KI16B_HUMAN
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 03-AUG-2022, entry version 190.
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};
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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; 75.
DR IntAct; Q96L93; 24.
DR MINT; Q96L93; -.
DR STRING; 9606.ENSP00000384164; -.
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; Q96L93; -.
DR PeptideAtlas; Q96L93; -.
DR PRIDE; 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 Antibodypedia; 24366; 108 antibodies from 16 providers.
DR DNASU; 55614; -.
DR Ensembl; ENST00000354981.7; ENSP00000347076.2; ENSG00000089177.19. [Q96L93-1]
DR Ensembl; ENST00000408042.5; ENSP00000384164.1; ENSG00000089177.19. [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 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; 76316at2759; -.
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 BioGRID-ORCS; 55614; 10 hits in 1075 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 179 other tissues.
DR ExpressionAtlas; Q96L93; baseline and differential.
DR Genevisible; Q96L93; HS.
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:0003777; F:microtubule motor activity; 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 Gene3D; 3.30.1520.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 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; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 1.
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 microtubule-
FT dependent motor activity, leading to impair EGFR
FT 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 PtdIns(3)P-
FT binding; when associated with A-1229 and A-1232."
FT /evidence="ECO:0000269|PubMed:17641687"
FT MUTAGEN 1229
FT /note="K->A: Induces a 3-fold decrease in PtdIns(3)P-
FT binding; when associated with A-1225 and A-1232."
FT /evidence="ECO:0000269|PubMed:17641687"
FT MUTAGEN 1232
FT /note="K->A: Induces a 3-fold decrease in PtdIns(3)P-
FT binding; when associated with A-1225 and A-1229."
FT /evidence="ECO:0000269|PubMed:17641687"
FT MUTAGEN 1248
FT /note="L->A: Induces a 7-fold decrease in PtdIns(3)P-
FT binding and abolishes endosome localization. Induces a 25-
FT fold decrease in PtdIns(3)P-binding; when associated with
FT A-1249."
FT /evidence="ECO:0000269|PubMed:17641687"
FT MUTAGEN 1248
FT /note="L->V: Induces a 6-fold decrease in PtdIns(3)P-
FT binding."
FT /evidence="ECO:0000269|PubMed:17641687"
FT MUTAGEN 1249
FT /note="F->A: Induces a 5-fold decrease in PtdIns(3)P-
FT binding and abolishes endosome localization. Induces a 25-
FT fold decrease in PtdIns(3)P-binding; when associated with
FT A-1248."
FT /evidence="ECO:0000269|PubMed:17641687"
FT MUTAGEN 1260
FT /note="R->A: Induces a 30-fold decrease in PtdIns(3)P-
FT 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
