Details for: KIF23

Gene ID: 9493

Symbol: KIF23

Ensembl ID: ENSG00000137807

Description: kinesin family member 23

Associated with

Other Information

Genular Protein ID: 3477670255

Symbol: KIF23_HUMAN

Name: Kinesin-like protein KIF23

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 1406973

Title: A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles.

PubMed ID: 1406973

DOI: 10.1038/359543a0

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11782313

Title: Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity.

PubMed ID: 11782313

DOI: 10.1016/s1534-5807(01)00110-1

PubMed ID: 15297875

Title: Essential roles of KIF4 and its binding partner PRC1 in organized central spindle midzone formation.

PubMed ID: 15297875

DOI: 10.1038/sj.emboj.7600347

PubMed ID: 15197175

Title: Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis.

PubMed ID: 15197175

DOI: 10.1083/jcb.200311054

PubMed ID: 16213214

Title: Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission.

PubMed ID: 16213214

DOI: 10.1016/j.cell.2005.07.027

PubMed ID: 16103226

Title: An ECT2-centralspindlin complex regulates the localization and function of RhoA.

PubMed ID: 16103226

DOI: 10.1083/jcb.200501097

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16236794

Title: Dissecting the role of Rho-mediated signaling in contractile ring formation.

PubMed ID: 16236794

DOI: 10.1091/mbc.e05-06-0569

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18329369

Title: Final stages of cytokinesis and midbody ring formation are controlled by BRUCE.

PubMed ID: 18329369

DOI: 10.1016/j.cell.2008.01.012

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19468300

Title: Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation.

PubMed ID: 19468300

DOI: 10.1371/journal.pbio.1000110

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 22522702

Title: Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis.

PubMed ID: 22522702

DOI: 10.1038/emboj.2012.89

PubMed ID: 23570799

Title: Congenital dyserythropoietic anemia type III (CDA III) is caused by a mutation in kinesin family member, KIF23.

PubMed ID: 23570799

DOI: 10.1182/blood-2012-10-461392

PubMed ID: 33159567

Title: Congenital dyserythropoietic anemia types Ib, II, and III: novel variants in the CDIN1 gene and functional study of a novel variant in the KIF23 gene.

PubMed ID: 33159567

DOI: 10.1007/s00277-020-04319-5

Sequence Information:

  • Length: 960
  • Mass: 110059
  • Checksum: B2AA784D2D236A90
  • Sequence:
  • MKSARAKTPR KPTVKKGSQT NLKDPVGVYC RVRPLGFPDQ ECCIEVINNT TVQLHTPEGY 
    RLNRNGDYKE TQYSFKQVFG THTTQKELFD VVANPLVNDL IHGKNGLLFT YGVTGSGKTH 
    TMTGSPGEGG LLPRCLDMIF NSIGSFQAKR YVFKSNDRNS MDIQCEVDAL LERQKREAMP 
    NPKTSSSKRQ VDPEFADMIT VQEFCKAEEV DEDSVYGVFV SYIEIYNNYI YDLLEEVPFD 
    PIKPKPPQSK LLREDKNHNM YVAGCTEVEV KSTEEAFEVF WRGQKKRRIA NTHLNRESSR 
    SHSVFNIKLV QAPLDADGDN VLQEKEQITI SQLSLVDLAG SERTNRTRAE GNRLREAGNI 
    NQSLMTLRTC MDVLRENQMY GTNKMVPYRD SKLTHLFKNY FDGEGKVRMI VCVNPKAEDY 
    EENLQVMRFA EVTQEVEVAR PVDKAICGLT PGRRYRNQPR GPVGNEPLVT DVVLQSFPPL 
    PSCEILDIND EQTLPRLIEA LEKRHNLRQM MIDEFNKQSN AFKALLQEFD NAVLSKENHM 
    QGKLNEKEKM ISGQKLEIER LEKKNKTLEY KIEILEKTTT IYEEDKRNLQ QELETQNQKL 
    QRQFSDKRRL EARLQGMVTE TTMKWEKECE RRVAAKQLEM QNKLWVKDEK LKQLKAIVTE 
    PKTEKPERPS RERDREKVTQ RSVSPSPVPL SSNYIAQISN GQQLMSQPQL HRRSNSCSSI 
    SVASCISEWE QKIPTYNTPL KVTSIARRRQ QEPGQSKTCI VSDRRRGMYW TEGREVVPTF 
    RNEIEIEEDH CGRLLFQPDQ NAPPIRLRHR RSRSAGDRWV DHKPASNMQT ETVMQPHVPH 
    AITVSVANEK ALAKCEKYML THQELASDGE IETKLIKGDI YKTRGGGQSV QFTDIETLKQ 
    ESPNGSRKRR SSTVAPAQPD GAESEWTDVE TRCSVAVEMR AGSQLGPGYQ HHAQPKRKKP

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.