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Protein

Kinesin heavy chain

Gene

Khc

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi92 – 998ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent microtubule motor activity, plus-end-directed Source: FlyBase
  • microtubule binding Source: FlyBase
  • microtubule motor activity Source: FlyBase
  • motor activity Source: FlyBase

GO - Biological processi

  • actin filament bundle organization Source: FlyBase
  • axo-dendritic transport Source: FlyBase
  • axon guidance Source: FlyBase
  • axonogenesis Source: FlyBase
  • centrosome separation Source: FlyBase
  • cytoplasmic transport Source: FlyBase
  • cytoplasmic transport, nurse cell to oocyte Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • establishment of localization by movement along microtubule Source: FlyBase
  • establishment of nucleus localization Source: FlyBase
  • eye photoreceptor cell differentiation Source: FlyBase
  • intracellular distribution of mitochondria Source: FlyBase
  • intracellular protein transport Source: FlyBase
  • larval locomotory behavior Source: FlyBase
  • maintenance of cell polarity Source: FlyBase
  • microtubule-based movement Source: FlyBase
  • microtubule polymerization Source: FlyBase
  • microtubule sliding Source: FlyBase
  • mitochondrion distribution Source: FlyBase
  • mitochondrion transport along microtubule Source: FlyBase
  • neuronal action potential propagation Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • neurotransmitter secretion Source: FlyBase
  • oocyte dorsal/ventral axis specification Source: FlyBase
  • oocyte microtubule cytoskeleton polarization Source: FlyBase
  • pole plasm assembly Source: FlyBase
  • pole plasm oskar mRNA localization Source: FlyBase
  • regulation of pole plasm oskar mRNA localization Source: FlyBase
  • skeletal muscle fiber development Source: FlyBase
  • stress granule disassembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin heavy chain
Gene namesi
Name:Khc
Synonyms:kin
ORF Names:CG7765
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0001308. Khc.

Subcellular locationi

GO - Cellular componenti

  • actin cap Source: FlyBase
  • cytoplasm Source: FlyBase
  • kinesin complex Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • microtubule plus-end Source: FlyBase
  • neuron projection Source: GOC
  • presynapse Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Disruption phenotypei

Flies display impaired action potential propagation and neurotransmitter release at neuromuscular junctions, but are still capable of transporting certain membranes, including synaptic vesicles, to the nerve terminal.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 975975Kinesin heavy chainPRO_0000125350Add
BLAST

Proteomic databases

PaxDbiP17210.

Expressioni

Gene expression databases

BgeeiP17210.
ExpressionAtlasiP17210. differential.
GenevisibleiP17210. DM.

Interactioni

Subunit structurei

Oligomer composed of two heavy chains and two light chains.

GO - Molecular functioni

  • microtubule binding Source: FlyBase

Protein-protein interaction databases

BioGridi62529. 26 interactions.
DIPiDIP-20367N.
IntActiP17210. 5 interactions.
MINTiMINT-868666.
STRINGi7227.FBpp0086328.

Structurei

Secondary structure

1
975
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Beta strandi14 – 196Combined sources
Helixi24 – 285Combined sources
Beta strandi39 – 413Combined sources
Beta strandi45 – 484Combined sources
Beta strandi51 – 544Combined sources
Beta strandi56 – 594Combined sources
Helixi65 – 728Combined sources
Helixi74 – 818Combined sources
Beta strandi86 – 916Combined sources
Helixi98 – 1025Combined sources
Turni109 – 1113Combined sources
Helixi114 – 12815Combined sources
Beta strandi133 – 14513Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi178 – 1803Combined sources
Helixi183 – 19715Combined sources
Turni198 – 2003Combined sources
Helixi204 – 2096Combined sources
Beta strandi211 – 22313Combined sources
Turni224 – 2263Combined sources
Beta strandi229 – 23810Combined sources
Helixi263 – 27715Combined sources
Helixi285 – 2873Combined sources
Helixi289 – 2935Combined sources
Helixi295 – 2973Combined sources
Beta strandi300 – 31011Combined sources
Helixi314 – 3163Combined sources
Helixi317 – 33014Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi340 – 3423Combined sources
Helixi346 – 3505Combined sources
Helixi352 – 3609Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y5WX-ray2.70A/B1-365[»]
2Y65X-ray2.20A/B/C/D1-365[»]
W/X/Y937-952[»]
ProteinModelPortaliP17210.
SMRiP17210. Positions 7-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 333322Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni180 – 321142Microtubule-bindingAdd
BLAST
Regioni810 – 89182Necessary for associating with miltAdd
BLAST
Regioni932 – 97544GlobularAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili335 – 931597Add
BLAST

Domaini

Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.1 Publication

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0240. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00840000129683.
InParanoidiP17210.
KOiK10396.
OMAiQHEMDEM.
OrthoDBiEOG7T4MJD.
PhylomeDBiP17210.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. 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.
[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.

P17210-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEREIPAE DSIKVVCRFR PLNDSEEKAG SKFVVKFPNN VEENCISIAG
60 70 80 90 100
KVYLFDKVFK PNASQEKVYN EAAKSIVTDV LAGYNGTIFA YGQTSSGKTH
110 120 130 140 150
TMEGVIGDSV KQGIIPRIVN DIFNHIYAME VNLEFHIKVS YYEIYMDKIR
160 170 180 190 200
DLLDVSKVNL SVHEDKNRVP YVKGATERFV SSPEDVFEVI EEGKSNRHIA
210 220 230 240 250
VTNMNEHSSR SHSVFLINVK QENLENQKKL SGKLYLVDLA GSEKVSKTGA
260 270 280 290 300
EGTVLDEAKN INKSLSALGN VISALADGNK THIPYRDSKL TRILQESLGG
310 320 330 340 350
NARTTIVICC SPASFNESET KSTLDFGRRA KTVKNVVCVN EELTAEEWKR
360 370 380 390 400
RYEKEKEKNA RLKGKVEKLE IELARWRAGE TVKAEEQINM EDLMEASTPN
410 420 430 440 450
LEVEAAQTAA AEAALAAQRT ALANMSASVA VNEQARLATE CERLYQQLDD
460 470 480 490 500
KDEEINQQSQ YAEQLKEQVM EQEELIANAR REYETLQSEM ARIQQENESA
510 520 530 540 550
KEEVKEVLQA LEELAVNYDQ KSQEIDNKNK DIDALNEELQ QKQSVFNAAS
560 570 580 590 600
TELQQLKDMS SHQKKRITEM LTNLLRDLGE VGQAIAPGES SIDLKMSALA
610 620 630 640 650
GTDASKVEED FTMARLFISK MKTEAKNIAQ RCSNMETQQA DSNKKISEYE
660 670 680 690 700
KDLGEYRLLI SQHEARMKSL QESMREAENK KRTLEEQIDS LREECAKLKA
710 720 730 740 750
AEHVSAVNAE EKQRAEELRS MFDSQMDELR EAHTRQVSEL RDEIAAKQHE
760 770 780 790 800
MDEMKDVHQK LLLAHQQMTA DYEKVRQEDA EKSSELQNII LTNERREQAR
810 820 830 840 850
KDLKGLEDTV AKELQTLHNL RKLFVQDLQQ RIRKNVVNEE SEEDGGSLAQ
860 870 880 890 900
KQKISFLENN LDQLTKVHKQ LVRDNADLRC ELPKLEKRLR CTMERVKALE
910 920 930 940 950
TALKEAKEGA MRDRKRYQYE VDRIKEAVRQ KHLGRRGPQA QIAKPIRSGQ
960 970
GAIAIRGGGA VGGPSPLAQV NPVNS
Length:975
Mass (Da):110,399
Last modified:October 18, 2001 - v2
Checksum:i24840EF414790888
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti515 – 5151A → T in AAA28652 (PubMed:2522352).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24441 mRNA. Translation: AAA28652.1.
AE013599 Genomic DNA. Translation: AAF58029.1.
AY094959 mRNA. Translation: AAM11312.1.
PIRiA31497.
RefSeqiNP_476590.1. NM_057242.5.
UniGeneiDm.7076.

Genome annotation databases

EnsemblMetazoaiFBtr0087184; FBpp0086328; FBgn0001308.
GeneIDi36810.
KEGGidme:Dmel_CG7765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24441 mRNA. Translation: AAA28652.1.
AE013599 Genomic DNA. Translation: AAF58029.1.
AY094959 mRNA. Translation: AAM11312.1.
PIRiA31497.
RefSeqiNP_476590.1. NM_057242.5.
UniGeneiDm.7076.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y5WX-ray2.70A/B1-365[»]
2Y65X-ray2.20A/B/C/D1-365[»]
W/X/Y937-952[»]
ProteinModelPortaliP17210.
SMRiP17210. Positions 7-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62529. 26 interactions.
DIPiDIP-20367N.
IntActiP17210. 5 interactions.
MINTiMINT-868666.
STRINGi7227.FBpp0086328.

Proteomic databases

PaxDbiP17210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087184; FBpp0086328; FBgn0001308.
GeneIDi36810.
KEGGidme:Dmel_CG7765.

Organism-specific databases

CTDi36810.
FlyBaseiFBgn0001308. Khc.

Phylogenomic databases

eggNOGiKOG0240. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00840000129683.
InParanoidiP17210.
KOiK10396.
OMAiQHEMDEM.
OrthoDBiEOG7T4MJD.
PhylomeDBiP17210.

Enzyme and pathway databases

ReactomeiR-DME-983189. Kinesins.

Miscellaneous databases

GenomeRNAii36810.
NextBioi800509.
PROiP17210.

Gene expression databases

BgeeiP17210.
ExpressionAtlasiP17210. differential.
GenevisibleiP17210. DM.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. 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.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses."
    Yang J.T., Laymon R.A., Goldstein L.S.B.
    Cell 56:879-889(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Effects of kinesin mutations on neuronal functions."
    Gho M., McDonald K., Ganetzky B., Saxton W.M.
    Science 258:313-316(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent."
    Glater E.E., Megeath L.J., Stowers R.S., Schwarz T.L.
    J. Cell Biol. 173:545-557(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiKINH_DROME
AccessioniPrimary (citable) accession number: P17210
Secondary accession number(s): Q9V7L9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 18, 2001
Last modified: May 11, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar 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 one 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.