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Q15058 (KIF14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF14
Gene names
Name:KIF14
Synonyms:KIAA0042
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1648 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in cytokinesis. Ref.6 Ref.8

Subunit structure

Directly interacts with PRC1 within a complex also containing KIF4A, KIF20A and KIF23. Directly interacts with CIT depending on the activation state of the kinase (stronger interaction with the kinase-dead form). Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Ref.6 Ref.7

Subcellular location

Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle. Note: Nuclear localization observed during interphase in Ref.6 or triggered by entry into mitosis in Ref.8. Cytoplasmic in interphase (Ref.8) and metaphase cells (Ref.6). 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. Ref.6 Ref.8

Developmental stage

Up-regulated in cells progressing through G2/M phase. Ref.8

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.

Contains 1 FHA domain.

Contains 1 kinesin motor domain.

Sequence caution

The sequence BAA05392.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processestablishment of protein localization

Inferred from direct assay PubMed 23209302. Source: MGI

microtubule-based movement

Inferred from electronic annotation. Source: InterPro

negative regulation of integrin activation

Inferred from mutant phenotype PubMed 23209302. Source: MGI

regulation of Rap protein signal transduction

Inferred from mutant phenotype PubMed 23209302. Source: MGI

regulation of cell adhesion

Inferred from mutant phenotype PubMed 23209302. Source: MGI

regulation of cell migration

Inferred from mutant phenotype PubMed 23209302. Source: MGI

substrate adhesion-dependent cell spreading

Inferred from direct assay PubMed 23209302. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from direct assay PubMed 23209302. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

PDZ domain binding

Inferred from direct assay PubMed 23209302. Source: MGI

microtubule motor activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SVILO463853EBI-1045252,EBI-6995105From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16481648Kinesin-like protein KIF14
PRO_0000125449

Regions

Domain358 – 701344Kinesin motor
Domain825 – 89167FHA
Nucleotide binding447 – 4548ATP By similarity
Region1 – 356356Required for PRC1-binding
Region901 – 1648748Required for CIT-binding
Coiled coil705 – 79187 Potential
Coiled coil922 – 1079158 Potential
Coiled coil1332 – 134817 Potential
Coiled coil1468 – 150033 Potential

Amino acid modifications

Modified residue121Phosphoserine Ref.11
Modified residue12921Phosphoserine Ref.5
Cross-link275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Natural variant16331P → A. Ref.4
Corresponds to variant rs12120084 [ dbSNP | Ensembl ].
VAR_037777

Experimental info

Sequence conflict6601W → C in AAH98582. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q15058 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FB1423668A7B79D7

FASTA1,648186,492
        10         20         30         40         50         60 
MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND DPLLRSAGKV 

        70         80         90        100        110        120 
RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES SLLVSELEDT TEKTAETRLT 

       130        140        150        160        170        180 
LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE TENNGVSKES RTNVRIVNNA KNSFVASSVP 

       190        200        210        220        230        240 
LDEDPQVIEM MADKKYKETF SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT 

       250        260        270        280        290        300 
QSKLDIKVLG TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA 

       310        320        330        340        350        360 
PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD PLKVENSQVT 

       370        380        390        400        410        420 
VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN FIYDVSFWSF DECHPHYASQ 

       430        440        450        460        470        480 
TTVYEKLAAP LLERAFEGFN TCLFAYGQTG SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR 

       490        500        510        520        530        540 
KQTQEVSYHI EMSFFEVYNE KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS 

       550        560        570        580        590        600 
SYADIQSWLE LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN 

       610        620        630        640        650        660 
LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF IPYRESVLTW 

       670        680        690        700        710        720 
LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL IVNIAKVNED MNAKLIRELK 

       730        740        750        760        770        780 
AEIAKLKAAQ RNSRNIDPER YRLCRQEITS LRMKLHQQER DMAEMQRVWK EKFEQAEKRK 

       790        800        810        820        830        840 
LQETKELQKA GIMFQMDNHL PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL 

       850        860        870        880        890        900 
SGVLIADDHC TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH 

       910        920        930        940        950        960 
PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA KEEMMQGIQI 

       970        980        990       1000       1010       1020 
AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN NQKANHKIEE LEKAKQHLEQ 

      1030       1040       1050       1060       1070       1080 
EIYVNKKRLE METLATKQAL EDHSIRHARI LEALETEKQK IAKEVQILQQ NRNNRDKTFT 

      1090       1100       1110       1120       1130       1140 
VQTTWSSMKL SMMIQEANAI SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL 

      1150       1160       1170       1180       1190       1200 
EKFESKLAAM KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS 

      1210       1220       1230       1240       1250       1260 
GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL DFFGQSYDEE 

      1270       1280       1290       1300       1310       1320 
RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD RAIQSLTIQT ACAFEQLVVL 

      1330       1340       1350       1360       1370       1380 
MKHWLSDLLP CTNIARLEDE LRQEVKKLGG YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ 

      1390       1400       1410       1420       1430       1440 
AVKYVGQLAV LKGSKLHFLE NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ 

      1450       1460       1470       1480       1490       1500 
HELFRQCTKN EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA 

      1510       1520       1530       1540       1550       1560 
PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS VPSTSVGSYE 

      1570       1580       1590       1600       1610       1620 
SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN TKEEHQQSKS SGIDGSKNKG 

      1630       1640 
VPKRVYELHG SSPAVSSEEC TPSRIQWV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"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.
[6]"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.
[7]"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.
[8]"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, DEVELOPMENTAL STAGE.
[9]"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.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS30963.1.
RefSeqNP_055690.1. NM_014875.2.
UniGeneHs.3104.

3D structure databases

ProteinModelPortalQ15058.
SMRQ15058. Positions 357-699, 777-906.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115256. 7 interactions.
IntActQ15058. 3 interactions.
MINTMINT-4989440.
STRING9606.ENSP00000356319.

Chemistry

BindingDBQ15058.
ChEMBLCHEMBL5576.

PTM databases

PhosphoSiteQ15058.

Polymorphism databases

DMDM23396633.

Proteomic databases

MaxQBQ15058.
PaxDbQ15058.
PRIDEQ15058.

Protocols and materials databases

DNASU9928.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367350; ENSP00000356319; ENSG00000118193.
GeneID9928.
KEGGhsa:9928.
UCSCuc010ppj.1. human.

Organism-specific databases

CTD9928.
GeneCardsGC01M200521.
HGNCHGNC:19181. KIF14.
HPAHPA038061.
MIM611279. gene.
neXtProtNX_Q15058.
PharmGKBPA38820.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000113224.
HOVERGENHBG052249.
InParanoidQ15058.
KOK17915.
OMAFLQGCCS.
OrthoDBEOG74TWXS.
PhylomeDBQ15058.
TreeFamTF105221.

Gene expression databases

BgeeQ15058.
CleanExHS_KIF14.
GenevestigatorQ15058.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProIPR000253. FHA_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PfamPF00498. FHA. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKIF14.
GenomeRNAi9928.
NextBio37458.
PROQ15058.
SOURCESearch...

Entry information

Entry nameKIF14_HUMAN
AccessionPrimary (citable) accession number: Q15058
Secondary accession number(s): Q14CI8, Q4G0A5, Q5T1W3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM