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UniProtKB - P46863 (KL61_DROME)

Entry version 170 (12 Aug 2020)
Sequence version 2 (28 Nov 2002)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi103 – 110ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMotor protein
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-DME-6811434, COPI-dependent Golgi-to-ER retrograde traffic
R-DME-983189, Kinesins

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Kinesin-like protein Klp61F1 Publication
Alternative name(s):
Bipolar kinesin KRP-1301 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Klp61FImported
Synonyms:KLP2
ORF Names:CG9191Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3L

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0004378, Klp61F

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1795160

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001253711 – 1066Kinesin-like protein Klp61FAdd BLAST1066

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei520Phosphothreonine1 Publication1
Modified residuei933Phosphothreonine1 Publication1
Modified residuei949Phosphoserine2 Publications1
Modified residuei1043Phosphoserine1 Publication1
Modified residuei1045Phosphothreonine1 Publication1
Modified residuei1050Phosphoserine1 Publication1
Modified residuei1054Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P46863

PRoteomics IDEntifications database

More...PRIDEi		P46863

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P46863

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0004378, Expressed in embryo and 41 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P46863, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P46863, DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		63681, 7 interactors

Database of interacting proteins

More...DIPi		DIP-22047N

Protein interaction database and analysis system

More...IntActi		P46863, 9 interactors

Molecular INTeraction database

More...MINTi		P46863

STRING: functional protein association networks

More...STRINGi		7227.FBpp0072616

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11066
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P46863

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P46863

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 356Kinesin motorPROSITE-ProRule annotationAdd BLAST338

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. BimC subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0243, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155921

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001485_33_4_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P46863

KEGG Orthology (KO)

More...KOi		K10398

Identification of Orthologs from Complete Genome Data

More...OMAi		PGHKDIE

Database of Orthologous Groups

More...OrthoDBi		179272at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P46863

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.850.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR025901, Kinesin-assoc_MT-bd_dom
IPR027640, Kinesin-like_fam
IPR019821, Kinesin_motor_CS
IPR001752, Kinesin_motor_dom
IPR036961, Kinesin_motor_dom_sf
IPR027417, P-loop_NTPase

The PANTHER Classification System

More...PANTHERi		PTHR24115, PTHR24115, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00225, Kinesin, 1 hit
PF13931, Microtub_bind, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00380, KINESINHEAVY

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00129, KISc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00411, KINESIN_MOTOR_1, 1 hit
PS50067, KINESIN_MOTOR_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i363647366EE0721F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti962L → Q in AAA03718 (PubMed:8227131).Curated1
Sequence conflicti983V → D in AAA03718 (PubMed:8227131).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		A48669

NCBI Reference Sequences

More...RefSeqi		NP_476818.1, NM_057470.5

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0072733; FBpp0072616; FBgn0004378

Database of genes from NCBI RefSeq genomes

More...GeneIDi		38135

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG9191

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WBEelectron microscopy9.40C1-368[»]
4PXTX-ray2.90A/B634-837[»]
4PXUX-ray2.60A/B634-837[»]
6VPOelectron microscopy4.40C1-369[»]
6VPPelectron microscopy4.40C1-369[»]
SMRiP46863
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi63681, 7 interactors
DIPiDIP-22047N
IntActiP46863, 9 interactors
MINTiP46863
STRINGi7227.FBpp0072616

Chemistry databases

ChEMBLiCHEMBL1795160

PTM databases

iPTMnetiP46863

Proteomic databases

PaxDbiP46863
PRIDEiP46863

Genome annotation databases

EnsemblMetazoaiFBtr0072733; FBpp0072616; FBgn0004378
GeneIDi38135
KEGGidme:Dmel_CG9191

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		38135
FlyBaseiFBgn0004378, Klp61F

Phylogenomic databases

eggNOGiKOG0243, Eukaryota
GeneTreeiENSGT00940000155921
HOGENOMiCLU_001485_33_4_1
InParanoidiP46863
KOiK10398
OMAiPGHKDIE
OrthoDBi179272at2759
PhylomeDBiP46863

Enzyme and pathway databases

ReactomeiR-DME-6811434, COPI-dependent Golgi-to-ER retrograde traffic
R-DME-983189, Kinesins

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		38135, 1 hit in 1 CRISPR screen
EvolutionaryTraceiP46863

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		38135

Protein Ontology

More...PROi		PR:P46863

Gene expression databases

BgeeiFBgn0004378, Expressed in embryo and 41 other tissues
ExpressionAtlasiP46863, baseline and differential
GenevisibleiP46863, DM

Family and domain databases

Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR025901, Kinesin-assoc_MT-bd_dom
IPR027640, Kinesin-like_fam
IPR019821, Kinesin_motor_CS
IPR001752, Kinesin_motor_dom
IPR036961, Kinesin_motor_dom_sf
IPR027417, P-loop_NTPase
PANTHERiPTHR24115, PTHR24115, 1 hit
PfamiView protein in Pfam
PF00225, Kinesin, 1 hit
PF13931, Microtub_bind, 1 hit
PRINTSiPR00380, KINESINHEAVY
SMARTiView protein in SMART
SM00129, KISc, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00411, KINESIN_MOTOR_1, 1 hit
PS50067, KINESIN_MOTOR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKL61_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P46863
Secondary accession number(s): Q8T0A6, Q9W0I8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 28, 2002
Last modified: August 12, 2020
This is version 170 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
UniProt is an ELIXIR core data resource
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