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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi92 – 99ATPPROSITE-ProRule annotation8

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, nurse cell to oocyte Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • dorsal appendage formation 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
  • neuron projection morphogenesis 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
  • transport along microtubule Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
  • cytosol Source: GOC
  • kinesin complex Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • microtubule plus-end Source: FlyBase
  • neuron projection 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)DescriptionActionsGraphical viewLength
ChainiPRO_00001253501 – 975Kinesin heavy chainAdd BLAST975

Proteomic databases

PaxDbiP17210.
PRIDEiP17210.

Expressioni

Gene expression databases

BgeeiFBgn0001308.
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 interactors.
DIPiDIP-20367N.
IntActiP17210. 5 interactors.
MINTiMINT-868666.
STRINGi7227.FBpp0086328.

Structurei

Secondary structure

1975
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Beta strandi14 – 19Combined sources6
Helixi24 – 28Combined sources5
Beta strandi39 – 41Combined sources3
Beta strandi45 – 48Combined sources4
Beta strandi51 – 54Combined sources4
Beta strandi56 – 59Combined sources4
Helixi65 – 72Combined sources8
Helixi74 – 81Combined sources8
Beta strandi86 – 91Combined sources6
Helixi98 – 102Combined sources5
Turni109 – 111Combined sources3
Helixi114 – 128Combined sources15
Beta strandi133 – 145Combined sources13
Beta strandi148 – 151Combined sources4
Beta strandi162 – 164Combined sources3
Beta strandi166 – 168Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi178 – 180Combined sources3
Helixi183 – 197Combined sources15
Turni198 – 200Combined sources3
Helixi204 – 209Combined sources6
Beta strandi211 – 223Combined sources13
Turni224 – 226Combined sources3
Beta strandi229 – 238Combined sources10
Helixi263 – 277Combined sources15
Helixi285 – 287Combined sources3
Helixi289 – 293Combined sources5
Helixi295 – 297Combined sources3
Beta strandi300 – 310Combined sources11
Helixi314 – 316Combined sources3
Helixi317 – 330Combined sources14
Beta strandi334 – 336Combined sources3
Beta strandi340 – 342Combined sources3
Helixi345 – 365Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y5WX-ray2.70A/B1-365[»]
2Y65X-ray2.20A/B/C/D1-365[»]
W/X/Y937-952[»]
5JVRX-ray2.10A/B/C/D/E/F/G/H345-358[»]
5JVSX-ray2.25A334-392[»]
5JVUX-ray1.95A/B334-365[»]
A/B386-410[»]
ProteinModelPortaliP17210.
SMRiP17210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 333Kinesin motorPROSITE-ProRule annotationAdd BLAST322

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni180 – 321Microtubule-bindingAdd BLAST142
Regioni810 – 891Necessary for associating with miltAdd BLAST82
Regioni932 – 975GlobularAdd BLAST44

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili335 – 931Add BLAST597

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.
GeneTreeiENSGT00860000133684.
InParanoidiP17210.
KOiK10396.
OMAiDEMKDVH.
OrthoDBiEOG091G02A2.
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)DescriptionActionsGraphical viewLength
Sequence conflicti515A → T in AAA28652 (PubMed:2522352).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y5WX-ray2.70A/B1-365[»]
2Y65X-ray2.20A/B/C/D1-365[»]
W/X/Y937-952[»]
5JVRX-ray2.10A/B/C/D/E/F/G/H345-358[»]
5JVSX-ray2.25A334-392[»]
5JVUX-ray1.95A/B334-365[»]
A/B386-410[»]
ProteinModelPortaliP17210.
SMRiP17210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP17210.
PRIDEiP17210.

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.
GeneTreeiENSGT00860000133684.
InParanoidiP17210.
KOiK10396.
OMAiDEMKDVH.
OrthoDBiEOG091G02A2.
PhylomeDBiP17210.

Miscellaneous databases

GenomeRNAii36810.
PROiP17210.

Gene expression databases

BgeeiFBgn0001308.
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...

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: November 30, 2016
This is version 157 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.