KIF3B_HUMAN
ID KIF3B_HUMAN Reviewed; 747 AA.
AC O15066; B2RMP4; B4DSR5; E1P5M5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Kinesin-like protein KIF3B;
DE AltName: Full=HH0048;
DE AltName: Full=Microtubule plus end-directed kinesin motor 3B;
DE Contains:
DE RecName: Full=Kinesin-like protein KIF3B, N-terminally processed;
GN Name=KIF3B; Synonyms=KIAA0359;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 IDENTIFICATION IN A COMPLEX WITH SMC3 AND KIFAP3.
RX PubMed=9506951; DOI=10.1074/jbc.273.12.6591;
RA Shimizu K., Shirataki H., Honda T., Minami S., Takai Y.;
RT "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein,
RT with a human chromosome-associated polypeptide.";
RL J. Biol. Chem. 273:6591-6594(1998).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [9]
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 [10]
RP INTERACTION WITH FLCN.
RX PubMed=27072130; DOI=10.1074/jbc.m116.719997;
RA Zhong M., Zhao X., Li J., Yuan W., Yan G., Tong M., Guo S., Zhu Y.,
RA Jiang Y., Liu Y., Jiang Y.;
RT "Tumor suppressor folliculin regulates mTORC1 through primary cilia.";
RL J. Biol. Chem. 291:11689-11697(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-359 IN COMPLEX WITH ADP.
RG Structural genomics consortium (SGC);
RT "Motor domain of human kinesin family member 3B in complex with ADP.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [12]
RP INVOLVEMENT IN RP89, VARIANTS RP89 GLN-250 AND PRO-523, CHARACTERIZATION OF
RP VARIANTS RP89 GLN-250 AND PRO-523, FUNCTION, AND MUTAGENESIS OF VAL-435.
RX PubMed=32386558; DOI=10.1016/j.ajhg.2020.04.005;
RG 99 Lives Consortium;
RA Cogne B., Latypova X., Senaratne L.D.S., Martin L., Koboldt D.C.,
RA Kellaris G., Fievet L., Le Meur G., Caldari D., Debray D., Nizon M.,
RA Frengen E., Bowne S.J., Cadena E.L., Daiger S.P., Bujakowska K.M.,
RA Pierce E.A., Gorin M., Katsanis N., Bezieau S., Petersen-Jones S.M.,
RA Occelli L.M., Lyons L.A., Legeai-Mallet L., Sullivan L.S., Davis E.E.,
RA Isidor B.;
RT "Mutations in the Kinesin-2 Motor KIF3B Cause an Autosomal-Dominant
RT Ciliopathy.";
RL Am. J. Hum. Genet. 106:893-904(2020).
CC -!- FUNCTION: Microtubule-based molecular motor that transport
CC intracellular cargos, such as vesicles, organelles and protein
CC complexes. Uses ATP hydrolysis to generate force to bind and move along
CC the microtubule (By similarity). Plays a role in cilia formation
CC (PubMed:32386558). Involved in photoreceptor integrity and opsin
CC trafficking in rod photoreceptors (PubMed:32386558). Transports
CC vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A
CC into neuronal dendrites (By similarity). {ECO:0000250|UniProtKB:Q61771,
CC ECO:0000269|PubMed:32386558}.
CC -!- SUBUNIT: Heterodimer of KIF3A and KIF3B (By similarity). KIF3A/KIF3B
CC heterodimer interacts with KIFAP3 forming a heterotrimeric
CC (KIF3A/KIF3B/KIFAP3) complex (By similarity). Interacts directly with
CC IFT20 (By similarity). Interacts with the SMC3 subunit of the cohesin
CC complex (PubMed:9506951). Interacts with FLCN (PubMed:27072130).
CC {ECO:0000250|UniProtKB:Q61771, ECO:0000269|PubMed:27072130,
CC ECO:0000269|PubMed:9506951}.
CC -!- INTERACTION:
CC O15066; O15013: ARHGEF10; NbExp=3; IntAct=EBI-3931791, EBI-2515636;
CC O15066; P51795: CLCN5; NbExp=6; IntAct=EBI-3931791, EBI-13619183;
CC O15066; Q92845: KIFAP3; NbExp=7; IntAct=EBI-3931791, EBI-954040;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q61771}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:Q61771}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15066-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15066-2; Sequence=VSP_056489, VSP_056490;
CC -!- DISEASE: Retinitis pigmentosa 89 (RP89) [MIM:618955]: A form of
CC retinitis pigmentosa, a retinal dystrophy belonging to the group of
CC pigmentary retinopathies. Retinitis pigmentosa is characterized by
CC retinal pigment deposits visible on fundus examination and primary loss
CC of rod photoreceptor cells followed by secondary loss of cone
CC photoreceptors. Patients typically have night vision blindness and loss
CC of midperipheral visual field. RP89 is an autosomal dominant form
CC associated with features of ciliopathy, including postaxial
CC polydactyly, and renal and hepatic disease.
CC {ECO:0000269|PubMed:32386558}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin II subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20815.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002357; BAA20815.2; ALT_INIT; mRNA.
DR EMBL; AK299877; BAG61727.1; -; mRNA.
DR EMBL; AL121897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76381.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76382.1; -; Genomic_DNA.
DR EMBL; BC136310; AAI36311.1; -; mRNA.
DR EMBL; BC136311; AAI36312.1; -; mRNA.
DR CCDS; CCDS13200.1; -. [O15066-1]
DR RefSeq; NP_004789.1; NM_004798.3. [O15066-1]
DR PDB; 3B6U; X-ray; 1.80 A; A/B=6-359.
DR PDBsum; 3B6U; -.
DR AlphaFoldDB; O15066; -.
DR SMR; O15066; -.
DR BioGRID; 114772; 39.
DR ComplexPortal; CPX-3138; KIF3 complex variant AB.
DR ComplexPortal; CPX-3201; KIF3 complex variant AB-KAP3.
DR CORUM; O15066; -.
DR IntAct; O15066; 18.
DR MINT; O15066; -.
DR STRING; 9606.ENSP00000364864; -.
DR BindingDB; O15066; -.
DR ChEMBL; CHEMBL6109; -.
DR iPTMnet; O15066; -.
DR MetOSite; O15066; -.
DR PhosphoSitePlus; O15066; -.
DR SwissPalm; O15066; -.
DR BioMuta; KIF3B; -.
DR EPD; O15066; -.
DR jPOST; O15066; -.
DR MassIVE; O15066; -.
DR MaxQB; O15066; -.
DR PaxDb; O15066; -.
DR PeptideAtlas; O15066; -.
DR PRIDE; O15066; -.
DR ProteomicsDB; 48416; -. [O15066-1]
DR ProteomicsDB; 5044; -.
DR Antibodypedia; 1560; 115 antibodies from 22 providers.
DR DNASU; 9371; -.
DR Ensembl; ENST00000375712.4; ENSP00000364864.3; ENSG00000101350.8. [O15066-1]
DR GeneID; 9371; -.
DR KEGG; hsa:9371; -.
DR MANE-Select; ENST00000375712.4; ENSP00000364864.3; NM_004798.4; NP_004789.1.
DR UCSC; uc002wxq.4; human. [O15066-1]
DR CTD; 9371; -.
DR DisGeNET; 9371; -.
DR GeneCards; KIF3B; -.
DR HGNC; HGNC:6320; KIF3B.
DR HPA; ENSG00000101350; Low tissue specificity.
DR MalaCards; KIF3B; -.
DR MIM; 603754; gene.
DR MIM; 618955; phenotype.
DR neXtProt; NX_O15066; -.
DR OpenTargets; ENSG00000101350; -.
DR PharmGKB; PA30103; -.
DR VEuPathDB; HostDB:ENSG00000101350; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000153739; -.
DR HOGENOM; CLU_001485_22_4_1; -.
DR InParanoid; O15066; -.
DR OMA; LESKMLC; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; O15066; -.
DR TreeFam; TF105223; -.
DR PathwayCommons; O15066; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; O15066; -.
DR BioGRID-ORCS; 9371; 13 hits in 1089 CRISPR screens.
DR ChiTaRS; KIF3B; human.
DR EvolutionaryTrace; O15066; -.
DR GeneWiki; KIF3B; -.
DR GenomeRNAi; 9371; -.
DR Pharos; O15066; Tbio.
DR PRO; PR:O15066; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O15066; protein.
DR Bgee; ENSG00000101350; Expressed in middle temporal gyrus and 205 other tissues.
DR Genevisible; O15066; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005813; C:centrosome; NAS:BHF-UCL.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016939; C:kinesin II complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005873; C:plus-end kinesin complex; TAS:ProtInc.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0120170; F:intraciliary transport particle B binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; TAS:ProtInc.
DR GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL.
DR GO; GO:0008089; P:anterograde axonal transport; TAS:ProtInc.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; TAS:ProtInc.
DR GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007100; P:mitotic centrosome separation; TAS:BHF-UCL.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:BHF-UCL.
DR GO; GO:0007052; P:mitotic spindle organization; TAS:BHF-UCL.
DR GO; GO:0036372; P:opsin transport; IMP:UniProtKB.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; TAS:BHF-UCL.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl.
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; Alternative splicing; ATP-binding;
KW Cell projection; Ciliopathy; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Retinitis pigmentosa; Synapse.
FT CHAIN 1..747
FT /note="Kinesin-like protein KIF3B"
FT /id="PRO_0000125395"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..747
FT /note="Kinesin-like protein KIF3B, N-terminally processed"
FT /id="PRO_0000424495"
FT DOMAIN 9..340
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 374..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..747
FT /note="Globular"
FT REGION 699..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..579
FT /evidence="ECO:0000255"
FT COMPBIAS 392..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.11, ECO:0007744|PDB:3B6U"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylserine; in Kinesin-like protein KIF3B, N-
FT terminally processed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056489"
FT VAR_SEQ 375..436
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056490"
FT VARIANT 250
FT /note="E -> Q (in RP89; increase in primary cilia length;
FT does not affect protein stability; significant increase of
FT rhodopsin in the rod inner segment when expressed in
FT zebrafish; coinjection with wild-type rescued the rhodopsin
FT mislocalization defects)"
FT /evidence="ECO:0000269|PubMed:32386558"
FT /id="VAR_084674"
FT VARIANT 523
FT /note="L -> P (in RP89; increase in primary cilia length;
FT does not affect protein stability; significant increase of
FT rhodopsin in the rod inner segment when expressed in
FT zebrafish; coinjection with wild-type rescued the rhodopsin
FT mislocalization defects)"
FT /evidence="ECO:0000269|PubMed:32386558"
FT /id="VAR_084675"
FT MUTAGEN 435
FT /note="V->I: Does not affect protein stability nor cilia
FT length."
FT /evidence="ECO:0000269|PubMed:32386558"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3B6U"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3B6U"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 137..148
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3B6U"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:3B6U"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 215..228
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:3B6U"
FT TURN 301..306
FT /evidence="ECO:0007829|PDB:3B6U"
FT STRAND 307..317
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:3B6U"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:3B6U"
SQ SEQUENCE 747 AA; 85125 MW; 97FA4573AFA87023 CRC64;
MSKLKSSESV RVVVRCRPMN GKEKAASYDK VVDVDVKLGQ VSVKNPKGTA HEMPKTFTFD
AVYDWNAKQF ELYDETFRPL VDSVLQGFNG TIFAYGQTGT GKTYTMEGIR GDPEKRGVIP
NSFDHIFTHI SRSQNQQYLV RASYLEIYQE EIRDLLSKDQ TKRLELKERP DTGVYVKDLS
SFVTKSVKEI EHVMNVGNQN RSVGATNMNE HSSRSHAIFV ITIECSEVGL DGENHIRVGK
LNLVDLAGSE RQAKTGAQGE RLKEATKINL SLSALGNVIS ALVDGKSTHI PYRDSKLTRL
LQDSLGGNAK TVMVANVGPA SYNVEETLTT LRYANRAKNI KNKPRVNEDP KDALLREFQE
EIARLKAQLE KRSIGRRKRR EKRREGGGSG GGGEEEEEEG EEGEEEGDDK DDYWREQQEK
LEIEKRAIVE DHSLVAEEKM RLLKEKEKKM EDLRREKDAA EMLGAKIKAM ESKLLVGGKN
IVDHTNEQQK ILEQKRQEIA EQKRREREIQ QQMESRDEET LELKETYSSL QQEVDIKTKK
LKKLFSKLQA VKAEIHDLQE EHIKERQELE QTQNELTREL KLKHLIIENF IPLEEKSKIM
NRAFFDEEED HWKLHPITRL ENQQMMKRPV SAVGYKRPLS QHARMSMMIR PEARYRAENI
VLLELDMPSR TTRDYEGPAI APKVQAALDA ALQDEDEIQV DASSFESTAN KKSKARPKSG
RKSGSSSSSS GTPASQLYPQ SRGLVPK
