ID KI16B_HUMAN Reviewed; 1317 AA. AC Q96L93; A6NKJ9; A7E2A8; B1AKG3; B1AKT7; C9JDN5; C9JI52; C9JSM8; C9JWJ7; AC Q2TBF5; Q5HYC0; Q5HYK1; Q5JWW3; Q5TFK5; Q86VL9; Q86YS5; Q8IYU0; Q9BQJ8; AC Q9BQM0; Q9BQM1; Q9BQM5; Q9H5U0; Q9HCI2; Q9NXN9; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=Kinesin-like protein KIF16B; DE AltName: Full=Sorting nexin-23; GN Name=KIF16B; Synonyms=C20orf23, KIAA1590, SNX23; 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 2), AND VARIANT THR-1027. RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 557-1317 (ISOFORM 4), AND VARIANT THR-1027. RC TISSUE=Adipose tissue, and Salivary gland; 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 MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Guo J.H.; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 916-1317 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 1056-1317 (ISOFORM 3), AND VARIANT THR-1027. RC TISSUE=Hippocampus, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-948 (ISOFORMS 1/2/3), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1085-1317 (ISOFORMS 1/4). RC TISSUE=Colon, Lung, and Tongue; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1114-1317 (ISOFORMS 1/4). RA Hong W.; RT "A new member (SNX23) of the sorting nexin family."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION, DOMAIN PX, PHOSPHATIDYLINOSITOL-BINDING, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-109. RX PubMed=15882625; DOI=10.1016/j.cell.2005.02.017; RA Hoepfner S., Severin F., Cabezas A., Habermann B., Runge A., Gillooly D., RA Stenmark H., Zerial M.; RT "Modulation of receptor recycling and degradation by the endosomal kinesin RT KIF16B."; RL Cell 121:437-450(2005). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=18445686; DOI=10.1242/jcs.019174; RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T., RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.; RT "EML3 is a nuclear microtubule-binding protein required for the correct RT alignment of chromosomes in metaphase."; RL J. Cell Sci. 121:1718-1726(2008). RN [11] RP INTERACTION WITH PTPN21. RX PubMed=20923765; DOI=10.1074/jbc.m110.174706; RA Carlucci A., Porpora M., Garbi C., Galgani M., Santoriello M., Mascolo M., RA di Lorenzo D., Altieri V., Quarto M., Terracciano L., Gottesman M.E., RA Insabato L., Feliciello A.; RT "PTPD1 supports receptor stability and mitogenic signaling in bladder RT cancer cells."; RL J. Biol. Chem. 285:39260-39270(2010). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398; THR-577; SER-582 AND RP SER-1052, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1179-1312, SUBCELLULAR LOCATION, RP PHOSPHATIDYLINOSITOL-BINDING, DOMAIN PX, AND MUTAGENESIS OF ARG-1220; RP ARG-1225; LYS-1229; LYS-1232; LEU-1248; PHE-1249 AND ARG-1260. RX PubMed=17641687; DOI=10.1038/sj.emboj.7601800; RA Blatner N.R., Wilson M.I., Lei C., Hong W., Murray D., Williams R.L., RA Cho W.; RT "The structural basis of novel endosome anchoring activity of KIF16B RT kinesin."; RL EMBO J. 26:3709-3719(2007). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] THR-772. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plus end-directed microtubule-dependent motor protein CC involved in endosome transport and receptor recycling and degradation. CC Regulates the plus end motility of early endosomes and the balance CC between recycling and degradation of receptors such as EGF receptor CC (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome CC transport of FGFR-containing vesicles during early development, a key CC process for developing basement membrane and epiblast and primitive CC endoderm lineages during early postimplantation development. CC {ECO:0000269|PubMed:15882625}. CC -!- SUBUNIT: Interacts with RAB14 (By similarity). Interacts with PTPN21. CC {ECO:0000250, ECO:0000269|PubMed:20923765}. CC -!- INTERACTION: CC Q96L93-6; P60520: GABARAPL2; NbExp=3; IntAct=EBI-10988217, EBI-720116; CC Q96L93-6; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-10988217, EBI-747500; CC Q96L93-6; Q14005-2: IL16; NbExp=3; IntAct=EBI-10988217, EBI-17178971; CC Q96L93-6; P17931: LGALS3; NbExp=3; IntAct=EBI-10988217, EBI-1170392; CC Q96L93-6; P54646: PRKAA2; NbExp=3; IntAct=EBI-10988217, EBI-1383852; CC Q96L93-6; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-10988217, EBI-8463848; CC Q96L93-6; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-10988217, EBI-11955057; CC Q96L93-6; Q969E8: TSR2; NbExp=3; IntAct=EBI-10988217, EBI-746981; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Early CC endosome membrane {ECO:0000269|PubMed:15882625}. Cytoplasm CC {ECO:0000269|PubMed:18445686}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:18445686}. Note=It is unclear whether association CC with endosomes is mediated via phosphatidylinositol 3-phosphate CC (PtdIns(3)P)-binding or via its interaction with RAB14. CC {ECO:0000269|PubMed:15882625}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q96L93-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96L93-2; Sequence=VSP_010851; CC Name=3; CC IsoId=Q96L93-4; Sequence=VSP_010852; CC Name=4; CC IsoId=Q96L93-5; Sequence=VSP_015858; CC Name=5; CC IsoId=Q96L93-6; Sequence=VSP_041318; CC -!- TISSUE SPECIFICITY: Primarily expressed in brain. Also present in CC kidney, liver, intestine, placenta, leukocytes, heart and skeletal CC muscle (at protein level). {ECO:0000269|PubMed:15882625}. CC -!- DOMAIN: The PX domain mediates binding to phosphatidylinositol 3- CC phosphate (PtdIns(3)P), phosphatidylinositol 3,4-bisphosphate CC (PtdIns(3,4)P2), phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) CC and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). Does CC not bind phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). CC {ECO:0000269|PubMed:15882625, ECO:0000269|PubMed:17641687}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA90971.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA90971.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAB13416.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15530.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AB046810; BAB13416.2; ALT_INIT; mRNA. DR EMBL; BX647572; CAI46105.1; -; mRNA. DR EMBL; BX648426; CAI46266.1; -; mRNA. DR EMBL; AY166853; AAO17292.1; -; mRNA. DR EMBL; AL049794; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL117376; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL118509; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10290.1; -; Genomic_DNA. DR EMBL; BC034984; AAH34984.2; -; mRNA. DR EMBL; BC110317; AAI10318.1; -; mRNA. DR EMBL; BC150261; AAI50262.1; -; mRNA. DR EMBL; AY044654; AAK98768.1; -; mRNA. DR EMBL; AK000142; BAA90971.1; ALT_SEQ; mRNA. DR EMBL; AK026698; BAB15530.1; ALT_INIT; mRNA. DR EMBL; AK095322; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS13122.1; -. [Q96L93-1] DR CCDS; CCDS56178.1; -. [Q96L93-2] DR RefSeq; NP_001186794.1; NM_001199865.1. DR RefSeq; NP_001186795.1; NM_001199866.1. [Q96L93-2] DR RefSeq; NP_078980.3; NM_024704.4. [Q96L93-1] DR RefSeq; XP_016883415.1; XM_017027926.1. [Q96L93-6] DR PDB; 2V14; X-ray; 2.20 A; A=1179-1312. DR PDB; 6EE0; X-ray; 2.52 A; A/B/C=1182-1312. DR PDBsum; 2V14; -. DR PDBsum; 6EE0; -. DR AlphaFoldDB; Q96L93; -. DR SMR; Q96L93; -. DR BioGRID; 120754; 80. DR IntAct; Q96L93; 25. DR MINT; Q96L93; -. DR STRING; 9606.ENSP00000384164; -. DR TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt). DR iPTMnet; Q96L93; -. DR MetOSite; Q96L93; -. DR PhosphoSitePlus; Q96L93; -. DR BioMuta; KIF16B; -. DR DMDM; 50403793; -. DR EPD; Q96L93; -. DR jPOST; Q96L93; -. DR MassIVE; Q96L93; -. DR MaxQB; Q96L93; -. DR PaxDb; 9606-ENSP00000384164; -. DR PeptideAtlas; Q96L93; -. DR ProteomicsDB; 77165; -. [Q96L93-1] DR ProteomicsDB; 77166; -. [Q96L93-2] DR ProteomicsDB; 77167; -. [Q96L93-4] DR ProteomicsDB; 77168; -. [Q96L93-5] DR ProteomicsDB; 77169; -. [Q96L93-6] DR Pumba; Q96L93; -. DR Antibodypedia; 24366; 129 antibodies from 16 providers. DR DNASU; 55614; -. DR Ensembl; ENST00000354981.7; ENSP00000347076.2; ENSG00000089177.20. [Q96L93-1] DR Ensembl; ENST00000408042.5; ENSP00000384164.1; ENSG00000089177.20. [Q96L93-2] DR GeneID; 55614; -. DR KEGG; hsa:55614; -. DR MANE-Select; ENST00000354981.7; ENSP00000347076.2; NM_024704.5; NP_078980.3. DR UCSC; uc002wpg.3; human. [Q96L93-1] DR AGR; HGNC:15869; -. DR CTD; 55614; -. DR DisGeNET; 55614; -. DR GeneCards; KIF16B; -. DR HGNC; HGNC:15869; KIF16B. DR HPA; ENSG00000089177; Low tissue specificity. DR MIM; 618171; gene. DR neXtProt; NX_Q96L93; -. DR OpenTargets; ENSG00000089177; -. DR PharmGKB; PA162393227; -. DR VEuPathDB; HostDB:ENSG00000089177; -. DR eggNOG; KOG0245; Eukaryota. DR eggNOG; KOG2101; Eukaryota. DR GeneTree; ENSGT00940000162838; -. DR HOGENOM; CLU_001485_35_0_1; -. DR InParanoid; Q96L93; -. DR OMA; HWHGAQQ; -. DR OrthoDB; 126886at2759; -. DR PhylomeDB; Q96L93; -. DR TreeFam; TF105221; -. DR BRENDA; 5.6.1.3; 2681. DR PathwayCommons; Q96L93; -. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-983189; Kinesins. DR SignaLink; Q96L93; -. DR SIGNOR; Q96L93; -. DR BioGRID-ORCS; 55614; 11 hits in 1154 CRISPR screens. DR ChiTaRS; KIF16B; human. DR EvolutionaryTrace; Q96L93; -. DR GeneWiki; KIF16B; -. DR GenomeRNAi; 55614; -. DR Pharos; Q96L93; Tbio. DR PRO; PR:Q96L93; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q96L93; Protein. DR Bgee; ENSG00000089177; Expressed in sural nerve and 181 other cell types or tissues. DR ExpressionAtlas; Q96L93; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005819; C:spindle; 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:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB. DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB. DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB. DR GO; GO:0007492; P:endoderm development; ISS:UniProtKB. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0001704; P:formation of primary germ layer; ISS:UniProtKB. DR GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central. DR GO; GO:0032801; P:receptor catabolic process; IMP:UniProtKB. DR GO; GO:0001919; P:regulation of receptor recycling; IMP:UniProtKB. DR CDD; cd22732; FHA_KIF16B; 1. DR CDD; cd01365; KISc_KIF1A_KIF1B; 1. DR CDD; cd06874; PX_KIF16B_SNX23; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR InterPro; IPR000253; FHA_dom. 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 InterPro; IPR001683; PX_dom. DR InterPro; IPR036871; PX_dom_sf. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1. DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF00225; Kinesin; 1. DR Pfam; PF00787; PX; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR SMART; SM00312; PX; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF64268; PX domain; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR PROSITE; PS50195; PX; 1. DR Genevisible; Q96L93; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; KW Cytoskeleton; Endosome; Lipid-binding; Membrane; Microtubule; KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Transport. FT CHAIN 1..1317 FT /note="Kinesin-like protein KIF16B" FT /id="PRO_0000125466" FT DOMAIN 3..358 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT DOMAIN 478..529 FT /note="FHA" FT DOMAIN 1182..1296 FT /note="PX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147" FT REGION 1036..1057 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 370..425 FT /evidence="ECO:0000255" FT COILED 595..882 FT /evidence="ECO:0000255" FT COILED 936..1087 FT /evidence="ECO:0000255" FT COMPBIAS 1036..1053 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 102..109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 577 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 582 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1052 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 685..840 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_015858" FT VAR_SEQ 1167..1317 FT /note="RMVSRSLGANPDDLKDPIKISIPRYVLCGQGKDAHFEFEVKITVLDETWTVF FT RRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSVMLQ FT SATSPLHINKVGLTLSKHTICEFSPFFKKGVFDYSSHGTG -> LCRDLLCVLMPEPDA FT AACANHPLLQQDLVQLSLDWKTEIPDLVLPNGVQVSSKFQTTLVDMIYFLHGNMEVNVP FT SLAEVQLLLYTTVKVMGDSGHDQCQSLVLLNTHIALVKEDCVFYPRIRSRNIPPPGAQF FT DVIKCHALSEFRCVVVPEKKNVSTVELVFLQKLKPSVGSRNSPPEHLQEAPNVQLFTTP FT LYLQGSQNVAPEVWKLTFNSQDEALWLISHLTRL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10997877, FT ECO:0000303|PubMed:15489334" FT /id="VSP_010851" FT VAR_SEQ 1167..1207 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041318" FT VAR_SEQ 1208..1237 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010852" FT VARIANT 772 FT /note="K -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036218" FT VARIANT 810 FT /note="G -> R (in dbSNP:rs2236145)" FT /id="VAR_049700" FT VARIANT 824 FT /note="R -> S (in dbSNP:rs2236144)" FT /id="VAR_019396" FT VARIANT 999 FT /note="K -> N (in dbSNP:rs8116503)" FT /id="VAR_065248" FT VARIANT 1027 FT /note="M -> T (in dbSNP:rs6034464)" FT /evidence="ECO:0000269|PubMed:10997877, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005" FT /id="VAR_019397" FT VARIANT 1119 FT /note="N -> S (in dbSNP:rs8123195)" FT /id="VAR_019398" FT MUTAGEN 109 FT /note="S->A: Impairs plus end-directed FT microtubule-dependent motor activity, leading to impair FT EGFR recycling." FT /evidence="ECO:0000269|PubMed:15882625" FT MUTAGEN 1220 FT /note="R->A: Abolishes PtdIns(3)P-binding." FT /evidence="ECO:0000269|PubMed:17641687" FT MUTAGEN 1225 FT /note="R->A: Induces a 3-fold decrease in FT PtdIns(3)P-binding; when associated with A-1229 and FT A-1232." FT /evidence="ECO:0000269|PubMed:17641687" FT MUTAGEN 1229 FT /note="K->A: Induces a 3-fold decrease in FT PtdIns(3)P-binding; when associated with A-1225 and FT A-1232." FT /evidence="ECO:0000269|PubMed:17641687" FT MUTAGEN 1232 FT /note="K->A: Induces a 3-fold decrease in FT PtdIns(3)P-binding; when associated with A-1225 and FT A-1229." FT /evidence="ECO:0000269|PubMed:17641687" FT MUTAGEN 1248 FT /note="L->A: Induces a 7-fold decrease in FT PtdIns(3)P-binding and abolishes endosome localization. FT Induces a 25-fold decrease in PtdIns(3)P-binding; when FT associated with A-1249." FT /evidence="ECO:0000269|PubMed:17641687" FT MUTAGEN 1248 FT /note="L->V: Induces a 6-fold decrease in FT PtdIns(3)P-binding." FT /evidence="ECO:0000269|PubMed:17641687" FT MUTAGEN 1249 FT /note="F->A: Induces a 5-fold decrease in FT PtdIns(3)P-binding and abolishes endosome localization. FT Induces a 25-fold decrease in PtdIns(3)P-binding; when FT associated with A-1248." FT /evidence="ECO:0000269|PubMed:17641687" FT MUTAGEN 1260 FT /note="R->A: Induces a 30-fold decrease in FT PtdIns(3)P-binding." FT /evidence="ECO:0000269|PubMed:17641687" FT CONFLICT 18 FT /note="K -> E (in Ref. 7; AK095322)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="N -> D (in Ref. 2; CAI46105)" FT /evidence="ECO:0000305" FT CONFLICT 583 FT /note="R -> H (in Ref. 7; BAA90971)" FT /evidence="ECO:0000305" FT CONFLICT 649 FT /note="L -> H (in Ref. 2; CAI46266)" FT /evidence="ECO:0000305" FT CONFLICT 1056..1057 FT /note="EQ -> SE (in Ref. 6; AAH34984)" FT /evidence="ECO:0000305" FT CONFLICT 1100 FT /note="S -> N (in Ref. 2; CAI46105)" FT /evidence="ECO:0000305" FT CONFLICT 1108 FT /note="S -> L (in Ref. 6; AAH34984)" FT /evidence="ECO:0000305" FT CONFLICT 1244 FT /note="P -> A (in Ref. 3; AAO17292 and 7; BAB15530)" FT /evidence="ECO:0000305" FT STRAND 1184..1196 FT /evidence="ECO:0007829|PDB:2V14" FT STRAND 1201..1210 FT /evidence="ECO:0007829|PDB:2V14" FT STRAND 1213..1219 FT /evidence="ECO:0007829|PDB:2V14" FT HELIX 1221..1234 FT /evidence="ECO:0007829|PDB:2V14" FT HELIX 1236..1240 FT /evidence="ECO:0007829|PDB:2V14" FT HELIX 1254..1277 FT /evidence="ECO:0007829|PDB:2V14" FT HELIX 1285..1287 FT /evidence="ECO:0007829|PDB:6EE0" FT HELIX 1294..1300 FT /evidence="ECO:0007829|PDB:2V14" FT HELIX 1302..1304 FT /evidence="ECO:0007829|PDB:2V14" SQ SEQUENCE 1317 AA; 152011 MW; 278E9CB88D9C04DF CRC64; MASVKVAVRV RPMNRREKDL EAKFIIQMEK SKTTITNLKI PEGGTGDSGR ERTKTFTYDF SFYSADTKSP DYVSQEMVFK TLGTDVVKSA FEGYNACVFA YGQTGSGKSY TMMGNSGDSG LIPRICEGLF SRINETTRWD EASFRTEVSY LEIYNERVRD LLRRKSSKTF NLRVREHPKE GPYVEDLSKH LVQNYGDVEE LMDAGNINRT TAATGMNDVS SRSHAIFTIK FTQAKFDSEM PCETVSKIHL VDLAGSERAD ATGATGVRLK EGGNINKSLV TLGNVISALA DLSQDAANTL AKKKQVFVPY RDSVLTWLLK DSLGGNSKTI MIATISPADV NYGETLSTLR YANRAKNIIN KPTINEDANV KLIRELRAEI ARLKTLLAQG NQIALLDSPT ALSMEEKLQQ NEARVQELTK EWTNKWNETQ NILKEQTLAL RKEGIGVVLD SELPHLIGID DDLLSTGIIL YHLKEGQTYV GRDDASTEQD IVLHGLDLES EHCIFENIGG TVTLIPLSGS QCSVNGVQIV EATHLNQGAV ILLGRTNMFR FNHPKEAAKL REKRKSGLLS SFSLSMTDLS KSRENLSAVM LYNPGLEFER QQREELEKLE SKRKLIEEME EKQKSDKAEL ERMQQEVETQ RKETEIVQLQ IRKQEESLKR RSFHIENKLK DLLAEKEKFE EERLREQQEI ELQKKRQEEE TFLRVQEELQ RLKELNNNEK AEKFQIFQEL DQLQKEKDEQ YAKLELEKKR LEEQEKEQVM LVAHLEEQLR EKQEMIQLLR RGEVQWVEEE KRDLEGIRES LLRVKEARAG GDEDGEELEK AQLRFFEFKR RQLVKLVNLE KDLVQQKDIL KKEVQEEQEI LECLKCEHDK ESRLLEKHDE SVTDVTEVPQ DFEKIKPVEY RLQYKERQLQ YLLQNHLPTL LEEKQRAFEI LDRGPLSLDN TLYQVEKEME EKEEQLAQYQ ANANQLQKLQ ATFEFTANIA RQEEKVRKKE KEILESREKQ QREALERALA RLERRHSALQ RHSTLGMEIE EQRQKLASLN SGSREQSGLQ ASLEAEQEAL EKDQERLEYE IQQLKQKIYE VDGVQKDHHG TLEGKVASSS LPVSAEKSHL VPLMDARINA YIEEEVQRRL QDLHRVISEG CSTSADTMKD NEKLHNGTIQ RKLKYERMVS RSLGANPDDL KDPIKISIPR YVLCGQGKDA HFEFEVKITV LDETWTVFRR YSRFREMHKT LKLKYAELAA LEFPPKKLFG NKDERVIAER RSHLEKYLRD FFSVMLQSAT SPLHINKVGL TLSKHTICEF SPFFKKGVFD YSSHGTG //