KLC4_HUMAN
ID KLC4_HUMAN Reviewed; 619 AA.
AC Q9NSK0; B3KNY4; B3KPI3; B3KSQ3; B4DME9; Q66K28; Q96EG6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Kinesin light chain 4;
DE Short=KLC 4;
DE AltName: Full=Kinesin-like protein 8;
GN Name=KLC4; Synonyms=KNSL8;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5), AND
RP VARIANT HIS-72.
RC TISSUE=Adrenal gland, Brain, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala, and Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Prostate, and Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, AND
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP 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 [LARGE SCALE ANALYSIS] AT SER-590 AND THR-612, AND
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, AND
RP 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; SER-566 AND SER-590, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP 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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NSK0; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-949319, EBI-742038;
CC Q9NSK0; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-949319, EBI-11752486;
CC Q9NSK0; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-949319, EBI-10181988;
CC Q9NSK0; Q9BW62: KATNAL1; NbExp=6; IntAct=EBI-949319, EBI-743591;
CC Q9NSK0; A1A4E9: KRT13; NbExp=3; IntAct=EBI-949319, EBI-10171552;
CC Q9NSK0; P19012: KRT15; NbExp=3; IntAct=EBI-949319, EBI-739566;
CC Q9NSK0; P08779: KRT16; NbExp=3; IntAct=EBI-949319, EBI-356410;
CC Q9NSK0; Q15323: KRT31; NbExp=6; IntAct=EBI-949319, EBI-948001;
CC Q9NSK0; Q14525: KRT33B; NbExp=3; IntAct=EBI-949319, EBI-1049638;
CC Q9NSK0; O76011: KRT34; NbExp=3; IntAct=EBI-949319, EBI-1047093;
CC Q9NSK0; P50222: MEOX2; NbExp=3; IntAct=EBI-949319, EBI-748397;
CC Q9NSK0; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-949319, EBI-10172876;
CC Q9NSK0; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-949319, EBI-748601;
CC Q9NSK0; Q7RTY1: SLC16A9; NbExp=3; IntAct=EBI-949319, EBI-10232636;
CC Q9NSK0; Q8N205: SYNE4; NbExp=3; IntAct=EBI-949319, EBI-7131783;
CC Q9NSK0; O75478: TADA2A; NbExp=3; IntAct=EBI-949319, EBI-742268;
CC Q9NSK0; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-949319, EBI-739895;
CC Q9NSK0; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-949319, EBI-10252492;
CC Q9NSK0; P0DTC9: N; Xeno; NbExp=3; IntAct=EBI-949319, EBI-25475856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9NSK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSK0-2; Sequence=VSP_037875, VSP_037876;
CC Name=3;
CC IsoId=Q9NSK0-3; Sequence=VSP_038083;
CC Name=4;
CC IsoId=Q9NSK0-4; Sequence=VSP_043324, VSP_043325;
CC Name=5;
CC IsoId=Q9NSK0-5; Sequence=VSP_057231;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86788.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK055293; BAG51496.1; -; mRNA.
DR EMBL; AK056393; BAG51695.1; -; mRNA.
DR EMBL; AK094102; BAG52815.1; -; mRNA.
DR EMBL; AK127018; BAC86788.1; ALT_SEQ; mRNA.
DR EMBL; AK127894; BAC87179.1; -; mRNA.
DR EMBL; AK297433; BAG59861.1; -; mRNA.
DR EMBL; AL162078; CAB82411.1; -; mRNA.
DR EMBL; AL136304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04149.1; -; Genomic_DNA.
DR EMBL; BC012357; AAH12357.1; -; mRNA.
DR EMBL; BC080637; AAH80637.1; -; mRNA.
DR EMBL; BC103727; AAI03728.1; -; mRNA.
DR EMBL; BX640717; CAE45836.1; -; mRNA.
DR CCDS; CCDS47429.1; -. [Q9NSK0-4]
DR CCDS; CCDS4882.1; -. [Q9NSK0-3]
DR CCDS; CCDS4883.1; -. [Q9NSK0-1]
DR CCDS; CCDS75459.1; -. [Q9NSK0-5]
DR PIR; T47147; T47147.
DR RefSeq; NP_001275963.1; NM_001289034.1. [Q9NSK0-1]
DR RefSeq; NP_001275964.1; NM_001289035.1. [Q9NSK0-5]
DR RefSeq; NP_612352.1; NM_138343.3. [Q9NSK0-4]
DR RefSeq; NP_958929.1; NM_201521.2. [Q9NSK0-1]
DR RefSeq; NP_958930.1; NM_201522.2. [Q9NSK0-1]
DR RefSeq; NP_958931.1; NM_201523.2. [Q9NSK0-3]
DR AlphaFoldDB; Q9NSK0; -.
DR SMR; Q9NSK0; -.
DR BioGRID; 124648; 110.
DR IntAct; Q9NSK0; 64.
DR MINT; Q9NSK0; -.
DR STRING; 9606.ENSP00000259708; -.
DR GlyGen; Q9NSK0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NSK0; -.
DR PhosphoSitePlus; Q9NSK0; -.
DR BioMuta; KLC4; -.
DR DMDM; 116242607; -.
DR EPD; Q9NSK0; -.
DR jPOST; Q9NSK0; -.
DR MassIVE; Q9NSK0; -.
DR MaxQB; Q9NSK0; -.
DR PaxDb; Q9NSK0; -.
DR PeptideAtlas; Q9NSK0; -.
DR PRIDE; Q9NSK0; -.
DR ProteomicsDB; 4604; -.
DR ProteomicsDB; 82562; -. [Q9NSK0-1]
DR ProteomicsDB; 82563; -. [Q9NSK0-2]
DR ProteomicsDB; 82564; -. [Q9NSK0-3]
DR ProteomicsDB; 82565; -. [Q9NSK0-4]
DR Antibodypedia; 30259; 77 antibodies from 18 providers.
DR DNASU; 89953; -.
DR Ensembl; ENST00000259708.7; ENSP00000259708.3; ENSG00000137171.15. [Q9NSK0-3]
DR Ensembl; ENST00000347162.10; ENSP00000340221.5; ENSG00000137171.15. [Q9NSK0-1]
DR Ensembl; ENST00000394056.6; ENSP00000377620.2; ENSG00000137171.15. [Q9NSK0-1]
DR Ensembl; ENST00000453940.6; ENSP00000395806.2; ENSG00000137171.15. [Q9NSK0-5]
DR Ensembl; ENST00000458460.6; ENSP00000410358.2; ENSG00000137171.15. [Q9NSK0-4]
DR Ensembl; ENST00000467906.5; ENSP00000418759.1; ENSG00000137171.15. [Q9NSK0-2]
DR Ensembl; ENST00000479388.5; ENSP00000418031.1; ENSG00000137171.15. [Q9NSK0-1]
DR GeneID; 89953; -.
DR KEGG; hsa:89953; -.
DR MANE-Select; ENST00000347162.10; ENSP00000340221.5; NM_201521.3; NP_958929.1.
DR UCSC; uc003otu.4; human. [Q9NSK0-1]
DR CTD; 89953; -.
DR DisGeNET; 89953; -.
DR GeneCards; KLC4; -.
DR HGNC; HGNC:21624; KLC4.
DR HPA; ENSG00000137171; Tissue enhanced (liver).
DR neXtProt; NX_Q9NSK0; -.
DR OpenTargets; ENSG00000137171; -.
DR PharmGKB; PA134934134; -.
DR VEuPathDB; HostDB:ENSG00000137171; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000161323; -.
DR HOGENOM; CLU_1926883_0_0_1; -.
DR InParanoid; Q9NSK0; -.
DR OMA; LQHEGHE; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q9NSK0; -.
DR TreeFam; TF314010; -.
DR PathwayCommons; Q9NSK0; -.
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-983189; Kinesins.
DR SignaLink; Q9NSK0; -.
DR BioGRID-ORCS; 89953; 20 hits in 1082 CRISPR screens.
DR ChiTaRS; KLC4; human.
DR GeneWiki; KLC4; -.
DR GenomeRNAi; 89953; -.
DR Pharos; Q9NSK0; Tdark.
DR PRO; PR:Q9NSK0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NSK0; protein.
DR Bgee; ENSG00000137171; Expressed in right lobe of liver and 168 other tissues.
DR ExpressionAtlas; Q9NSK0; baseline and differential.
DR Genevisible; Q9NSK0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..619
FT /note="Kinesin light chain 4"
FT /id="PRO_0000215097"
FT REPEAT 55..88
FT /note="TPR 1"
FT REPEAT 211..244
FT /note="TPR 2"
FT REPEAT 253..286
FT /note="TPR 3"
FT REPEAT 295..328
FT /note="TPR 4"
FT REPEAT 337..370
FT /note="TPR 5"
FT REPEAT 379..412
FT /note="TPR 6"
FT REPEAT 464..497
FT /note="TPR 7"
FT REGION 154..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..150
FT /evidence="ECO:0000255"
FT COMPBIAS 154..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBS5"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07866"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQM2"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1
FT /note="M -> MEVTGFGVTRPGKVPQARM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038083"
FT VAR_SEQ 87..163
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057231"
FT VAR_SEQ 87..131
FT /note="VMLALASHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQQRLQ -> NLE
FT LRGCAHLGDAGSSQPPEHSGVGETEAAGSGAAAMPGEPVAAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037875"
FT VAR_SEQ 132..619
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037876"
FT VAR_SEQ 295..315
FT /note="AATLNNLAVLYGKRGKYKEAE -> SIPCPPHPTPRTPHHCCFGLS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043324"
FT VAR_SEQ 316..619
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043325"
FT VARIANT 72
FT /note="R -> H (in dbSNP:rs11558979)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_049708"
FT CONFLICT 54
FT /note="L -> LQTIECL (in Ref. 1; BAC87179)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="T -> S (in Ref. 1; BAG51695)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="I -> T (in Ref. 1; BAG51695)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="M -> L (in Ref. 1; BAG52815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 68640 MW; 32DFC2A9A91B5574 CRC64;
MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT IECLQQGGHE
EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR
DELAGTQQRL QRSEQAVAQL EEEKKHLEFL GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP
NEEEEDPSNG LSRGQGATAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED
LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVAATLNN
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TNHPDVAKQL NNLALLCQNQ GKYEAVERYY
QRALAIYEGQ LGPDNPNVAR TKNNLASCYL KQGKYAEAET LYKEILTRAH VQEFGSVDDD
HKPIWMHAEE REEMSKSRHH EGGTPYAEYG GWYKACKVSS PTVNTTLRNL GALYRRQGKL
EAAETLEECA LRSRRQGTDP ISQTKVAELL GESDGRRTSQ EGPGDSVKFE GGEDASVAVE
WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPSAA
PLQVSRGLSA STMDLSSSS
