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Q15058

- KIF14_HUMAN

UniProt

Q15058 - KIF14_HUMAN

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Protein

Kinesin-like protein KIF14

Gene

KIF14

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

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. ATPase activity Source: RefGenome
  2. ATP binding Source: UniProtKB-KW
  3. microtubule motor activity Source: RefGenome
  4. PDZ domain binding Source: MGI

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cytoskeleton-dependent intracellular transport Source: RefGenome
  3. establishment of protein localization Source: MGI
  4. metabolic process Source: GOC
  5. microtubule-based movement Source: RefGenome
  6. negative regulation of integrin activation Source: MGI
  7. regulation of cell adhesion Source: MGI
  8. regulation of cell migration Source: MGI
  9. regulation of Rap protein signal transduction Source: MGI
  10. substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

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-KW
  2. kinesin complex Source: RefGenome
  3. membrane Source: UniProtKB
  4. microtubule Source: MGI
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

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. 15 interactions.
IntActiQ15058. 3 interactions.
MINTiMINT-4989440.
STRINGi9606.ENSP00000356319.

Structurei

3D structure databases

ProteinModelPortaliQ15058.
SMRiQ15058. Positions 357-725, 754-906.
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.
GeneTreeiENSGT00760000118802.
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.

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.
ENST00000614960; ENSP00000483069; 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 357-725, 754-906.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115256. 15 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 .
ENST00000614960 ; ENSP00000483069 ; 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.
GeneTreei ENSGT00760000118802.
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

« 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. "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 29, 2014
This is version 129 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