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Q15058

- KIF14_HUMAN

UniProt

Q15058 - KIF14_HUMAN

Protein

Kinesin-like protein KIF14

Gene

KIF14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Plays an essential role in cytokinesis.2 Publications

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule motor activity Source: InterPro
    3. PDZ domain binding Source: MGI
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. establishment of protein localization Source: MGI
    2. microtubule-based movement Source: InterPro
    3. negative regulation of integrin activation Source: MGI
    4. regulation of cell adhesion Source: MGI
    5. regulation of cell migration Source: MGI
    6. regulation of Rap protein signal transduction Source: MGI
    7. substrate adhesion-dependent cell spreading Source: MGI

    Keywords - Molecular functioni

    Motor protein

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin-like protein KIF14
    Gene namesi
    Name:KIF14
    Synonyms:KIAA0042
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19181. KIF14.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle
    Note: Nuclear localization observed during interphase in PubMed:16431929 or triggered by entry into mitosis in PubMed:16648480. Cytoplasmic in interphase (PubMed:16648480) and 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.2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. kinesin complex Source: InterPro
    3. membrane Source: UniProtKB
    4. microtubule Source: MGI
    5. nucleus Source: UniProtKB-SubCell
    6. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38820.

    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

    Developmental stagei

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

    Gene expression databases

    BgeeiQ15058.
    CleanExiHS_KIF14.
    GenevestigatoriQ15058.

    Organism-specific databases

    HPAiHPA038061.

    Interactioni

    Subunit structurei

    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.2 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi115256. 7 interactions.
    IntActiQ15058. 3 interactions.
    MINTiMINT-4989440.
    STRINGi9606.ENSP00000356319.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15058.
    SMRiQ15058. Positions 357-699, 777-906.
    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
    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

    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.
    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

    MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND     50
    DPLLRSAGKV RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES 100
    SLLVSELEDT TEKTAETRLT LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE 150
    TENNGVSKES RTNVRIVNNA KNSFVASSVP LDEDPQVIEM MADKKYKETF 200
    SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT QSKLDIKVLG 250
    TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA 300
    PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD 350
    PLKVENSQVT VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN 400
    FIYDVSFWSF DECHPHYASQ TTVYEKLAAP LLERAFEGFN TCLFAYGQTG 450
    SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR KQTQEVSYHI EMSFFEVYNE 500
    KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS SYADIQSWLE 550
    LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN 600
    LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF 650
    IPYRESVLTW LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL 700
    IVNIAKVNED MNAKLIRELK AEIAKLKAAQ RNSRNIDPER YRLCRQEITS 750
    LRMKLHQQER DMAEMQRVWK EKFEQAEKRK LQETKELQKA GIMFQMDNHL 800
    PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL SGVLIADDHC 850
    TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH 900
    PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA 950
    KEEMMQGIQI AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN 1000
    NQKANHKIEE LEKAKQHLEQ EIYVNKKRLE METLATKQAL EDHSIRHARI 1050
    LEALETEKQK IAKEVQILQQ NRNNRDKTFT VQTTWSSMKL SMMIQEANAI 1100
    SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL EKFESKLAAM 1150
    KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS 1200
    GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL 1250
    DFFGQSYDEE RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD 1300
    RAIQSLTIQT ACAFEQLVVL MKHWLSDLLP CTNIARLEDE LRQEVKKLGG 1350
    YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ AVKYVGQLAV LKGSKLHFLE 1400
    NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ HELFRQCTKN 1450
    EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA 1500
    PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS 1550
    VPSTSVGSYE SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN 1600
    TKEEHQQSKS SGIDGSKNKG VPKRVYELHG SSPAVSSEEC TPSRIQWV 1648
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi9928.
    KEGGihsa:9928.
    UCSCiuc010ppj.1. human.

    Polymorphism databases

    DMDMi23396633.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS30963.1.
    RefSeqi NP_055690.1. NM_014875.2.
    UniGenei Hs.3104.

    3D structure databases

    ProteinModelPortali Q15058.
    SMRi Q15058. Positions 357-699, 777-906.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115256. 7 interactions.
    IntActi Q15058. 3 interactions.
    MINTi MINT-4989440.
    STRINGi 9606.ENSP00000356319.

    Chemistry

    BindingDBi Q15058.
    ChEMBLi CHEMBL5576.

    PTM databases

    PhosphoSitei Q15058.

    Polymorphism databases

    DMDMi 23396633.

    Proteomic databases

    MaxQBi Q15058.
    PaxDbi Q15058.
    PRIDEi Q15058.

    Protocols and materials databases

    DNASUi 9928.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367350 ; ENSP00000356319 ; ENSG00000118193 .
    GeneIDi 9928.
    KEGGi hsa:9928.
    UCSCi uc010ppj.1. human.

    Organism-specific databases

    CTDi 9928.
    GeneCardsi GC01M200521.
    HGNCi HGNC:19181. KIF14.
    HPAi HPA038061.
    MIMi 611279. gene.
    neXtProti NX_Q15058.
    PharmGKBi PA38820.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000113224.
    HOVERGENi HBG052249.
    InParanoidi Q15058.
    KOi K17915.
    OMAi FLQGCCS.
    OrthoDBi EOG74TWXS.
    PhylomeDBi Q15058.
    TreeFami TF105221.

    Miscellaneous databases

    GeneWikii KIF14.
    GenomeRNAii 9928.
    NextBioi 37458.
    PROi Q15058.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15058.
    CleanExi HS_KIF14.
    Genevestigatori Q15058.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    3.40.850.10. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    IPR008984. SMAD_FHA_domain.
    [Graphical view ]
    PANTHERi PTHR24115. PTHR24115. 1 hit.
    Pfami PF00498. FHA. 1 hit.
    PF00225. Kinesin. 1 hit.
    [Graphical view ]
    PRINTSi PR00380. KINESINHEAVY.
    SMARTi SM00240. FHA. 1 hit.
    SM00129. KISc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    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: October 1, 2014
    This is version 128 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

    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