KI20B_HUMAN
ID KI20B_HUMAN Reviewed; 1820 AA.
AC Q96Q89; A8MXM7; O43277; Q09471; Q2KQ73; Q32NE1; Q561V3; Q58EX8; Q5T9M8;
AC Q5T9M9; Q5T9N0; Q5T9N1; Q7KZ68; Q7Z5E0; Q7Z5E1; Q7Z6M9; Q86X82; Q9H3R8;
AC Q9H6Q9; Q9H755; Q9NTC1; Q9UFR5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Kinesin-like protein KIF20B {ECO:0000305};
DE AltName: Full=Cancer/testis antigen 90;
DE Short=CT90;
DE AltName: Full=Kinesin family member 20B {ECO:0000312|HGNC:HGNC:7212};
DE AltName: Full=Kinesin-related motor interacting with PIN1 {ECO:0000303|PubMed:11470801};
DE AltName: Full=M-phase phosphoprotein 1 {ECO:0000303|PubMed:12740395};
DE Short=MPP1 {ECO:0000303|PubMed:12740395};
GN Name=KIF20B {ECO:0000312|HGNC:HGNC:7212};
GN Synonyms=KRMP1 {ECO:0000303|PubMed:11470801},
GN MPHOSPH1 {ECO:0000303|PubMed:12740395};
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] (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, INTERACTION WITH PIN1, PHOSPHORYLATION AT THR-1644,
RP AND VARIANTS ILE-756; LEU-789 AND ARG-1177.
RX PubMed=11470801; DOI=10.1074/jbc.m106207200;
RA Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M.;
RT "Identification of a novel kinesin-related protein, KRMP1, as a target for
RT mitotic peptidyl-prolyl isomerase Pin1.";
RL J. Biol. Chem. 276:37520-37528(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ASP-490
RP AND ARG-1177.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 779-1480 (ISOFORMS 1/2/3/4), AND VARIANT ARG-1177.
RC TISSUE=Colon;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-957 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 705-1820 (ISOFORM 1), FUNCTION, INTERACTION WITH MICROTUBULES,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS
RP ILE-756; LEU-789 AND ARG-1177.
RX PubMed=12740395; DOI=10.1074/jbc.m304522200;
RA Abaza A., Soleilhac J.-M., Westendorf J., Piel M., Crevel I., Roux A.,
RA Pirollet F.;
RT "M phase phosphoprotein 1 is a human plus-end-directed kinesin-related
RT protein required for cytokinesis.";
RL J. Biol. Chem. 278:27844-27852(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-740 (ISOFORM 3), AND VARIANT
RP ASP-490.
RC TISSUE=Lung, Lymph, 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 575-1820 (ISOFORM 3).
RC TISSUE=Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1068-1820 (ISOFORMS 1/2/3), AND VARIANT
RP ARG-1177.
RX PubMed=10695267;
RA Fritzler M.J., Kerfoot S.M., Feasby T.E., Zochodne D.W., Westendorf J.M.,
RA Dalmau J.O., Chan E.K.;
RT "Autoantibodies from patients with idiopathic ataxia bind to M-phase
RT phosphoprotein-1 (MPP1).";
RL J. Invest. Med. 48:28-39(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1106-1820 (ISOFORM 4), AND VARIANT ARG-1177.
RA Dohnal A.M., Panzer-Gruemayer R.E.;
RT "Anti-leukemia-specific humoral immune response in children with T-lineage
RT acute lymphoblastic leukemia.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1255-1820 (ISOFORMS 1/2/3).
RX PubMed=8290587; DOI=10.1073/pnas.91.2.714;
RA Westendorf J.M., Rao P.N., Gerace L.;
RT "Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2
RT monoclonal antibody and determination of the phosphorylated epitope.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:714-718(1994).
RN [11]
RP FUNCTION, INTERACTION WITH PRC1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17409436; DOI=10.1158/0008-5472.can-06-3748;
RA Kanehira M., Katagiri T., Shimo A., Takata R., Shuin T., Miki T.,
RA Fujioka T., Nakamura Y.;
RT "Oncogenic role of MPHOSPH1, a cancer-testis antigen specific to human
RT bladder cancer.";
RL Cancer Res. 67:3276-3285(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1658, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560; SER-1588; SER-1658;
RP SER-1715 AND SER-1740, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
RP VARIANTS VAL-1148 AND TYR-1589.
RX PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
RG Care4Rare Canada Consortium;
RA Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
RA Schwartzentruber J., Martin B., Patry L., Nassif C., Dionne-Laporte A.,
RA Ospina L.H., Lemyre E., Massicotte C., Laframboise R., Maranda B.,
RA Labuda D., Decarie J.C., Rypens F., Goldsher D., Fallet-Bianco C.,
RA Soucy J.F., Laberge A.M., Maftei C., Boycott K., Brais B., Boucher R.M.,
RA Rouleau G.A., Katsanis N., Majewski J., Elpeleg O., Kukolich M.K.,
RA Shalev S., Michaud J.L.;
RT "Joubert Syndrome in French Canadians and Identification of Mutations in
RT CEP104.";
RL Am. J. Hum. Genet. 97:744-753(2015).
CC -!- FUNCTION: Plus-end-directed motor enzyme that is required for
CC completion of cytokinesis (PubMed:11470801, PubMed:12740395). Required
CC for proper midbody organization and abscission in polarized cortical
CC stem cells. Plays a role in the regulation of neuronal polarization by
CC mediating the transport of specific cargos. Participates in the
CC mobilization of SHTN1 and in the accumulation of PIP3 in the growth
CC cone of primary hippocampal neurons in a tubulin and actin-dependent
CC manner. In the developing telencephalon, cooperates with SHTN1 to
CC promote both the transition from the multipolar to the bipolar stage
CC and the radial migration of cortical neurons from the ventricular zone
CC toward the superficial layer of the neocortex. Involved in cerebral
CC cortex growth (By similarity). Acts as an oncogene for promoting
CC bladder cancer cells proliferation, apoptosis inhibition and
CC carcinogenic progression (PubMed:17409436).
CC {ECO:0000250|UniProtKB:Q80WE4, ECO:0000269|PubMed:11470801,
CC ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}.
CC -!- SUBUNIT: Oligomerizes (via kinesin motor domain) (PubMed:11470801).
CC Associates with microtubules (PubMed:12740395). Interacts (via C-
CC terminal globular tail region) with PIN1 (via WW domain)
CC (PubMed:11470801). Interacts with PRC1 (PubMed:17409436). Interacts
CC with SHTN1 (via N-terminus); the interaction is direct and promotes the
CC association of SHTN1 to microtubules in primary neurons.
CC {ECO:0000250|UniProtKB:Q80WE4, ECO:0000269|PubMed:11470801,
CC ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12740395,
CC ECO:0000269|PubMed:17409436}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:11470801}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:11470801}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11470801}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:11470801, ECO:0000269|PubMed:12740395}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:11470801}. Midbody
CC {ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q80WE4}. Cell projection,
CC growth cone {ECO:0000250|UniProtKB:Q80WE4}. Note=Localizes mainly in
CC the nucleus during interphase although it is also detected in the
CC cytoplasm without clear association with microtubules
CC (PubMed:12740395). Localized to the central spindle during cytokinetic
CC furrowing and with the midbody during abscission (PubMed:12740395,
CC PubMed:17409436). A 2-3 fold expression increase is seen as cells
CC progress from G1 to G2/M phase (PubMed:12740395). During prophase and
CC metaphase it is found throughout the cytoplasm and at anaphase
CC accumulates at the midplan of the cell and forms a distinct band
CC extending across the spindle midzone (PubMed:12740395). At anaphase it
CC is concentrated in the midbody (PubMed:12740395). Colocalized partially
CC along microtubules in primary neurons. Colocalized with SHTN1 along
CC microtubules to the tip of the growing cone in primary hippocampal
CC neurons. Localized in midbodies between dividing radial progenitors in
CC the ventricular zone (By similarity). Colocalized with PRC1 in the
CC nucleus of bladder carcinoma cells at the interphase. Colocalized with
CC PRC1 in bladder carcinoma cells at prophase, metaphase, early anaphase,
CC at the midzone in late anaphase and at the contractile ring in
CC telophase (PubMed:17409436). {ECO:0000250|UniProtKB:Q80WE4,
CC ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96Q89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96Q89-2; Sequence=VSP_022620;
CC Name=3;
CC IsoId=Q96Q89-3; Sequence=VSP_022619;
CC Name=4;
CC IsoId=Q96Q89-4; Sequence=VSP_022621, VSP_022622;
CC Name=5;
CC IsoId=Q96Q89-5; Sequence=VSP_022618;
CC -!- TISSUE SPECIFICITY: Brain, ovary, kidney and testis (at protein level)
CC (PubMed:12740395). Overexpressed in bladder cancer cells (at protein
CC level) (PubMed:17409436). Expressed in testis. Overexpressed in bladder
CC cancer cells (PubMed:17409436). {ECO:0000269|PubMed:12740395,
CC ECO:0000269|PubMed:17409436}.
CC -!- PTM: Phosphorylated during mitosis by CDK1 (PubMed:11470801,
CC PubMed:12740395). {ECO:0000269|PubMed:11470801,
CC ECO:0000269|PubMed:12740395}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46134.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH58913.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH93089.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI08689.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB15043.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB033337; BAB69456.1; -; mRNA.
DR EMBL; AB033338; BAB20417.1; -; mRNA.
DR EMBL; AL117496; CAB55962.1; -; mRNA.
DR EMBL; AK024959; BAB15043.1; ALT_SEQ; mRNA.
DR EMBL; AK025628; BAB15194.1; -; mRNA.
DR EMBL; AL157389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY282406; AAP40330.1; -; mRNA.
DR EMBL; AY282407; AAP40331.1; -; mRNA.
DR EMBL; BC046134; AAH46134.1; ALT_SEQ; mRNA.
DR EMBL; BC058913; AAH58913.1; ALT_SEQ; mRNA.
DR EMBL; BC093089; AAH93089.1; ALT_SEQ; mRNA.
DR EMBL; BC108688; AAI08689.1; ALT_SEQ; mRNA.
DR EMBL; AL137392; CAB70720.1; -; mRNA.
DR EMBL; U93121; AAB88727.1; -; mRNA.
DR EMBL; AY739715; AAW65984.1; -; mRNA.
DR EMBL; L16782; AAC37542.1; -; mRNA.
DR CCDS; CCDS60590.1; -. [Q96Q89-1]
DR CCDS; CCDS7407.1; -. [Q96Q89-3]
DR PIR; T17272; T17272.
DR RefSeq; NP_001271188.1; NM_001284259.1. [Q96Q89-1]
DR RefSeq; NP_057279.2; NM_016195.3. [Q96Q89-3]
DR AlphaFoldDB; Q96Q89; -.
DR SMR; Q96Q89; -.
DR BioGRID; 114953; 58.
DR DIP; DIP-103N; -.
DR IntAct; Q96Q89; 35.
DR MINT; Q96Q89; -.
DR STRING; 9606.ENSP00000360793; -.
DR BindingDB; Q96Q89; -.
DR ChEMBL; CHEMBL2021752; -.
DR CarbonylDB; Q96Q89; -.
DR GlyGen; Q96Q89; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q96Q89; -.
DR PhosphoSitePlus; Q96Q89; -.
DR BioMuta; KIF20B; -.
DR DMDM; 308153587; -.
DR EPD; Q96Q89; -.
DR jPOST; Q96Q89; -.
DR MassIVE; Q96Q89; -.
DR MaxQB; Q96Q89; -.
DR PaxDb; Q96Q89; -.
DR PeptideAtlas; Q96Q89; -.
DR PRIDE; Q96Q89; -.
DR ProteomicsDB; 77838; -. [Q96Q89-1]
DR ProteomicsDB; 77839; -. [Q96Q89-2]
DR ProteomicsDB; 77840; -. [Q96Q89-3]
DR ProteomicsDB; 77841; -. [Q96Q89-4]
DR ProteomicsDB; 77842; -. [Q96Q89-5]
DR Antibodypedia; 30294; 98 antibodies from 20 providers.
DR DNASU; 9585; -.
DR Ensembl; ENST00000260753.8; ENSP00000260753.4; ENSG00000138182.15. [Q96Q89-3]
DR Ensembl; ENST00000371728.8; ENSP00000360793.3; ENSG00000138182.15. [Q96Q89-1]
DR GeneID; 9585; -.
DR KEGG; hsa:9585; -.
DR MANE-Select; ENST00000371728.8; ENSP00000360793.3; NM_001284259.2; NP_001271188.1.
DR UCSC; uc001kgr.3; human. [Q96Q89-1]
DR CTD; 9585; -.
DR DisGeNET; 9585; -.
DR GeneCards; KIF20B; -.
DR HGNC; HGNC:7212; KIF20B.
DR HPA; ENSG00000138182; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 605498; gene.
DR neXtProt; NX_Q96Q89; -.
DR OpenTargets; ENSG00000138182; -.
DR PharmGKB; PA162393285; -.
DR VEuPathDB; HostDB:ENSG00000138182; -.
DR eggNOG; KOG0247; Eukaryota.
DR GeneTree; ENSGT00940000155989; -.
DR HOGENOM; CLU_002380_0_0_1; -.
DR InParanoid; Q96Q89; -.
DR OMA; DQHHNRL; -.
DR OrthoDB; 314538at2759; -.
DR PhylomeDB; Q96Q89; -.
DR TreeFam; TF105232; -.
DR PathwayCommons; Q96Q89; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q96Q89; -.
DR SIGNOR; Q96Q89; -.
DR BioGRID-ORCS; 9585; 63 hits in 1089 CRISPR screens.
DR ChiTaRS; KIF20B; human.
DR GeneWiki; MPHOSPH1; -.
DR GenomeRNAi; 9585; -.
DR Pharos; Q96Q89; Tbio.
DR PRO; PR:Q96Q89; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96Q89; protein.
DR Bgee; ENSG00000138182; Expressed in oocyte and 131 other tissues.
DR ExpressionAtlas; Q96Q89; baseline and differential.
DR Genevisible; Q96Q89; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0070938; C:contractile ring; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; ISS:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0035372; P:protein localization to microtubule; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; NAS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; NAS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR028828; KIF20B.
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 PANTHER; PTHR24115:SF534; PTHR24115:SF534; 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 Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Mitosis; Motor protein; Nucleotide-binding; Nucleus; Oncogene;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1820
FT /note="Kinesin-like protein KIF20B"
FT /id="PRO_0000274053"
FT DOMAIN 58..479
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 829..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1107
FT /note="Necessary and sufficient for interaction with SHTN1"
FT /evidence="ECO:0000250|UniProtKB:Q80WE4"
FT REGION 1247..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1820
FT /note="Interaction with PIN1"
FT /evidence="ECO:0000269|PubMed:11470801"
FT REGION 1760..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 523..603
FT /evidence="ECO:0000255"
FT COILED 674..793
FT /evidence="ECO:0000255"
FT COMPBIAS 829..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 560
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80WE4"
FT MOD_RES 1588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1644
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:11470801"
FT MOD_RES 1658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1308
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022618"
FT VAR_SEQ 668..707
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:12740395, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022619"
FT VAR_SEQ 849
FT /note="G -> GTTSAASSRRLRKLISKPKKGVNRTRQTEGHSLV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11470801"
FT /id="VSP_022620"
FT VAR_SEQ 1664..1722
FT /note="DLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSSKKTYSLRSQAS
FT IIGVNLA -> SASPPPKECSSSPAMEQSWKENDFDKLREEGFRRSNYSELQEEIQTKG
FT KEVENFEKNLD (in isoform 4)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_022621"
FT VAR_SEQ 1723..1820
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_022622"
FT VARIANT 50
FT /note="A -> G (in dbSNP:rs1129777)"
FT /id="VAR_030181"
FT VARIANT 490
FT /note="E -> D (in dbSNP:rs17484219)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_030182"
FT VARIANT 756
FT /note="N -> I (in dbSNP:rs12572012)"
FT /evidence="ECO:0000269|PubMed:11470801,
FT ECO:0000269|PubMed:12740395"
FT /id="VAR_030183"
FT VARIANT 789
FT /note="H -> L (in dbSNP:rs3758388)"
FT /evidence="ECO:0000269|PubMed:11470801,
FT ECO:0000269|PubMed:12740395"
FT /id="VAR_030184"
FT VARIANT 1011
FT /note="D -> E (in dbSNP:rs1062465)"
FT /id="VAR_030185"
FT VARIANT 1127
FT /note="E -> Q (in dbSNP:rs11185863)"
FT /id="VAR_030186"
FT VARIANT 1148
FT /note="A -> V (in dbSNP:rs117564945)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075704"
FT VARIANT 1177
FT /note="C -> R (in dbSNP:rs1886996)"
FT /evidence="ECO:0000269|PubMed:10695267,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:11470801,
FT ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:14702039,
FT ECO:0000269|Ref.9"
FT /id="VAR_030187"
FT VARIANT 1219
FT /note="N -> S (in dbSNP:rs1886997)"
FT /id="VAR_030188"
FT VARIANT 1589
FT /note="F -> Y (in dbSNP:rs117258675)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075705"
FT VARIANT 1789
FT /note="I -> V (in dbSNP:rs3758390)"
FT /id="VAR_030189"
FT CONFLICT 266
FT /note="S -> T (in Ref. 1; BAB69456)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..297
FT /note="KR -> NT (in Ref. 1; BAB69456)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="V -> I (in Ref. 1; BAB69456)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="M -> V (in Ref. 1; BAB69456)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> K (in Ref. 6; AAI08689)"
FT /evidence="ECO:0000305"
FT CONFLICT 705..707
FT /note="DPQ -> ETE (in Ref. 5; AAP40331)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="E -> K (in Ref. 1; BAB69456)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="N -> S (in Ref. 3; BAB15043)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="N -> S (in Ref. 3; BAB15043)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="F -> S (in Ref. 3; BAB15043)"
FT /evidence="ECO:0000305"
FT CONFLICT 1105
FT /note="K -> R (in Ref. 3; BAB15043)"
FT /evidence="ECO:0000305"
FT CONFLICT 1302
FT /note="V -> E (in Ref. 10; AAC37542)"
FT /evidence="ECO:0000305"
FT CONFLICT 1459
FT /note="R -> S (in Ref. 10; AAC37542)"
FT /evidence="ECO:0000305"
FT CONFLICT 1608
FT /note="V -> A (in Ref. 1; BAB69456)"
FT /evidence="ECO:0000305"
FT CONFLICT 1649
FT /note="K -> E (in Ref. 2; CAB55962 and 3; BAB15194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1820 AA; 210629 MW; 8A6FE95A6F3BA20C CRC64;
MESNFNQEGV PRPSYVFSAD PIARPSEINF DGIKLDLSHE FSLVAPNTEA NSFESKDYLQ
VCLRIRPFTQ SEKELESEGC VHILDSQTVV LKEPQCILGR LSEKSSGQMA QKFSFSKVFG
PATTQKEFFQ GCIMQPVKDL LKGQSRLIFT YGLTNSGKTY TFQGTEENIG ILPRTLNVLF
DSLQERLYTK MNLKPHRSRE YLRLSSEQEK EEIASKSALL RQIKEVTVHN DSDDTLYGSL
TNSLNISEFE ESIKDYEQAN LNMANSIKFS VWVSFFEIYN EYIYDLFVPV SSKFQKRKML
RLSQDVKGYS FIKDLQWIQV SDSKEAYRLL KLGIKHQSVA FTKLNNASSR SHSIFTVKIL
QIEDSEMSRV IRVSELSLCD LAGSERTMKT QNEGERLRET GNINTSLLTL GKCINVLKNS
EKSKFQQHVP FRESKLTHYF QSFFNGKGKI CMIVNISQCY LAYDETLNVL KFSAIAQKVC
VPDTLNSSQE KLFGPVKSSQ DVSLDSNSNS KILNVKRATI SWENSLEDLM EDEDLVEELE
NAEETQNVET KLLDEDLDKT LEENKAFISH EEKRKLLDLI EDLKKKLINE KKEKLTLEFK
IREEVTQEFT QYWAQREADF KETLLQEREI LEENAERRLA IFKDLVGKCD TREEAAKDIC
ATKVETEETH NYVGFEDIID SLQDNVADIK KQAEIAHLYI ASLPDPQEAT ACLELKFNQI
KAELAKTKGE LIKTKEELKK RENESDSLIQ ELETSNKKII TQNQRIKELI NIIDQKEDTI
NEFQNLKSHM ENTFKCNDKA DTSSLIINNK LICNETVEVP KDSKSKICSE RKRVNENELQ
QDEPPAKKGS IHVSSAITED QKKSEEVRPN IAEIEDIRVL QENNEGLRAF LLTIENELKN
EKEEKAELNK QIVHFQQELS LSEKKNLTLS KEVQQIQSNY DIAIAELHVQ KSKNQEQEEK
IMKLSNEIET ATRSITNNVS QIKLMHTKID ELRTLDSVSQ ISNIDLLNLR DLSNGSEEDN
LPNTQLDLLG NDYLVSKQVK EYRIQEPNRE NSFHSSIEAI WEECKEIVKA SSKKSHQIEE
LEQQIEKLQA EVKGYKDENN RLKEKEHKNQ DDLLKEKETL IQQLKEELQE KNVTLDVQIQ
HVVEGKRALS ELTQGVTCYK AKIKELETIL ETQKVECSHS AKLEQDILEK ESIILKLERN
LKEFQEHLQD SVKNTKDLNV KELKLKEEIT QLTNNLQDMK HLLQLKEEEE ETNRQETEKL
KEELSASSAR TQNLKADLQR KEEDYADLKE KLTDAKKQIK QVQKEVSVMR DEDKLLRIKI
NELEKKKNQC SQELDMKQRT IQQLKEQLNN QKVEEAIQQY ERACKDLNVK EKIIEDMRMT
LEEQEQTQVE QDQVLEAKLE EVERLATELE KWKEKCNDLE TKNNQRSNKE HENNTDVLGK
LTNLQDELQE SEQKYNADRK KWLEEKMMLI TQAKEAENIR NKEMKKYAED RERFFKQQNE
MEILTAQLTE KDSDLQKWRE ERDQLVAALE IQLKALISSN VQKDNEIEQL KRIISETSKI
ETQIMDIKPK RISSADPDKL QTEPLSTSFE ISRNKIEDGS VVLDSCEVST ENDQSTRFPK
PELEIQFTPL QPNKMAVKHP GCTTPVTVKI PKARKRKSNE MEEDLVKCEN KKNATPRTNL
KFPISDDRNS SVKKEQKVAI RPSSKKTYSL RSQASIIGVN LATKKKEGTL QKFGDFLQHS
PSILQSKAKK IIETMSSSKL SNVEASKENV SQPKRAKRKL YTSEISSPID ISGQVILMDQ
KMKESDHQII KRRLRTKTAK
