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Kinesin-like protein KIF20B (Cancer/testis antigen 90) (CT90) (Kinesin family member 20B) (Kinesin-related motor interacting with PIN1) (M-phase phosphoprotein 1) (MPP1)

 KI20B_HUMAN             Reviewed;        1820 AA.
Q96Q89; A8MXM7; O43277; Q09471; Q2KQ73; Q32NE1; Q561V3; Q58EX8;
Q5T9M8; Q5T9M9; Q5T9N0; Q5T9N1; Q7KZ68; Q7Z5E0; Q7Z5E1; Q7Z6M9;
Q86X82; Q9H3R8; Q9H6Q9; Q9H755; Q9NTC1; Q9UFR5;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
25-OCT-2017, entry version 134.
RecName: Full=Kinesin-like protein KIF20B {ECO:0000305};
AltName: Full=Cancer/testis antigen 90;
Short=CT90;
AltName: Full=Kinesin family member 20B {ECO:0000312|HGNC:HGNC:7212};
AltName: Full=Kinesin-related motor interacting with PIN1 {ECO:0000303|PubMed:11470801};
AltName: Full=M-phase phosphoprotein 1 {ECO:0000303|PubMed:12740395};
Short=MPP1 {ECO:0000303|PubMed:12740395};
Name=KIF20B {ECO:0000312|HGNC:HGNC:7212};
Synonyms=KRMP1 {ECO:0000303|PubMed:11470801},
MPHOSPH1 {ECO:0000303|PubMed:12740395};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, INTERACTION WITH PIN1, PHOSPHORYLATION AT
THR-1644, AND VARIANTS ILE-756; LEU-789 AND ARG-1177.
PubMed=11470801; DOI=10.1074/jbc.M106207200;
Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M.;
"Identification of a novel kinesin-related protein, KRMP1, as a target
for mitotic peptidyl-prolyl isomerase Pin1.";
J. Biol. Chem. 276:37520-37528(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS
ASP-490 AND ARG-1177.
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 779-1480 (ISOFORMS 1/2/3/4), AND
VARIANT ARG-1177.
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-957 (ISOFORM 3), NUCLEOTIDE SEQUENCE
[MRNA] OF 705-1820 (ISOFORM 1), FUNCTION, INTERACTION WITH
MICROTUBULES, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND VARIANTS ILE-756; LEU-789 AND ARG-1177.
PubMed=12740395; DOI=10.1074/jbc.M304522200;
Abaza A., Soleilhac J.-M., Westendorf J., Piel M., Crevel I., Roux A.,
Pirollet F.;
"M phase phosphoprotein 1 is a human plus-end-directed kinesin-related
protein required for cytokinesis.";
J. Biol. Chem. 278:27844-27852(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-740 (ISOFORM 3), AND
VARIANT ASP-490.
TISSUE=Lung, Lymph, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 575-1820 (ISOFORM 3).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1068-1820 (ISOFORMS 1/2/3), AND VARIANT
ARG-1177.
PubMed=10695267;
Fritzler M.J., Kerfoot S.M., Feasby T.E., Zochodne D.W.,
Westendorf J.M., Dalmau J.O., Chan E.K.;
"Autoantibodies from patients with idiopathic ataxia bind to M-phase
phosphoprotein-1 (MPP1).";
J. Invest. Med. 48:28-39(2000).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1106-1820 (ISOFORM 4), AND VARIANT
ARG-1177.
Dohnal A.M., Panzer-Gruemayer R.E.;
"Anti-leukemia-specific humoral immune response in children with T-
lineage acute lymphoblastic leukemia.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1255-1820 (ISOFORMS 1/2/3).
PubMed=8290587; DOI=10.1073/pnas.91.2.714;
Westendorf J.M., Rao P.N., Gerace L.;
"Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2
monoclonal antibody and determination of the phosphorylated epitope.";
Proc. Natl. Acad. Sci. U.S.A. 91:714-718(1994).
[11]
FUNCTION, INTERACTION WITH PRC1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=17409436; DOI=10.1158/0008-5472.CAN-06-3748;
Kanehira M., Katagiri T., Shimo A., Takata R., Shuin T., Miki T.,
Fujioka T., Nakamura Y.;
"Oncogenic role of MPHOSPH1, a cancer-testis antigen specific to human
bladder cancer.";
Cancer Res. 67:3276-3285(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1658, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560; SER-1588; SER-1658;
SER-1715 AND SER-1740, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
VARIANTS VAL-1148 AND TYR-1589.
PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
Care4Rare Canada Consortium;
Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
Schwartzentruber J., Martin B., Patry L., Nassif C.,
Dionne-Laporte A., Ospina L.H., Lemyre E., Massicotte C.,
Laframboise R., Maranda B., Labuda D., Decarie J.C., Rypens F.,
Goldsher D., Fallet-Bianco C., Soucy J.F., Laberge A.M., Maftei C.,
Boycott K., Brais B., Boucher R.M., Rouleau G.A., Katsanis N.,
Majewski J., Elpeleg O., Kukolich M.K., Shalev S., Michaud J.L.;
"Joubert Syndrome in French Canadians and Identification of Mutations
in CEP104.";
Am. J. Hum. Genet. 97:744-753(2015).
-!- FUNCTION: Plus-end-directed motor enzyme that is required for
completion of cytokinesis (PubMed:11470801, PubMed:12740395).
Required for proper midbody organization and abscission in
polarized cortical stem cells. Plays a role in the regulation of
neuronal polarization by mediating the transport of specific
cargos. Participates in the mobilization of SHTN1 and in the
accumulation of PIP3 in the growth cone of primary hippocampal
neurons in a tubulin and actin-dependent manner. In the developing
telencephalon, cooperates with SHTN1 to promote both the
transition from the multipolar to the bipolar stage and the radial
migration of cortical neurons from the ventricular zone toward the
superficial layer of the neocortex. Involved in cerebral cortex
growth (By similarity). Acts as an oncogene for promoting bladder
cancer cells proliferation, apoptosis inhibition and carcinogenic
progression (PubMed:17409436). {ECO:0000250|UniProtKB:Q80WE4,
ECO:0000269|PubMed:11470801, ECO:0000269|PubMed:12740395,
ECO:0000269|PubMed:17409436}.
-!- SUBUNIT: Oligomerizes (via kinesin motor domain)
(PubMed:11470801). Associates with microtubules (PubMed:12740395).
Interacts (via C-terminal globular tail region) with PIN1 (via WW
domain) (PubMed:11470801). Interacts with PRC1 (PubMed:17409436).
Interacts with SHTN1 (via N-terminus); the interaction is direct
and promotes the association of SHTN1 to microtubules in primary
neurons. {ECO:0000250|UniProtKB:Q80WE4,
ECO:0000269|PubMed:11470801, ECO:0000269|PubMed:12740395,
ECO:0000269|PubMed:17409436}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12740395,
ECO:0000269|PubMed:17409436}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:11470801}.
Nucleus, nucleolus {ECO:0000269|PubMed:11470801}. Nucleus,
nucleoplasm {ECO:0000269|PubMed:11470801}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:11470801,
ECO:0000269|PubMed:12740395}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:11470801}. Midbody
{ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}. Cell
projection, axon {ECO:0000250|UniProtKB:Q80WE4}. Cell projection,
growth cone {ECO:0000250|UniProtKB:Q80WE4}. Note=Localizes mainly
in the nucleus during interphase although it is also detected in
the cytoplasm without clear association with microtubules
(PubMed:12740395). Localized to the central spindle during
cytokinetic furrowing and with the midbody during abscission
(PubMed:12740395, PubMed:17409436). A 2-3 fold expression increase
is seen as cells progress from G1 to G2/M phase (PubMed:12740395).
During prophase and metaphase it is found throughout the cytoplasm
and at anaphase accumulates at the midplan of the cell and forms a
distinct band extending across the spindle midzone
(PubMed:12740395). At anaphase it is concentrated in the midbody
(PubMed:12740395). Colocalized partially along microtubules in
primary neurons. Colocalized with SHTN1 along microtubules to the
tip of the growing cone in primary hippocampal neurons. Localized
in midbodies between dividing radial progenitors in the
ventricular zone (By similarity). Colocalized with PRC1 in the
nucleus of bladder carcinoma cells at the interphase. Colocalized
with PRC1 in bladder carcinoma cells at prophase, metaphase, early
anaphase, at the midzone in late anaphase and at the contractile
ring in telophase (PubMed:17409436).
{ECO:0000250|UniProtKB:Q80WE4, ECO:0000269|PubMed:12740395,
ECO:0000269|PubMed:17409436}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q96Q89-1; Sequence=Displayed;
Name=2;
IsoId=Q96Q89-2; Sequence=VSP_022620;
Name=3;
IsoId=Q96Q89-3; Sequence=VSP_022619;
Name=4;
IsoId=Q96Q89-4; Sequence=VSP_022621, VSP_022622;
Name=5;
IsoId=Q96Q89-5; Sequence=VSP_022618;
-!- TISSUE SPECIFICITY: Brain, ovary, kidney and testis (at protein
level) (PubMed:12740395). Overexpressed in bladder cancer cells
(at protein level) (PubMed:17409436). Expressed in testis.
Overexpressed in bladder cancer cells (PubMed:17409436).
{ECO:0000269|PubMed:12740395, ECO:0000269|PubMed:17409436}.
-!- PTM: Phosphorylated during mitosis by CDK1 (PubMed:11470801,
PubMed:12740395). {ECO:0000269|PubMed:11470801,
ECO:0000269|PubMed:12740395}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
-!- SEQUENCE CAUTION:
Sequence=AAH46134.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH58913.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH93089.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAI08689.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAB15043.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=CAI12885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI16829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB033337; BAB69456.1; -; mRNA.
EMBL; AB033338; BAB20417.1; -; mRNA.
EMBL; AL117496; CAB55962.1; -; mRNA.
EMBL; AK024959; BAB15043.1; ALT_SEQ; mRNA.
EMBL; AK025628; BAB15194.1; -; mRNA.
EMBL; AL157389; CAI12885.1; ALT_SEQ; Genomic_DNA.
EMBL; AL157400; CAI12885.1; JOINED; Genomic_DNA.
EMBL; AL157389; CAI12886.1; -; Genomic_DNA.
EMBL; AL157400; CAI12886.1; JOINED; Genomic_DNA.
EMBL; AL157389; CAI12887.1; -; Genomic_DNA.
EMBL; AL157400; CAI12887.1; JOINED; Genomic_DNA.
EMBL; AL157400; CAI16829.1; ALT_SEQ; Genomic_DNA.
EMBL; AL157389; CAI16829.1; JOINED; Genomic_DNA.
EMBL; AL157400; CAI16830.1; -; Genomic_DNA.
EMBL; AL157389; CAI16830.1; JOINED; Genomic_DNA.
EMBL; AL157400; CAI16831.1; -; Genomic_DNA.
EMBL; AL157389; CAI16831.1; JOINED; Genomic_DNA.
EMBL; AL157400; CAI16832.1; -; Genomic_DNA.
EMBL; AY282406; AAP40330.1; -; mRNA.
EMBL; AY282407; AAP40331.1; -; mRNA.
EMBL; BC046134; AAH46134.1; ALT_SEQ; mRNA.
EMBL; BC058913; AAH58913.1; ALT_SEQ; mRNA.
EMBL; BC093089; AAH93089.1; ALT_SEQ; mRNA.
EMBL; BC108688; AAI08689.1; ALT_SEQ; mRNA.
EMBL; AL137392; CAB70720.1; -; mRNA.
EMBL; U93121; AAB88727.1; -; mRNA.
EMBL; AY739715; AAW65984.1; -; mRNA.
EMBL; L16782; AAC37542.1; -; mRNA.
CCDS; CCDS60590.1; -. [Q96Q89-1]
CCDS; CCDS7407.1; -. [Q96Q89-3]
PIR; T17272; T17272.
RefSeq; NP_001271188.1; NM_001284259.1. [Q96Q89-1]
RefSeq; NP_057279.2; NM_016195.3. [Q96Q89-3]
UniGene; Hs.240; -.
ProteinModelPortal; Q96Q89; -.
SMR; Q96Q89; -.
BioGrid; 114953; 27.
DIP; DIP-103N; -.
IntAct; Q96Q89; 19.
MINT; MINT-4712270; -.
STRING; 9606.ENSP00000260753; -.
ChEMBL; CHEMBL2021752; -.
iPTMnet; Q96Q89; -.
PhosphoSitePlus; Q96Q89; -.
BioMuta; KIF20B; -.
DMDM; 308153587; -.
EPD; Q96Q89; -.
MaxQB; Q96Q89; -.
PaxDb; Q96Q89; -.
PeptideAtlas; Q96Q89; -.
PRIDE; Q96Q89; -.
DNASU; 9585; -.
Ensembl; ENST00000260753; ENSP00000260753; ENSG00000138182. [Q96Q89-3]
Ensembl; ENST00000371728; ENSP00000360793; ENSG00000138182. [Q96Q89-1]
GeneID; 9585; -.
KEGG; hsa:9585; -.
UCSC; uc001kgr.3; human. [Q96Q89-1]
CTD; 9585; -.
DisGeNET; 9585; -.
EuPathDB; HostDB:ENSG00000138182.14; -.
GeneCards; KIF20B; -.
HGNC; HGNC:7212; KIF20B.
HPA; HPA031263; -.
HPA; HPA050214; -.
MIM; 605498; gene.
neXtProt; NX_Q96Q89; -.
OpenTargets; ENSG00000138182; -.
PharmGKB; PA162393285; -.
eggNOG; KOG0247; Eukaryota.
eggNOG; COG5059; LUCA.
GeneTree; ENSGT00870000136438; -.
HOVERGEN; HBG106760; -.
InParanoid; Q96Q89; -.
KO; K10402; -.
OMA; GIKHQSV; -.
OrthoDB; EOG091G00AY; -.
PhylomeDB; Q96Q89; -.
TreeFam; TF105232; -.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-983189; Kinesins.
ChiTaRS; KIF20B; human.
GeneWiki; MPHOSPH1; -.
GenomeRNAi; 9585; -.
PRO; PR:Q96Q89; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138182; -.
ExpressionAtlas; Q96Q89; baseline and differential.
Genevisible; Q96Q89; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0070938; C:contractile ring; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008574; F:ATP-dependent microtubule motor activity, plus-end-directed; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; NAS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; ISS:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
GO; GO:0035372; P:protein localization to microtubule; ISS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; NAS:UniProtKB.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR028828; KIF20B.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24115; PTHR24115; 4.
PANTHER; PTHR24115:SF534; PTHR24115:SF534; 4.
Pfam; PF00225; Kinesin; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00129; KISc; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell cycle; Cell division;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
Nucleus; Oncogene; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 1820 Kinesin-like protein KIF20B.
/FTId=PRO_0000274053.
DOMAIN 58 479 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
NP_BIND 152 159 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
REGION 1050 1107 Necessary and sufficient for interaction
with SHTN1.
{ECO:0000250|UniProtKB:Q80WE4}.
REGION 1560 1820 Interaction with PIN1.
{ECO:0000269|PubMed:11470801}.
COILED 523 603 {ECO:0000255}.
COILED 674 793 {ECO:0000255}.
COMPBIAS 1247 1251 Poly-Glu.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 560 560 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 997 997 Phosphoserine.
{ECO:0000250|UniProtKB:Q80WE4}.
MOD_RES 1588 1588 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1644 1644 Phosphothreonine; by CDK1.
{ECO:0000269|PubMed:11470801}.
MOD_RES 1658 1658 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1715 1715 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1740 1740 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1308 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_022618.
VAR_SEQ 668 707 Missing (in isoform 3).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:12740395,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_022619.
VAR_SEQ 849 849 G -> GTTSAASSRRLRKLISKPKKGVNRTRQTEGHSLV
(in isoform 2).
{ECO:0000303|PubMed:11470801}.
/FTId=VSP_022620.
VAR_SEQ 1664 1722 DLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSS
KKTYSLRSQASIIGVNLA -> SASPPPKECSSSPAMEQSW
KENDFDKLREEGFRRSNYSELQEEIQTKGKEVENFEKNLD
(in isoform 4). {ECO:0000303|Ref.9}.
/FTId=VSP_022621.
VAR_SEQ 1723 1820 Missing (in isoform 4).
{ECO:0000303|Ref.9}.
/FTId=VSP_022622.
VARIANT 50 50 A -> G (in dbSNP:rs1129777).
/FTId=VAR_030181.
VARIANT 490 490 E -> D (in dbSNP:rs17484219).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_030182.
VARIANT 756 756 N -> I (in dbSNP:rs12572012).
{ECO:0000269|PubMed:11470801,
ECO:0000269|PubMed:12740395}.
/FTId=VAR_030183.
VARIANT 789 789 H -> L (in dbSNP:rs3758388).
{ECO:0000269|PubMed:11470801,
ECO:0000269|PubMed:12740395}.
/FTId=VAR_030184.
VARIANT 1011 1011 D -> E (in dbSNP:rs1062465).
/FTId=VAR_030185.
VARIANT 1127 1127 E -> Q (in dbSNP:rs11185863).
/FTId=VAR_030186.
VARIANT 1148 1148 A -> V (in dbSNP:rs117564945).
{ECO:0000269|PubMed:26477546}.
/FTId=VAR_075704.
VARIANT 1177 1177 C -> R (in dbSNP:rs1886996).
{ECO:0000269|PubMed:10695267,
ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:11470801,
ECO:0000269|PubMed:12740395,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.9}.
/FTId=VAR_030187.
VARIANT 1219 1219 N -> S (in dbSNP:rs1886997).
/FTId=VAR_030188.
VARIANT 1589 1589 F -> Y (in dbSNP:rs117258675).
{ECO:0000269|PubMed:26477546}.
/FTId=VAR_075705.
VARIANT 1789 1789 I -> V (in dbSNP:rs3758390).
/FTId=VAR_030189.
CONFLICT 266 266 S -> T (in Ref. 1; BAB69456).
{ECO:0000305}.
CONFLICT 296 297 KR -> NT (in Ref. 1; BAB69456).
{ECO:0000305}.
CONFLICT 357 357 V -> I (in Ref. 1; BAB69456).
{ECO:0000305}.
CONFLICT 388 388 M -> V (in Ref. 1; BAB69456).
{ECO:0000305}.
CONFLICT 593 593 E -> K (in Ref. 6; AAI08689).
{ECO:0000305}.
CONFLICT 705 707 DPQ -> ETE (in Ref. 5; AAP40331).
{ECO:0000305}.
CONFLICT 753 753 E -> K (in Ref. 1; BAB69456).
{ECO:0000305}.
CONFLICT 797 797 N -> S (in Ref. 3; BAB15043).
{ECO:0000305}.
CONFLICT 870 870 N -> S (in Ref. 3; BAB15043).
{ECO:0000305}.
CONFLICT 915 915 F -> S (in Ref. 3; BAB15043).
{ECO:0000305}.
CONFLICT 1105 1105 K -> R (in Ref. 3; BAB15043).
{ECO:0000305}.
CONFLICT 1302 1302 V -> E (in Ref. 10; AAC37542).
{ECO:0000305}.
CONFLICT 1459 1459 R -> S (in Ref. 10; AAC37542).
{ECO:0000305}.
CONFLICT 1608 1608 V -> A (in Ref. 1; BAB69456).
{ECO:0000305}.
CONFLICT 1649 1649 K -> E (in Ref. 2; CAB55962 and 3;
BAB15194). {ECO:0000305}.
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


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