KIF22_MOUSE
ID KIF22_MOUSE Reviewed; 660 AA.
AC Q3V300; O35232; Q99LC7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Kinesin-like protein KIF22;
GN Name=Kif22;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 127-274.
RX PubMed=9339368; DOI=10.1006/geno.1997.4901;
RA Yang Z., Hanlon D.W., Marszalek J.R., Goldstein L.S.;
RT "Identification, partial characterization, and genetic mapping of kinesin-
RT like protein genes in mouse.";
RL Genomics 45:123-131(1997).
CC -!- FUNCTION: Kinesin family member that is involved in spindle formation
CC and the movements of chromosomes during mitosis and meiosis. Binds to
CC microtubules and to DNA. Plays a role in congression of laterally
CC attached chromosomes in NDC80-depleted cells.
CC {ECO:0000250|UniProtKB:Q14807, ECO:0000250|UniProtKB:Q9I869}.
CC -!- SUBUNIT: Interacts with FAM83D and SIAH1.
CC {ECO:0000250|UniProtKB:Q14807}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14807}.
CC Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q14807}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AK075922; BAE43356.1; -; mRNA.
DR EMBL; BC003427; AAH03427.1; -; mRNA.
DR EMBL; AF013119; AAC39968.1; -; mRNA.
DR CCDS; CCDS21855.1; -.
DR RefSeq; NP_663563.1; NM_145588.1.
DR AlphaFoldDB; Q3V300; -.
DR SMR; Q3V300; -.
DR BioGRID; 225240; 8.
DR IntAct; Q3V300; 7.
DR STRING; 10090.ENSMUSP00000032915; -.
DR iPTMnet; Q3V300; -.
DR PhosphoSitePlus; Q3V300; -.
DR EPD; Q3V300; -.
DR MaxQB; Q3V300; -.
DR PaxDb; Q3V300; -.
DR PeptideAtlas; Q3V300; -.
DR PRIDE; Q3V300; -.
DR ProteomicsDB; 263603; -.
DR Antibodypedia; 13324; 263 antibodies from 31 providers.
DR DNASU; 110033; -.
DR Ensembl; ENSMUST00000032915; ENSMUSP00000032915; ENSMUSG00000030677.
DR GeneID; 110033; -.
DR KEGG; mmu:110033; -.
DR UCSC; uc009jud.1; mouse.
DR CTD; 3835; -.
DR MGI; MGI:109233; Kif22.
DR VEuPathDB; HostDB:ENSMUSG00000030677; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000159632; -.
DR HOGENOM; CLU_001485_27_1_1; -.
DR InParanoid; Q3V300; -.
DR OMA; VIREDRW; -.
DR OrthoDB; 787964at2759; -.
DR PhylomeDB; Q3V300; -.
DR TreeFam; TF105233; -.
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; 110033; 3 hits in 108 CRISPR screens.
DR ChiTaRS; Kif22; mouse.
DR PRO; PR:Q3V300; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3V300; protein.
DR Bgee; ENSMUSG00000030677; Expressed in late embryo and 261 other tissues.
DR ExpressionAtlas; Q3V300; baseline and differential.
DR Genevisible; Q3V300; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005819; C:spindle; IDA: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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR026986; KIF22.
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 InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF801; PTHR24115:SF801; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW Isopeptide bond; Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..660
FT /note="Kinesin-like protein KIF22"
FT /id="PRO_0000262921"
FT DOMAIN 38..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..505
FT /evidence="ECO:0000255"
FT COMPBIAS 404..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT CROSSLNK 460
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT CONFLICT 60
FT /note="C -> R (in Ref. 1; BAE43356)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="L -> I (in Ref. 1; BAE43356)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="V -> E (in Ref. 1; BAE43356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 73190 MW; AA8B99477BC49B3C CRC64;
MSLRAKTCPQ RREMASATSG PGRCVSKGGL GRRPPLARVR VAVRLRPFMD GETEAKELPC
VRAIDSCSLE VANWKKYQET LKYQFDAFYG EKSTQQEVYV GSVQPILRHL LEGQNASVLA
YGPTGAGKTH TMLGSPEQPG VIPRALMDLL QLAREESAEG RPWDVSVAMS YLEIYQEKVL
DLLDPASGDL VIREDCRGNI LIPGLTQKPI TSFSDFEQHF LPASRNRAVG ATRLNQRSSR
SHAVLLVKVD QRERLTPFRQ REGKLYLIDL AGSEDNRRTG NQGIRLKESG AINTSLFVLG
KVVDALNQGL PRIPYRDSKL TRLLQDSLGG SAHSILIANI APERRFYQDT ISALNFTARS
KEVINRPFTN ESLQPHALAP VKLSQKELLG PSEAKKAKGP EEESTGSPES TAAPASASQK
LSLLQKLSNM DPAMLENLLS MERLLGSQGS QGTPLLNTPK RERMVLMKTV EEKNLEIERL
KMKQKELEAK VLAQEAPDPR EKENTPTILQ PPASYSGTVA KPLKKAVVMP LQRIQKQRES
SNQIQLLKKG PKRKLEPSPE SEAVEKDEDY WEVQISPELL AHGRKKLLDL LNEGSARELR
SLQRIGQKKA QLIVGWRELH GPFSEVEDLE QVEGISGKQV ESFLKANLLS LAASQHSGPS
