KIF15_MOUSE
ID KIF15_MOUSE Reviewed; 1387 AA.
AC Q6P9L6; O35065; Q70MX5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Kinesin-like protein KIF15;
DE AltName: Full=Kinesin-like protein 2;
DE AltName: Full=Kinesin-like protein 7;
GN Name=Kif15; Synonyms=Klp2, Knsl7;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Embryo;
RX PubMed=14618103; DOI=10.1023/a:1027332432740;
RA Buster D.W., Baird D.H., Yu W., Solowska J.M., Chauviere M., Mazurek A.,
RA Kress M., Baas P.W.;
RT "Expression of the mitotic kinesin Kif15 in postmitotic neurons:
RT implications for neuronal migration and development.";
RL J. Neurocytol. 32:79-96(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-270, AND TISSUE SPECIFICITY.
RC STRAIN=ICR;
RX PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y.,
RA Hirokawa N.;
RT "Identification and classification of 16 new kinesin superfamily (KIF)
RT proteins in mouse genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Plus-end directed kinesin-like motor enzyme involved in
CC mitotic spindle assembly. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MKI67 and TPX2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Note=Detected during the interphase in the
CC cytoplasm as finely punctuate pattern and irregularly shaped dots.
CC Localizes at the spindle poles and microtubules prior to anaphase.
CC Localizes at the central spindle at anaphase. Localizes at the sites of
CC invaginating cell membranes, a position that corresponds to the
CC location of the contractile actomyosin ring of dividing cells.
CC Colocalizes with actin in interphase. Colocalizes in dendrites and in
CC growth cone of axons with microtubules. Colocalizes with TPX2 in
CC mitosis (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (neurons in the external
CC germinal layer of the cerebellum and in ventricular zones) (at protein
CC level). Expressed in spleen and testis. {ECO:0000269|PubMed:14618103,
CC ECO:0000269|PubMed:9275178}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KLP2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AJ560623; CAD90258.1; -; mRNA.
DR EMBL; BC060710; AAH60710.1; -; mRNA.
DR EMBL; AB001432; BAA22392.1; -; mRNA.
DR CCDS; CCDS23651.1; -.
DR RefSeq; NP_034750.1; NM_010620.1.
DR AlphaFoldDB; Q6P9L6; -.
DR SMR; Q6P9L6; -.
DR BioGRID; 229105; 8.
DR IntAct; Q6P9L6; 8.
DR MINT; Q6P9L6; -.
DR STRING; 10090.ENSMUSP00000035490; -.
DR iPTMnet; Q6P9L6; -.
DR PhosphoSitePlus; Q6P9L6; -.
DR EPD; Q6P9L6; -.
DR MaxQB; Q6P9L6; -.
DR PaxDb; Q6P9L6; -.
DR PeptideAtlas; Q6P9L6; -.
DR PRIDE; Q6P9L6; -.
DR ProteomicsDB; 269300; -.
DR Antibodypedia; 29484; 205 antibodies from 25 providers.
DR DNASU; 209737; -.
DR Ensembl; ENSMUST00000040717; ENSMUSP00000035490; ENSMUSG00000036768.
DR GeneID; 209737; -.
DR KEGG; mmu:209737; -.
DR UCSC; uc009sfl.1; mouse.
DR CTD; 56992; -.
DR MGI; MGI:1098258; Kif15.
DR VEuPathDB; HostDB:ENSMUSG00000036768; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156463; -.
DR HOGENOM; CLU_005295_0_0_1; -.
DR InParanoid; Q6P9L6; -.
DR OMA; AIRVFIR; -.
DR OrthoDB; 241787at2759; -.
DR PhylomeDB; Q6P9L6; -.
DR TreeFam; TF320478; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 209737; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Kif15; mouse.
DR PRO; PR:Q6P9L6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6P9L6; protein.
DR Bgee; ENSMUSG00000036768; Expressed in embryonic post-anal tail and 124 other tissues.
DR ExpressionAtlas; Q6P9L6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:InterPro.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR031794; HMMR_C.
DR InterPro; IPR044986; KIF15/KIN-12E.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR37739; PTHR37739; 1.
DR Pfam; PF15908; HMMR_C; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1387
FT /note="Kinesin-like protein KIF15"
FT /id="PRO_0000328685"
FT DOMAIN 26..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..1132
FT /evidence="ECO:0000255"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS87"
FT MOD_RES 1009
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS87"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS87"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS87"
FT CONFLICT 126
FT /note="D -> G (in Ref. 1; CAD90258)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="S -> N (in Ref. 1; CAD90258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1387 AA; 160120 MW; 0FFA8F93B45D740A CRC64;
MAPGCKSELR NVTNSHSNQP SNEGDAIKVF VRIRPAEEGA RSADGEQSFC LSVLSQTTLR
LHSNPDPKTF VFDYVAGMDT TQESVFSTVA KSIVESCMSG YNGTIFAYGQ TGSGKTFTMM
GPSDSDNFSH NLRGIIPRSF EYLFSLIDRE KEKAGAGKSF LCKCSFIEVY NEQIYDLLDS
ASVGLYLREH IKKGVFVVGA VEQAVTSAAE TYQVLSRGWR NRRVASTSMN RESSRSHAVF
TITIESMEKS SETVNIRTSL LNLVDLAGSE RQKDTHAEGM RLKEAGNINR SLSCLGQVIT
ALVDVGNGKQ RHICYRDSKL TFLLRDSLGG NAKTAIIANV HPGSRCFGET LSTLNFAQRA
KLIKNKAVVN EDTQGNVSQL QAEVKRLKEQ LSQFTSGQIT PESLLARDKE KTNYIEYFLE
AMLFFKKSEQ EKKSLIEKIT QLEDLTLKKE KFIQSNKMIV KFREDQIMRL ERLHKEGRGS
FLPEEQDRLL SELRDEVQTL REHVEHHPRL AKYAMENHSL REENRRLKLL APVKRAHEID
AQSIARLEKA FAEVSSTETN DKGLQGFSPK ALKESSFFTN TEKLKAQLLQ IQTELNNSKQ
EYEEFKELTR KKQLELESEL QSLQKANLNL ENLLEATKVC KRQEVSQLNK LHAETLKIIT
TPTKAYQLCS RLVPKSSPEV GSFGFLCTES SSRLDNDILN EPVPPEMSEQ ALEAVSEELR
TVQEQLSVLQ VKLDEEERKN LKLQQNVDKL EHHSTQMQEL FSSERSDWTK QQQEHVTQLS
DLEKQLQDAQ TKNEFLKCEV HDLRIVLNSA DKELSLVKLE YSTFKENHEK ELSQLSERHV
QVQLQLDNAR LENEKLLESQ ACLQDSYDNL QEVMKFEIDQ LSKNLQNCKQ ENETLKSDLH
NLVELFEAEK ERNNKLSLQF EEDKENSSKE ILKVLETVRQ EKQKEMAKCE KQMAKIQKLE
ESLLATENVI SSLEKSRESD KELVTNLMNQ IQELRISIGE KSETIATLKQ ELQDINCKYN
ASLADKEESK ELIRRQEVDI LELKETLRLR ILSEDIERDM LCEDLAHATE QLNMLTEASK
KHSGLLQSAQ EELTRKEALI QELQHKLNQE KEEVEQKKNE FSLKMRQLEH VMGSATEYPQ
SPKTPPHFQA HLAKLLETQE QEIEDGRASK TSLQHLVTKL NEDREVKNAE ILRMKDQLCE
MENLRLESQQ LREKNWLLQR QLDDVKRQQE SGDQSHPDSQ QLKNEHEEII KERLAKNKLI
EEMLKMKTNL EEVQSALHSK EKACHRMSEE IERTRTLESR AFQEKEQLRS KLEEMYEERE
RTFLEMEMLK KQLEFLAEEN GKLVGHQNLH QKIQYVVRLK KENIRLTEET EKLRAENLFL
KEKKKEF
