
AC Q86V78; Q86V79; Q96H62;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Kinesin light chain 1;
DE Short=KLC 1;
GN Name=KLC1; Synonyms=KLC, KNS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=8274221;
RA Cabeza-Arvelaiz Y., Shih L.-C.N., Hardman N., Asselbergs F., Bilbe G.,
RA Schmitz A., White B., Siciliano M.J., Lachman L.B.;
RT "Cloning and genetic characterization of the human kinesin light-chain
RT (KLC) gene.";
RL DNA Cell Biol. 12:881-892(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; D; G; I; P AND S), AND
RP NUCLEOTIDE SEQUENCE [MRNA] OF 444-573 (ISOFORMS J; K AND N).
RC TISSUE=Brain, Foreskin, and Liver;
RX PubMed=12839500;
RA McCart A.E., Mahony D., Rothnagel J.A.;
RT "Alternatively spliced products of the human kinesin light chain 1
RT (KNS2) gene.";
RL Traffic 4:576-580(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gerber S., Rozet J.-M., Perrault I., Ducroq D., Souied E., Munnich A.,
RA Kaplan J.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION AT SER-521 AND SER-524, AND MUTAGENESIS OF SER-521 AND
RP SER-524.
RX PubMed=20074060; DOI=10.1042/BST0380205;
RA McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G.,
RA Rutter G.A.;
RT "Cell-wide analysis of secretory granule dynamics in three dimensions
RT in living pancreatic beta-cells: evidence against a role for AMPK-
RT dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose-
RT stimulated insulin granule movement.";
RL Biochem. Soc. Trans. 38:205-208(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 (ISOFORMS I AND J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 (ISOFORM J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-622 (ISOFORM
RP N), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578
RP (ISOFORM P), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP INTERACTION WITH ADENOVIRUS HEXON-INTERLACING PROTEIN.
RX PubMed=21925109; DOI=10.1016/j.chom.2011.08.010;
RA Strunze S., Engelke M.F., Wang I.H., Puntener D., Boucke K.,
RA Schleich S., Way M., Schoenenberger P., Burckhardt C.J., Greber U.F.;
RT "Kinesin-1-mediated capsid disassembly and disruption of the nuclear
RT pore complex promote virus infection.";
RL Cell Host Microbe 10:210-223(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 (ISOFORMS I AND J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 (ISOFORM J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-622 (ISOFORM
RP N), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578
RP (ISOFORM P), AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 205-497.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the TPR domain of kinesin light chain 1.";
RL Submitted (MAY-2011) to the PDB data bank.
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing
CC protein that may play a role in organelle transport. The light
CC chain may function in coupling of cargo to the heavy chain or in
CC the modulation of its ATPase activity.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two
CC light chains. Interacts with SPAG9 (By similarity). Interacts with
CC ATCAY; may link mitochondria to KLC1 and regulate mitochondria
CC localization into neuron projections (By similarity). Interacts
CC with adenovirus hexon-interlacing protein; this interaction leads
CC to capsid disruption at the nuclear pore complex during virus
CC entry into host cell.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Comment=Additional isoforms seem to exist. Has the potential to
CC produce 285'919 splice forms;
CC Name=A;
CC IsoId=Q07866-1; Sequence=Displayed;
CC Name=C; Synonyms=KLC1C, R, KLC1R;
CC IsoId=Q07866-2; Sequence=VSP_008018;
CC Name=G; Synonyms=KLC1G;
CC IsoId=Q07866-3; Sequence=VSP_008017;
CC Name=J; Synonyms=KLC1J;
CC IsoId=Q07866-4; Sequence=VSP_008019, VSP_008020;
CC Note=Ref.2 (AAO62555) sequence is in conflict in position:
CC 631:S->T. Contains a phosphoserine at position 600. Contains a
CC phosphoserine at position 631;
CC Name=K; Synonyms=KLC1K;
CC IsoId=Q07866-5; Sequence=VSP_008019;
CC Name=N; Synonyms=KLC1N;
CC IsoId=Q07866-6; Sequence=VSP_008017, VSP_008019, VSP_008020;
CC Note=Ref.2 (AAO62551) sequence is in conflict in position:
CC 622:S->T. Contains a phosphoserine at position 591. Contains a
CC phosphoserine at position 622;
CC Name=P; Synonyms=KLC1P;
CC IsoId=Q07866-7; Sequence=VSP_008021;
CC Note=Contains a phosphoserine at position 547. Contains a
CC phosphoserine at position 578;
CC Name=S; Synonyms=KLC1S, Q, KLC1Q;
CC IsoId=Q07866-8; Sequence=VSP_008017, VSP_008018;
CC Name=I;
CC IsoId=Q07866-9; Sequence=VSP_023323;
CC Note=Contains a phosphoserine at position 600;
CC Name=D; Synonyms=KLC1D;
CC IsoId=Q07866-10; Sequence=VSP_046424;
CC -!- TISSUE SPECIFICITY: Found in a variety of tissues. Mostly abundant
CC in brain and spine.
CC -!- PTM: Isoform I is phosphorylated on Ser-600. Isoform J is
CC phosphorylated on Ser-631.
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC -!- SIMILARITY: Contains 6 TPR repeats.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16576.1; Type=Erroneous initiation;
CC Sequence=AAF72543.1; Type=Erroneous initiation;
CC Sequence=AAO62549.1; Type=Erroneous initiation;
CC Sequence=DAA01265.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01266.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01268.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01289.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01291.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01292.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01295.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01296.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01297.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; L04733; AAA16576.1; ALT_INIT; mRNA.
DR EMBL; AY180163; AAO62548.1; -; mRNA.
DR EMBL; AY180164; AAO62549.1; ALT_INIT; mRNA.
DR EMBL; AY180165; AAO62550.1; -; mRNA.
DR EMBL; AY180166; AAO62551.1; -; mRNA.
DR EMBL; AY180168; AAO62553.1; -; mRNA.
DR EMBL; AY180167; AAO62552.1; -; mRNA.
DR EMBL; AY180169; AAO62554.1; -; mRNA.
DR EMBL; AY180170; AAO62555.1; -; mRNA.
DR EMBL; AY244715; AAO64641.1; -; mRNA.
DR EMBL; AF267530; AAF72543.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF267518; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267519; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267520; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267521; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267522; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267523; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267524; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267525; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267526; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267527; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267528; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267529; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AL049840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81834.1; -; Genomic_DNA.
DR EMBL; BC008881; AAH08881.1; -; mRNA.
DR EMBL; BK000681; DAA01265.1; ALT_INIT; mRNA.
DR EMBL; BK000682; DAA01266.1; ALT_INIT; mRNA.
DR EMBL; BK000684; DAA01268.1; ALT_INIT; mRNA.
DR EMBL; BK001163; DAA01289.1; ALT_INIT; mRNA.
DR EMBL; BK001165; DAA01291.1; ALT_INIT; mRNA.
DR EMBL; BK001166; DAA01292.1; ALT_INIT; mRNA.
DR EMBL; BK001169; DAA01295.1; ALT_INIT; mRNA.
DR EMBL; BK001170; DAA01296.1; ALT_INIT; mRNA.
DR EMBL; BK001171; DAA01297.1; ALT_INIT; mRNA.
DR PIR; I53013; I53013.
DR RefSeq; NP_001123579.1; NM_001130107.1.
DR RefSeq; NP_005543.2; NM_005552.4.
DR RefSeq; NP_891553.2; NM_182923.3.
DR RefSeq; XP_005267662.1; XM_005267605.1.
DR RefSeq; XP_005267663.1; XM_005267606.1.
DR RefSeq; XP_005267669.1; XM_005267612.1.
DR RefSeq; XP_005267681.1; XM_005267624.1.
DR RefSeq; XP_005267684.1; XM_005267627.1.
DR RefSeq; XP_005267685.1; XM_005267628.1.
DR UniGene; Hs.20107; -.
DR UniGene; Hs.657678; -.
DR PDB; 3NF1; X-ray; 2.80 A; A=205-497.
DR PDBsum; 3NF1; -.
DR ProteinModelPortal; Q07866; -.
DR SMR; Q07866; 203-495.
DR IntAct; Q07866; 5.
DR MINT; MINT-1417975; -.
DR PhosphoSite; Q07866; -.
DR DMDM; 223590110; -.
DR UCD-2DPAGE; Q07866; -.
DR PRIDE; Q07866; -.
DR DNASU; 3831; -.
DR Ensembl; ENST00000246489; ENSP00000246489; ENSG00000126214.
DR Ensembl; ENST00000334553; ENSP00000334523; ENSG00000126214.
DR Ensembl; ENST00000347839; ENSP00000334618; ENSG00000126214.
DR Ensembl; ENST00000348520; ENSP00000341154; ENSG00000126214.
DR Ensembl; ENST00000389744; ENSP00000374394; ENSG00000126214.
DR Ensembl; ENST00000452929; ENSP00000414982; ENSG00000126214.
DR Ensembl; ENST00000553286; ENSP00000452487; ENSG00000126214.
DR Ensembl; ENST00000554228; ENSP00000450616; ENSG00000126214.
DR Ensembl; ENST00000557450; ENSP00000450648; ENSG00000126214.
DR GeneID; 3831; -.
DR KEGG; hsa:3831; -.
DR UCSC; uc010tyf.2; human.
DR CTD; 3831; -.
DR GeneCards; GC14P104028; -.
DR HGNC; HGNC:6387; KLC1.
DR HPA; CAB009798; -.
DR MIM; 600025; gene.
DR neXtProt; NX_Q07866; -.
DR PharmGKB; PA162393424; -.
DR HOVERGEN; HBG006217; -.
DR KO; K10407; -.
DR OMA; MREDMST; -.
DR OrthoDB; EOG7TXKGD; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; KLC1; human.
DR GeneWiki; KLC1; -.
DR GenomeRNAi; 3831; -.
DR NextBio; 15055; -.
DR PRO; PR:Q07866; -.
DR ArrayExpress; Q07866; -.
DR Bgee; Q07866; -.
DR Genevestigator; Q07866; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:HGNC.
DR GO; GO:0005871; C:kinesin complex; ISS:HGNC.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0003774; F:motor activity; TAS:ProtInc.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0008088; P:axon cargo transport; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
DR GO; GO:0035617; P:stress granule disassembly; ISS:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015792; Kinesin_light_repeat.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF00515; TPR_1; 3.
DR Pfam; PF07719; TPR_2; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR PROSITE; PS01160; KINESIN_LIGHT; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; Host-virus interaction; Microtubule;
KW Motor protein; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 573 Kinesin light chain 1.
FT /FTId=PRO_0000215092.
FT REPEAT 213 246 TPR 1.
FT REPEAT 255 288 TPR 2.
FT REPEAT 297 330 TPR 3.
FT REPEAT 339 372 TPR 4.
FT REPEAT 381 414 TPR 5.
FT REPEAT 464 497 TPR 6.
FT COILED 27 156
FT MOD_RES 449 449 Phosphotyrosine (By similarity).
FT MOD_RES 521 521 Phosphoserine; by AMPK.
FT MOD_RES 524 524 Phosphoserine; by AMPK.
FT VAR_SEQ 542 573 VSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR -> MKRAS
FT SLNVLNVGGKAAEDRFQERNNCLADSRALSASHTDLAH
FT (in isoform P).
FT /FTId=VSP_008021.
FT VAR_SEQ 542 550 Missing (in isoform G, isoform N and
FT isoform S).
FT /FTId=VSP_008017.
FT VAR_SEQ 550 550 G -> GDGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSS
FT RESEPKNPGMKRASSLNVLNVGGKAAEDRFQ (in
FT isoform I).
FT /FTId=VSP_023323.
FT VAR_SEQ 551 573 GVSGRASFCGKRQQQQWPGRRHR -> MRKMKLGLVN (in
FT isoform C and isoform S).
FT /FTId=VSP_008018.
FT VAR_SEQ 551 573 GVSGRASFCGKRQQQQWPGRRHR -> DGTGSLKRSGSFSK
FT LRASIRRSSEKLVRKLKGGSSRESEPKNPGASLAEPLFVEN
FT DSSSSGLEDATAN (in isoform D).
FT /FTId=VSP_046424.
FT VAR_SEQ 551 551 G -> DGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSR
FT ESEPKNPG (in isoform J, isoform K and
FT isoform N).
FT /FTId=VSP_008019.
FT VAR_SEQ 552 573 VSGRASFCGKRQQQQWPGRRHR -> MKRASSLNVLNVGGK
FT AAEDRFQERNNCLADSRALSASHTDLAH (in isoform
FT J and isoform N).
FT /FTId=VSP_008020.
FT MUTAGEN 521 521 S->A,D: No effect on motor function; when
FT associated with A/D-524.
FT MUTAGEN 524 524 S->A,D: No effect on motor function; when
FT associated with A/D-521.
FT CONFLICT 4 4 N -> T (in Ref. 1; AAA16576, 2; AAO62548/
FT AAO62549/AAO62550/AAO62551/AAO62553/
FT AAO62552/AAO62554/AAO62555/AAO64641 and
FT 3; AAF72543).
FT STRAND 203 205
FT HELIX 211 225
FT HELIX 229 247
FT STRAND 249 251
FT HELIX 252 267
FT HELIX 271 289
FT HELIX 294 308
FT TURN 309 311
FT HELIX 313 331
FT HELIX 336 350
FT TURN 351 353
FT HELIX 355 371
FT HELIX 378 394
FT HELIX 397 416
FT HELIX 426 435
FT HELIX 461 477
FT HELIX 480 494
SQ SEQUENCE 573 AA; 65310 MW; A66E3915C57C2764 CRC64;
MYDNMSTMVY IKEDKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
ESNLVEEKSN MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQKLRAQV RRLCQENQWL
RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDTD STKEPLDDLF
PNDEDDPGQG IQQQHSSAAA AAQQGGYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL
EDLEKTSGHD HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG KDHPAVAATL
NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ NQGKYEEVEY
YYQRALEIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA ETLYKEILTR AHEREFGSVD
DENKPIWMHA EEREECKGKQ KDGTSFGEYG GWYKACKVDS PTVTTTLKNL GALYRRQGKF
EAAETLEEAA MRSRKQGLDN VHKQRVAEVL NDPENMEKRR SRESLNVDVV KYESGPDGGE
EVSMSVEWNG GVSGRASFCG KRQQQQWPGR RHR
//
ID KLC1_HUMAN Reviewed; 573 AA.
AC Q07866; A6NF62; F8VTM4; Q7RTM2; Q7RTM3; Q7RTM5; Q7RTP9; Q7RTQ3;
read moreAC Q7RTQ5; Q7RTQ6; Q86SF5; Q86TF5; Q86V74; Q86V75; Q86V76; Q86V77;
AC Q86V78; Q86V79; Q96H62;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Kinesin light chain 1;
DE Short=KLC 1;
GN Name=KLC1; Synonyms=KLC, KNS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=8274221;
RA Cabeza-Arvelaiz Y., Shih L.-C.N., Hardman N., Asselbergs F., Bilbe G.,
RA Schmitz A., White B., Siciliano M.J., Lachman L.B.;
RT "Cloning and genetic characterization of the human kinesin light-chain
RT (KLC) gene.";
RL DNA Cell Biol. 12:881-892(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; D; G; I; P AND S), AND
RP NUCLEOTIDE SEQUENCE [MRNA] OF 444-573 (ISOFORMS J; K AND N).
RC TISSUE=Brain, Foreskin, and Liver;
RX PubMed=12839500;
RA McCart A.E., Mahony D., Rothnagel J.A.;
RT "Alternatively spliced products of the human kinesin light chain 1
RT (KNS2) gene.";
RL Traffic 4:576-580(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gerber S., Rozet J.-M., Perrault I., Ducroq D., Souied E., Munnich A.,
RA Kaplan J.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION AT SER-521 AND SER-524, AND MUTAGENESIS OF SER-521 AND
RP SER-524.
RX PubMed=20074060; DOI=10.1042/BST0380205;
RA McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G.,
RA Rutter G.A.;
RT "Cell-wide analysis of secretory granule dynamics in three dimensions
RT in living pancreatic beta-cells: evidence against a role for AMPK-
RT dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose-
RT stimulated insulin granule movement.";
RL Biochem. Soc. Trans. 38:205-208(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 (ISOFORMS I AND J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 (ISOFORM J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-622 (ISOFORM
RP N), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578
RP (ISOFORM P), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP INTERACTION WITH ADENOVIRUS HEXON-INTERLACING PROTEIN.
RX PubMed=21925109; DOI=10.1016/j.chom.2011.08.010;
RA Strunze S., Engelke M.F., Wang I.H., Puntener D., Boucke K.,
RA Schleich S., Way M., Schoenenberger P., Burckhardt C.J., Greber U.F.;
RT "Kinesin-1-mediated capsid disassembly and disruption of the nuclear
RT pore complex promote virus infection.";
RL Cell Host Microbe 10:210-223(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 (ISOFORMS I AND J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 (ISOFORM J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-622 (ISOFORM
RP N), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578
RP (ISOFORM P), AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 205-497.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the TPR domain of kinesin light chain 1.";
RL Submitted (MAY-2011) to the PDB data bank.
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing
CC protein that may play a role in organelle transport. The light
CC chain may function in coupling of cargo to the heavy chain or in
CC the modulation of its ATPase activity.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two
CC light chains. Interacts with SPAG9 (By similarity). Interacts with
CC ATCAY; may link mitochondria to KLC1 and regulate mitochondria
CC localization into neuron projections (By similarity). Interacts
CC with adenovirus hexon-interlacing protein; this interaction leads
CC to capsid disruption at the nuclear pore complex during virus
CC entry into host cell.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Comment=Additional isoforms seem to exist. Has the potential to
CC produce 285'919 splice forms;
CC Name=A;
CC IsoId=Q07866-1; Sequence=Displayed;
CC Name=C; Synonyms=KLC1C, R, KLC1R;
CC IsoId=Q07866-2; Sequence=VSP_008018;
CC Name=G; Synonyms=KLC1G;
CC IsoId=Q07866-3; Sequence=VSP_008017;
CC Name=J; Synonyms=KLC1J;
CC IsoId=Q07866-4; Sequence=VSP_008019, VSP_008020;
CC Note=Ref.2 (AAO62555) sequence is in conflict in position:
CC 631:S->T. Contains a phosphoserine at position 600. Contains a
CC phosphoserine at position 631;
CC Name=K; Synonyms=KLC1K;
CC IsoId=Q07866-5; Sequence=VSP_008019;
CC Name=N; Synonyms=KLC1N;
CC IsoId=Q07866-6; Sequence=VSP_008017, VSP_008019, VSP_008020;
CC Note=Ref.2 (AAO62551) sequence is in conflict in position:
CC 622:S->T. Contains a phosphoserine at position 591. Contains a
CC phosphoserine at position 622;
CC Name=P; Synonyms=KLC1P;
CC IsoId=Q07866-7; Sequence=VSP_008021;
CC Note=Contains a phosphoserine at position 547. Contains a
CC phosphoserine at position 578;
CC Name=S; Synonyms=KLC1S, Q, KLC1Q;
CC IsoId=Q07866-8; Sequence=VSP_008017, VSP_008018;
CC Name=I;
CC IsoId=Q07866-9; Sequence=VSP_023323;
CC Note=Contains a phosphoserine at position 600;
CC Name=D; Synonyms=KLC1D;
CC IsoId=Q07866-10; Sequence=VSP_046424;
CC -!- TISSUE SPECIFICITY: Found in a variety of tissues. Mostly abundant
CC in brain and spine.
CC -!- PTM: Isoform I is phosphorylated on Ser-600. Isoform J is
CC phosphorylated on Ser-631.
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC -!- SIMILARITY: Contains 6 TPR repeats.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16576.1; Type=Erroneous initiation;
CC Sequence=AAF72543.1; Type=Erroneous initiation;
CC Sequence=AAO62549.1; Type=Erroneous initiation;
CC Sequence=DAA01265.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01266.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01268.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01289.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01291.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01292.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01295.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01296.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=DAA01297.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; L04733; AAA16576.1; ALT_INIT; mRNA.
DR EMBL; AY180163; AAO62548.1; -; mRNA.
DR EMBL; AY180164; AAO62549.1; ALT_INIT; mRNA.
DR EMBL; AY180165; AAO62550.1; -; mRNA.
DR EMBL; AY180166; AAO62551.1; -; mRNA.
DR EMBL; AY180168; AAO62553.1; -; mRNA.
DR EMBL; AY180167; AAO62552.1; -; mRNA.
DR EMBL; AY180169; AAO62554.1; -; mRNA.
DR EMBL; AY180170; AAO62555.1; -; mRNA.
DR EMBL; AY244715; AAO64641.1; -; mRNA.
DR EMBL; AF267530; AAF72543.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF267518; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267519; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267520; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267521; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267522; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267523; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267524; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267525; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267526; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267527; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267528; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AF267529; AAF72543.1; JOINED; Genomic_DNA.
DR EMBL; AL049840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81834.1; -; Genomic_DNA.
DR EMBL; BC008881; AAH08881.1; -; mRNA.
DR EMBL; BK000681; DAA01265.1; ALT_INIT; mRNA.
DR EMBL; BK000682; DAA01266.1; ALT_INIT; mRNA.
DR EMBL; BK000684; DAA01268.1; ALT_INIT; mRNA.
DR EMBL; BK001163; DAA01289.1; ALT_INIT; mRNA.
DR EMBL; BK001165; DAA01291.1; ALT_INIT; mRNA.
DR EMBL; BK001166; DAA01292.1; ALT_INIT; mRNA.
DR EMBL; BK001169; DAA01295.1; ALT_INIT; mRNA.
DR EMBL; BK001170; DAA01296.1; ALT_INIT; mRNA.
DR EMBL; BK001171; DAA01297.1; ALT_INIT; mRNA.
DR PIR; I53013; I53013.
DR RefSeq; NP_001123579.1; NM_001130107.1.
DR RefSeq; NP_005543.2; NM_005552.4.
DR RefSeq; NP_891553.2; NM_182923.3.
DR RefSeq; XP_005267662.1; XM_005267605.1.
DR RefSeq; XP_005267663.1; XM_005267606.1.
DR RefSeq; XP_005267669.1; XM_005267612.1.
DR RefSeq; XP_005267681.1; XM_005267624.1.
DR RefSeq; XP_005267684.1; XM_005267627.1.
DR RefSeq; XP_005267685.1; XM_005267628.1.
DR UniGene; Hs.20107; -.
DR UniGene; Hs.657678; -.
DR PDB; 3NF1; X-ray; 2.80 A; A=205-497.
DR PDBsum; 3NF1; -.
DR ProteinModelPortal; Q07866; -.
DR SMR; Q07866; 203-495.
DR IntAct; Q07866; 5.
DR MINT; MINT-1417975; -.
DR PhosphoSite; Q07866; -.
DR DMDM; 223590110; -.
DR UCD-2DPAGE; Q07866; -.
DR PRIDE; Q07866; -.
DR DNASU; 3831; -.
DR Ensembl; ENST00000246489; ENSP00000246489; ENSG00000126214.
DR Ensembl; ENST00000334553; ENSP00000334523; ENSG00000126214.
DR Ensembl; ENST00000347839; ENSP00000334618; ENSG00000126214.
DR Ensembl; ENST00000348520; ENSP00000341154; ENSG00000126214.
DR Ensembl; ENST00000389744; ENSP00000374394; ENSG00000126214.
DR Ensembl; ENST00000452929; ENSP00000414982; ENSG00000126214.
DR Ensembl; ENST00000553286; ENSP00000452487; ENSG00000126214.
DR Ensembl; ENST00000554228; ENSP00000450616; ENSG00000126214.
DR Ensembl; ENST00000557450; ENSP00000450648; ENSG00000126214.
DR GeneID; 3831; -.
DR KEGG; hsa:3831; -.
DR UCSC; uc010tyf.2; human.
DR CTD; 3831; -.
DR GeneCards; GC14P104028; -.
DR HGNC; HGNC:6387; KLC1.
DR HPA; CAB009798; -.
DR MIM; 600025; gene.
DR neXtProt; NX_Q07866; -.
DR PharmGKB; PA162393424; -.
DR HOVERGEN; HBG006217; -.
DR KO; K10407; -.
DR OMA; MREDMST; -.
DR OrthoDB; EOG7TXKGD; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; KLC1; human.
DR GeneWiki; KLC1; -.
DR GenomeRNAi; 3831; -.
DR NextBio; 15055; -.
DR PRO; PR:Q07866; -.
DR ArrayExpress; Q07866; -.
DR Bgee; Q07866; -.
DR Genevestigator; Q07866; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:HGNC.
DR GO; GO:0005871; C:kinesin complex; ISS:HGNC.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0003774; F:motor activity; TAS:ProtInc.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0008088; P:axon cargo transport; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
DR GO; GO:0035617; P:stress granule disassembly; ISS:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015792; Kinesin_light_repeat.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF00515; TPR_1; 3.
DR Pfam; PF07719; TPR_2; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR PROSITE; PS01160; KINESIN_LIGHT; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; Host-virus interaction; Microtubule;
KW Motor protein; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 573 Kinesin light chain 1.
FT /FTId=PRO_0000215092.
FT REPEAT 213 246 TPR 1.
FT REPEAT 255 288 TPR 2.
FT REPEAT 297 330 TPR 3.
FT REPEAT 339 372 TPR 4.
FT REPEAT 381 414 TPR 5.
FT REPEAT 464 497 TPR 6.
FT COILED 27 156
FT MOD_RES 449 449 Phosphotyrosine (By similarity).
FT MOD_RES 521 521 Phosphoserine; by AMPK.
FT MOD_RES 524 524 Phosphoserine; by AMPK.
FT VAR_SEQ 542 573 VSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR -> MKRAS
FT SLNVLNVGGKAAEDRFQERNNCLADSRALSASHTDLAH
FT (in isoform P).
FT /FTId=VSP_008021.
FT VAR_SEQ 542 550 Missing (in isoform G, isoform N and
FT isoform S).
FT /FTId=VSP_008017.
FT VAR_SEQ 550 550 G -> GDGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSS
FT RESEPKNPGMKRASSLNVLNVGGKAAEDRFQ (in
FT isoform I).
FT /FTId=VSP_023323.
FT VAR_SEQ 551 573 GVSGRASFCGKRQQQQWPGRRHR -> MRKMKLGLVN (in
FT isoform C and isoform S).
FT /FTId=VSP_008018.
FT VAR_SEQ 551 573 GVSGRASFCGKRQQQQWPGRRHR -> DGTGSLKRSGSFSK
FT LRASIRRSSEKLVRKLKGGSSRESEPKNPGASLAEPLFVEN
FT DSSSSGLEDATAN (in isoform D).
FT /FTId=VSP_046424.
FT VAR_SEQ 551 551 G -> DGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSR
FT ESEPKNPG (in isoform J, isoform K and
FT isoform N).
FT /FTId=VSP_008019.
FT VAR_SEQ 552 573 VSGRASFCGKRQQQQWPGRRHR -> MKRASSLNVLNVGGK
FT AAEDRFQERNNCLADSRALSASHTDLAH (in isoform
FT J and isoform N).
FT /FTId=VSP_008020.
FT MUTAGEN 521 521 S->A,D: No effect on motor function; when
FT associated with A/D-524.
FT MUTAGEN 524 524 S->A,D: No effect on motor function; when
FT associated with A/D-521.
FT CONFLICT 4 4 N -> T (in Ref. 1; AAA16576, 2; AAO62548/
FT AAO62549/AAO62550/AAO62551/AAO62553/
FT AAO62552/AAO62554/AAO62555/AAO64641 and
FT 3; AAF72543).
FT STRAND 203 205
FT HELIX 211 225
FT HELIX 229 247
FT STRAND 249 251
FT HELIX 252 267
FT HELIX 271 289
FT HELIX 294 308
FT TURN 309 311
FT HELIX 313 331
FT HELIX 336 350
FT TURN 351 353
FT HELIX 355 371
FT HELIX 378 394
FT HELIX 397 416
FT HELIX 426 435
FT HELIX 461 477
FT HELIX 480 494
SQ SEQUENCE 573 AA; 65310 MW; A66E3915C57C2764 CRC64;
MYDNMSTMVY IKEDKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
ESNLVEEKSN MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQKLRAQV RRLCQENQWL
RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDTD STKEPLDDLF
PNDEDDPGQG IQQQHSSAAA AAQQGGYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL
EDLEKTSGHD HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG KDHPAVAATL
NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ NQGKYEEVEY
YYQRALEIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA ETLYKEILTR AHEREFGSVD
DENKPIWMHA EEREECKGKQ KDGTSFGEYG GWYKACKVDS PTVTTTLKNL GALYRRQGKF
EAAETLEEAA MRSRKQGLDN VHKQRVAEVL NDPENMEKRR SRESLNVDVV KYESGPDGGE
EVSMSVEWNG GVSGRASFCG KRQQQQWPGR RHR
//
MIM
600025
*RECORD*
*FIELD* NO
600025
*FIELD* TI
*600025 KINESIN LIGHT CHAIN 1; KLC1
;;KINESIN 2; KNS2;;
KNS2A;;
KLC
*FIELD* TX
DESCRIPTION
read more
Kinesins are tubulin (see 191130) molecular motors that transport
organelles within cells and move chromosomes along microtubules during
cell division. In sea urchin and mammalian cells, kinesins have been
characterized as tetrameric proteins containing 2 heavy (alpha) chains
of approximately 120 kD and 2 light (beta) chains of approximately 70
kD. The alpha chains provide the tubulin binding site and the ATPase
domains, whereas the beta chains are responsible for the specific
attachment of the organelle to be moved by the kinesin tetramer.
Kinesins transport their bound organelle to the plus end of the
microtubule (summary by Chernajovsky et al., 1996).
CLONING
Chernajovsky et al. (1996) noted that differential splicing occurs for
the kinesin beta (light chain) cDNA sequences at the 3-prime end of the
rat kinesin mRNA, producing kinesins having different C-terminal ends
that seem to confer the kinesin specificity for organelle binding.
Cabeza-Arvelaiz et al. (1993) isolated and sequenced a cDNA encoding the
human kinesin light chain protein (KLC). The cDNA encodes a deduced
polypeptide of 569 amino acids with a predicted molecular mass of 64,789
Da. The predicted secondary internal structure of the KLC molecule
consists of about 27 contiguous repeats, each of approximately 21 amino
acids, and could be divided into 3 domains.
Rahman et al. (1998) cloned mouse Klc1. The deduced 581-amino acid
protein has an N-terminal coiled-coil region of about 100 amino acids
and 6 imperfect tetratricopeptide repeats of about 34 amino acids each.
Northern and Western blot analyses detected Klc1 predominantly in mouse
central and peripheral neuronal tissues. Immunofluorescence analysis of
cultured rat hippocampal precursor cells showed that Klc1 levels
increased with differentiation. In situ hybridization of mouse brain
showed that both Klc1 and Klc2 (611729) were enriched in olfactory bulb,
hippocampus, dentate gyrus, and the granular layer of cerebellum. Klc1
was expressed in a subset of cells in the sciatic nerve and showed
diffuse axonal staining. Fractionation of whole mouse brain extracts
revealed Klc1 and Klc2 in the cytosolic fraction and Klc2 in the
microsomal fraction.
GENE FUNCTION
Chernajovsky et al. (1996) characterized the human KNS2 gene product of
a differentially spliced, T-cell-derived mRNA and cloned its promoter
region. The promoter region transcribes constitutively. In permanently
transfected human HeLa and NB100 neuroblastoma cells, a reporter gene
containing the promoter and part of the first exon of beta kinesin was
75-fold more active than the HSV-tk promoter. The first exon contains a
5-prime untranslated sequence capable of forming a stable double-hairpin
loop, which functions as a translational enhancer. Its deletion
decreases the efficiency of in vitro translation of beta kinesin mRNA.
Kamal et al. (2000) demonstrated that the axonal transport of APP
(104760) in neurons is mediated by the direct binding of APP to the
light chain subunit of kinesin-1.
Using anti-mouse Klc1 antibodies to immunoprecipitate proteins from
mouse brain lysates, Rahman et al. (1998) showed that Klc1 associated
with Nkhc (KIF5A; 602821) and Ukhc (KIF5B; 602809), but not with Klc2.
In the presence of a nonhydrolyzable ATP analog, both Klc1 and Klc2
cosedimented with taxol-stabilized mouse brain microtubules.
GENE STRUCTURE
Chernajovsky et al. (1996) determined that the entire KNS2 gene spans 90
kb and encodes a 70-kD protein.
MAPPING
Cabeza-Arvelaiz et al. (1993) assigned the KLC gene to chromosome 14 by
screening of a human/hamster somatic cell hybrid panel. Goedert et al.
(1996) mapped the KNS2 gene to 14q32.3 by fluorescence in situ
hybridization.
*FIELD* RF
1. 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 organization of the human kinesin light-chain
(KLC) gene. DNA Cell Biol. 12: 881-892, 1993.
2. Chernajovsky, Y.; Brown, A.; Clark, J.: Human kinesin light (beta)
chain gene: DNA sequence and functional characterization of its promoter
and first exon. DNA Cell Biol. 15: 965-974, 1996.
3. Goedert, M.; Marsh, S.; Carter, N.: Localization of the human
kinesin light chain gene (KNS2) to chromosome 14q32.3 by fluorescence
in situ hybridization. Genomics 32: 173-175, 1996.
4. Kamal, A.; Stokin, G. B.; Yang, Z.; Xia, C.; Goldstein, L. S.:
Axonal transport of amyloid precursor protein is mediated by direct
binding to the kinesin light chain subunit of kinesin-I. Neuron 28:
449-459, 2000.
5. Rahman, A.; Friedman, D. S.; Goldstein, L. S. B.: Two kinesin
light chain genes in mice: identification and characterization of
the encoded proteins. J. Biol. Chem. 273: 15395-15403, 1998. Note:
Erratum: J. Biol. Chem. 273: 24280 only, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 12/12/2007
Ada Hamosh - updated: 1/8/2002
Ethylin Wang Jabs - updated: 8/29/1997
*FIELD* CD
Victor A. McKusick: 7/12/1994
*FIELD* ED
carol: 07/26/2013
terry: 4/4/2013
carol: 3/9/2009
mgross: 1/16/2008
terry: 12/12/2007
joanna: 3/9/2007
alopez: 1/8/2002
mark: 9/16/1997
mark: 7/8/1996
terry: 6/26/1996
mark: 3/13/1996
mark: 3/11/1996
terry: 3/7/1996
mimadm: 7/30/1994
jason: 7/12/1994
*RECORD*
*FIELD* NO
600025
*FIELD* TI
*600025 KINESIN LIGHT CHAIN 1; KLC1
;;KINESIN 2; KNS2;;
KNS2A;;
KLC
*FIELD* TX
DESCRIPTION
read more
Kinesins are tubulin (see 191130) molecular motors that transport
organelles within cells and move chromosomes along microtubules during
cell division. In sea urchin and mammalian cells, kinesins have been
characterized as tetrameric proteins containing 2 heavy (alpha) chains
of approximately 120 kD and 2 light (beta) chains of approximately 70
kD. The alpha chains provide the tubulin binding site and the ATPase
domains, whereas the beta chains are responsible for the specific
attachment of the organelle to be moved by the kinesin tetramer.
Kinesins transport their bound organelle to the plus end of the
microtubule (summary by Chernajovsky et al., 1996).
CLONING
Chernajovsky et al. (1996) noted that differential splicing occurs for
the kinesin beta (light chain) cDNA sequences at the 3-prime end of the
rat kinesin mRNA, producing kinesins having different C-terminal ends
that seem to confer the kinesin specificity for organelle binding.
Cabeza-Arvelaiz et al. (1993) isolated and sequenced a cDNA encoding the
human kinesin light chain protein (KLC). The cDNA encodes a deduced
polypeptide of 569 amino acids with a predicted molecular mass of 64,789
Da. The predicted secondary internal structure of the KLC molecule
consists of about 27 contiguous repeats, each of approximately 21 amino
acids, and could be divided into 3 domains.
Rahman et al. (1998) cloned mouse Klc1. The deduced 581-amino acid
protein has an N-terminal coiled-coil region of about 100 amino acids
and 6 imperfect tetratricopeptide repeats of about 34 amino acids each.
Northern and Western blot analyses detected Klc1 predominantly in mouse
central and peripheral neuronal tissues. Immunofluorescence analysis of
cultured rat hippocampal precursor cells showed that Klc1 levels
increased with differentiation. In situ hybridization of mouse brain
showed that both Klc1 and Klc2 (611729) were enriched in olfactory bulb,
hippocampus, dentate gyrus, and the granular layer of cerebellum. Klc1
was expressed in a subset of cells in the sciatic nerve and showed
diffuse axonal staining. Fractionation of whole mouse brain extracts
revealed Klc1 and Klc2 in the cytosolic fraction and Klc2 in the
microsomal fraction.
GENE FUNCTION
Chernajovsky et al. (1996) characterized the human KNS2 gene product of
a differentially spliced, T-cell-derived mRNA and cloned its promoter
region. The promoter region transcribes constitutively. In permanently
transfected human HeLa and NB100 neuroblastoma cells, a reporter gene
containing the promoter and part of the first exon of beta kinesin was
75-fold more active than the HSV-tk promoter. The first exon contains a
5-prime untranslated sequence capable of forming a stable double-hairpin
loop, which functions as a translational enhancer. Its deletion
decreases the efficiency of in vitro translation of beta kinesin mRNA.
Kamal et al. (2000) demonstrated that the axonal transport of APP
(104760) in neurons is mediated by the direct binding of APP to the
light chain subunit of kinesin-1.
Using anti-mouse Klc1 antibodies to immunoprecipitate proteins from
mouse brain lysates, Rahman et al. (1998) showed that Klc1 associated
with Nkhc (KIF5A; 602821) and Ukhc (KIF5B; 602809), but not with Klc2.
In the presence of a nonhydrolyzable ATP analog, both Klc1 and Klc2
cosedimented with taxol-stabilized mouse brain microtubules.
GENE STRUCTURE
Chernajovsky et al. (1996) determined that the entire KNS2 gene spans 90
kb and encodes a 70-kD protein.
MAPPING
Cabeza-Arvelaiz et al. (1993) assigned the KLC gene to chromosome 14 by
screening of a human/hamster somatic cell hybrid panel. Goedert et al.
(1996) mapped the KNS2 gene to 14q32.3 by fluorescence in situ
hybridization.
*FIELD* RF
1. 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 organization of the human kinesin light-chain
(KLC) gene. DNA Cell Biol. 12: 881-892, 1993.
2. Chernajovsky, Y.; Brown, A.; Clark, J.: Human kinesin light (beta)
chain gene: DNA sequence and functional characterization of its promoter
and first exon. DNA Cell Biol. 15: 965-974, 1996.
3. Goedert, M.; Marsh, S.; Carter, N.: Localization of the human
kinesin light chain gene (KNS2) to chromosome 14q32.3 by fluorescence
in situ hybridization. Genomics 32: 173-175, 1996.
4. Kamal, A.; Stokin, G. B.; Yang, Z.; Xia, C.; Goldstein, L. S.:
Axonal transport of amyloid precursor protein is mediated by direct
binding to the kinesin light chain subunit of kinesin-I. Neuron 28:
449-459, 2000.
5. Rahman, A.; Friedman, D. S.; Goldstein, L. S. B.: Two kinesin
light chain genes in mice: identification and characterization of
the encoded proteins. J. Biol. Chem. 273: 15395-15403, 1998. Note:
Erratum: J. Biol. Chem. 273: 24280 only, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 12/12/2007
Ada Hamosh - updated: 1/8/2002
Ethylin Wang Jabs - updated: 8/29/1997
*FIELD* CD
Victor A. McKusick: 7/12/1994
*FIELD* ED
carol: 07/26/2013
terry: 4/4/2013
carol: 3/9/2009
mgross: 1/16/2008
terry: 12/12/2007
joanna: 3/9/2007
alopez: 1/8/2002
mark: 9/16/1997
mark: 7/8/1996
terry: 6/26/1996
mark: 3/13/1996
mark: 3/11/1996
terry: 3/7/1996
mimadm: 7/30/1994
jason: 7/12/1994