Reviewed, UniProtKB/Swiss-Prot Q15058 (KIF14_HUMAN)

Names and origin

Protein names

Recommended name:
    Kinesin-like protein KIF14

Gene names

Name:	KIF14
Synonyms:	KIAA0042

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1648 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays an essential role in cytokinesis. Ref.5 Ref.6
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). Ref.5
Subcellular location	Nucleus. Cytoplasm. Spindle. Note: Nuclear localization observed during interphase in Ref.5 or triggered by entry into mitosis in Ref.6. Cytoplasmic in interphase (Ref.6) and metaphase cells (Ref.5). 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.5 Ref.6
Developmental stage	Up-regulated in cells progressing through G2/M phase. Ref.6
Sequence similarities	Belongs to the kinesin-like protein family. Contains 1 FHA domain. Contains 1 kinesin-motor domain.

Ontologies

Keywords
Cellular component	Cytoplasm Microtubule Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	microtubule-based movement Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1648	1648	Kinesin-like protein KIF14		PRO_0000125449
Regions
	Domain	355 – 628	274	Kinesin-motor
	Domain	825 – 891	67	FHA
	Nucleotide binding	447 – 454	8	ATP By similarity
	Region	1 – 356	356	Required for PRC1-binding
	Region	901 – 1648	748	Required for CIT-binding
	Coiled coil	705 – 791	87	Potential
	Coiled coil	922 – 1079	158	Potential
	Coiled coil	1332 – 1348	17	Potential
	Coiled coil	1468 – 1500	33	Potential
Amino acid modifications
	Modified residue	196	1	Phosphotyrosine Ref.7
	Modified residue	1200	1	Phosphoserine Ref.7
	Modified residue	1292	1	Phosphoserine Ref.7
	Cross-link	275		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Natural variations
	Natural variant	1633	1	P → A: dbSNP rs12120084. Ref.4		VAR_037777
Experimental info
	Sequence conflict	660	1	W → C in AAH98582. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q15058-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: FB1423668A7B79D7	FASTA	1,648	186,492
	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

References

	« Hide 'large scale' referencesShow '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: 7584044] [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: 16710414] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-1633. Tissue: Uterus.
[5]	"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: 16431929] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRC1 AND CIT.
[6]	"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: 16648480] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196; SER-1200 AND SER-1292, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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: 17203973] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-275, MASS SPECTROMETRY. Tissue: Lung adenocarcinoma.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00299554.
RefSeq	NP_055690.1.
UniGene	Hs.3104
3D structure databases
HSSP	HSSP built from PDB template 1I6I based on UniProtKB P33173.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15058. 2 interactions.
PTM databases
PhosphoSite	Q15058.
Proteomic databases
PRIDE	Q15058.
Genome annotation databases
Ensembl	ENSG00000118193. Homo sapiens. [Contig view]
GeneID	9928.
KEGG	hsa:9928.
Organism-specific databases
GeneCards	GC01M198787.
HGNC	HGNC:19181. KIF14.
MIM	611279. gene.
PharmGKB	PA38820.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q15058.
OMA	Q15058. KMQEINN.
Gene expression databases
ArrayExpress	Q15058.
Bgee	Q15058.
CleanEx	HS_KIF14.
GermOnline	ENSG00000118193. Homo sapiens.
Family and domain databases
InterPro	IPR000253. FHA. IPR001752. Kinesin_motor. IPR019821. Kinesin_motor_CS. [Graphical view]
Pfam	PF00498. FHA. 1 hit. PF00225. Kinesin. 1 hit. [Graphical view]
PRINTS	PR00380. KINESINHEAVY.
SMART	SM00240. FHA. 1 hit. SM00129. KISc. 1 hit. [Graphical view]
PROSITE	PS50006. FHA_DOMAIN. False negative. PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit. PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	37458.
SOURCE	Search...

Entry information

Entry name

KIF14_HUMAN

Accession

Primary (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:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)