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P52732

- KIF11_HUMAN

UniProt

P52732 - KIF11_HUMAN

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Protein
Kinesin-like protein KIF11
Gene
KIF11, EG5, KNSL1, TRIP5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1128ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microtubule motor activity Source: ProtInc
  3. protein complex binding Source: UniProtKB
  4. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. blood coagulation Source: Reactome
  3. metabolic process Source: GOC
  4. microtubule-based movement Source: Reactome
  5. mitotic centrosome separation Source: Ensembl
  6. mitotic nuclear division Source: ProtInc
  7. mitotic spindle organization Source: ProtInc
  8. spindle assembly involved in mitosis Source: UniProtKB
  9. spindle organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_25201. Kinesins.

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
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:6388. KIF11.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeletonspindle pole 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. kinesin complex Source: ProtInc
  4. microtubule Source: UniProtKB
  5. spindle Source: UniProtKB
  6. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441F → L in MCLMR. 1 Publication
VAR_067829
Natural varianti234 – 2341R → C in MCLMR. 1 Publication
VAR_067830
Natural varianti235 – 2351S → C in MCLMR. 1 Publication
VAR_067831
Natural varianti944 – 9441R → C in MCLMR. 1 Publication
VAR_067832

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi926 – 9261T → A: No mitotic phosphorylation. No binding to spindle apparatus. 1 Publication
Mutagenesisi1033 – 10331S → A: Still binds to the mitotic spindle but mitotic progression is impaired. 1 Publication
Mutagenesisi1033 – 10331S → D: Still binds to the mitotic spindle but mitotic progression is impaired. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi152950. phenotype.
Orphaneti2526. Microcephaly - lymphedema - chorioretinopathy.
PharmGKBiPA30177.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10561056Kinesin-like protein KIF11
PRO_0000125372Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461N6-acetyllysine1 Publication
Modified residuei458 – 4581Phosphothreonine1 Publication
Modified residuei926 – 9261Phosphothreonine; by CDK13 Publications
Modified residuei1033 – 10331Phosphoserine; 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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52732.
PaxDbiP52732.
PeptideAtlasiP52732.
PRIDEiP52732.

PTM databases

PhosphoSiteiP52732.

Expressioni

Gene expression databases

BgeeiP52732.
CleanExiHS_KIF11.
GenevestigatoriP52732.

Organism-specific databases

HPAiCAB017617.
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

BioGridi110030. 20 interactions.
IntActiP52732. 5 interactions.
MINTiMINT-1152202.
STRINGi9606.ENSP00000260731.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 257
Helixi30 – 345
Beta strandi41 – 444
Turni45 – 484
Beta strandi49 – 535
Beta strandi58 – 603
Beta strandi63 – 675
Beta strandi69 – 724
Helixi78 – 9417
Beta strandi98 – 1069
Helixi111 – 1155
Helixi121 – 1233
Turni127 – 1293
Helixi130 – 1323
Helixi135 – 14814
Turni149 – 1513
Beta strandi153 – 16412
Beta strandi167 – 1715
Beta strandi174 – 1763
Beta strandi183 – 1864
Beta strandi188 – 1903
Beta strandi194 – 1974
Beta strandi202 – 2043
Helixi207 – 22317
Helixi226 – 2338
Beta strandi235 – 24814
Beta strandi250 – 2523
Beta strandi254 – 26512
Helixi269 – 2713
Helixi272 – 2754
Helixi280 – 2834
Turni287 – 2893
Helixi290 – 30415
Helixi311 – 3133
Helixi315 – 3206
Helixi321 – 3233
Beta strandi324 – 3274
Beta strandi330 – 3367
Helixi340 – 3423
Helixi343 – 35715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP52732.
SMRiP52732. Positions 15-386.

Miscellaneous databases

EvolutionaryTraceiP52732.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 359342Kinesin motor
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili364 – 480117 Reviewed prediction
Add
BLAST
Coiled coili736 – 76328 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
HOGENOMiHOG000116164.
HOVERGENiHBG005572.
InParanoidiP52732.
KOiK10398.
OMAiQPNSSAK.
OrthoDBiEOG7VX8V8.
PhylomeDBiP52732.
TreeFamiTF105230.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR025901. Kinesin-assoc_MT-bd_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
PF13931. Microtub_bind. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52732-1 [UniParc]FASTAAdd to Basket

« Hide

MASQPNSSAK KKEEKGKNIQ VVVRCRPFNL AERKASAHSI VECDPVRKEV     50
SVRTGGLADK SSRKTYTFDM VFGASTKQID VYRSVVCPIL DEVIMGYNCT 100
IFAYGQTGTG KTFTMEGERS PNEEYTWEED PLAGIIPRTL HQIFEKLTDN 150
GTEFSVKVSL LEIYNEELFD LLNPSSDVSE RLQMFDDPRN KRGVIIKGLE 200
EITVHNKDEV YQILEKGAAK RTTAATLMNA YSSRSHSVFS VTIHMKETTI 250
DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT 300
ALVERTPHVP YRESKLTRIL QDSLGGRTRT SIIATISPAS LNLEETLSTL 350
EYAHRAKNIL NKPEVNQKLT KKALIKEYTE EIERLKRDLA AAREKNGVYI 400
SEENFRVMSG KLTVQEEQIV ELIEKIGAVE EELNRVTELF MDNKNELDQC 450
KSDLQNKTQE LETTQKHLQE TKLQLVKEEY ITSALESTEE KLHDAASKLL 500
NTVEETTKDV SGLHSKLDRK KAVDQHNAEA QDIFGKNLNS LFNNMEELIK 550
DGSSKQKAML EVHKTLFGNL LSSSVSALDT ITTVALGSLT SIPENVSTHV 600
SQIFNMILKE QSLAAESKTV LQELINVLKT DLLSSLEMIL SPTVVSILKI 650
NSQLKHIFKT SLTVADKIED QKKELDGFLS ILCNNLHELQ ENTICSLVES 700
QKQCGNLTED LKTIKQTHSQ ELCKLMNLWT ERFCALEEKC ENIQKPLSSV 750
QENIQQKSKD IVNKMTFHSQ KFCADSDGFS QELRNFNQEG TKLVEESVKH 800
SDKLNGNLEK ISQETEQRCE SLNTRTVYFS EQWVSSLNER EQELHNLLEV 850
VSQCCEASSS DITEKSDGRK AAHEKQHNIF LDQMTIDEDK LIAQNLELNE 900
TIKIGLTKLN CFLEQDLKLD IPTGTTPQRK SYLYPSTLVR TEPREHLLDQ 950
LKRKQPELLM MLNCSENNKE ETIPDVDVEE AVLGQYTEEP LSQEPSVDAG 1000
VDCSSIGGVP FFQHKKSHGK DKENRGINTL ERSKVEETTE HLVTKSRLPL 1050
RAQINL 1056
Length:1,056
Mass (Da):119,159
Last modified:October 17, 2006 - v2
Checksum:iC7F2606FE68DA8EA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441F → L in MCLMR. 1 Publication
VAR_067829
Natural varianti234 – 2341R → C in MCLMR. 1 Publication
VAR_067830
Natural varianti235 – 2351S → C in MCLMR. 1 Publication
VAR_067831
Natural varianti944 – 9441R → C in MCLMR. 1 Publication
VAR_067832
Natural varianti1042 – 10421L → F.
Corresponds to variant rs34417963 [ dbSNP | Ensembl ].
VAR_049682

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti674 – 6752EL → RNS in CAA59449. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS7422.1.
PIRiG02157.
RefSeqiNP_004514.2. NM_004523.3.
UniGeneiHs.8878.

Genome annotation databases

EnsembliENST00000260731; ENSP00000260731; ENSG00000138160.
GeneIDi3832.
KEGGihsa:3832.
UCSCiuc001kic.3. human.

Polymorphism databases

DMDMi116242604.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1II6 X-ray 2.10 A/B 1-368 [» ]
1Q0B X-ray 1.90 A/B 2-368 [» ]
1X88 X-ray 1.80 A/B 10-368 [» ]
1YRS X-ray 2.50 A/B 1-368 [» ]
2FKY X-ray 2.30 A/B 2-368 [» ]
2FL2 X-ray 2.50 A/B 2-368 [» ]
2FL6 X-ray 2.50 A/B 2-368 [» ]
2FME X-ray 2.10 A/B 1-368 [» ]
2G1Q X-ray 2.51 A/B 1-368 [» ]
2GM1 X-ray 2.30 A/B/D/E 1-368 [» ]
2IEH X-ray 2.70 A/B 2-368 [» ]
2PG2 X-ray 1.85 A/B 1-368 [» ]
2Q2Y X-ray 2.50 A/B 2-368 [» ]
2Q2Z X-ray 3.00 A/B 2-368 [» ]
2UYI X-ray 2.10 A/B 1-368 [» ]
2UYM X-ray 2.11 A/B 1-368 [» ]
2WOG X-ray 2.00 A/B/C 1-368 [» ]
2X2R X-ray 2.20 A/B/C 1-368 [» ]
2X7C X-ray 1.90 A/B 1-368 [» ]
2X7D X-ray 2.30 A/B 1-368 [» ]
2X7E X-ray 2.40 A/B 1-368 [» ]
2XAE X-ray 2.60 A/B/C 1-368 [» ]
3CJO X-ray 2.28 A/B 2-368 [» ]
3HQD X-ray 2.19 A/B 1-369 [» ]
3K3B X-ray 2.40 A/B 1-368 [» ]
3K5E X-ray 1.97 A/B 1-368 [» ]
3KEN X-ray 2.50 A 1-369 [» ]
3L9H X-ray 2.00 A/B 1-368 [» ]
3ZCW X-ray 1.69 A 16-363 [» ]
4A1Z X-ray 2.80 A/B 1-368 [» ]
4A28 X-ray 2.55 A/B 1-368 [» ]
4A50 X-ray 2.75 A 1-368 [» ]
4A51 X-ray 2.75 A/B/C/D/E/F/G 1-368 [» ]
4A5Y X-ray 2.45 A/B/C 1-368 [» ]
4AP0 X-ray 2.59 A/B/C/D 1-368 [» ]
4AQV electron microscopy 9.70 C 1-367 [» ]
4AQW electron microscopy 9.50 C 1-367 [» ]
4AS7 X-ray 2.40 A 1-368 [» ]
4B7B X-ray 2.50 A 1-368 [» ]
4BBG X-ray 2.75 A 1-368 [» ]
4BXN X-ray 2.79 A/B 1-368 [» ]
4CK5 electron microscopy 10.00 C 1-367 [» ]
4CK6 electron microscopy 9.20 C 1-367 [» ]
4CK7 electron microscopy 9.20 C 1-367 [» ]
ProteinModelPortali P52732.
SMRi P52732. Positions 15-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110030. 20 interactions.
IntActi P52732. 5 interactions.
MINTi MINT-1152202.
STRINGi 9606.ENSP00000260731.

Chemistry

BindingDBi P52732.
ChEMBLi CHEMBL4581.

PTM databases

PhosphoSitei P52732.

Polymorphism databases

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 GC10P094352.
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.
HOGENOMi HOG000116164.
HOVERGENi HBG005572.
InParanoidi P52732.
KOi K10398.
OMAi QPNSSAK.
OrthoDBi EOG7VX8V8.
PhylomeDBi P52732.
TreeFami TF105230.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_25201. Kinesins.

Miscellaneous databases

EvolutionaryTracei P52732.
GeneWikii Kinesin_family_member_11.
GenomeRNAii 3832.
NextBioi 15061.
PROi P52732.
SOURCEi Search...

Gene expression databases

Bgeei P52732.
CleanExi HS_KIF11.
Genevestigatori P52732.

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

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. Cited for: VARIANTS MCLMR LEU-144; CYS-234; CYS-235 AND CYS-944.

Entry informationi

Entry nameiKIF11_HUMAN
AccessioniPrimary (citable) accession number: P52732
Secondary accession number(s): A0AV49
, B2RMV3, Q15716, Q5VWX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 146 of the entry and version 2 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

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

External Data

Dasty 3

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