KLC1_HUMAN
ID KLC1_HUMAN Reviewed; 573 AA.
AC Q07866; A6NF62; F8VTM4; Q7RTM2; Q7RTM3; Q7RTM5; Q7RTP9; Q7RTQ3; Q7RTQ5;
AC Q7RTQ6; Q86SF5; Q86TF5; Q86V74; Q86V75; Q86V76; Q86V77; Q86V78; Q86V79;
AC Q96H62;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 211.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=8274221; DOI=10.1089/dna.1993.12.881;
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; DOI=10.1034/j.1600-0854.2003.00113.x;
RA McCart A.E., Mahony D., Rothnagel J.A.;
RT "Alternatively spliced products of the human kinesin light chain 1 (KNS2)
RT 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., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., 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., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBUNIT, INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14970196; DOI=10.1074/jbc.m401332200;
RA Kamm C., Boston H., Hewett J., Wilbur J., Corey D.P., Hanson P.I.,
RA Ramesh V., Breakefield X.O.;
RT "The early onset dystonia protein torsinA interacts with kinesin light
RT chain 1.";
RL J. Biol. Chem. 279:19882-19892(2004).
RN [8]
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
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 [12]
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 [13]
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., Rutter G.A.;
RT "Cell-wide analysis of secretory granule dynamics in three dimensions in
RT living pancreatic beta-cells: evidence against a role for AMPK-dependent
RT phosphorylation of KLC1 at Ser517/Ser520 in glucose-stimulated insulin
RT granule movement.";
RL Biochem. Soc. Trans. 38:205-208(2010).
RN [14]
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 N),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578 (ISOFORM P),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP INTERACTION WITH ADENOVIRUS HEXON-INTERLACING PROTEIN (MICROBIAL
RP INFECTION).
RX PubMed=21925109; DOI=10.1016/j.chom.2011.08.010;
RA Strunze S., Engelke M.F., Wang I.H., Puntener D., Boucke K., Schleich S.,
RA Way M., Schoenenberger P., Burckhardt C.J., Greber U.F.;
RT "Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore
RT complex promote virus infection.";
RL Cell Host Microbe 10:210-223(2011).
RN [16]
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 N),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578 (ISOFORM P),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 (ISOFORMS I AND J),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 (ISOFORM N),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 (ISOFORM P), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INTERACTION WITH BORCS5.
RX PubMed=25898167; DOI=10.1016/j.devcel.2015.02.011;
RA Pu J., Schindler C., Jia R., Jarnik M., Backlund P., Bonifacino J.S.;
RT "BORC, a multisubunit complex that regulates lysosome positioning.";
RL Dev. Cell 33:176-188(2015).
RN [19]
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 protein
CC that may play a role in organelle transport. The light chain may
CC function in coupling of cargo to the heavy chain or in the modulation
CC of its ATPase activity.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains. Interacts with SPAG9. Interacts with ATCAY; may link
CC mitochondria to KLC1 and regulate mitochondria localization into neuron
CC projections (By similarity). Interacts (via TPR repeats) with TOR1A;
CC the interaction associates TOR1A with the kinesin oligomeric complex
CC (PubMed:14970196). Interacts with BORCS5 (PubMed:25898167). Interacts
CC with MAPK8IP3/JIP3 and NTRK2/TRKB; interaction with NTRK2/TRKB is
CC mediated by MAPK8IP3/JIP3 (By similarity).
CC {ECO:0000250|UniProtKB:P37285, ECO:0000269|PubMed:14970196,
CC ECO:0000269|PubMed:25898167}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus hexon-
CC interlacing protein; this interaction leads to capsid disruption at the
CC nuclear pore complex during virus entry into host cell.
CC {ECO:0000269|PubMed:21925109}.
CC -!- INTERACTION:
CC Q07866; Q12982: BNIP2; NbExp=3; IntAct=EBI-721019, EBI-752094;
CC Q07866; Q15323: KRT31; NbExp=3; IntAct=EBI-721019, EBI-948001;
CC Q07866; Q96M63: ODAD1; NbExp=3; IntAct=EBI-721019, EBI-10173858;
CC Q07866; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-721019, EBI-25475856;
CC Q07866; Q8ZMM8: pipB2; Xeno; NbExp=4; IntAct=EBI-721019, EBI-15598815;
CC Q07866-2; Q63HQ0-2: AP1AR; NbExp=3; IntAct=EBI-11979975, EBI-12016808;
CC Q07866-2; P05067: APP; NbExp=3; IntAct=EBI-11979975, EBI-77613;
CC Q07866-2; Q86WG3: ATCAY; NbExp=3; IntAct=EBI-11979975, EBI-1783328;
CC Q07866-2; Q12982: BNIP2; NbExp=3; IntAct=EBI-11979975, EBI-752094;
CC Q07866-2; Q9UPT6: MAPK8IP3; NbExp=3; IntAct=EBI-11979975, EBI-717887;
CC Q07866-2; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-11979975, EBI-2554984;
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone {ECO:0000250}.
CC Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:14970196}.
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 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 Name=P; Synonyms=KLC1P;
CC IsoId=Q07866-7; Sequence=VSP_008021;
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 Name=D; Synonyms=KLC1D;
CC IsoId=Q07866-10; Sequence=VSP_046424;
CC -!- TISSUE SPECIFICITY: Found in a variety of tissues. Mostly abundant in
CC brain and spine. {ECO:0000269|PubMed:14970196}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16576.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF72543.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO62549.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01265.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01266.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01268.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01289.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01291.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01292.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01295.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01296.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA01297.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS32165.1; -. [Q07866-2]
DR CCDS; CCDS41996.1; -. [Q07866-1]
DR CCDS; CCDS45168.1; -. [Q07866-10]
DR PIR; I53013; I53013.
DR RefSeq; NP_001123579.1; NM_001130107.1. [Q07866-10]
DR RefSeq; NP_005543.2; NM_005552.4. [Q07866-2]
DR RefSeq; NP_891553.2; NM_182923.3. [Q07866-1]
DR PDB; 3NF1; X-ray; 2.80 A; A=203-497.
DR PDB; 5OJ8; X-ray; 2.25 A; A=185-418.
DR PDB; 7AI4; X-ray; 2.79 A; A/B=206-418, A/B=459-502.
DR PDB; 7AIE; X-ray; 3.29 A; A/B/C/D=185-418.
DR PDBsum; 3NF1; -.
DR PDBsum; 5OJ8; -.
DR PDBsum; 7AI4; -.
DR PDBsum; 7AIE; -.
DR AlphaFoldDB; Q07866; -.
DR SMR; Q07866; -.
DR BioGRID; 110029; 118.
DR CORUM; Q07866; -.
DR DIP; DIP-40371N; -.
DR ELM; Q07866; -.
DR IntAct; Q07866; 83.
DR MINT; Q07866; -.
DR STRING; 9606.ENSP00000414982; -.
DR GlyGen; Q07866; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q07866; -.
DR MetOSite; Q07866; -.
DR PhosphoSitePlus; Q07866; -.
DR SwissPalm; Q07866; -.
DR BioMuta; KLC1; -.
DR DMDM; 223590110; -.
DR UCD-2DPAGE; Q07866; -.
DR EPD; Q07866; -.
DR jPOST; Q07866; -.
DR MassIVE; Q07866; -.
DR MaxQB; Q07866; -.
DR PaxDb; Q07866; -.
DR PeptideAtlas; Q07866; -.
DR PRIDE; Q07866; -.
DR ProteomicsDB; 28642; -.
DR ProteomicsDB; 58544; -. [Q07866-1]
DR ProteomicsDB; 58545; -. [Q07866-2]
DR ProteomicsDB; 58546; -. [Q07866-3]
DR ProteomicsDB; 58547; -. [Q07866-4]
DR ProteomicsDB; 58548; -. [Q07866-5]
DR ProteomicsDB; 58549; -. [Q07866-6]
DR ProteomicsDB; 58550; -. [Q07866-7]
DR ProteomicsDB; 58551; -. [Q07866-8]
DR ProteomicsDB; 58552; -. [Q07866-9]
DR Antibodypedia; 4068; 291 antibodies from 36 providers.
DR DNASU; 3831; -.
DR Ensembl; ENST00000246489.11; ENSP00000246489.7; ENSG00000126214.22. [Q07866-4]
DR Ensembl; ENST00000334553.11; ENSP00000334523.6; ENSG00000126214.22. [Q07866-9]
DR Ensembl; ENST00000347839.10; ENSP00000334618.7; ENSG00000126214.22. [Q07866-6]
DR Ensembl; ENST00000348520.10; ENSP00000341154.6; ENSG00000126214.22. [Q07866-1]
DR Ensembl; ENST00000389744.8; ENSP00000374394.3; ENSG00000126214.22. [Q07866-2]
DR Ensembl; ENST00000452929.6; ENSP00000414982.2; ENSG00000126214.22. [Q07866-10]
DR Ensembl; ENST00000553286.5; ENSP00000452487.1; ENSG00000126214.22. [Q07866-2]
DR Ensembl; ENST00000554228.5; ENSP00000450616.1; ENSG00000126214.22. [Q07866-2]
DR Ensembl; ENST00000557450.5; ENSP00000450648.1; ENSG00000126214.22. [Q07866-3]
DR Ensembl; ENST00000634686.1; ENSP00000488938.1; ENSG00000126214.22. [Q07866-7]
DR GeneID; 3831; -.
DR KEGG; hsa:3831; -.
DR MANE-Select; ENST00000334553.11; ENSP00000334523.6; NM_001394837.1; NP_001381766.1. [Q07866-9]
DR UCSC; uc001ynm.2; human. [Q07866-1]
DR CTD; 3831; -.
DR DisGeNET; 3831; -.
DR GeneCards; KLC1; -.
DR HGNC; HGNC:6387; KLC1.
DR HPA; ENSG00000126214; Tissue enhanced (brain).
DR MIM; 600025; gene.
DR neXtProt; NX_Q07866; -.
DR OpenTargets; ENSG00000126214; -.
DR PharmGKB; PA162393424; -.
DR VEuPathDB; HostDB:ENSG00000126214; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000155555; -.
DR InParanoid; Q07866; -.
DR PhylomeDB; Q07866; -.
DR TreeFam; TF314010; -.
DR PathwayCommons; Q07866; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q07866; -.
DR SIGNOR; Q07866; -.
DR BioGRID-ORCS; 3831; 6 hits in 1074 CRISPR screens.
DR ChiTaRS; KLC1; human.
DR GeneWiki; KLC1; -.
DR GenomeRNAi; 3831; -.
DR Pharos; Q07866; Tbio.
DR PRO; PR:Q07866; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q07866; protein.
DR Bgee; ENSG00000126214; Expressed in right hemisphere of cerebellum and 206 other tissues.
DR ExpressionAtlas; Q07866; baseline and differential.
DR Genevisible; Q07866; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:HGNC-UCL.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; ISS:HGNC-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13176; TPR_7; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
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; Cell projection; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Host-virus interaction;
KW Microtubule; Motor protein; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..573
FT /note="Kinesin light chain 1"
FT /id="PRO_0000215092"
FT REPEAT 213..246
FT /note="TPR 1"
FT REPEAT 255..288
FT /note="TPR 2"
FT REPEAT 297..330
FT /note="TPR 3"
FT REPEAT 339..372
FT /note="TPR 4"
FT REPEAT 381..414
FT /note="TPR 5"
FT REPEAT 464..497
FT /note="TPR 6"
FT REGION 155..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..156
FT COMPBIAS 155..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37285"
FT MOD_RES 449
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88447"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88447"
FT MOD_RES 521
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:20074060"
FT MOD_RES 524
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:20074060"
FT VAR_SEQ 542..573
FT /note="VSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR -> MKRASSLNVLNVGGKA
FT AEDRFQERNNCLADSRALSASHTDLAH (in isoform P)"
FT /evidence="ECO:0000303|PubMed:12839500"
FT /id="VSP_008021"
FT VAR_SEQ 542..550
FT /note="Missing (in isoform G, isoform N and isoform S)"
FT /evidence="ECO:0000303|PubMed:12839500"
FT /id="VSP_008017"
FT VAR_SEQ 550
FT /note="G -> GDGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESEPKNPGMK
FT RASSLNVLNVGGKAAEDRFQ (in isoform I)"
FT /evidence="ECO:0000303|PubMed:12839500"
FT /id="VSP_023323"
FT VAR_SEQ 551..573
FT /note="GVSGRASFCGKRQQQQWPGRRHR -> MRKMKLGLVN (in isoform C
FT and isoform S)"
FT /evidence="ECO:0000303|PubMed:12839500,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008018"
FT VAR_SEQ 551..573
FT /note="GVSGRASFCGKRQQQQWPGRRHR -> DGTGSLKRSGSFSKLRASIRRSSEK
FT LVRKLKGGSSRESEPKNPGASLAEPLFVENDSSSSGLEDATAN (in isoform D)"
FT /evidence="ECO:0000303|PubMed:12839500"
FT /id="VSP_046424"
FT VAR_SEQ 551
FT /note="G -> DGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESEPKNPG
FT (in isoform J, isoform K and isoform N)"
FT /evidence="ECO:0000303|PubMed:12839500"
FT /id="VSP_008019"
FT VAR_SEQ 552..573
FT /note="VSGRASFCGKRQQQQWPGRRHR -> MKRASSLNVLNVGGKAAEDRFQERNN
FT CLADSRALSASHTDLAH (in isoform J and isoform N)"
FT /evidence="ECO:0000303|PubMed:12839500"
FT /id="VSP_008020"
FT MUTAGEN 521
FT /note="S->A,D: No effect on motor function; when associated
FT with A/D-524."
FT /evidence="ECO:0000269|PubMed:20074060"
FT MUTAGEN 524
FT /note="S->A,D: No effect on motor function; when associated
FT with A/D-521."
FT /evidence="ECO:0000269|PubMed:20074060"
FT CONFLICT 4
FT /note="N -> T (in Ref. 1; AAA16576, 2; AAO62548/AAO62549/
FT AAO62550/AAO62551/AAO62553/AAO62552/AAO62554/AAO62555/
FT AAO64641 and 3; AAF72543)"
FT /evidence="ECO:0000305"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3NF1"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 229..247
FT /evidence="ECO:0007829|PDB:5OJ8"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 252..267
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 271..289
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 313..331
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:5OJ8"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 355..372
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 378..394
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 397..415
FT /evidence="ECO:0007829|PDB:5OJ8"
FT HELIX 426..435
FT /evidence="ECO:0007829|PDB:3NF1"
FT HELIX 463..477
FT /evidence="ECO:0007829|PDB:7AI4"
FT HELIX 480..494
FT /evidence="ECO:0007829|PDB:7AI4"
FT MOD_RES Q07866-4:600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES Q07866-4:631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CONFLICT Q07866-4:631
FT /note="S -> T (in Ref. 2; AAO62555)"
FT /evidence="ECO:0000305"
FT MOD_RES Q07866-6:591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES Q07866-6:622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CONFLICT Q07866-6:622
FT /note="S -> T (in Ref. 2; AAO62551)"
FT /evidence="ECO:0000305"
FT MOD_RES Q07866-7:547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES Q07866-7:578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q07866-9:600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
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
