KINH_HUMAN
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 03-AUG-2022, entry version 213.
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=2; IntAct=EBI-355878, EBI-347088;
CC P33176; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-355878, EBI-742740;
CC P33176; Q8CII8: Syne4; Xeno; NbExp=2; IntAct=EBI-355878, EBI-15752280;
CC P33176; P68619: VACWR159; Xeno; NbExp=3; IntAct=EBI-355878, EBI-7133540;
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}.
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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 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 AlphaFoldDB; P33176; -.
DR SMR; P33176; -.
DR BioGRID; 110000; 174.
DR CORUM; P33176; -.
DR DIP; DIP-29244N; -.
DR IntAct; P33176; 101.
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 GlyGen; P33176; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
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; P33176; -.
DR PeptideAtlas; P33176; -.
DR PRIDE; P33176; -.
DR ProteomicsDB; 54901; -.
DR Antibodypedia; 4077; 476 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 CTD; 3799; -.
DR DisGeNET; 3799; -.
DR GeneCards; KIF5B; -.
DR HGNC; HGNC:6324; KIF5B.
DR HPA; ENSG00000170759; Low tissue specificity.
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; RMAKMMA; -.
DR OrthoDB; 1334528at2759; -.
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; 12 hits in 1077 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 211 other tissues.
DR ExpressionAtlas; P33176; baseline and differential.
DR Genevisible; P33176; HS.
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: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:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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 interferon-gamma; IEA:Ensembl.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0007028; P:cytoplasm organization; IEA:Ensembl.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 Gene3D; 3.40.850.10; -; 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; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
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
