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   27-MAR-2024, entry version 142.
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   GlyGen; Q3V300; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3V300; -.
DR   PhosphoSitePlus; Q3V300; -.
DR   EPD; Q3V300; -.
DR   MaxQB; Q3V300; -.
DR   PaxDb; 10090-ENSMUSP00000032915; -.
DR   PeptideAtlas; Q3V300; -.
DR   ProteomicsDB; 263603; -.
DR   Pumba; Q3V300; -.
DR   Antibodypedia; 13324; 309 antibodies from 31 providers.
DR   DNASU; 110033; -.
DR   Ensembl; ENSMUST00000032915.8; ENSMUSP00000032915.7; ENSMUSG00000030677.9.
DR   GeneID; 110033; -.
DR   KEGG; mmu:110033; -.
DR   UCSC; uc009jud.1; mouse.
DR   AGR; MGI:109233; -.
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; 129693at2759; -.
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 113 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 264 other cell types or tissues.
DR   ExpressionAtlas; Q3V300; baseline and differential.
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 chromosome alignment; ISS:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISS:UniProtKB.
DR   GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR   CDD; cd01376; KISc_KID_like; 1.
DR   Gene3D; 1.10.150.280; AF1531-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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:SF1000; KINESIN-LIKE PROTEIN KIF22; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF12836; HHH_3; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00278; HhH1; 2.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   Genevisible; Q3V300; MM.
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
//