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Kinesin-like protein KIF14

 KIF14_HUMAN             Reviewed;        1648 AA.
Q15058; Q14CI8; Q4G0A5; Q5T1W3;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=Kinesin-like protein KIF14 {ECO:0000305};
Name=KIF14 {ECO:0000312|HGNC:HGNC:19181};
Synonyms=KIAA0042 {ECO:0000312|HGNC:HGNC:19181};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. II.
The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 1:223-229(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-1633.
TISSUE=Uterus;
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).
[5]
FUNCTION.
PubMed=15843429; DOI=10.1091/mbc.E05-02-0167;
Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E.,
Fan J.-B., Abraham R.T., Jiang W.;
"Functional analysis of human microtubule-based motor proteins, the
kinesins and dyneins, in mitosis/cytokinesis using RNA interference.";
Mol. Biol. Cell 16:3187-3199(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1292, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRC1 AND CIT.
PubMed=16431929; DOI=10.1083/jcb.200511061;
Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B.,
Nigg E.A., Barr F.A.;
"KIF14 and citron kinase act together to promote efficient
cytokinesis.";
J. Cell Biol. 172:363-372(2006).
[8]
INTERACTION WITH ARRB2.
PubMed=16820410; DOI=10.1242/jcs.03046;
Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
"Novel function of beta-arrestin2 in the nucleus of mature
spermatozoa.";
J. Cell Sci. 119:3047-3056(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=16648480; DOI=10.1128/MCB.26.10.3853-3863.2006;
Carleton M., Mao M., Biery M., Warrener P., Kim S., Buser C.,
Marshall C.G., Fernandes C., Annis J., Linsley P.S.;
"RNA interference-mediated silencing of mitotic kinesin KIF14 disrupts
cell cycle progression and induces cytokinesis failure.";
Mol. Cell. Biol. 26:3853-3863(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
INTERACTION WITH SVIL, AND SUBCELLULAR LOCATION.
PubMed=20309963; DOI=10.1002/cm.20449;
Smith T.C., Fang Z., Luna E.J.;
"Novel interactors and a role for supervillin in early cytokinesis.";
Cytoskeleton 67:346-364(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RADIL.
PubMed=23209302; DOI=10.1083/jcb.201206051;
Ahmed S.M., Theriault B.L., Uppalapati M., Chiu C.W., Gallie B.L.,
Sidhu S.S., Angers S.;
"KIF14 negatively regulates Rap1a-Radil signaling during breast cancer
progression.";
J. Cell Biol. 199:951-967(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-272; THR-277;
SER-346; THR-915; SER-937 AND SER-1292, 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).
[16]
FUNCTION.
PubMed=24854087; DOI=10.1038/emm.2014.23;
Xu H., Choe C., Shin S.H., Park S.W., Kim H.S., Jung S.H., Yim S.H.,
Kim T.M., Chung Y.J.;
"Silencing of KIF14 interferes with cell cycle progression and
cytokinesis by blocking the p27(Kip1) ubiquitination pathway in
hepatocellular carcinoma.";
Exp. Mol. Med. 46:E97-E97(2014).
[17]
FUNCTION, AND INTERACTION WITH AKT1.
PubMed=24784001; DOI=10.1016/j.neo.2014.03.008;
Singel S.M., Cornelius C., Zaganjor E., Batten K., Sarode V.R.,
Buckley D.L., Peng Y., John G.B., Li H.C., Sadeghi N., Wright W.E.,
Lum L., Corson T.W., Shay J.W.;
"KIF14 promotes AKT phosphorylation and contributes to chemoresistance
in triple-negative breast cancer.";
Neoplasia 16:247-256(2014).
[18]
INVOLVEMENT IN MKS12.
PubMed=24128419; DOI=10.1111/cge.12301;
Filges I., Nosova E., Bruder E., Tercanli S., Townsend K.,
Gibson W.T., Roethlisberger B., Heinimann K., Hall J.G.,
Gregory-Evans C.Y., Wasserman W.W., Miny P., Friedman J.M.;
"Exome sequencing identifies mutations in KIF14 as a novel cause of an
autosomal recessive lethal fetal ciliopathy phenotype.";
Clin. Genet. 86:220-228(2014).
-!- FUNCTION: Microtubule motor protein that binds to microtubules
with high affinity through each tubulin heterodimer and has an
ATPase activity (By similarity). Plays a role in many processes
like cell division, cytokinesis and also in cell proliferation and
apoptosis (PubMed:24784001, PubMed:16648480). During cytokinesis,
targets to central spindle and midbody through its interaction
with PRC1 and CIT respectively (PubMed:16431929). Regulates cell
growth through regulation of cell cycle progression and
cytokinesis (PubMed:24854087). During cell cycle progression acts
through SCF-dependent proteasomal ubiquitin-dependent protein
catabolic process which controls CDKN1B degradation, resulting in
positive regulation of cyclins, including CCNE1, CCND1 and CCNB1
(PubMed:24854087). During late neurogenesis, regulates the
cerebellar, cerebral cortex and olfactory bulb development through
regulation of apoptosis, cell proliferation and cell division (By
similarity). Also is required for chromosome congression and
alignment during mitotic cell cycle process (PubMed:15843429).
Regulates cell spreading, focal adhesion dynamics, and cell
migration through its interaction with RADIL resulting in
regulation of RAP1A-mediated inside-out integrin activation by
tethering RADIL on microtubules (PubMed:23209302).
{ECO:0000250|UniProtKB:L0N7N1, ECO:0000269|PubMed:15843429,
ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:16648480,
ECO:0000269|PubMed:23209302, ECO:0000269|PubMed:24784001,
ECO:0000269|PubMed:24854087}.
-!- SUBUNIT: Directly interacts with PRC1 within a complex also
containing KIF4A, KIF20A and KIF23; targets to the central
spindle. Directly interacts with CIT depending on the activation
state of the kinase (stronger interaction with the kinase-dead
form); targets to the midbody. Interacts with ARRB2; the
interaction is detected in the nucleus upon OR1D2 stimulation.
Interacts with AKT1; the interaction is detected in the plasma
membrane upon INS stimulation and promotes AKT1 phosphorylation.
Interacts with SVIL; at midbody during cytokinesis. Interacts with
RADIL (via PDZ domain); recruits RADIL to the microtubule network
restricting RADIL from interaction with activated RAP1A
(PubMed:23209302). {ECO:0000269|PubMed:16431929,
ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:20309963,
ECO:0000269|PubMed:23209302, ECO:0000269|PubMed:24784001}.
-!- INTERACTION:
O46385:SVIL (xeno); NbExp=3; IntAct=EBI-1045252, EBI-6995105;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16431929}.
Cytoplasm {ECO:0000269|PubMed:16648480}. Cytoplasm, cytoskeleton,
spindle {ECO:0000269|PubMed:16431929}. Midbody
{ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:20309963}.
Note=Nuclear localization observed during interphase
(PubMed:16431929). Nuclear localization triggered by entry into
mitosis (PubMed:16648480). Cytoplasmic in interphase
(PubMed:16648480). Cytoplasmic in metaphase cells
(PubMed:16431929). From prophase to metaphase, accumulates at the
developing spindle poles and their associated microtubules. During
anaphase, accumulates at the spindle midzone. Localization to the
central spindle and midbody during anaphase is dependent upon PRC1
and CIT presence. In cells ready to undergo abscission,
concentrates at the contractile ring.
{ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:16648480}.
-!- INDUCTION: Up-regulated in cells progressing through G2/M phase.
{ECO:0000269|PubMed:16648480}.
-!- DOMAIN: The kinesin motor domain binds to microtubules with high
affinity and has a robust ATPase activity but a very slow
motility. The kinesin motor domain protects microtubules from cold
depolymerization. Binds to each tubulin heterodimer resulting in a
microtubule complexes. Binds at the tubulin intradimer interface,
at the crest of the protofilament, and orients slightly toward the
next protofilament. {ECO:0000250|UniProtKB:L0N7N1}.
-!- DISEASE: Meckel syndrome 12 (MKS12) [MIM:616258]: A form of Meckel
syndrome, a disorder characterized by a combination of renal cysts
and variably associated features including developmental anomalies
of the central nervous system (typically encephalocele), hepatic
ductal dysplasia and cysts, and polydactyly.
{ECO:0000269|PubMed:24128419}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: It is resistant to docetaxel anhydrous.
{ECO:0000269|PubMed:24784001}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
-!- SEQUENCE CAUTION:
Sequence=BAA05392.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KIF14ID44138ch1q32.html";
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EMBL; D26361; BAA05392.2; ALT_INIT; mRNA.
EMBL; AL445483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91316.1; -; Genomic_DNA.
EMBL; BC098582; AAH98582.1; -; mRNA.
EMBL; BC113742; AAI13743.1; -; mRNA.
CCDS; CCDS30963.1; -.
RefSeq; NP_001292721.1; NM_001305792.1.
RefSeq; NP_055690.1; NM_014875.2.
RefSeq; XP_011508533.1; XM_011510231.2.
RefSeq; XP_011508534.1; XM_011510232.2.
RefSeq; XP_016858494.1; XM_017003005.1.
UniGene; Hs.3104; -.
ProteinModelPortal; Q15058; -.
SMR; Q15058; -.
BioGrid; 115256; 73.
IntAct; Q15058; 39.
MINT; MINT-4989440; -.
STRING; 9606.ENSP00000356319; -.
BindingDB; Q15058; -.
ChEMBL; CHEMBL5576; -.
iPTMnet; Q15058; -.
PhosphoSitePlus; Q15058; -.
BioMuta; KIF14; -.
DMDM; 23396633; -.
EPD; Q15058; -.
MaxQB; Q15058; -.
PaxDb; Q15058; -.
PeptideAtlas; Q15058; -.
PRIDE; Q15058; -.
DNASU; 9928; -.
Ensembl; ENST00000367350; ENSP00000356319; ENSG00000118193.
Ensembl; ENST00000614960; ENSP00000483069; ENSG00000118193.
GeneID; 9928; -.
KEGG; hsa:9928; -.
UCSC; uc010ppk.2; human.
CTD; 9928; -.
DisGeNET; 9928; -.
EuPathDB; HostDB:ENSG00000118193.11; -.
GeneCards; KIF14; -.
HGNC; HGNC:19181; KIF14.
HPA; HPA038061; -.
HPA; HPA058220; -.
MalaCards; KIF14; -.
MIM; 611279; gene.
MIM; 616258; phenotype.
neXtProt; NX_Q15058; -.
OpenTargets; ENSG00000118193; -.
PharmGKB; PA38820; -.
eggNOG; KOG0245; Eukaryota.
eggNOG; COG5059; LUCA.
GeneTree; ENSGT00890000139327; -.
HOGENOM; HOG000113224; -.
HOVERGEN; HBG052249; -.
InParanoid; Q15058; -.
KO; K17915; -.
OMA; CSDISSM; -.
OrthoDB; EOG091G0159; -.
PhylomeDB; Q15058; -.
TreeFam; TF105221; -.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
GeneWiki; KIF14; -.
GenomeRNAi; 9928; -.
PRO; PR:Q15058; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000118193; -.
CleanEx; HS_KIF14; -.
Genevisible; Q15058; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:MGI.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0008574; F:ATP-dependent microtubule motor activity, plus-end-directed; ISS:UniProtKB.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IMP:UniProtKB.
GO; GO:0051301; P:cell division; IEA:Ensembl.
GO; GO:0021846; P:cell proliferation in forebrain; ISS:UniProtKB.
GO; GO:0021695; P:cerebellar cortex development; ISS:UniProtKB.
GO; GO:0021685; P:cerebellar granular layer structural organization; ISS:UniProtKB.
GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; ISS:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
GO; GO:0045184; P:establishment of protein localization; IDA:MGI.
GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0033624; P:negative regulation of integrin activation; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
GO; GO:1903429; P:regulation of cell maturation; IEA:Ensembl.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0032487; P:regulation of Rap protein signal transduction; IMP:MGI.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
CDD; cd00060; FHA; 1.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR032405; Kinesin_assoc.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008984; SMAD_FHA_domain.
PANTHER; PTHR24115; PTHR24115; 1.
Pfam; PF00498; FHA; 1.
Pfam; PF00225; Kinesin; 1.
Pfam; PF16183; Kinesin_assoc; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00240; FHA; 1.
SMART; SM00129; KISc; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
1: Evidence at protein level;
ATP-binding; Ciliopathy; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Meckel syndrome; Microtubule; Motor protein;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 1648 Kinesin-like protein KIF14.
/FTId=PRO_0000125449.
DOMAIN 358 701 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
DOMAIN 825 891 FHA.
NP_BIND 447 454 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
REGION 1 356 Required for PRC1-binding.
REGION 356 737 Required for microtubule-binding with
high affinity.
{ECO:0000250|UniProtKB:L0N7N1}.
REGION 901 1648 Required for CIT-binding.
COILED 705 791 {ECO:0000255}.
COILED 922 1079 {ECO:0000255}.
COILED 1332 1348 {ECO:0000255}.
COILED 1468 1500 {ECO:0000255}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 277 277 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 915 915 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 937 937 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1292 1292 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
VARIANT 1633 1633 P -> A (in dbSNP:rs12120084).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037777.
CONFLICT 660 660 W -> C (in Ref. 4; AAH98582).
{ECO:0000305}.
SEQUENCE 1648 AA; 186492 MW; FB1423668A7B79D7 CRC64;
MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND DPLLRSAGKV
RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES SLLVSELEDT TEKTAETRLT
LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE TENNGVSKES RTNVRIVNNA KNSFVASSVP
LDEDPQVIEM MADKKYKETF SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT
QSKLDIKVLG TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA
PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD PLKVENSQVT
VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN FIYDVSFWSF DECHPHYASQ
TTVYEKLAAP LLERAFEGFN TCLFAYGQTG SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR
KQTQEVSYHI EMSFFEVYNE KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS
SYADIQSWLE LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN
LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF IPYRESVLTW
LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL IVNIAKVNED MNAKLIRELK
AEIAKLKAAQ RNSRNIDPER YRLCRQEITS LRMKLHQQER DMAEMQRVWK EKFEQAEKRK
LQETKELQKA GIMFQMDNHL PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL
SGVLIADDHC TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH
PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA KEEMMQGIQI
AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN NQKANHKIEE LEKAKQHLEQ
EIYVNKKRLE METLATKQAL EDHSIRHARI LEALETEKQK IAKEVQILQQ NRNNRDKTFT
VQTTWSSMKL SMMIQEANAI SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL
EKFESKLAAM KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS
GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL DFFGQSYDEE
RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD RAIQSLTIQT ACAFEQLVVL
MKHWLSDLLP CTNIARLEDE LRQEVKKLGG YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ
AVKYVGQLAV LKGSKLHFLE NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ
HELFRQCTKN EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA
PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS VPSTSVGSYE
SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN TKEEHQQSKS SGIDGSKNKG
VPKRVYELHG SSPAVSSEEC TPSRIQWV


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