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P52732 (KIF11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF11
Alternative name(s):
Kinesin-like protein 1
Kinesin-like spindle protein HKSP
Kinesin-related motor protein Eg5
Thyroid receptor-interacting protein 5
Short name=TR-interacting protein 5
Short name=TRIP-5
Gene names
Name:KIF11
Synonyms:EG5, KNSL1, TRIP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1056 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays. Ref.8

Subunit structure

Interacts with the thyroid hormone receptor in the presence of thyroid hormone. Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Interacts (via C-terminus) with the kinase NEK6 in both interphase and mitosis. Ref.8 Ref.15

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonspindle pole Ref.8.

Post-translational modification

Phosphorylated exclusively on serine during S phase, but on both serine and Thr-926 during mitosis, so controlling the association of KIF11 with the spindle apparatus (probably during early prophase). Ref.1 Ref.8

A subset of this protein primarily localized at the spindle pole is phosphorylated by NEK6 during mitosis; phosphorylation is required for mitotic function. Ref.1 Ref.8

Involvement in disease

Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR) [MIM:152950]: An autosomal dominant disorder that involves an overlapping but variable spectrum of central nervous system and ocular developmental anomalies. Microcephaly ranges from mild to severe and is often associated with mild to moderate developmental delay and a characteristic facial phenotype with upslanting palpebral fissures, broad nose with rounded tip, long philtrum with thin upper lip, prominent chin, and prominent ears. Chorioretinopathy is the most common eye abnormality, but retinal folds, microphthalmia, and myopic and hypermetropic astigmatism have also been reported, and some individuals have no overt ocular phenotype. Congenital lymphedema, when present, is typically confined to the dorsa of the feet, and lymphoscintigraphy reveals the absence of radioactive isotope uptake from the webspaces between the toes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

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

Contains 1 kinesin motor domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

metabolic process

Traceable author statement Ref.1. Source: GOC

microtubule-based movement

Traceable author statement. Source: Reactome

mitotic centrosome separation

Inferred from electronic annotation. Source: Ensembl

mitotic nuclear division

Traceable author statement Ref.1. Source: ProtInc

mitotic spindle organization

Traceable author statement Ref.1. Source: ProtInc

spindle assembly involved in mitosis

Inferred from direct assay Ref.8. Source: UniProtKB

spindle organization

Inferred from mutant phenotype PubMed 14718566. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinesin complex

Traceable author statement Ref.1. Source: ProtInc

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

spindle

Inferred from direct assay Ref.8. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule motor activity

Traceable author statement Ref.1. Source: ProtInc

protein complex binding

Inferred from direct assay Ref.15. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10561056Kinesin-like protein KIF11
PRO_0000125372

Regions

Domain18 – 359342Kinesin motor
Nucleotide binding105 – 1128ATP By similarity
Coiled coil364 – 480117 Potential
Coiled coil736 – 76328 Potential

Amino acid modifications

Modified residue1461N6-acetyllysine Ref.10
Modified residue4581Phosphothreonine Ref.7
Modified residue9261Phosphothreonine; by CDK1 Ref.1 Ref.8 Ref.11
Modified residue10331Phosphoserine; by NEK6 Ref.8

Natural variations

Natural variant1441F → L in MCLMR. Ref.16
VAR_067829
Natural variant2341R → C in MCLMR. Ref.16
VAR_067830
Natural variant2351S → C in MCLMR. Ref.16
VAR_067831
Natural variant9441R → C in MCLMR. Ref.16
VAR_067832
Natural variant10421L → F.
Corresponds to variant rs34417963 [ dbSNP | Ensembl ].
VAR_049682

Experimental info

Mutagenesis9261T → A: No mitotic phosphorylation. No binding to spindle apparatus. Ref.8
Mutagenesis10331S → A: Still binds to the mitotic spindle but mitotic progression is impaired. Ref.8
Mutagenesis10331S → D: Still binds to the mitotic spindle but mitotic progression is impaired. Ref.8
Sequence conflict674 – 6752EL → RNS in CAA59449. Ref.1

Secondary structure

........................................................................ 1056
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52732 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: C7F2606FE68DA8EA

FASTA1,056119,159
        10         20         30         40         50         60 
MASQPNSSAK KKEEKGKNIQ VVVRCRPFNL AERKASAHSI VECDPVRKEV SVRTGGLADK 

        70         80         90        100        110        120 
SSRKTYTFDM VFGASTKQID VYRSVVCPIL DEVIMGYNCT IFAYGQTGTG KTFTMEGERS 

       130        140        150        160        170        180 
PNEEYTWEED PLAGIIPRTL HQIFEKLTDN GTEFSVKVSL LEIYNEELFD LLNPSSDVSE 

       190        200        210        220        230        240 
RLQMFDDPRN KRGVIIKGLE EITVHNKDEV YQILEKGAAK RTTAATLMNA YSSRSHSVFS 

       250        260        270        280        290        300 
VTIHMKETTI DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT 

       310        320        330        340        350        360 
ALVERTPHVP YRESKLTRIL QDSLGGRTRT SIIATISPAS LNLEETLSTL EYAHRAKNIL 

       370        380        390        400        410        420 
NKPEVNQKLT KKALIKEYTE EIERLKRDLA AAREKNGVYI SEENFRVMSG KLTVQEEQIV 

       430        440        450        460        470        480 
ELIEKIGAVE EELNRVTELF MDNKNELDQC KSDLQNKTQE LETTQKHLQE TKLQLVKEEY 

       490        500        510        520        530        540 
ITSALESTEE KLHDAASKLL NTVEETTKDV SGLHSKLDRK KAVDQHNAEA QDIFGKNLNS 

       550        560        570        580        590        600 
LFNNMEELIK DGSSKQKAML EVHKTLFGNL LSSSVSALDT ITTVALGSLT SIPENVSTHV 

       610        620        630        640        650        660 
SQIFNMILKE QSLAAESKTV LQELINVLKT DLLSSLEMIL SPTVVSILKI NSQLKHIFKT 

       670        680        690        700        710        720 
SLTVADKIED QKKELDGFLS ILCNNLHELQ ENTICSLVES QKQCGNLTED LKTIKQTHSQ 

       730        740        750        760        770        780 
ELCKLMNLWT ERFCALEEKC ENIQKPLSSV QENIQQKSKD IVNKMTFHSQ KFCADSDGFS 

       790        800        810        820        830        840 
QELRNFNQEG TKLVEESVKH SDKLNGNLEK ISQETEQRCE SLNTRTVYFS EQWVSSLNER 

       850        860        870        880        890        900 
EQELHNLLEV VSQCCEASSS DITEKSDGRK AAHEKQHNIF LDQMTIDEDK LIAQNLELNE 

       910        920        930        940        950        960 
TIKIGLTKLN CFLEQDLKLD IPTGTTPQRK SYLYPSTLVR TEPREHLLDQ LKRKQPELLM 

       970        980        990       1000       1010       1020 
MLNCSENNKE ETIPDVDVEE AVLGQYTEEP LSQEPSVDAG VDCSSIGGVP FFQHKKSHGK 

      1030       1040       1050 
DKENRGINTL ERSKVEETTE HLVTKSRLPL RAQINL 

« Hide

References

« Hide 'large scale' references
[1]"Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo."
Blangy A., Lane H.A., D'Herin P., Harper M., Kress M., Nigg E.A.
Cell 83:1159-1169(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-926, MUTAGENESIS.
[2]"Expanding the role of HsEg5 within the mitotic and post-mitotic phases of the cell cycle."
Whitehead C.M., Rattner J.B.
J. Cell Sci. 111:2551-2561(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Lung.
[5]"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 818-867.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation."
Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C., Avruch J., Roig J.
J. Cell Sci. 121:3912-3921(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NEK6, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-926 AND SER-1033, MUTAGENESIS OF THR-926 AND SER-1033.
[9]"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.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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 THR-926, 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].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker."
Turner J., Anderson R., Guo J., Beraud C., Fletterick R., Sakowicz R.
J. Biol. Chem. 276:25496-25502(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-368.
[15]"A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation."
Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G.
Mol. Cell 27:609-621(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
[16]"Mutations in KIF11 cause autosomal-dominant microcephaly variably associated with congenital lymphedema and chorioretinopathy."
Ostergaard P., Simpson M.A., Mendola A., Vasudevan P., Connell F.C., van Impel A., Moore A.T., Loeys B.L., Ghalamkarpour A., Onoufriadis A., Martinez-Corral I., Devery S., Leroy J.G., van Laer L., Singer A., Bialer M.G., McEntagart M., Quarrell O. expand/collapse author list , Brice G., Trembath R.C., Schulte-Merker S., Makinen T., Vikkula M., Mortimer P.S., Mansour S., Jeffery S.
Am. J. Hum. Genet. 90:356-362(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MCLMR LEU-144; CYS-234; CYS-235 AND CYS-944.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85137 mRNA. Translation: CAA59449.1.
U37426 mRNA. Translation: AAA86132.1.
AL360222, AL356128 Genomic DNA. Translation: CAH72288.1.
AL356128, AL360222 Genomic DNA. Translation: CAI13671.1.
BC126211 mRNA. Translation: AAI26212.1.
BC136474 mRNA. Translation: AAI36475.1.
L40372 mRNA. Translation: AAC41739.1.
CCDSCCDS7422.1.
PIRG02157.
RefSeqNP_004514.2. NM_004523.3.
UniGeneHs.8878.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1II6X-ray2.10A/B1-368[»]
1Q0BX-ray1.90A/B2-368[»]
1X88X-ray1.80A/B10-368[»]
1YRSX-ray2.50A/B1-368[»]
2FKYX-ray2.30A/B2-368[»]
2FL2X-ray2.50A/B2-368[»]
2FL6X-ray2.50A/B2-368[»]
2FMEX-ray2.10A/B1-368[»]
2G1QX-ray2.51A/B1-368[»]
2GM1X-ray2.30A/B/D/E1-368[»]
2IEHX-ray2.70A/B2-368[»]
2PG2X-ray1.85A/B1-368[»]
2Q2YX-ray2.50A/B2-368[»]
2Q2ZX-ray3.00A/B2-368[»]
2UYIX-ray2.10A/B1-368[»]
2UYMX-ray2.11A/B1-368[»]
2WOGX-ray2.00A/B/C1-368[»]
2X2RX-ray2.20A/B/C1-368[»]
2X7CX-ray1.90A/B1-368[»]
2X7DX-ray2.30A/B1-368[»]
2X7EX-ray2.40A/B1-368[»]
2XAEX-ray2.60A/B/C1-368[»]
3CJOX-ray2.28A/B2-368[»]
3HQDX-ray2.19A/B1-369[»]
3K3BX-ray2.40A/B1-368[»]
3K5EX-ray1.97A/B1-368[»]
3KENX-ray2.50A1-369[»]
3L9HX-ray2.00A/B1-368[»]
3ZCWX-ray1.69A16-363[»]
4A1ZX-ray2.80A/B1-368[»]
4A28X-ray2.55A/B1-368[»]
4A50X-ray2.75A1-368[»]
4A51X-ray2.75A/B/C/D/E/F/G1-368[»]
4A5YX-ray2.45A/B/C1-368[»]
4AP0X-ray2.59A/B/C/D1-368[»]
4AQVelectron microscopy9.70C1-367[»]
4AQWelectron microscopy9.50C1-367[»]
4AS7X-ray2.40A1-368[»]
4B7BX-ray2.50A1-368[»]
4BBGX-ray2.75A1-368[»]
4BXNX-ray2.79A/B1-368[»]
4CK5electron microscopy10.00C1-367[»]
4CK6electron microscopy9.20C1-367[»]
4CK7electron microscopy9.20C1-367[»]
ProteinModelPortalP52732.
SMRP52732. Positions 15-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110030. 20 interactions.
IntActP52732. 5 interactions.
MINTMINT-1152202.
STRING9606.ENSP00000260731.

Chemistry

BindingDBP52732.
ChEMBLCHEMBL4581.

PTM databases

PhosphoSiteP52732.

Polymorphism databases

DMDM116242604.

Proteomic databases

MaxQBP52732.
PaxDbP52732.
PeptideAtlasP52732.
PRIDEP52732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260731; ENSP00000260731; ENSG00000138160.
GeneID3832.
KEGGhsa:3832.
UCSCuc001kic.3. human.

Organism-specific databases

CTD3832.
GeneCardsGC10P094352.
HGNCHGNC:6388. KIF11.
HPACAB017617.
HPA006916.
HPA010568.
MIM148760. gene.
152950. phenotype.
neXtProtNX_P52732.
Orphanet2526. Microcephaly - lymphedema - chorioretinopathy.
PharmGKBPA30177.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000116164.
HOVERGENHBG005572.
InParanoidP52732.
KOK10398.
OMAQPNSSAK.
OrthoDBEOG7VX8V8.
PhylomeDBP52732.
TreeFamTF105230.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

BgeeP52732.
CleanExHS_KIF11.
GenevestigatorP52732.

Family and domain databases

Gene3D3.40.850.10. 1 hit.
InterProIPR025901. Kinesin-assoc_MT-bd_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PfamPF00225. Kinesin. 1 hit.
PF13931. Microtub_bind. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52732.
GeneWikiKinesin_family_member_11.
GenomeRNAi3832.
NextBio15061.
PROP52732.
SOURCESearch...

Entry information

Entry nameKIF11_HUMAN
AccessionPrimary (citable) accession number: P52732
Secondary accession number(s): A0AV49 expand/collapse secondary AC list , B2RMV3, Q15716, Q5VWX0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 145 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 10

Human chromosome 10: entries, gene names and cross-references to MIM