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Protein

Kinesin-like protein Klp61F

Gene

Klp61F

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

Functioni

Important role in mitotic dividing cells (PubMed:8227131). Microtubule motor required for spindle body separation (PubMed:8918872). Slow plus-end directed microtubule motor capable of cross-linking and sliding apart antiparallel microtubules, thereby pushing apart the associated spindle poles during spindle assembly and function (PubMed:8918872, PubMed:8589456, PubMed:19062285). Forms cross-links between microtubules within interpolar microtubule bundles (PubMed:9885249, PubMed:19158379). Contributes to the length of the metaphase spindle, maintains the prometaphase spindle by antagonizing Ncd, drives anaphase B, and also contributes to normal chromosome congression, kinetochore spacing, and anaphase A rates (PubMed:19158379). Displays microtubule-stimulated ATPase activity (PubMed:8589456). Required for normal fusome organization (PubMed:10469596). Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (PubMed:23857769).8 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi103 – 110ATPPROSITE-ProRule annotation8

GO - Molecular functioni

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

GO - Biological processi

  • adult chitin-containing cuticle pigmentation Source: FlyBase
  • cell division Source: UniProtKB-KW
  • centrosome duplication Source: FlyBase
  • centrosome separation Source: FlyBase
  • chromosome segregation Source: GO_Central
  • fusome organization Source: UniProtKB
  • Golgi organization Source: FlyBase
  • microtubule-based movement Source: UniProtKB
  • microtubule bundle formation Source: FlyBase
  • mitotic cell cycle Source: FlyBase
  • mitotic centrosome separation Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • mitotic spindle assembly Source: GO_Central
  • mitotic spindle organization Source: FlyBase
  • neurogenesis Source: FlyBase
  • plus-end directed microtubule sliding Source: FlyBase
  • positive regulation of Golgi to plasma membrane protein transport Source: UniProtKB
  • protein homotetramerization Source: FlyBase
  • protein secretion Source: FlyBase
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

ReactomeiR-DME-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein Klp61F1 Publication
Alternative name(s):
Bipolar kinesin KRP-1301 Publication
Gene namesi
Name:Klp61FImported
Synonyms:KLP2
ORF Names:CG9191Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004378. Klp61F.

Subcellular locationi

GO - Cellular componenti

  • aster Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: FlyBase
  • fusome Source: UniProtKB
  • Golgi apparatus Source: FlyBase
  • kinesin complex Source: FlyBase
  • microtubule Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitotic spindle Source: UniProtKB
  • mitotic spindle microtubule Source: FlyBase
  • mitotic spindle pole Source: UniProtKB
  • nucleus Source: UniProtKB
  • spindle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23Y → F: Spindle defects and greatly reduced phosphorylation by Wee1 in vitro; when associated with F-152 and F-207. 1 Publication1
Mutagenesisi152Y → F: Spindle defects and greatly reduced phosphorylation by Wee1 in vitro; when associated with F-23 and F-207. 1 Publication1
Mutagenesisi207Y → F: Spindle defects and greatly reduced phosphorylation by Wee1 in vitro; when associated with F-23 and F-152. 1 Publication1
Mutagenesisi669F → E: Remains tetrameric. 1 Publication1
Mutagenesisi726L → D: Mainly tetrameric. Mainly dimeric; when associated with R-775. 1 Publication1
Mutagenesisi726L → K: Mainly tetrameric. 1 Publication1
Mutagenesisi729 – 730MM → EE: Mainly monomeric. 1 Publication2
Mutagenesisi740R → A: Formation of tetramers, dimers and monomers. 1 Publication1
Mutagenesisi761R → A: Formation of tetramers and dimers. 1 Publication1
Mutagenesisi775Y → R: Mainly tetrameric with formation of some monomers. Mainly dimeric; when associated with D-726. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1795160.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001253711 – 1066Kinesin-like protein Klp61FAdd BLAST1066

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei520Phosphothreonine1 Publication1
Modified residuei933Phosphothreonine1 Publication1
Modified residuei949Phosphoserine2 Publications1
Modified residuei1043Phosphoserine1 Publication1
Modified residuei1045Phosphothreonine1 Publication1
Modified residuei1050Phosphoserine1 Publication1
Modified residuei1054Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylation is required for localization to mitotic spindles (PubMed:9885249). Phosphorylation of Thr-933 during mitosis controls association with the spindle apparatus (By similarity). Phosphorylated in vitro by Wee1 (PubMed:19800237).By similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP46863.
PRIDEiP46863.

PTM databases

iPTMnetiP46863.

Expressioni

Developmental stagei

Specifically expressed in proliferating tissues during embryonic and larval development.1 Publication

Gene expression databases

BgeeiFBgn0004378.
GenevisibleiP46863. DM.

Interactioni

Subunit structurei

Homotetramer (PubMed:8538794, PubMed:9885249, PubMed:24714498). Consists of two pairs of polypeptides associated by coiled-coil interactions to form two homodimers (PubMed:8538794). The homodimers are linked by lateral interactions between their coiled-coil regions to form a bipolar homotetramer consisting of a central rod with two motor domains projecting from either end (PubMed:8538794). Parallel coiled coils extend from each pair of motor heads, switch to two antiparallel coiled coils in the central region and then back to parallel coiled coils (PubMed:24714498). Interacts with Wee1 (PubMed:19800237).4 Publications

GO - Molecular functioni

  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi63681. 2 interactors.
DIPiDIP-22047N.
IntActiP46863. 9 interactors.
MINTiMINT-807581.
STRINGi7227.FBpp0072616.

Structurei

Secondary structure

11066
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi641 – 695Combined sources55
Helixi698 – 790Combined sources93
Helixi792 – 794Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WBEelectron microscopy9.40C1-368[»]
4PXTX-ray2.90A/B634-837[»]
4PXUX-ray2.60A/B634-837[»]
ProteinModelPortaliP46863.
SMRiP46863.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46863.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 356Kinesin motorPROSITE-ProRule annotationAdd BLAST338

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili362 – 462Sequence analysisAdd BLAST101
Coiled coili540 – 569Sequence analysisAdd BLAST30
Coiled coili639 – 738Sequence analysisAdd BLAST100
Coiled coili808 – 875Sequence analysisAdd BLAST68
Coiled coili889 – 918Sequence analysisAdd BLAST30

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 coil

Phylogenomic databases

eggNOGiKOG0243. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00840000129680.
InParanoidiP46863.
KOiK10398.
OMAiRQQLQIC.
OrthoDBiEOG091G013C.
PhylomeDBiP46863.

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. 2 hits.
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.

P46863-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDISGGNTSR QPQKKSNQNI QVYVRVRPLN SRERCIRSAE VVDVVGPREV
60 70 80 90 100
VTRHTLDSKL TKKFTFDRSF GPESKQCDVY SVVVSPLIEE VLNGYNCTVF
110 120 130 140 150
AYGQTGTGKT HTMVGNETAE LKSSWEDDSD IGIIPRALSH LFDELRMMEV
160 170 180 190 200
EYTMRISYLE LYNEELCDLL STDDTTKIRI FDDSTKKGSV IIQGLEEIPV
210 220 230 240 250
HSKDDVYKLL EKGKERRKTA TTLMNAQSSR SHTVFSIVVH IRENGIEGED
260 270 280 290 300
MLKIGKLNLV DLAGSENVSK AGNEKGIRVR ETVNINQSLL TLGRVITALV
310 320 330 340 350
DRAPHVPYRE SKLTRLLQES LGGRTKTSII ATISPGHKDI EETLSTLEYA
360 370 380 390 400
HRAKNIQNKP EVNQKLTKKT VLKEYTEEID KLKRDLMAAR DKNGIYLAEE
410 420 430 440 450
TYGEITLKLE SQNRELNEKM LLLKALKDEL QNKEKIFSEV SMSLVEKTQE
460 470 480 490 500
LKKTEENLLN TKGTLLLTKK VLTKTKRRYK EKKELVASHM KTEQVLTTQA
510 520 530 540 550
QEILAAADLA TDDTHQLHGT IERRRELDEK IRRSCDQFKD RMQDNLEMIG
560 570 580 590 600
GSLNLYQDQQ AALKEQLSQE MVNSSYVSQR LALNSSKSIE MLKEMCAQSL
610 620 630 640 650
QDQTNLHNKL IGEVMKISDQ HSQAFVAKLM EQMQQQQLLM SKEIQTNLQV
660 670 680 690 700
IEENNQRHKA MLDSMQEKFA TIIDSSLQSV EEHAKQMHKK LEQLGAMSLP
710 720 730 740 750
DAEELQNLQE ELANERALAQ QEDALLESMM MQMEQIKNLR SKNSISMSVH
760 770 780 790 800
LNKMEESRLT RNHRIDDIKS GIQDYQKLGI EASQSAQAEL TSQMEAGMLC
810 820 830 840 850
LDQGVANCSM LQVHMKNLNQ KYEKETNENV GSVRVHHNQV EIICQESKQQ
860 870 880 890 900
LEAVQEKTEV NLEQMVDARQ QLITEDRQRF IGHATVATDL VQESNRQFSE
910 920 930 940 950
HAEHQRQQLQ ICEQELVRFQ QSELKTYAPT GTTPSKRDFV YPRTLVATSP
960 970 980 990 1000
HQEIVRRYRQ ELDWSDLDTT ATIDECSEGE HDVSMHSVQE LSETETIMNS
1010 1020 1030 1040 1050
TPIEPVDGVT VKRGCGTTRN SNSNALKPPV ATGGKRSSSL SRSLTPSKTS
1060
PRGSPAFVRH NKENVA
Length:1,066
Mass (Da):121,163
Last modified:November 28, 2002 - v2
Checksum:i363647366EE0721F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti962L → Q in AAA03718 (PubMed:8227131).Curated1
Sequence conflicti983V → D in AAA03718 (PubMed:8227131).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01842 mRNA. Translation: AAA03718.1.
AE014296 Genomic DNA. Translation: AAF47458.2.
AY069442 mRNA. Translation: AAL39587.1.
M74428 Genomic DNA. Translation: AAA28655.1.
PIRiA48669.
RefSeqiNP_476818.1. NM_057470.5.
UniGeneiDm.804.

Genome annotation databases

EnsemblMetazoaiFBtr0072733; FBpp0072616; FBgn0004378.
GeneIDi38135.
KEGGidme:Dmel_CG9191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01842 mRNA. Translation: AAA03718.1.
AE014296 Genomic DNA. Translation: AAF47458.2.
AY069442 mRNA. Translation: AAL39587.1.
M74428 Genomic DNA. Translation: AAA28655.1.
PIRiA48669.
RefSeqiNP_476818.1. NM_057470.5.
UniGeneiDm.804.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WBEelectron microscopy9.40C1-368[»]
4PXTX-ray2.90A/B634-837[»]
4PXUX-ray2.60A/B634-837[»]
ProteinModelPortaliP46863.
SMRiP46863.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63681. 2 interactors.
DIPiDIP-22047N.
IntActiP46863. 9 interactors.
MINTiMINT-807581.
STRINGi7227.FBpp0072616.

Chemistry databases

ChEMBLiCHEMBL1795160.

PTM databases

iPTMnetiP46863.

Proteomic databases

PaxDbiP46863.
PRIDEiP46863.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072733; FBpp0072616; FBgn0004378.
GeneIDi38135.
KEGGidme:Dmel_CG9191.

Organism-specific databases

CTDi38135.
FlyBaseiFBgn0004378. Klp61F.

Phylogenomic databases

eggNOGiKOG0243. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00840000129680.
InParanoidiP46863.
KOiK10398.
OMAiRQQLQIC.
OrthoDBiEOG091G013C.
PhylomeDBiP46863.

Enzyme and pathway databases

ReactomeiR-DME-983189. Kinesins.

Miscellaneous databases

EvolutionaryTraceiP46863.
GenomeRNAii38135.
PROiP46863.

Gene expression databases

BgeeiFBgn0004378.
GenevisibleiP46863. DM.

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. 2 hits.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiKL61_DROME
AccessioniPrimary (citable) accession number: P46863
Secondary accession number(s): Q8T0A6, Q9W0I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 28, 2002
Last modified: November 30, 2016
This is version 146 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, Direct protein sequencing, 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.