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Protein

Kinesin-like protein KIF23

Gene

Kif23

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi112 – 1198ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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

ReactomeiREACT_309373. Mitotic Telophase/Cytokinesis.
REACT_316383. MHC class II antigen presentation.
REACT_342780. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF23
Gene namesi
Name:Kif23
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1919069. Kif23.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Midbody 1 Publication

  • Note: Localizes to the interzone of mitotic spindles (By similarity). Detected at the midbody during later stages of mitotic cytokinesis.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 953953Kinesin-like protein KIF23PRO_0000425085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei160 – 1601PhosphoserineBy similarity
Modified residuei606 – 6061PhosphoserineBy similarity
Modified residuei739 – 7391PhosphothreonineBy similarity
Modified residuei807 – 8071PhosphoserineBy similarity
Modified residuei860 – 8601Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated. Deubiquitinated by USP8/UBPY (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiE9Q5G3.
PRIDEiE9Q5G3.

Expressioni

Tissue specificityi

Detected in testis and ovary from newborn mice (at protein level). Detected in brain, spinal cord and small intestine.2 Publications

Gene expression databases

BgeeiE9Q5G3.
GenevisibleiE9Q5G3. MM.

Interactioni

Subunit structurei

Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Interacts with RACGAP1; the interaction is direct. Interacts with ECT2 and PRC1. Interacts with ANXA11 during cytokinesis. Interacts with BIRC6/bruce and USP8/UBPY (By similarity). Interacts with ARF6, forming heterodimers and heterotetramers.By similarity1 Publication

Protein-protein interaction databases

BioGridi214951. 10 interactions.
IntActiE9Q5G3. 12 interactions.
STRINGi10090.ENSMUSP00000034815.

Structurei

3D structure databases

ProteinModelPortaliE9Q5G3.
SMRiE9Q5G3. Positions 21-436, 811-896.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 436412Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili542 – 61877Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 115Nuclear localization signalSequence Analysis

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00770000120528.
HOGENOMiHOG000273893.
InParanoidiE9Q5G3.
KOiK17387.
OMAiIHESSID.
OrthoDBiEOG7PCJG5.
TreeFamiTF105232.

Family and domain databases

Gene3Di3.40.850.10. 2 hits.
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. 3 hits.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9Q5G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSAKAKTVR KPVIKKGSQT NLKDPVGVYC RVRPLSFPDQ ECCVEVINST
60 70 80 90 100
TLQLHTPEGY RLNRNGDYKE TQYSFKRVFG THTTQKELFD VVANPLVDDL
110 120 130 140 150
IHGKNGLLFT YGVTGSGKTY TMTGSPGSGG LLPRCLNMIF NSIGSFQAKR
160 170 180 190 200
YVFKSNDRNS MEIQCEVDAL LERQKREALP IPKTPSSKRQ ADPEFADMIN
210 220 230 240 250
VQEFCKAEEV DEDSVYGVFV SYIEIYNNYI YDLLEEVQFD PIKPKLPQSK
260 270 280 290 300
TLREDKNHNM YVAGCTEVEV KSTEEAFEVF WRGQKKRRIA NTHLNRESSR
310 320 330 340 350
SHSVFSIKLV QAPLDADGDN VLQEKEQITI SQLSLVDLAG SERTNRTKAE
360 370 380 390 400
GNRLREAGNI NQSLMTLRTC MEVLRENQTY GTNKMVPYRD SKLTHLFKNY
410 420 430 440 450
FDGEGKVRMI VCVNPKAEDY EESLQVMRFA EVTQEVEVAR PVDKVICGLT
460 470 480 490 500
PGRRYRNLPR GGPVGDEPLV PEVILQSFPP LPPCKLLDIN DEETLPKLAD
510 520 530 540 550
TLEKRHHLRQ LMTEDLNKKC LAFKALLKEF DNSLSNKENY VQEKLNEREK
560 570 580 590 600
VISGQKLEIE RLEKKNKTLE YKIEILEKTT TIYEEDKRNL QQELESQNQK
610 620 630 640 650
LQRQFSDKRR LEARLQGMVT ETSMKWQKEC ERRVAATQLE MQNKLWVKDE
660 670 680 690 700
KLKQLKAIVT EPKPEKPERP SRERDREKII PRSVSPSPLP LSSNNIAQIS
710 720 730 740 750
NGQQLMSQPQ LHRRSNSCSS ISVASCISEW EQKLSPFSTP VNVTSLARHR
760 770 780 790 800
QQEPGQSKTC IVSDRRRGMC WTEGREMVPT FSSEIGVEED HCRRNTPIPV
810 820 830 840 850
RHRRSRSAGS RWVDHKPASN VQTETVMQPH VPHAITVSVA NEKALAKCEK
860 870 880 890 900
YMLTHQELAS DGEIQTKVIK GDVYKTRGGG QSVQFTDIET LKQELPTGSR
910 920 930 940 950
KRRSSTLAPA QPDGTESEWT DVETRCSVAV EMRAGSQLGP GYQHHAQPKR

KKP
Length:953
Mass (Da):108,776
Last modified:April 5, 2011 - v1
Checksum:iDE6E050D59A18513
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 4641V → I in AAH47273 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC151969 Genomic DNA. No translation available.
BC047273 mRNA. Translation: AAH47273.1.
AB054027 Genomic DNA. Translation: BAB32491.1.
CCDSiCCDS40662.1.
RefSeqiNP_077207.3. NM_024245.4.
UniGeneiMm.259374.

Genome annotation databases

EnsembliENSMUST00000034815; ENSMUSP00000034815; ENSMUSG00000032254.
GeneIDi71819.
KEGGimmu:71819.
UCSCiuc009pzu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC151969 Genomic DNA. No translation available.
BC047273 mRNA. Translation: AAH47273.1.
AB054027 Genomic DNA. Translation: BAB32491.1.
CCDSiCCDS40662.1.
RefSeqiNP_077207.3. NM_024245.4.
UniGeneiMm.259374.

3D structure databases

ProteinModelPortaliE9Q5G3.
SMRiE9Q5G3. Positions 21-436, 811-896.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214951. 10 interactions.
IntActiE9Q5G3. 12 interactions.
STRINGi10090.ENSMUSP00000034815.

Proteomic databases

MaxQBiE9Q5G3.
PRIDEiE9Q5G3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034815; ENSMUSP00000034815; ENSMUSG00000032254.
GeneIDi71819.
KEGGimmu:71819.
UCSCiuc009pzu.2. mouse.

Organism-specific databases

CTDi9493.
MGIiMGI:1919069. Kif23.

Phylogenomic databases

GeneTreeiENSGT00770000120528.
HOGENOMiHOG000273893.
InParanoidiE9Q5G3.
KOiK17387.
OMAiIHESSID.
OrthoDBiEOG7PCJG5.
TreeFamiTF105232.

Enzyme and pathway databases

ReactomeiREACT_309373. Mitotic Telophase/Cytokinesis.
REACT_316383. MHC class II antigen presentation.
REACT_342780. Kinesins.

Miscellaneous databases

NextBioi334596.
PROiE9Q5G3.
SOURCEiSearch...

Gene expression databases

BgeeiE9Q5G3.
GenevisibleiE9Q5G3. MM.

Family and domain databases

Gene3Di3.40.850.10. 2 hits.
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. 3 hits.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  3. "All kinesin superfamily protein, KIF, genes in mouse and human."
    Miki H., Setou M., Kaneshiro K.
    Proc. Natl. Acad. Sci. U.S.A. 98:7004-7011(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-340, TISSUE SPECIFICITY.
  4. "Mouse TEX14 is required for embryonic germ cell intercellular bridges but not female fertility."
    Greenbaum M.P., Iwamori N., Agno J.E., Matzuk M.M.
    Biol. Reprod. 80:449-457(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis."
    Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A., Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M., Kawasaki M., Kato R., Wakatsuki S., Nakayama K.
    EMBO J. 31:2590-2603(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF6.

Entry informationi

Entry nameiKIF23_MOUSE
AccessioniPrimary (citable) accession number: E9Q5G3
Secondary accession number(s): Q80V30, Q99PT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: April 5, 2011
Last modified: June 24, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.