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Protein

Kinesin-like protein KIF14

Gene

KIF14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi447 – 4548ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • activation of protein kinase activity Source: UniProtKB
  • cell proliferation in forebrain Source: UniProtKB
  • cerebellar cortex development Source: UniProtKB
  • cerebellar granular layer structural organization Source: UniProtKB
  • cerebellar Purkinje cell layer structural organization Source: UniProtKB
  • cerebral cortex development Source: UniProtKB
  • cytoskeleton-dependent intracellular transport Source: GO_Central
  • establishment of protein localization Source: MGI
  • hippocampus development Source: UniProtKB
  • microtubule-based movement Source: GO_Central
  • mitotic cell cycle process Source: UniProtKB
  • mitotic metaphase plate congression Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of integrin activation Source: MGI
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • olfactory bulb development Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of cytokinesis Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • regulation of cell adhesion Source: MGI
  • regulation of cell growth Source: UniProtKB
  • regulation of cell migration Source: MGI
  • regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
  • regulation of myelination Source: UniProtKB
  • regulation of neuron apoptotic process Source: UniProtKB
  • regulation of Rap protein signal transduction Source: MGI
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • small GTPase mediated signal transduction Source: Reactome
  • substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_355303. RHO GTPases activate CIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF14Curated
Gene namesi
Name:KIF14Imported
Synonyms:KIAA0042Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:19181. KIF14.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • kinesin complex Source: GO_Central
  • membrane Source: UniProtKB
  • microtubule Source: MGI
  • midbody Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • spindle midzone Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

Meckel syndrome 12 (MKS12)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:616258

Keywords - Diseasei

Ciliopathy, Meckel syndrome

Organism-specific databases

MIMi616258. phenotype.
PharmGKBiPA38820.

Polymorphism and mutation databases

BioMutaiKIF14.
DMDMi23396633.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16481648Kinesin-like protein KIF14PRO_0000125449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication
Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1292 – 12921Phosphoserine1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15058.
PaxDbiQ15058.
PRIDEiQ15058.

PTM databases

PhosphoSiteiQ15058.

Expressioni

Inductioni

Up-regulated in cells progressing through G2/M phase.1 Publication

Gene expression databases

BgeeiQ15058.
CleanExiHS_KIF14.
GenevisibleiQ15058. HS.

Organism-specific databases

HPAiHPA038061.

Interactioni

Subunit structurei

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).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SVILO463853EBI-1045252,EBI-6995105From a different organism.

Protein-protein interaction databases

BioGridi115256. 18 interactions.
IntActiQ15058. 3 interactions.
MINTiMINT-4989440.
STRINGi9606.ENSP00000356319.

Structurei

3D structure databases

ProteinModelPortaliQ15058.
SMRiQ15058. Positions 355-699.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini358 – 701344Kinesin motorPROSITE-ProRule annotationAdd
BLAST
Domaini825 – 89167FHAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 356356Required for PRC1-bindingAdd
BLAST
Regioni356 – 737382Required for microtubule-binding with high affinityBy similarityAdd
BLAST
Regioni901 – 1648748Required for CIT-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili705 – 79187Sequence AnalysisAdd
BLAST
Coiled coili922 – 1079158Sequence AnalysisAdd
BLAST
Coiled coili1332 – 134817Sequence AnalysisAdd
BLAST
Coiled coili1468 – 150033Sequence AnalysisAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
Contains 1 FHA domain.Curated
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00770000120451.
HOGENOMiHOG000113224.
HOVERGENiHBG052249.
InParanoidiQ15058.
KOiK17915.
OMAiFLQGCCS.
OrthoDBiEOG74TWXS.
PhylomeDBiQ15058.
TreeFamiTF105221.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00498. FHA. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15058-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND
60 70 80 90 100
DPLLRSAGKV RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES
110 120 130 140 150
SLLVSELEDT TEKTAETRLT LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE
160 170 180 190 200
TENNGVSKES RTNVRIVNNA KNSFVASSVP LDEDPQVIEM MADKKYKETF
210 220 230 240 250
SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT QSKLDIKVLG
260 270 280 290 300
TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA
310 320 330 340 350
PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD
360 370 380 390 400
PLKVENSQVT VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN
410 420 430 440 450
FIYDVSFWSF DECHPHYASQ TTVYEKLAAP LLERAFEGFN TCLFAYGQTG
460 470 480 490 500
SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR KQTQEVSYHI EMSFFEVYNE
510 520 530 540 550
KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS SYADIQSWLE
560 570 580 590 600
LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN
610 620 630 640 650
LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF
660 670 680 690 700
IPYRESVLTW LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL
710 720 730 740 750
IVNIAKVNED MNAKLIRELK AEIAKLKAAQ RNSRNIDPER YRLCRQEITS
760 770 780 790 800
LRMKLHQQER DMAEMQRVWK EKFEQAEKRK LQETKELQKA GIMFQMDNHL
810 820 830 840 850
PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL SGVLIADDHC
860 870 880 890 900
TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH
910 920 930 940 950
PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA
960 970 980 990 1000
KEEMMQGIQI AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN
1010 1020 1030 1040 1050
NQKANHKIEE LEKAKQHLEQ EIYVNKKRLE METLATKQAL EDHSIRHARI
1060 1070 1080 1090 1100
LEALETEKQK IAKEVQILQQ NRNNRDKTFT VQTTWSSMKL SMMIQEANAI
1110 1120 1130 1140 1150
SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL EKFESKLAAM
1160 1170 1180 1190 1200
KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS
1210 1220 1230 1240 1250
GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL
1260 1270 1280 1290 1300
DFFGQSYDEE RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD
1310 1320 1330 1340 1350
RAIQSLTIQT ACAFEQLVVL MKHWLSDLLP CTNIARLEDE LRQEVKKLGG
1360 1370 1380 1390 1400
YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ AVKYVGQLAV LKGSKLHFLE
1410 1420 1430 1440 1450
NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ HELFRQCTKN
1460 1470 1480 1490 1500
EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA
1510 1520 1530 1540 1550
PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS
1560 1570 1580 1590 1600
VPSTSVGSYE SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN
1610 1620 1630 1640
TKEEHQQSKS SGIDGSKNKG VPKRVYELHG SSPAVSSEEC TPSRIQWV
Length:1,648
Mass (Da):186,492
Last modified:November 1, 1996 - v1
Checksum:iFB1423668A7B79D7
GO

Sequence cautioni

The sequence BAA05392.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti660 – 6601W → C in AAH98582 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1633 – 16331P → A.1 Publication
Corresponds to variant rs12120084 [ dbSNP | Ensembl ].
VAR_037777

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26361 mRNA. Translation: BAA05392.2. Different initiation.
AL445483 Genomic DNA. Translation: CAI17049.1.
CH471067 Genomic DNA. Translation: EAW91316.1.
BC098582 mRNA. Translation: AAH98582.1.
BC113742 mRNA. Translation: AAI13743.1.
CCDSiCCDS30963.1.
RefSeqiNP_055690.1. NM_014875.2.
UniGeneiHs.3104.

Genome annotation databases

EnsembliENST00000367350; ENSP00000356319; ENSG00000118193.
ENST00000614960; ENSP00000483069; ENSG00000118193.
GeneIDi9928.
KEGGihsa:9928.
UCSCiuc010ppj.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26361 mRNA. Translation: BAA05392.2. Different initiation.
AL445483 Genomic DNA. Translation: CAI17049.1.
CH471067 Genomic DNA. Translation: EAW91316.1.
BC098582 mRNA. Translation: AAH98582.1.
BC113742 mRNA. Translation: AAI13743.1.
CCDSiCCDS30963.1.
RefSeqiNP_055690.1. NM_014875.2.
UniGeneiHs.3104.

3D structure databases

ProteinModelPortaliQ15058.
SMRiQ15058. Positions 355-699.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115256. 18 interactions.
IntActiQ15058. 3 interactions.
MINTiMINT-4989440.
STRINGi9606.ENSP00000356319.

Chemistry

BindingDBiQ15058.
ChEMBLiCHEMBL5576.

PTM databases

PhosphoSiteiQ15058.

Polymorphism and mutation databases

BioMutaiKIF14.
DMDMi23396633.

Proteomic databases

MaxQBiQ15058.
PaxDbiQ15058.
PRIDEiQ15058.

Protocols and materials databases

DNASUi9928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367350; ENSP00000356319; ENSG00000118193.
ENST00000614960; ENSP00000483069; ENSG00000118193.
GeneIDi9928.
KEGGihsa:9928.
UCSCiuc010ppj.1. human.

Organism-specific databases

CTDi9928.
GeneCardsiGC01M200521.
HGNCiHGNC:19181. KIF14.
HPAiHPA038061.
MIMi611279. gene.
616258. phenotype.
neXtProtiNX_Q15058.
PharmGKBiPA38820.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00770000120451.
HOGENOMiHOG000113224.
HOVERGENiHBG052249.
InParanoidiQ15058.
KOiK17915.
OMAiFLQGCCS.
OrthoDBiEOG74TWXS.
PhylomeDBiQ15058.
TreeFamiTF105221.

Enzyme and pathway databases

ReactomeiREACT_355303. RHO GTPases activate CIT.

Miscellaneous databases

GeneWikiiKIF14.
GenomeRNAii9928.
NextBioi37458.
PROiQ15058.
SOURCEiSearch...

Gene expression databases

BgeeiQ15058.
CleanExiHS_KIF14.
GenevisibleiQ15058. HS.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00498. FHA. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-1633.
    Tissue: Uterus.
  5. "Functional analysis of human microtubule-based motor proteins, the kinesins and dyneins, in mitosis/cytokinesis using RNA interference."
    Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B., Abraham R.T., Jiang W.
    Mol. Biol. Cell 16:3187-3199(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "KIF14 and citron kinase act together to promote efficient cytokinesis."
    Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B., Nigg E.A., Barr F.A.
    J. Cell Biol. 172:363-372(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRC1 AND CIT.
  8. "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
    Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
    J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2.
  9. "RNA interference-mediated silencing of mitotic kinesin KIF14 disrupts cell cycle progression and induces cytokinesis failure."
    Carleton M., Mao M., Biery M., Warrener P., Kim S., Buser C., Marshall C.G., Fernandes C., Annis J., Linsley P.S.
    Mol. Cell. Biol. 26:3853-3863(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  10. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
    Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
    J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-275.
    Tissue: Lung adenocarcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Novel interactors and a role for supervillin in early cytokinesis."
    Smith T.C., Fang Z., Luna E.J.
    Cytoskeleton 67:346-364(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SVIL, SUBCELLULAR LOCATION.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "KIF14 negatively regulates Rap1a-Radil signaling during breast cancer progression."
    Ahmed S.M., Theriault B.L., Uppalapati M., Chiu C.W., Gallie B.L., Sidhu S.S., Angers S.
    J. Cell Biol. 199:951-967(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RADIL.
  16. "Silencing of KIF14 interferes with cell cycle progression and cytokinesis by blocking the p27(Kip1) ubiquitination pathway in hepatocellular carcinoma."
    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.
    Exp. Mol. Med. 46:E97-E97(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "KIF14 promotes AKT phosphorylation and contributes to chemoresistance in triple-negative breast cancer."
    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.
    Neoplasia 16:247-256(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AKT1.
  18. "Exome sequencing identifies mutations in KIF14 as a novel cause of an autosomal recessive lethal fetal ciliopathy phenotype."
    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.
    Clin. Genet. 86:220-228(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MKS12.

Entry informationi

Entry nameiKIF14_HUMAN
AccessioniPrimary (citable) accession number: Q15058
Secondary accession number(s): Q14CI8, Q4G0A5, Q5T1W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

It is resistant to docetaxel anhydrous.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.