KIF2A_MOUSE
ID KIF2A_MOUSE Reviewed; 705 AA.
AC P28740; O54744; Q91W03;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Kinesin-like protein KIF2A;
DE AltName: Full=Kinesin-2;
GN Name=Kif2a; Synonyms=Kif2, Kns2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1447303; DOI=10.1083/jcb.119.5.1287;
RA Aizawa H., Sekine Y., Takemura R., Zhang Z., Nangaku M., Hirokawa N.;
RT "Kinesin family in murine central nervous system.";
RL J. Cell Biol. 119:1287-1296(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6 X SJL; TISSUE=Hippocampus;
RX PubMed=9774330; DOI=10.1093/emboj/17.20.5855;
RA Santama N., Krijnse-Locker J., Griffiths G., Noda Y., Hirokawa N.,
RA Dotti C.G.;
RT "KIF2beta, a new kinesin superfamily protein in non-neuronal cells, is
RT associated with lysosomes and may be implicated in their centrifugal
RT translocation.";
RL EMBO J. 17:5855-5867(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12887924; DOI=10.1016/s0092-8674(03)00522-1;
RA Homma N., Takei Y., Tanaka Y., Nakata T., Terada S., Kikkawa M., Noda Y.,
RA Hirokawa N.;
RT "Kinesin superfamily protein 2A (KIF2A) functions in suppression of
RT collateral branch extension.";
RL Cell 114:229-239(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-528 AND SER-545 (ISOFORM 1), AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=24339785; DOI=10.1371/journal.pgen.1003960;
RA Kraehling A.M., Alvarez L., Debowski K., Van Q., Gunkel M., Irsen S.,
RA Al-Amoudi A., Struenker T., Kremmer E., Krause E., Voigt I., Woertge S.,
RA Waisman A., Weyand I., Seifert R., Kaupp U.B., Wachten D.;
RT "CRIS-a novel cAMP-binding protein controlling spermiogenesis and the
RT development of flagellar bending.";
RL PLoS Genet. 9:E1003960-E1003960(2013).
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC normal brain development. May regulate microtubule dynamics during
CC axonal growth. Required for normal progression through mitosis.
CC Required for normal congress of chromosomes at the metaphase plate.
CC Required for normal spindle dynamics during mitosis. Promotes spindle
CC turnover. Implicated in formation of bipolar mitotic spindles. Has
CC microtubule depolymerization activity (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12887924, ECO:0000269|PubMed:9774330}.
CC -!- SUBUNIT: Interacts with AURKA, PSRC1 and PLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9774330}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:9774330}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:9774330}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Lysosome
CC {ECO:0000269|PubMed:9774330}. Note=Localized to the spindle
CC microtubules and spindle poles from prophase to metaphase. Efficient
CC targeting to spindle microtubules and spindle poles requires the kinase
CC activity of PLK1. Recruited to mitotic spindles by interaction with
CC PSRC1 (By similarity). Associated with lysosomes in NIH3T3 cells.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=P28740-3; Sequence=Displayed;
CC Name=1; Synonyms=Kif2;
CC IsoId=P28740-1; Sequence=VSP_028377, VSP_028379;
CC Name=2; Synonyms=Kif2-beta;
CC IsoId=P28740-2; Sequence=VSP_028377, VSP_028378;
CC -!- TISSUE SPECIFICITY: Highest level in lung. High level in ovary,
CC moderate levels in heart, kidney, placenta, skeletal muscle and spleen
CC (at protein level). Pancreas and spleen express a shorter isoform (at
CC protein level). Expressed in the flagellum of elongated spermatids and
CC sperm in the testis lumen (at protein level) (PubMed:24339785). Isoform
CC 1 expressed in neuronal cells. Isoform 2 expressed in astrocytes and
CC fibroblasts. {ECO:0000269|PubMed:24339785, ECO:0000269|PubMed:9774330}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 expressed at low level in 13 dpc
CC embryonic hippocampus, higher level by stage 15 persisting into
CC juvenile and adult stages. Isoform 2 expressed in 13 dpc and 15 dpc
CC embryonic hippocampus declining to very low levels in juvenile and
CC adult neurons. High level of isoform 1 and very low level of isoform 2
CC in stage 2 and 5 hippocampal neurons in culture.
CC {ECO:0000269|PubMed:9774330}.
CC -!- DISRUPTION PHENOTYPE: Mice show overextension of collateral branches of
CC developing axons and defects in neuronal migration in the brain. They
CC die within 24 hours of birth. {ECO:0000269|PubMed:12887924}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; D12644; BAA02165.1; -; mRNA.
DR EMBL; Y15894; CAA75815.1; -; mRNA.
DR EMBL; BC006803; AAH06803.2; -; mRNA.
DR CCDS; CCDS26759.1; -. [P28740-1]
DR CCDS; CCDS49356.1; -. [P28740-3]
DR PIR; A44259; A44259.
DR RefSeq; NP_001139251.1; NM_001145779.1. [P28740-3]
DR RefSeq; XP_006517602.1; XM_006517539.3.
DR AlphaFoldDB; P28740; -.
DR SMR; P28740; -.
DR BioGRID; 200938; 20.
DR IntAct; P28740; 13.
DR MINT; P28740; -.
DR STRING; 10090.ENSMUSP00000112715; -.
DR iPTMnet; P28740; -.
DR PhosphoSitePlus; P28740; -.
DR EPD; P28740; -.
DR jPOST; P28740; -.
DR MaxQB; P28740; -.
DR PeptideAtlas; P28740; -.
DR PRIDE; P28740; -.
DR ProteomicsDB; 263534; -. [P28740-3]
DR ProteomicsDB; 263535; -. [P28740-1]
DR ProteomicsDB; 263536; -. [P28740-2]
DR Antibodypedia; 1353; 217 antibodies from 28 providers.
DR DNASU; 16563; -.
DR Ensembl; ENSMUST00000022204; ENSMUSP00000022204; ENSMUSG00000021693. [P28740-3]
DR Ensembl; ENSMUST00000117423; ENSMUSP00000113921; ENSMUSG00000021693. [P28740-2]
DR Ensembl; ENSMUST00000122233; ENSMUSP00000112715; ENSMUSG00000021693. [P28740-1]
DR GeneID; 16563; -.
DR KEGG; mmu:16563; -.
DR UCSC; uc007rub.2; mouse. [P28740-3]
DR UCSC; uc007ruc.2; mouse. [P28740-1]
DR CTD; 3796; -.
DR MGI; MGI:108390; Kif2a.
DR VEuPathDB; HostDB:ENSMUSG00000021693; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000155570; -.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; P28740; -.
DR OMA; XDVDATN; -.
DR PhylomeDB; P28740; -.
DR TreeFam; TF105222; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16563; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Kif2a; mouse.
DR PRO; PR:P28740; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P28740; protein.
DR Bgee; ENSMUSG00000021693; Expressed in barrel cortex and 263 other tissues.
DR ExpressionAtlas; P28740; baseline and differential.
DR Genevisible; P28740; MM.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:MGI.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Lysosome; Microtubule; Mitosis; Motor protein;
KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..705
FT /note="Kinesin-like protein KIF2A"
FT /id="PRO_0000125415"
FT DOMAIN 222..552
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..216
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 65..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 659..698
FT /evidence="ECO:0000255"
FT COMPBIAS 119..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 312..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00139"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:1447303,
FT ECO:0000303|PubMed:9774330"
FT /id="VSP_028377"
FT VAR_SEQ 133..152
FT /note="GSVSDISPVQAAKKEFGPPS -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9774330"
FT /id="VSP_028378"
FT VAR_SEQ 551
FT /note="E -> EFGISPSDIPFSQGGGSRPDLSPSYDYDDFSPSITRVKE (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:1447303,
FT ECO:0000303|PubMed:9774330"
FT /id="VSP_028379"
FT CONFLICT 99
FT /note="A -> ARA (in Ref. 2; CAA75815)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..118
FT /note="Missing (in Ref. 2; CAA75815)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="A -> R (in Ref. 1; BAA02165)"
FT /evidence="ECO:0000305"
FT MOD_RES P28740-1:528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P28740-1:545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 705 AA; 79756 MW; ACEBB35CC0F4A68E CRC64;
MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF
SLNPDLVPDE DIEPSPELPP PSSSSKVNKI VKNRRTVAAV KNDPPPRDNR VVGSARARPS
QLPEQSSSAQ QNGSVSDISP VQAAKKEFGP PSRRKSNCVK EVEKLQEKRE KRRLQQQELR
EKRAQDVDAT NPNYEIMCMI RDFRGSLDYR PLTTADPIDE HRICVCVRKR PLNKKETQMK
DLDVITIPSK DVVMVHEPKQ KVDLTRYLEN QTFRFDYAFD DSAPNEMVYR FTARPLVETI
FERGMATCFA YGQTGSGKTH TMGGDFSGKN QDCSKGIYAL AARDVFLMLK KPNYKKLELQ
VYATFFEIYS GKVFDLLNRK TKLRVLEDGK QQVQVVGLQE REVKCVEDVL KLIDIGNSCR
TSGQTSANAH SSRSHAVFQI ILRRKGKLHG KFSLIDLAGN ERGADTSSAD RQTRLEGAEI
NKSLLALKEC IRALGRNKPH TPFRASKLTQ VLRDSFIGEN SRTCMIATIS PGMASCENTL
NTLRYANRVK ELTVNPAAAG DVHPIMHHPP SQIDDLETQW GVGSSPQRDD LKLLCEQNEE
EVSPQLFTFH EAVSQMVEME EQVVEDHRAV FQESIRWIED EKALLEMTEE VDYDVDSYAT
QLEAILEQKI DILTELRDKV KSFRAALQEE EQASKQINPK RPRAL
