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Protein

Kinesin-like protein KIF11

Gene

KIF11

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

Functioni

Motor protein required for establishing a bipolar spindle during mitosis (PubMed:19001501). Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (PubMed:23857769).2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi105 – 112ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent microtubule motor activity, plus-end-directed Source: GO_Central
  • microtubule binding Source: InterPro
  • microtubule motor activity Source: ProtInc
  • protein complex binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: GO_Central
  • microtubule-based movement Source: GO_Central
  • mitotic cell cycle Source: ProtInc
  • mitotic centrosome separation Source: Ensembl
  • mitotic spindle assembly Source: UniProtKB
  • mitotic spindle organization Source: ProtInc
  • regulation of mitotic centrosome separation Source: UniProtKB
  • retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
  • spindle organization Source: UniProtKB

Keywordsi

Molecular functionMotor protein
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.4. 2681.
ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.
SIGNORiP52732.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:KIF11
Synonyms:EG5, KNSL1, TRIP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000138160.5.
HGNCiHGNC:6388. KIF11.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:152950
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067829144F → L in MCLMR. 1 Publication1
Natural variantiVAR_067830234R → C in MCLMR. 1 Publication1
Natural variantiVAR_067831235S → C in MCLMR. 1 PublicationCorresponds to variant dbSNP:rs387906643Ensembl.1
Natural variantiVAR_067832944R → C in MCLMR. 1 PublicationCorresponds to variant dbSNP:rs387906642Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi926T → A: No mitotic phosphorylation. No binding to spindle apparatus. 1 Publication1
Mutagenesisi1033S → A: Still binds to the mitotic spindle but mitotic progression is impaired. 1 Publication1
Mutagenesisi1033S → D: Still binds to the mitotic spindle but mitotic progression is impaired. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3832.
MalaCardsiKIF11.
MIMi152950. phenotype.
OpenTargetsiENSG00000138160.
Orphaneti2526. Microcephaly - lymphedema - chorioretinopathy.
PharmGKBiPA30177.

Chemistry databases

ChEMBLiCHEMBL4581.
DrugBankiDB04331. Monastrol.
GuidetoPHARMACOLOGYi2788.

Polymorphism and mutation databases

BioMutaiKIF11.
DMDMi116242604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001253721 – 1056Kinesin-like protein KIF11Add BLAST1056

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei146N6-acetyllysineCombined sources1
Modified residuei458PhosphothreonineCombined sources1
Cross-linki477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei925PhosphothreonineCombined sources1
Modified residuei926Phosphothreonine; by CDK1Combined sources2 Publications1
Modified residuei1033Phosphoserine; by NEK6Combined sources1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP52732.
MaxQBiP52732.
PaxDbiP52732.
PeptideAtlasiP52732.
PRIDEiP52732.

PTM databases

iPTMnetiP52732.
PhosphoSitePlusiP52732.
SwissPalmiP52732.

Expressioni

Gene expression databases

BgeeiENSG00000138160.
CleanExiHS_KIF11.
GenevisibleiP52732. HS.

Organism-specific databases

HPAiCAB017617.
HPA006916.
HPA010093.
HPA010568.

Interactioni

Subunit structurei

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.2 Publications

GO - Molecular functioni

  • microtubule binding Source: InterPro
  • protein complex binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110030. 130 interactors.
CORUMiP52732.
DIPiDIP-53686N.
IntActiP52732. 90 interactors.
MINTiMINT-1152202.
STRINGi9606.ENSP00000260731.

Chemistry databases

BindingDBiP52732.

Structurei

Secondary structure

11056
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 25Combined sources7
Helixi30 – 34Combined sources5
Beta strandi41 – 44Combined sources4
Turni45 – 48Combined sources4
Beta strandi49 – 53Combined sources5
Beta strandi58 – 60Combined sources3
Beta strandi63 – 67Combined sources5
Beta strandi69 – 72Combined sources4
Helixi78 – 94Combined sources17
Beta strandi98 – 106Combined sources9
Helixi111 – 115Combined sources5
Helixi121 – 123Combined sources3
Turni127 – 129Combined sources3
Beta strandi131 – 133Combined sources3
Helixi135 – 148Combined sources14
Turni149 – 151Combined sources3
Beta strandi153 – 164Combined sources12
Beta strandi167 – 171Combined sources5
Beta strandi174 – 176Combined sources3
Beta strandi183 – 186Combined sources4
Beta strandi188 – 190Combined sources3
Beta strandi194 – 197Combined sources4
Beta strandi202 – 204Combined sources3
Helixi207 – 223Combined sources17
Helixi226 – 233Combined sources8
Beta strandi235 – 248Combined sources14
Beta strandi250 – 252Combined sources3
Beta strandi254 – 265Combined sources12
Helixi269 – 271Combined sources3
Helixi272 – 275Combined sources4
Helixi280 – 283Combined sources4
Turni287 – 289Combined sources3
Helixi290 – 304Combined sources15
Helixi311 – 313Combined sources3
Helixi315 – 320Combined sources6
Helixi321 – 323Combined sources3
Beta strandi324 – 327Combined sources4
Beta strandi330 – 336Combined sources7
Helixi340 – 342Combined sources3
Helixi343 – 357Combined sources15
Helixi372 – 391Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3WPNX-ray2.80A1-369[»]
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[»]
4ZCAX-ray2.30A/B1-369[»]
4ZHIX-ray2.30A/B1-369[»]
5JV3X-ray2.01A/B/C/D366-391[»]
ProteinModelPortaliP52732.
SMRiP52732.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52732.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 359Kinesin motorPROSITE-ProRule annotationAdd BLAST342

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili364 – 480Sequence analysisAdd BLAST117
Coiled coili736 – 763Sequence analysisAdd BLAST28

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0243. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00890000139323.
HOGENOMiHOG000116164.
HOVERGENiHBG005572.
InParanoidiP52732.
KOiK10398.
OMAiSERLQMF.
OrthoDBiEOG091G013C.
PhylomeDBiP52732.
TreeFamiTF105230.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiView protein in InterPro
IPR025901. Kinesin-assoc_MT-bd_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR036961. Kinesin_motor_dom_sf.
IPR027417. P-loop_NTPase.
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiView protein in Pfam
PF00225. Kinesin. 1 hit.
PF13931. Microtub_bind. 1 hit.
PRINTSiPR00380. KINESINHEAVY.
SMARTiView protein in SMART
SM00129. KISc. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P52732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQPNSSAK KKEEKGKNIQ VVVRCRPFNL AERKASAHSI VECDPVRKEV
60 70 80 90 100
SVRTGGLADK SSRKTYTFDM VFGASTKQID VYRSVVCPIL DEVIMGYNCT
110 120 130 140 150
IFAYGQTGTG KTFTMEGERS PNEEYTWEED PLAGIIPRTL HQIFEKLTDN
160 170 180 190 200
GTEFSVKVSL LEIYNEELFD LLNPSSDVSE RLQMFDDPRN KRGVIIKGLE
210 220 230 240 250
EITVHNKDEV YQILEKGAAK RTTAATLMNA YSSRSHSVFS VTIHMKETTI
260 270 280 290 300
DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT
310 320 330 340 350
ALVERTPHVP YRESKLTRIL QDSLGGRTRT SIIATISPAS LNLEETLSTL
360 370 380 390 400
EYAHRAKNIL NKPEVNQKLT KKALIKEYTE EIERLKRDLA AAREKNGVYI
410 420 430 440 450
SEENFRVMSG KLTVQEEQIV ELIEKIGAVE EELNRVTELF MDNKNELDQC
460 470 480 490 500
KSDLQNKTQE LETTQKHLQE TKLQLVKEEY ITSALESTEE KLHDAASKLL
510 520 530 540 550
NTVEETTKDV SGLHSKLDRK KAVDQHNAEA QDIFGKNLNS LFNNMEELIK
560 570 580 590 600
DGSSKQKAML EVHKTLFGNL LSSSVSALDT ITTVALGSLT SIPENVSTHV
610 620 630 640 650
SQIFNMILKE QSLAAESKTV LQELINVLKT DLLSSLEMIL SPTVVSILKI
660 670 680 690 700
NSQLKHIFKT SLTVADKIED QKKELDGFLS ILCNNLHELQ ENTICSLVES
710 720 730 740 750
QKQCGNLTED LKTIKQTHSQ ELCKLMNLWT ERFCALEEKC ENIQKPLSSV
760 770 780 790 800
QENIQQKSKD IVNKMTFHSQ KFCADSDGFS QELRNFNQEG TKLVEESVKH
810 820 830 840 850
SDKLNGNLEK ISQETEQRCE SLNTRTVYFS EQWVSSLNER EQELHNLLEV
860 870 880 890 900
VSQCCEASSS DITEKSDGRK AAHEKQHNIF LDQMTIDEDK LIAQNLELNE
910 920 930 940 950
TIKIGLTKLN CFLEQDLKLD IPTGTTPQRK SYLYPSTLVR TEPREHLLDQ
960 970 980 990 1000
LKRKQPELLM MLNCSENNKE ETIPDVDVEE AVLGQYTEEP LSQEPSVDAG
1010 1020 1030 1040 1050
VDCSSIGGVP FFQHKKSHGK DKENRGINTL ERSKVEETTE HLVTKSRLPL

RAQINL
Length:1,056
Mass (Da):119,159
Last modified:October 17, 2006 - v2
Checksum:iC7F2606FE68DA8EA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti674 – 675EL → RNS in CAA59449 (PubMed:8548803).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067829144F → L in MCLMR. 1 Publication1
Natural variantiVAR_067830234R → C in MCLMR. 1 Publication1
Natural variantiVAR_067831235S → C in MCLMR. 1 PublicationCorresponds to variant dbSNP:rs387906643Ensembl.1
Natural variantiVAR_067832944R → C in MCLMR. 1 PublicationCorresponds to variant dbSNP:rs387906642Ensembl.1
Natural variantiVAR_0496821042L → F. Corresponds to variant dbSNP:rs34417963Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85137 mRNA. Translation: CAA59449.1.
U37426 mRNA. Translation: AAA86132.1.
AL360222 Genomic DNA. No translation available.
AL356128 Genomic DNA. No translation available.
BC126211 mRNA. Translation: AAI26212.1.
BC136474 mRNA. Translation: AAI36475.1.
L40372 mRNA. Translation: AAC41739.1.
CCDSiCCDS7422.1.
PIRiG02157.
RefSeqiNP_004514.2. NM_004523.3.
UniGeneiHs.8878.

Genome annotation databases

EnsembliENST00000260731; ENSP00000260731; ENSG00000138160.
GeneIDi3832.
KEGGihsa:3832.
UCSCiuc001kic.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKIF11_HUMAN
AccessioniPrimary (citable) accession number: P52732
Secondary accession number(s): A0AV49
, B2RMV3, Q15716, Q5VWX0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: November 22, 2017
This is version 180 of the entry and version 2 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families