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Protein

Kinesin-2

Gene

ATK2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Possible role in mitosis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi472 – 4798ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • microtubule binding Source: TAIR
  • microtubule motor activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:GQT-2429-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-2
Alternative name(s):
Kinesin-like protein B
Gene namesi
Name:ATK2
Synonyms:KATB
Ordered Locus Names:At4g27180
ORF Names:T24A18.130
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G27180.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Kinesin-2PRO_0000125381Add
BLAST

Proteomic databases

PaxDbiP46864.
PRIDEiP46864.

PTM databases

iPTMnetiP46864.

Expressioni

Gene expression databases

GenevisibleiP46864. AT.

Interactioni

GO - Molecular functioni

  • microtubule binding Source: TAIR

Protein-protein interaction databases

BioGridi14113. 2 interactions.
STRINGi3702.AT4G27180.1.

Structurei

3D structure databases

ProteinModelPortaliP46864.
SMRiP46864. Positions 387-722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini387 – 724338Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3535GlobularAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili36 – 384349Add
BLAST

Domaini

Composed of three structural domains; a small globular N-terminal, a central alpha-helical coiled coil and a large globular C-terminal which is responsible for the motor activity (it hydrolyzes ATP and binds microtubules).

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0239. Eukaryota.
COG5059. LUCA.
HOGENOMiHOG000116164.
InParanoidiP46864.
KOiK10405.
OMAiKERCENT.
PhylomeDBiP46864.

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. 2 hits.
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.

P46864-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGEMTNNGR IRPSFPVKDL TSNEGSEYGG PVEFTREDVE TLLHERIKYK
60 70 80 90 100
SKYNYKERCE NTMDYVKRLR LCIRWFQELE LDYAFEQEKL KNAMEMNEKH
110 120 130 140 150
CADLEVNLKV KEEELNMVID ELRKNFASVQ VQLAKEQTEK LAANESLGKE
160 170 180 190 200
REARIAVESL QAAITEELAK TQGELQTANQ RIQAVNDMYK LLQEYNSSLQ
210 220 230 240 250
LYNSKLQGDL DEAHENIKRG EKERTGIVES IGNLKGQFKA LQDQLAASKV
260 270 280 290 300
SQDDVMKQKD ELVNEIVSLK VEIQQVKDDR DRHITEIETL QAEATKQNDF
310 320 330 340 350
KDTINELESK CSVQNKEIEE LQDQLVASER KLQVADLSTF EKMNEFEEQK
360 370 380 390 400
ESIMELKGRL EEAELKLIEG EKLRKKLHNT IQELKGNIRV FCRVRPLLSG
410 420 430 440 450
ENSSEEAKTI SYPTSLEALG RGIDLLQNGQ SHCFTFDKVF VPSASQEDVF
460 470 480 490 500
VEISQLVQSA LDGYKVCIFA YGQTGSGKTY TMMGRPGNPD EKGLIPRCLE
510 520 530 540 550
QIFQTRQSLR SQGWKYELQV SMLEIYNETI RDLLSTNKEA VRADNGVSPQ
560 570 580 590 600
KYAIKHDASG NTHVVELTVV DVRSSKQVSF LLDHAARNRS VGKTAMNEQS
610 620 630 640 650
SRSHFVFTLK ISGFNESTEQ QVQGVLNLID LAGSERLSKS GSTGDRLKET
660 670 680 690 700
QAINKSLSSL GDVIFALAKK EDHVPFRNSK LTYLLQPCLG GDSKTLMFVN
710 720 730 740
ITPEPSSTGE SLCSLRFAAR VNACEIGTAH RHVNARPLDY RLSLG
Length:745
Mass (Da):84,359
Last modified:November 1, 1995 - v1
Checksum:i6DB352FDF4FD7BC1
GO

Sequence cautioni

The sequence CAB38848.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79573.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21137 mRNA. Translation: BAA04673.1.
AL035680 Genomic DNA. Translation: CAB38848.1. Sequence problems.
AL161566 Genomic DNA. Translation: CAB79573.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85310.1.
PIRiT06048.
RefSeqiNP_567768.1. NM_118852.2.
UniGeneiAt.275.

Genome annotation databases

EnsemblPlantsiAT4G27180.1; AT4G27180.1; AT4G27180.
GeneIDi828826.
GrameneiAT4G27180.1; AT4G27180.1; AT4G27180.
KEGGiath:AT4G27180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21137 mRNA. Translation: BAA04673.1.
AL035680 Genomic DNA. Translation: CAB38848.1. Sequence problems.
AL161566 Genomic DNA. Translation: CAB79573.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85310.1.
PIRiT06048.
RefSeqiNP_567768.1. NM_118852.2.
UniGeneiAt.275.

3D structure databases

ProteinModelPortaliP46864.
SMRiP46864. Positions 387-722.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14113. 2 interactions.
STRINGi3702.AT4G27180.1.

PTM databases

iPTMnetiP46864.

Proteomic databases

PaxDbiP46864.
PRIDEiP46864.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G27180.1; AT4G27180.1; AT4G27180.
GeneIDi828826.
GrameneiAT4G27180.1; AT4G27180.1; AT4G27180.
KEGGiath:AT4G27180.

Organism-specific databases

TAIRiAT4G27180.

Phylogenomic databases

eggNOGiKOG0239. Eukaryota.
COG5059. LUCA.
HOGENOMiHOG000116164.
InParanoidiP46864.
KOiK10405.
OMAiKERCENT.
PhylomeDBiP46864.

Enzyme and pathway databases

BioCyciARA:GQT-2429-MONOMER.

Miscellaneous databases

PROiP46864.

Gene expression databases

GenevisibleiP46864. AT.

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. 2 hits.
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. "Sequencing and characterization of the kinesin-related genes katB and katC of Arabidopsis thaliana."
    Mitsui H., Nakatani K., Yamaguchi-Shinozaki K., Shinozaki K., Nishikawa K., Takahashi H.
    Plant Mol. Biol. 25:865-876(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiATK2_ARATH
AccessioniPrimary (citable) accession number: P46864
Secondary accession number(s): Q9T047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 17, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.