P52732 (KIF11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	KIF11
Synonyms:	EG5, KNSL1, TRIP5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1056 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9
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.9
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › spindle pole Ref.9.
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). Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 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.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Sequence similarities	Belongs to the kinesin-like protein family. BimC subfamily. Contains 1 kinesin-motor domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based movement Traceable author statement. Source: Reactome spindle assembly involved in mitosis Inferred from direct assay Ref.9. Source: UniProtKB
Cellular component	chromatin remodeling complex Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome kinesin complex Traceable author statement. Source: ProtInc microtubule Inferred from electronic annotation. Source: UniProtKB-KW spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Traceable author statement. Source: ProtInc protein kinase binding Inferred from physical interaction Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1056

1056

Kinesin-like protein KIF11

PRO_0000125372

Regions

Domain

16 – 363

348

Kinesin-motor

Nucleotide binding

105 – 112

8

ATP By similarity

Coiled coil

364 – 480

117

Potential

Coiled coil

736 – 763

28

Potential

Amino acid modifications

Modified residue

146

1

N6-acetyllysine Ref.12

Modified residue

458

1

Phosphothreonine Ref.7

Modified residue

926

1

Phosphothreonine; by CDK1 Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11

Modified residue

931

1

Phosphoserine Ref.6

Modified residue

1029

1

Phosphothreonine Ref.8

Modified residue

1033

1

Phosphoserine; by NEK6 Ref.8 Ref.9

Natural variations

Natural variant

1042

1

L → F.
Corresponds to variant rs34417963 [ dbSNP | Ensembl ].

VAR_049682

Experimental info

Mutagenesis

926

1

T → A: No mitotic phosphorylation. No binding to spindle apparatus. Ref.9

Mutagenesis

1033

1

S → A: Still binds to the mitotic spindle but mitotic progression is impaired. Ref.9

Mutagenesis

1033

1

S → D: Still binds to the mitotic spindle but mitotic progression is impaired. Ref.9

Sequence conflict

674 – 675

2

EL → RNS in CAA59449. Ref.1

Secondary structure

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1056

Helix Strand Turn

Details...

Beta strand

18 – 25

8

Helix

30 – 34

5

Beta strand

41 – 44

4

Turn

45 – 48

4

Beta strand

49 – 53

5

Beta strand

63 – 67

5

Beta strand

69 – 72

4

Helix

78 – 94

17

Beta strand

98 – 106

9

Helix

111 – 115

5

Helix

135 – 149

15

Beta strand

153 – 164

12

Beta strand

167 – 172

6

Beta strand

174 – 176

3

Beta strand

183 – 185

3

Beta strand

188 – 190

3

Beta strand

195 – 197

3

Beta strand

202 – 204

3

Helix

207 – 209

3

Helix

210 – 226

17

Helix

232 – 234

3

Beta strand

235 – 247

13

Beta strand

255 – 265

11

Helix

282 – 304

23

Helix

311 – 313

3

Helix

315 – 319

5

Helix

321 – 324

4

Beta strand

325 – 327

3

Beta strand

330 – 336

7

Helix

340 – 342

3

Helix

343 – 356

14

Sequences

	Sequence		Length	Mass (Da)
	P52732 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: C7F2606FE68DA8EA	FASTA	1,056	119,159
	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

References

	« Hide 'large scale' referencesShow '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: 8548803] [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: 9701554] [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: 15164054] [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: 15489334] [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: 7776974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 818-867.
[6]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926 AND SER-931, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-458, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926; THR-1029 AND SER-1033, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 19001501] [Abstract] Cited for: FUNCTION, INTERACTION WITH NEK6, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-926 AND SER-1033, MUTAGENESIS OF THR-926 AND SER-1033.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, MASS SPECTROMETRY.
[13]	"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: 21269460] [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: 11328809] [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: 17707232] [Abstract] Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
+	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.

IPI

IPI00305289.

PIR

G02157.

RefSeq

NP_004514.2. NM_004523.3.

UniGene

Hs.8878.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P52732.

SMR

P52732. Positions 17-366.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52732. 2 interactions.

MINT

MINT-1152202.

STRING

P52732.

PTM databases

PhosphoSite

P52732.

Polymorphism databases

DMDM

116242604.

Proteomic databases

PeptideAtlas

P52732.

PRIDE

P52732.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260731; ENSP00000260731; ENSG00000138160.

GeneID

3832.

KEGG

hsa:3832.

UCSC

uc001kic.1. human.

Organism-specific databases

CTD

3832.

GeneCards

GC10P094342.

H-InvDB

HIX0035402.

HGNC

HGNC:6388. KIF11.

HPA

CAB017617.
HPA006916.
HPA010568.

MIM

148760. gene.

neXtProt

NX_P52732.

PharmGKB

PA30177.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04666.

HOGENOM

HBG357588.

HOVERGEN

HBG005572.

InParanoid

P52732.

OMA

KAMLEVH.

OrthoDB

EOG4MKNFG.

PhylomeDB

P52732.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P52732.

Bgee

P52732.

CleanEx

HS_KIF11.

Genevestigator

P52732.

GermOnline

ENSG00000138160. Homo sapiens.

Family and domain databases

InterPro

IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]

Gene3D

G3DSA:3.40.850.10. kinesin_motor. 1 hit.

KO

K10398.

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

15061.

SOURCE

Search...

Entry information

Entry name

KIF11_HUMAN

Accession

Primary (citable) accession number: P52732
Secondary accession number(s): A0AV49 , B2RMV3, Q15716, Q5VWX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.