UniProtKB - P52732 (KIF11_HUMAN)
UniProt
P52732 - KIF11_HUMAN
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Protein
Kinesin-like protein KIF11
Gene
KIF11
Organism
Homo sapiens (Human)
Sequence features
Status
Functioni
Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays.1 Publication
Regions
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Nucleotide bindingi | 105 – 112 | 8 | ATPPROSITE-ProRule annotation |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ATP-dependent microtubule motor activity, plus-end-directed Source: GO_Central
- 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
- blood coagulation Source: Reactome
- cell division Source: UniProtKB-KW
- chromosome segregation Source: GO_Central
- microtubule-based movement Source: GO_Central
- mitotic centrosome separation Source: Ensembl
- mitotic nuclear division Source: ProtInc
- mitotic spindle assembly Source: UniProtKB
- mitotic spindle organization Source: ProtInc
- regulation of mitotic centrosome separation Source: UniProtKB
- spindle organization Source: UniProtKB
Keywords - Molecular functioni
Motor proteinKeywords - Biological processi
Cell cycle, Cell division, MitosisKeywords - Ligandi
ATP-binding, Nucleotide-bindingEnzyme and pathway databases
BRENDAi | 3.6.4.4. 2681. |
Reactomei | R-HSA-2132295. MHC class II antigen presentation. R-HSA-983189. Kinesins. |
Names & Taxonomyi
Protein namesi | Recommended name: Kinesin-like protein KIF11Alternative 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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi | UP000005640: Chromosome 10 Componenti |
Organism-specific databases
HGNCi | HGNC:6388. KIF11. |
Subcellular locationi
- Cytoplasm 1 Publication
- Cytoplasm › cytoskeleton › spindle pole 1 Publication
GO - Cellular componenti
- cytoplasm Source: HPA
- cytosol Source: Reactome
- kinesin complex Source: ProtInc
- membrane Source: UniProtKB
- microtubule Source: UniProtKB
- spindle Source: UniProtKB
- spindle pole Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, MicrotubulePathology & 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:152950Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Natural varianti | 144 – 144 | 1 | F → L in MCLMR. 1 Publication | VAR_067829 | ||
Natural varianti | 234 – 234 | 1 | R → C in MCLMR. 1 Publication | VAR_067830 | ||
Natural varianti | 235 – 235 | 1 | S → C in MCLMR. 1 Publication | VAR_067831 | ||
Natural varianti | 944 – 944 | 1 | R → C in MCLMR. 1 Publication | VAR_067832 |
Mutagenesis
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Mutagenesisi | 926 – 926 | 1 | T → A: No mitotic phosphorylation. No binding to spindle apparatus. 1 Publication | |||
Mutagenesisi | 1033 – 1033 | 1 | S → A: Still binds to the mitotic spindle but mitotic progression is impaired. 1 Publication | |||
Mutagenesisi | 1033 – 1033 | 1 | S → D: Still binds to the mitotic spindle but mitotic progression is impaired. 1 Publication |
Keywords - Diseasei
Disease mutationOrganism-specific databases
MIMi | 152950. phenotype. |
Orphaneti | 2526. Microcephaly - lymphedema - chorioretinopathy. |
PharmGKBi | PA30177. |
Polymorphism and mutation databases
BioMutai | KIF11. |
DMDMi | 116242604. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Chaini | 1 – 1056 | 1056 | Kinesin-like protein KIF11 | PRO_0000125372 | Add BLAST |
Amino acid modifications
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Modified residuei | 146 – 146 | 1 | N6-acetyllysineCombined sources | |||
Modified residuei | 458 – 458 | 1 | PhosphothreonineCombined sources | |||
Modified residuei | 926 – 926 | 1 | Phosphothreonine; by CDK1Combined sources2 Publications | |||
Modified residuei | 1033 – 1033 | 1 | Phosphoserine; by NEK61 Publication |
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.
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
MaxQBi | P52732. |
PaxDbi | P52732. |
PeptideAtlasi | P52732. |
PRIDEi | P52732. |
PTM databases
PhosphoSitei | P52732. |
Expressioni
Gene expression databases
Bgeei | P52732. |
CleanExi | HS_KIF11. |
Genevisiblei | P52732. HS. |
Organism-specific databases
HPAi | CAB017617. HPA006916. 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
Protein-protein interaction databases
BioGridi | 110030. 27 interactions. |
IntActi | P52732. 5 interactions. |
MINTi | MINT-1152202. |
STRINGi | 9606.ENSP00000260731. |
Structurei
Secondary structure
1
1056
Legend: HelixTurnBeta strand
Show more detailsFeature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Beta strandi | 19 – 25 | 7 | Combined sources | |||
Helixi | 30 – 34 | 5 | Combined sources | |||
Beta strandi | 41 – 44 | 4 | Combined sources | |||
Turni | 45 – 48 | 4 | Combined sources | |||
Beta strandi | 49 – 53 | 5 | Combined sources | |||
Beta strandi | 58 – 60 | 3 | Combined sources | |||
Beta strandi | 63 – 67 | 5 | Combined sources | |||
Beta strandi | 69 – 72 | 4 | Combined sources | |||
Helixi | 78 – 94 | 17 | Combined sources | |||
Beta strandi | 98 – 106 | 9 | Combined sources | |||
Helixi | 111 – 115 | 5 | Combined sources | |||
Helixi | 121 – 123 | 3 | Combined sources | |||
Turni | 127 – 129 | 3 | Combined sources | |||
Helixi | 130 – 132 | 3 | Combined sources | |||
Helixi | 135 – 148 | 14 | Combined sources | |||
Turni | 149 – 151 | 3 | Combined sources | |||
Beta strandi | 153 – 164 | 12 | Combined sources | |||
Beta strandi | 167 – 171 | 5 | Combined sources | |||
Beta strandi | 174 – 176 | 3 | Combined sources | |||
Beta strandi | 183 – 186 | 4 | Combined sources | |||
Beta strandi | 188 – 190 | 3 | Combined sources | |||
Beta strandi | 194 – 197 | 4 | Combined sources | |||
Beta strandi | 202 – 204 | 3 | Combined sources | |||
Helixi | 207 – 223 | 17 | Combined sources | |||
Helixi | 226 – 233 | 8 | Combined sources | |||
Beta strandi | 235 – 248 | 14 | Combined sources | |||
Beta strandi | 250 – 252 | 3 | Combined sources | |||
Beta strandi | 254 – 265 | 12 | Combined sources | |||
Helixi | 269 – 271 | 3 | Combined sources | |||
Helixi | 272 – 275 | 4 | Combined sources | |||
Helixi | 280 – 283 | 4 | Combined sources | |||
Turni | 287 – 289 | 3 | Combined sources | |||
Helixi | 290 – 304 | 15 | Combined sources | |||
Helixi | 311 – 313 | 3 | Combined sources | |||
Helixi | 315 – 320 | 6 | Combined sources | |||
Helixi | 321 – 323 | 3 | Combined sources | |||
Beta strandi | 324 – 327 | 4 | Combined sources | |||
Beta strandi | 330 – 336 | 7 | Combined sources | |||
Helixi | 340 – 342 | 3 | Combined sources | |||
Helixi | 343 – 357 | 15 | Combined sources |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ProteinModelPortali | P52732. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SMRi | P52732. Positions 15-386. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ModBasei | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P52732. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Domaini | 18 – 359 | 342 | Kinesin motorPROSITE-ProRule annotation | Add BLAST |
Coiled coil
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Coiled coili | 364 – 480 | 117 | Sequence Analysis | Add BLAST | ||
Coiled coili | 736 – 763 | 28 | Sequence Analysis | Add BLAST |
Sequence similaritiesi
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. BimC subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | COG5059. |
GeneTreei | ENSGT00770000120453. |
HOGENOMi | HOG000116164. |
HOVERGENi | HBG005572. |
InParanoidi | P52732. |
KOi | K10398. |
OMAi | NKNELDQ. |
OrthoDBi | EOG7VX8V8. |
PhylomeDBi | P52732. |
TreeFami | TF105230. |
Family and domain databases
Gene3Di | 3.40.850.10. 1 hit. |
InterProi | IPR025901. Kinesin-assoc_MT-bd_dom. IPR027640. Kinesin-like_fam. IPR019821. Kinesin_motor_CS. IPR001752. Kinesin_motor_dom. IPR027417. P-loop_NTPase. [Graphical view] |
PANTHERi | PTHR24115. PTHR24115. 1 hit. |
Pfami | PF00225. Kinesin. 1 hit. PF13931. Microtub_bind. 1 hit. [Graphical view] |
PRINTSi | PR00380. KINESINHEAVY. |
SMARTi | SM00129. KISc. 1 hit. [Graphical view] |
SUPFAMi | SSF52540. SSF52540. 1 hit. |
PROSITEi | PS00411. KINESIN_MOTOR_1. 1 hit. PS50067. KINESIN_MOTOR_2. 1 hit. [Graphical view] |
i Sequence
Sequence statusi: Complete.
P52732-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Sequence conflicti | 674 – 675 | 2 | EL → RNS in CAA59449 (PubMed:8548803).Curated |
Natural variant
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Natural varianti | 144 – 144 | 1 | F → L in MCLMR. 1 Publication | VAR_067829 | ||
Natural varianti | 234 – 234 | 1 | R → C in MCLMR. 1 Publication | VAR_067830 | ||
Natural varianti | 235 – 235 | 1 | S → C in MCLMR. 1 Publication | VAR_067831 | ||
Natural varianti | 944 – 944 | 1 | R → C in MCLMR. 1 Publication | VAR_067832 | ||
Natural varianti | 1042 – 1042 | 1 | L → F. Corresponds to variant rs34417963 [ dbSNP | Ensembl ]. | VAR_049682 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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. |
CCDSi | CCDS7422.1. |
PIRi | G02157. |
RefSeqi | NP_004514.2. NM_004523.3. |
UniGenei | Hs.8878. |
Genome annotation databases
Ensembli | ENST00000260731; ENSP00000260731; ENSG00000138160. |
GeneIDi | 3832. |
KEGGi | hsa:3832. |
UCSCi | uc001kic.3. human. |
Keywords - Coding sequence diversityi
PolymorphismCross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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. |
CCDSi | CCDS7422.1. |
PIRi | G02157. |
RefSeqi | NP_004514.2. NM_004523.3. |
UniGenei | Hs.8878. |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ProteinModelPortali | P52732. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SMRi | P52732. Positions 15-386. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ModBasei | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MobiDBi | Search... |
Protein-protein interaction databases
BioGridi | 110030. 27 interactions. |
IntActi | P52732. 5 interactions. |
MINTi | MINT-1152202. |
STRINGi | 9606.ENSP00000260731. |
Chemistry
BindingDBi | P52732. |
ChEMBLi | CHEMBL4581. |
GuidetoPHARMACOLOGYi | 2788. |
PTM databases
PhosphoSitei | P52732. |
Polymorphism and mutation databases
BioMutai | KIF11. |
DMDMi | 116242604. |
Proteomic databases
MaxQBi | P52732. |
PaxDbi | P52732. |
PeptideAtlasi | P52732. |
PRIDEi | P52732. |
Protocols and materials databases
Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembli | ENST00000260731; ENSP00000260731; ENSG00000138160. |
GeneIDi | 3832. |
KEGGi | hsa:3832. |
UCSCi | uc001kic.3. human. |
Organism-specific databases
CTDi | 3832. |
GeneCardsi | GC10P092593. |
HGNCi | HGNC:6388. KIF11. |
HPAi | CAB017617. HPA006916. HPA010568. |
MIMi | 148760. gene. 152950. phenotype. |
neXtProti | NX_P52732. |
Orphaneti | 2526. Microcephaly - lymphedema - chorioretinopathy. |
PharmGKBi | PA30177. |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | COG5059. |
GeneTreei | ENSGT00770000120453. |
HOGENOMi | HOG000116164. |
HOVERGENi | HBG005572. |
InParanoidi | P52732. |
KOi | K10398. |
OMAi | NKNELDQ. |
OrthoDBi | EOG7VX8V8. |
PhylomeDBi | P52732. |
TreeFami | TF105230. |
Enzyme and pathway databases
BRENDAi | 3.6.4.4. 2681. |
Reactomei | R-HSA-2132295. MHC class II antigen presentation. R-HSA-983189. Kinesins. |
Miscellaneous databases
ChiTaRSi | KIF11. human. |
EvolutionaryTracei | P52732. |
GeneWikii | Kinesin_family_member_11. |
GenomeRNAii | 3832. |
NextBioi | 15061. |
PROi | P52732. |
SOURCEi | Search... |
Gene expression databases
Bgeei | P52732. |
CleanExi | HS_KIF11. |
Genevisiblei | P52732. HS. |
Family and domain databases
Gene3Di | 3.40.850.10. 1 hit. |
InterProi | IPR025901. Kinesin-assoc_MT-bd_dom. IPR027640. Kinesin-like_fam. IPR019821. Kinesin_motor_CS. IPR001752. Kinesin_motor_dom. IPR027417. P-loop_NTPase. [Graphical view] |
PANTHERi | PTHR24115. PTHR24115. 1 hit. |
Pfami | PF00225. Kinesin. 1 hit. PF13931. Microtub_bind. 1 hit. [Graphical view] |
PRINTSi | PR00380. KINESINHEAVY. |
SMARTi | SM00129. KISc. 1 hit. [Graphical view] |
SUPFAMi | SSF52540. SSF52540. 1 hit. |
PROSITEi | PS00411. KINESIN_MOTOR_1. 1 hit. PS50067. KINESIN_MOTOR_2. 1 hit. [Graphical view] |
ProtoNeti | Search... |
Publicationsi
- "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. - "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]. - "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. Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. - "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. - "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. - "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. - "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. - "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. - "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. - "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]. - "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. - "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]. - "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]. - "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. - "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. - "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. 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.
Entry informationi
Entry namei | KIF11_HUMAN | ||||||||
Accessioni | P52732Primary (citable) accession number: P52732 Secondary accession number(s): A0AV49 Q5VWX0 | ||||||||
Entry historyi |
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Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Annotation program | Chordata Protein Annotation Program | ||||||||
Disclaimer | Any 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 proteomeDocuments
- Human chromosome 10Human chromosome 10: entries, gene names and cross-references to MIM
- Human entries with polymorphisms or disease mutationsList of human entries with polymorphisms or disease mutations
- Human polymorphisms and disease mutationsIndex of human polymorphisms and disease mutations
- MIM cross-referencesOnline Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
- PDB cross-referencesIndex of Protein Data Bank (PDB) cross-references
- SIMILARITY commentsIndex of protein domains and families
External Data
Dasty 3Similar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry. |
90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |