ID KINH_HUMAN Reviewed; 963 AA. AC P33176; A0AVB2; Q5VZ85; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 222. DE RecName: Full=Kinesin-1 heavy chain {ECO:0000305}; DE AltName: Full=Conventional kinesin heavy chain; DE AltName: Full=Ubiquitous kinesin heavy chain; DE Short=UKHC; GN Name=KIF5B {ECO:0000312|HGNC:HGNC:6324}; Synonyms=KNS, KNS1; 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]. RC TISSUE=Placenta; RX PubMed=1607388; DOI=10.1083/jcb.117.6.1263; RA Navone F., Niclas J., Hom-Booher N., Sparks L., Bernstein H.D., RA McCaffrey G., Vale R.D.; RT "Cloning and expression of a human kinesin heavy chain gene: interaction of RT the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 RT cells."; RL J. Cell Biol. 117:1263-1275(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP INTERACTION WITH SYBU. RX PubMed=15459722; DOI=10.1038/ncb1169; RA Su Q., Cai Q., Gerwin C., Smith C.L., Sheng Z.-H.; RT "Syntabulin is a microtubule-associated protein implicated in syntaxin RT transport in neurons."; RL Nat. Cell Biol. 6:941-953(2004). RN [5] RP INTERACTION WITH PLEKHM2. RX PubMed=15905402; DOI=10.1126/science.1110225; RA Boucrot E., Henry T., Borg J.-P., Gorvel J.-P., Meresse S.; RT "The intracellular fate of Salmonella depends on the recruitment of RT kinesin."; RL Science 308:1174-1178(2005). RN [6] 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 [7] RP INTERACTION WITH JAKMIP1. RX PubMed=17532644; DOI=10.1016/j.mcn.2007.04.008; RA Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S., RA Couve A.; RT "Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton RT and regulate receptor transport."; RL Mol. Cell. Neurosci. 35:501-512(2007). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [9] RP INTERACTION WITH ECPAS. RX PubMed=20682791; DOI=10.1074/jbc.m110.154120; RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., RA Rechsteiner M.; RT "A protein interaction network for Ecm29 links the 26 S proteasome to RT molecular motors and endosomal components."; RL J. Biol. Chem. 285:31616-31633(2010). RN [10] RP FUNCTION. RX PubMed=20386726; DOI=10.1371/journal.pbio.1000350; RA Splinter D., Tanenbaum M.E., Lindqvist A., Jaarsma D., Flotho A., Yu K.L., RA Grigoriev I., Engelsma D., Haasdijk E.D., Keijzer N., Demmers J., RA Fornerod M., Melchior F., Hoogenraad C.C., Medema R.H., Akhmanova A.; RT "Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes RT and regulate centrosome and nuclear positioning during mitotic entry."; RL PLoS Biol. 8:E1000350-E1000350(2010). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, AND IDENTIFICATION BY RP 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 [12] 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 [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22172677; DOI=10.1016/j.devcel.2011.10.007; RA Rosa-Ferreira C., Munro S.; RT "Arl8 and SKIP act together to link lysosomes to kinesin-1."; RL Dev. Cell 21:1171-1178(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [15] RP INTERACTION WITH APP. RX PubMed=23011729; DOI=10.1088/1478-3975/9/5/055005; RA Seamster P.E., Loewenberg M., Pascal J., Chauviere A., Gonzales A., RA Cristini V., Bearer E.L.; RT "Quantitative measurements and modeling of cargo-motor interactions during RT fast transport in the living axon."; RL Phys. Biol. 9:055005-055005(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24088571; DOI=10.1091/mbc.e13-05-0259; RA Tuli A., Thiery J., James A.M., Michelet X., Sharma M., Garg S., RA Sanborn K.B., Orange J.S., Lieberman J., Brenner M.B.; RT "Arf-like GTPase Arl8b regulates lytic granule polarization and natural RT killer cell-mediated cytotoxicity."; RL Mol. Biol. Cell 24:3721-3735(2013). RN [18] RP INTERACTION WITH OGT; RHOT1; RHOT2 AND TRAK1. RX PubMed=24995978; DOI=10.1016/j.cell.2014.06.007; RA Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.; RT "Glucose regulates mitochondrial motility via Milton modification by O- RT GlcNAc transferase."; RL Cell 158:54-68(2014). RN [19] 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 [20] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-956, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-213, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP. RX PubMed=8606779; DOI=10.1038/380550a0; RA Kull F.J., Sablin E.P., Lau R., Fletterick R.J., Vale R.D.; RT "Crystal structure of the kinesin motor domain reveals a structural RT similarity to myosin."; RL Nature 380:550-555(1996). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP. RX PubMed=12368902; DOI=10.1038/nsb852; RA Sindelar C.V., Budny M.J., Rice S., Naber N., Fletterick R., Cooke R.; RT "Two conformations in the human kinesin power stroke defined by X-ray RT crystallography and EPR spectroscopy."; RL Nat. Struct. Biol. 9:844-848(2002). RN [24] RP STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 1-325. RX PubMed=17470637; DOI=10.1083/jcb.200612090; RA Sindelar C.V., Downing K.H.; RT "The beginning of kinesin's force-generating cycle visualized at 9-A RT resolution."; RL J. Cell Biol. 177:377-385(2007). CC -!- FUNCTION: Microtubule-dependent motor required for normal distribution CC of mitochondria and lysosomes. Can induce formation of neurite-like CC membrane protrusions in non-neuronal cells in a ZFYVE27-dependent CC manner (By similarity). Regulates centrosome and nuclear positioning CC during mitotic entry. During the G2 phase of the cell cycle in a BICD2- CC dependent manner, antagonizes dynein function and drives the separation CC of nuclei and centrosomes (PubMed:20386726). Required for anterograde CC axonal transportation of MAPK8IP3/JIP3 which is essential for CC MAPK8IP3/JIP3 function in axon elongation (By similarity). Through CC binding with PLEKHM2 and ARL8B, directs lysosome movement toward CC microtubule plus ends (Probable). Involved in NK cell-mediated CC cytotoxicity. Drives the polarization of cytolytic granules and CC microtubule-organizing centers (MTOCs) toward the immune synapse CC between effector NK lymphocytes and target cells (PubMed:24088571). CC {ECO:0000250|UniProtKB:Q2PQA9, ECO:0000250|UniProtKB:Q61768, CC ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:24088571, CC ECO:0000305|PubMed:22172677, ECO:0000305|PubMed:24088571}. CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains. CC Interacts with GRIP1 and PPP1R42 (By similarity). Interacts with SYBU CC (PubMed:15459722). Interacts with JAKMIP1 (PubMed:17532644). Interacts CC with PLEKHM2 (PubMed:15905402). Interacts with ECPAS (PubMed:20682791). CC Interacts with ZFYVE27 (By similarity). Found in a complex with OGT, CC RHOT1, RHOT2 and TRAK1 (PubMed:24995978). Interacts with APP (via CC cytoplasmic domain) (PubMed:23011729). {ECO:0000250|UniProtKB:Q61768, CC ECO:0000269|PubMed:12368902, ECO:0000269|PubMed:15459722, CC ECO:0000269|PubMed:15905402, ECO:0000269|PubMed:17532644, CC ECO:0000269|PubMed:20682791, ECO:0000269|PubMed:23011729, CC ECO:0000269|PubMed:24995978, ECO:0000269|PubMed:8606779}. CC -!- INTERACTION: CC P33176; O95429: BAG4; NbExp=3; IntAct=EBI-355878, EBI-2949658; CC P33176; Q01850: CDR2; NbExp=3; IntAct=EBI-355878, EBI-1181367; CC P33176; Q14192: FHL2; NbExp=3; IntAct=EBI-355878, EBI-701903; CC P33176; Q9BQS8: FYCO1; NbExp=3; IntAct=EBI-355878, EBI-2869338; CC P33176; Q96CN9: GCC1; NbExp=3; IntAct=EBI-355878, EBI-746252; CC P33176; O75031: HSF2BP; NbExp=3; IntAct=EBI-355878, EBI-7116203; CC P33176; P33176: KIF5B; NbExp=5; IntAct=EBI-355878, EBI-355878; CC P33176; P52954: LBX1; NbExp=3; IntAct=EBI-355878, EBI-20141748; CC P33176; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-355878, EBI-16439278; CC P33176; P62487: POLR2G; NbExp=3; IntAct=EBI-355878, EBI-347928; CC P33176; P78424: POU6F2; NbExp=3; IntAct=EBI-355878, EBI-12029004; CC P33176; P31321: PRKAR1B; NbExp=3; IntAct=EBI-355878, EBI-2805516; CC P33176; P31323: PRKAR2B; NbExp=3; IntAct=EBI-355878, EBI-2930670; CC P33176; P63104: YWHAZ; NbExp=3; IntAct=EBI-355878, EBI-347088; CC P33176; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-355878, EBI-742740; CC P33176; P68619: OPG164; Xeno; NbExp=3; IntAct=EBI-355878, EBI-7133540; CC P33176; Q8CII8: Syne4; Xeno; NbExp=2; IntAct=EBI-355878, EBI-15752280; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q2PQA9}. Cytolytic granule membrane CC {ECO:0000269|PubMed:24088571}. Lysosome membrane CC {ECO:0000269|PubMed:22172677, ECO:0000269|PubMed:24088571}; Peripheral CC membrane protein {ECO:0000305|PubMed:22172677, CC ECO:0000305|PubMed:24088571}; Cytoplasmic side CC {ECO:0000305|PubMed:22172677, ECO:0000305|PubMed:24088571}. CC Note=Uniformly distributed between soma and neurites in hippocampal CC neurons. {ECO:0000250|UniProtKB:Q2PQA9}. CC -!- DOMAIN: Composed of three structural domains: a large globular N- CC terminal domain which is responsible for the motor activity of kinesin CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical CC coiled coil domain that mediates the heavy chain dimerization; and a CC small globular C-terminal domain which interacts with other proteins CC (such as the kinesin light chains), vesicles and membranous organelles. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00283}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X65873; CAA46703.1; -; mRNA. DR EMBL; AL161932; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC126279; AAI26280.1; -; mRNA. DR EMBL; BC126281; AAI26282.1; -; mRNA. DR CCDS; CCDS7171.1; -. DR PIR; A41919; A41919. DR RefSeq; NP_004512.1; NM_004521.2. DR PDB; 1BG2; X-ray; 1.80 A; A=1-325. DR PDB; 1MKJ; X-ray; 2.70 A; A=1-349. DR PDB; 2P4N; EM; 9.00 A; K=1-325. DR PDB; 3J8X; EM; 5.00 A; K=1-349. DR PDB; 3J8Y; EM; 5.00 A; K=1-349. DR PDB; 4HNA; X-ray; 3.19 A; K=1-349. DR PDB; 4LNU; X-ray; 2.19 A; K=1-325. DR PDB; 5LT0; X-ray; 2.00 A; A=1-325. DR PDB; 5LT1; X-ray; 1.95 A; A/B=1-325. DR PDB; 5LT2; X-ray; 2.60 A; A/B/C/D/E/K=1-325. DR PDB; 5LT3; X-ray; 2.59 A; A/B/C/D/E/K=1-325. DR PDB; 5LT4; X-ray; 2.88 A; A/B/C/D/E/K=1-325. DR PDB; 6OJQ; EM; 3.67 A; K=8-324. DR PDB; 7RIK; NMR; -; A=1-349. DR PDB; 8IXA; EM; 4.20 A; S/T/U/V/W/X/Y/Z/a=1-349. DR PDB; 8IXB; EM; 4.20 A; g/k/l/m=1-349. DR PDB; 8IXD; EM; 4.40 A; S/T/U/V/W/X/Y/Z/a=1-349. DR PDB; 8IXE; EM; 4.40 A; h/l/p/q=1-349. DR PDB; 8IXF; EM; 4.40 A; S/T/U/V/W/X/Y/Z/a=1-349. DR PDB; 8IXG; EM; 4.40 A; h/l/p/q=1-349. DR PDBsum; 1BG2; -. DR PDBsum; 1MKJ; -. DR PDBsum; 2P4N; -. DR PDBsum; 3J8X; -. DR PDBsum; 3J8Y; -. DR PDBsum; 4HNA; -. DR PDBsum; 4LNU; -. DR PDBsum; 5LT0; -. DR PDBsum; 5LT1; -. DR PDBsum; 5LT2; -. DR PDBsum; 5LT3; -. DR PDBsum; 5LT4; -. DR PDBsum; 6OJQ; -. DR PDBsum; 7RIK; -. DR PDBsum; 8IXA; -. DR PDBsum; 8IXB; -. DR PDBsum; 8IXD; -. DR PDBsum; 8IXE; -. DR PDBsum; 8IXF; -. DR PDBsum; 8IXG; -. DR AlphaFoldDB; P33176; -. DR EMDB; EMD-1340; -. DR EMDB; EMD-20092; -. DR EMDB; EMD-35790; -. DR EMDB; EMD-35791; -. DR EMDB; EMD-35792; -. DR EMDB; EMD-6188; -. DR EMDB; EMD-8546; -. DR EMDB; EMD-8547; -. DR SMR; P33176; -. DR BioGRID; 110000; 319. DR CORUM; P33176; -. DR DIP; DIP-29244N; -. DR IntAct; P33176; 110. DR MINT; P33176; -. DR STRING; 9606.ENSP00000307078; -. DR BindingDB; P33176; -. DR ChEMBL; CHEMBL5864; -. DR TCDB; 1.P.1.1.1; the polyoma virus sv40 er penetration channel (vpec) family. DR CarbonylDB; P33176; -. DR GlyConnect; 2938; 1 N-Linked glycan (1 site). DR GlyCosmos; P33176; 2 sites, 3 glycans. DR GlyGen; P33176; 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; P33176; -. DR MetOSite; P33176; -. DR PhosphoSitePlus; P33176; -. DR SwissPalm; P33176; -. DR BioMuta; KIF5B; -. DR DMDM; 417216; -. DR CPTAC; CPTAC-397; -. DR CPTAC; CPTAC-398; -. DR EPD; P33176; -. DR jPOST; P33176; -. DR MassIVE; P33176; -. DR PaxDb; 9606-ENSP00000307078; -. DR PeptideAtlas; P33176; -. DR ProteomicsDB; 54901; -. DR Pumba; P33176; -. DR Antibodypedia; 4077; 548 antibodies from 42 providers. DR DNASU; 3799; -. DR Ensembl; ENST00000302418.5; ENSP00000307078.4; ENSG00000170759.11. DR GeneID; 3799; -. DR KEGG; hsa:3799; -. DR MANE-Select; ENST00000302418.5; ENSP00000307078.4; NM_004521.3; NP_004512.1. DR AGR; HGNC:6324; -. DR CTD; 3799; -. DR DisGeNET; 3799; -. DR GeneCards; KIF5B; -. DR HGNC; HGNC:6324; KIF5B. DR HPA; ENSG00000170759; Low tissue specificity. DR MalaCards; KIF5B; -. DR MIM; 602809; gene. DR neXtProt; NX_P33176; -. DR OpenTargets; ENSG00000170759; -. DR PharmGKB; PA30108; -. DR VEuPathDB; HostDB:ENSG00000170759; -. DR eggNOG; KOG0240; Eukaryota. DR GeneTree; ENSGT00940000154801; -. DR HOGENOM; CLU_001485_11_1_1; -. DR InParanoid; P33176; -. DR OMA; HIYAMEV; -. DR OrthoDB; 5476186at2759; -. DR PhylomeDB; P33176; -. DR TreeFam; TF105225; -. DR BRENDA; 5.6.1.3; 2681. DR PathwayCommons; P33176; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-264876; Insulin processing. 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-9725371; Nuclear events stimulated by ALK signaling in cancer. DR Reactome; R-HSA-983189; Kinesins. DR SignaLink; P33176; -. DR SIGNOR; P33176; -. DR BioGRID-ORCS; 3799; 13 hits in 1155 CRISPR screens. DR ChiTaRS; KIF5B; human. DR EvolutionaryTrace; P33176; -. DR GeneWiki; KIF5B; -. DR GenomeRNAi; 3799; -. DR Pharos; P33176; Tbio. DR PRO; PR:P33176; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P33176; Protein. DR Bgee; ENSG00000170759; Expressed in cauda epididymis and 213 other cell types or tissues. DR ExpressionAtlas; P33176; baseline and differential. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl. DR GO; GO:0101004; C:cytolytic granule membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC. DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL. DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl. DR GO; GO:0031982; C:vesicle; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL. DR GO; GO:0003777; F:microtubule motor activity; IDA:ARUK-UCL. DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB. DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central. DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISS:ARUK-UCL. DR GO; GO:0007411; P:axon guidance; IBA:GO_Central. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB. DR GO; GO:0007028; P:cytoplasm organization; IEA:Ensembl. DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; TAS:ProtInc. DR GO; GO:0047497; P:mitochondrion transport along microtubule; IEA:Ensembl. DR GO; GO:0160040; P:mitocytosis; IEA:Ensembl. DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:UniProtKB. DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; IEA:Ensembl. DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:BHF-UCL. DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl. DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL. DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISS:ARUK-UCL. DR GO; GO:0035617; P:stress granule disassembly; ISS:BHF-UCL. DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central. DR GO; GO:0047496; P:vesicle transport along microtubule; IDA:ARUK-UCL. DR CDD; cd01369; KISc_KHC_KIF5; 1. DR Gene3D; 6.10.250.1590; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR InterPro; IPR027640; Kinesin-like_fam. DR InterPro; IPR019821; Kinesin_motor_CS. DR InterPro; IPR001752; Kinesin_motor_dom. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1. DR PANTHER; PTHR47968:SF57; KINESIN FAMILY MEMBER 5C; 1. DR Pfam; PF00225; Kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR Genevisible; P33176; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Coiled coil; Cytoplasm; KW Cytoskeleton; Isopeptide bond; Lysosome; Membrane; Methylation; KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..963 FT /note="Kinesin-1 heavy chain" FT /id="PRO_0000125351" FT DOMAIN 8..325 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT REGION 908..963 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 915..963 FT /note="Globular" FT COILED 329..914 FT BINDING 85..92 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 933 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 956 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 213 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT STRAND 8..15 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 20..25 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:1BG2" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 58..65 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 91..95 FT /evidence="ECO:0007829|PDB:1BG2" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 107..122 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 124..138 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 176..189 FT /evidence="ECO:0007829|PDB:1BG2" FT TURN 190..193 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 197..203 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 204..216 FT /evidence="ECO:0007829|PDB:1BG2" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 222..231 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 238..241 FT /evidence="ECO:0007829|PDB:4HNA" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 256..269 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 281..285 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 295..302 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:1BG2" FT HELIX 309..320 FT /evidence="ECO:0007829|PDB:1BG2" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:1MKJ" FT HELIX 337..348 FT /evidence="ECO:0007829|PDB:1MKJ" SQ SEQUENCE 963 AA; 109685 MW; A1FE5760C3250C8B CRC64; MADLAECNIK VMCRFRPLNE SEVNRGDKYI AKFQGEDTVV IASKPYAFDR VFQSSTSQEQ VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH DPEGMGIIPR IVQDIFNYIY SMDENLEFHI KVSYFEIYLD KIRDLLDVSK TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM DTIDEGKSNR HVAVTNMNEH SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK TGAEGAVLDE AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK NKILRNTIQW LENELNRWRN GETVPIDEQF DKEKANLEAF TVDKDITLTN DKPATAIGVI GNFTDAERRK CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK TQMLDQEELL ASTRRDQDNM QAELNRLQAE NDASKEEVKE VLQALEELAV NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL KEMTNHQKKR AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL QNVEQKKRQL EESVDALSEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA VEQQIQSHRE THQKQISSLR DEVEAKAKLI TDLQDQNQKM MLEQERLRVE HEKLKATDQE KSRKLHELTV MQDRREQARQ DLKGLEETVA KELQTLHNLR KLFVQDLATR VKKSAEIDSD DTGGSAAQKQ KISFLENNLE QLTKVHKQLV RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPSAI RGGGAFVQNS QPVAVRGGGG KQV //