KIF22_HUMAN
ID KIF22_HUMAN Reviewed; 665 AA.
AC Q14807; B2R5M0; B7Z265; O60845; O94814; Q53F58; Q9BT46;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 5.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Kinesin-like protein KIF22;
DE AltName: Full=Kinesin-like DNA-binding protein;
DE AltName: Full=Kinesin-like protein 4;
GN Name=KIF22; Synonyms=KID, KNSL4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=8599929; DOI=10.1002/j.1460-2075.1996.tb00378.x;
RA Tokai N., Fujimoto-Nishiyama A., Toyoshima Y., Yonemura S., Tsukita S.,
RA Inoue J., Yamamoto T.;
RT "Kid, a novel kinesin-like DNA binding protein, is localized to chromosomes
RT and the mitotic spindle.";
RL EMBO J. 15:457-467(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9790757; DOI=10.1006/geno.1998.5452;
RA Song J., Murakami H., Yang Z.Q., Koga C., Adati N., Murata T.,
RA Geltinger C., Saito-Ohara F., Ikeuchi T., Matsumura M., Itakura K.,
RA Kanazawa I., Sun K., Yokoyama K.K.;
RT "Human genes for KNSL4 and MAZ are located close to one another on
RT chromosome 16p11.2.";
RL Genomics 52:374-377(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adrenal gland, Amygdala, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney epithelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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 [10]
RP INTERACTION WITH SIAH1, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=11146551; DOI=10.1038/sj.onc.1204002;
RA Germani A., Bruzzoni-Giovanelli H., Fellous A., Gisselbrecht S.,
RA Varin-Blank N., Calvo F.;
RT "SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the
RT proteasome pathway during mitosis.";
RL Oncogene 19:5997-6006(2000).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP INTERACTION WITH FAM83D.
RX PubMed=18485706; DOI=10.1016/j.cub.2008.04.041;
RA Santamaria A., Nagel S., Sillje H.H.W., Nigg E.A.;
RT "The spindle protein CHICA mediates localization of the chromokinesin Kid
RT to the mitotic spindle.";
RL Curr. Biol. 18:723-729(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-543; SER-562 AND
RP SER-581, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP TISSUE SPECIFICITY, VARIANTS SEMDJL2 SER-148; LEU-148 AND GLN-149, AND
RP VARIANT GLN-232.
RX PubMed=22152677; DOI=10.1016/j.ajhg.2011.10.015;
RA Min B.J., Kim N., Chung T., Kim O.H., Nishimura G., Chung C.Y., Song H.R.,
RA Kim H.W., Lee H.R., Kim J., Kang T.H., Seo M.E., Yang S.D., Kim D.H.,
RA Lee S.B., Kim J.I., Seo J.S., Choi J.Y., Kang D., Kim D., Park W.Y.,
RA Cho T.J.;
RT "Whole-exome sequencing identifies mutations of KIF22 in
RT spondyloepimetaphyseal dysplasia with joint laxity, leptodactylic type.";
RL Am. J. Hum. Genet. 89:760-766(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-427 AND SER-562, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION.
RX PubMed=25743205; DOI=10.1038/ncomms7447;
RA Iemura K., Tanaka K.;
RT "Chromokinesin Kid and kinetochore kinesin CENP-E differentially support
RT chromosome congression without end-on attachment to microtubules.";
RL Nat. Commun. 6:6447-6447(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-465, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP STRUCTURE BY NMR OF 570-660.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-070, a C-terminal domain of kinesin-like
RT protein KIF22 from human.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [22]
RP VARIANTS SEMDJL2 LEU-148; GLN-149 AND LEU-149.
RX PubMed=22152678; DOI=10.1016/j.ajhg.2011.10.016;
RA Boyden E.D., Campos-Xavier A.B., Kalamajski S., Cameron T.L., Suarez P.,
RA Tanackovic G., Andria G., Ballhausen D., Briggs M.D., Hartley C.,
RA Cohn D.H., Davidson H.R., Hall C., Ikegawa S., Jouk P.S., Konig R.,
RA Megarbane A., Nishimura G., Lachman R.S., Mortier G., Rimoin D.L.,
RA Rogers R.C., Rossi M., Sawada H., Scott R., Unger S., Valadares E.R.,
RA Bateman J.F., Warman M.L., Superti-Furga A., Bonafe L.;
RT "Recurrent dominant mutations affecting two adjacent residues in the motor
RT domain of the monomeric kinesin KIF22 result in skeletal dysplasia and
RT joint laxity.";
RL Am. J. Hum. Genet. 89:767-772(2011).
RN [23]
RP ERRATUM OF PUBMED:22152678.
RA Boyden E.D., Campos-Xavier A.B., Kalamajski S., Cameron T.L., Suarez P.,
RA Tanackovic G., Andria G., Ballhausen D., Briggs M.D., Hartley C.,
RA Cohn D.H., Davidson H.R., Hall C., Ikegawa S., Jouk P.S., Konig R.,
RA Megarbane A., Nishimura G., Lachman R.S., Mortier G., Rimoin D.L.,
RA Rogers R.C., Rossi M., Sawada H., Scott R., Unger S., Valadares E.R.,
RA Bateman J.F., Warman M.L., Superti-Furga A., Bonafe L.;
RL Am. J. Hum. Genet. 90:170-170(2012).
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 (By similarity). Plays a role in congression of
CC laterally attached chromosomes in NDC80-depleted cells
CC (PubMed:25743205). {ECO:0000250|UniProtKB:Q9I869,
CC ECO:0000269|PubMed:25743205}.
CC -!- SUBUNIT: Interacts with FAM83D (PubMed:18485706). Interacts with SIAH1
CC (PubMed:11146551). {ECO:0000269|PubMed:11146551,
CC ECO:0000269|PubMed:18485706}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8599929}. Cytoplasm,
CC cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14807-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14807-2; Sequence=VSP_046428;
CC -!- TISSUE SPECIFICITY: Expressed in bone, cartilage, joint capsule,
CC ligament, skin, and primary cultured chondrocytes.
CC {ECO:0000269|PubMed:22152677}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation. {ECO:0000269|PubMed:11146551}.
CC -!- DISEASE: Spondyloepimetaphyseal dysplasia with joint laxity, 2
CC (SEMDJL2) [MIM:603546]: A bone disease characterized by short stature,
CC distinctive midface retrusion, progressive knee malalignment (genu
CC valgum and/or varum), generalized ligamentous laxity, and mild spinal
CC deformity. Intellectual development is not impaired. Radiographic
CC characteristics include significantly retarded epiphyseal ossification
CC that evolves into epiphyseal dysplasia and precocious osteoarthritis,
CC metaphyseal irregularities and vertical striations, constricted femoral
CC neck, slender metacarpals and metatarsals, and mild thoracolumbar
CC kyphosis or scoliosis with normal or mild platyspondyly. The most
CC distinctive features for differential diagnosis of SEMDJL2 are the
CC slender metacarpals and phalanges and the progressive degeneration of
CC carpal bones; however, these 2 features are evident only in older
CC children and young adults. The soft consistency of cartilage in the
CC airways leads to laryngotracheomalacia with proneness to respiratory
CC obstruction and inspiratory stridor in infancy and childhood.
CC {ECO:0000269|PubMed:22152677, ECO:0000269|PubMed:22152678}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAW80007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB017430; BAA33019.2; -; mRNA.
DR EMBL; AB017335; BAA33063.1; -; Genomic_DNA.
DR EMBL; BT007259; AAP35923.1; -; mRNA.
DR EMBL; AK294380; BAH11751.1; -; mRNA.
DR EMBL; AK312234; BAG35167.1; -; mRNA.
DR EMBL; AK316389; BAH14760.1; -; mRNA.
DR EMBL; AK223431; BAD97151.1; -; mRNA.
DR EMBL; AC002301; AAC08709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471238; EAW80005.1; -; Genomic_DNA.
DR EMBL; CH471238; EAW80007.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC004352; AAH04352.1; -; mRNA.
DR EMBL; BC028155; AAH28155.1; -; mRNA.
DR CCDS; CCDS10653.1; -. [Q14807-1]
DR CCDS; CCDS58444.1; -. [Q14807-2]
DR RefSeq; NP_001243198.1; NM_001256269.1. [Q14807-2]
DR RefSeq; NP_001243199.1; NM_001256270.1. [Q14807-2]
DR RefSeq; NP_015556.1; NM_007317.2. [Q14807-1]
DR PDB; 2EDU; NMR; -; A=570-660.
DR PDB; 6NJE; X-ray; 2.20 A; A=40-400.
DR PDBsum; 2EDU; -.
DR PDBsum; 6NJE; -.
DR AlphaFoldDB; Q14807; -.
DR SMR; Q14807; -.
DR BioGRID; 110033; 100.
DR IntAct; Q14807; 61.
DR MINT; Q14807; -.
DR STRING; 9606.ENSP00000160827; -.
DR ChEMBL; CHEMBL5470; -.
DR iPTMnet; Q14807; -.
DR PhosphoSitePlus; Q14807; -.
DR BioMuta; KIF22; -.
DR DMDM; 19863381; -.
DR EPD; Q14807; -.
DR jPOST; Q14807; -.
DR MassIVE; Q14807; -.
DR MaxQB; Q14807; -.
DR PaxDb; Q14807; -.
DR PeptideAtlas; Q14807; -.
DR PRIDE; Q14807; -.
DR ProteomicsDB; 60189; -. [Q14807-1]
DR ProteomicsDB; 6413; -.
DR Antibodypedia; 13324; 263 antibodies from 31 providers.
DR DNASU; 3835; -.
DR Ensembl; ENST00000160827.9; ENSP00000160827.5; ENSG00000079616.14. [Q14807-1]
DR Ensembl; ENST00000400751.9; ENSP00000383562.5; ENSG00000079616.14. [Q14807-2]
DR Ensembl; ENST00000561482.6; ENSP00000454957.1; ENSG00000079616.14. [Q14807-2]
DR Ensembl; ENST00000690258.1; ENSP00000509977.1; ENSG00000079616.14. [Q14807-2]
DR GeneID; 3835; -.
DR KEGG; hsa:3835; -.
DR MANE-Select; ENST00000160827.9; ENSP00000160827.5; NM_007317.3; NP_015556.1.
DR UCSC; uc002dts.5; human. [Q14807-1]
DR CTD; 3835; -.
DR DisGeNET; 3835; -.
DR GeneCards; KIF22; -.
DR HGNC; HGNC:6391; KIF22.
DR HPA; ENSG00000079616; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; KIF22; -.
DR MIM; 603213; gene.
DR MIM; 603546; phenotype.
DR neXtProt; NX_Q14807; -.
DR OpenTargets; ENSG00000079616; -.
DR Orphanet; 93360; Spondyloepimetaphyseal dysplasia with multiple dislocations.
DR PharmGKB; PA30180; -.
DR VEuPathDB; HostDB:ENSG00000079616; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000159632; -.
DR HOGENOM; CLU_001485_27_1_1; -.
DR InParanoid; Q14807; -.
DR OMA; VIREDRW; -.
DR OrthoDB; 787964at2759; -.
DR PhylomeDB; Q14807; -.
DR TreeFam; TF105233; -.
DR PathwayCommons; Q14807; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q14807; -.
DR SIGNOR; Q14807; -.
DR BioGRID-ORCS; 3835; 87 hits in 1082 CRISPR screens.
DR ChiTaRS; KIF22; human.
DR EvolutionaryTrace; Q14807; -.
DR GeneWiki; KIF22; -.
DR GenomeRNAi; 3835; -.
DR Pharos; Q14807; Tbio.
DR PRO; PR:Q14807; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q14807; protein.
DR Bgee; ENSG00000079616; Expressed in ventricular zone and 161 other tissues.
DR ExpressionAtlas; Q14807; baseline and differential.
DR Genevisible; Q14807; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; TAS:ProtInc.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
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; TAS:ProtInc.
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; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW Cytoskeleton; Disease variant; DNA-binding; Dwarfism; Isopeptide bond;
KW Microtubule; Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..665
FT /note="Kinesin-like protein KIF22"
FT /id="PRO_0000125433"
FT DOMAIN 43..368
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 379..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 465..508
FT /evidence="ECO:0000255"
FT COMPBIAS 394..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046428"
FT VARIANT 148
FT /note="P -> L (in SEMDJL2; dbSNP:rs193922921)"
FT /evidence="ECO:0000269|PubMed:22152677,
FT ECO:0000269|PubMed:22152678"
FT /id="VAR_067345"
FT VARIANT 148
FT /note="P -> S (in SEMDJL2; dbSNP:rs193922920)"
FT /evidence="ECO:0000269|PubMed:22152677"
FT /id="VAR_067346"
FT VARIANT 149
FT /note="R -> L (in SEMDJL2; dbSNP:rs193922922)"
FT /evidence="ECO:0000269|PubMed:22152678"
FT /id="VAR_067347"
FT VARIANT 149
FT /note="R -> Q (in SEMDJL2; dbSNP:rs193922922)"
FT /evidence="ECO:0000269|PubMed:22152677,
FT ECO:0000269|PubMed:22152678"
FT /id="VAR_067348"
FT VARIANT 232
FT /note="R -> Q (in dbSNP:rs201659270)"
FT /evidence="ECO:0000269|PubMed:22152677"
FT /id="VAR_067349"
FT CONFLICT 24
FT /note="Missing (in Ref. 2; BAA33063)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="S -> KV (in Ref. 2; BAA33063)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..169
FT /note="HTMLGSPEQPGVIPRALMDLLQLTREEGAEGRPWA -> THAGQPRATWGDP
FT AGSHGPPAAHKGGGCRGPAMG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="S -> N (in Ref. 5; BAD97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="L -> P (in Ref. 3; BAG35167)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="V -> A (in Ref. 2; BAA33063)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="H -> R (in Ref. 5; BAD97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..456
FT /note="APASASQKLSPLQKLSSMDPAMLERLLSLDRLLASQGSQ -> SSSLCLPET
FT QPPTEAKAAWTRPCGAPPQLGPSACLPGEP (in Ref. 2; BAA33063)"
FT /evidence="ECO:0000305"
FT CONFLICT 505..513
FT /note="ENHCPTMLR -> RTIVPQCSG (in Ref. 2; BAA33063)"
FT /evidence="ECO:0000305"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:6NJE"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 166..180
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 245..260
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:6NJE"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6NJE"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:6NJE"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6NJE"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:2EDU"
FT HELIX 582..598
FT /evidence="ECO:0007829|PDB:2EDU"
FT HELIX 601..606
FT /evidence="ECO:0007829|PDB:2EDU"
FT HELIX 612..625
FT /evidence="ECO:0007829|PDB:2EDU"
FT HELIX 631..636
FT /evidence="ECO:0007829|PDB:2EDU"
FT HELIX 642..658
FT /evidence="ECO:0007829|PDB:2EDU"
SQ SEQUENCE 665 AA; 73262 MW; C6C0AC96741DD387 CRC64;
MAAGGSTQQR RREMAAASAA AISGAGRCRL SKIGATRRPP PARVRVAVRL RPFVDGTAGA
SDPPCVRGMD SCSLEIANWR NHQETLKYQF DAFYGERSTQ QDIYAGSVQP ILRHLLEGQN
ASVLAYGPTG AGKTHTMLGS PEQPGVIPRA LMDLLQLTRE EGAEGRPWAL SVTMSYLEIY
QEKVLDLLDP ASGDLVIRED CRGNILIPGL SQKPISSFAD FERHFLPASR NRTVGATRLN
QRSSRSHAVL LVKVDQRERL APFRQREGKL YLIDLAGSED NRRTGNKGLR LKESGAINTS
LFVLGKVVDA LNQGLPRVPY RDSKLTRLLQ DSLGGSAHSI LIANIAPERR FYLDTVSALN
FAARSKEVIN RPFTNESLQP HALGPVKLSQ KELLGPPEAK RARGPEEEEI GSPEPMAAPA
SASQKLSPLQ KLSSMDPAML ERLLSLDRLL ASQGSQGAPL LSTPKRERMV LMKTVEEKDL
EIERLKTKQK ELEAKMLAQK AEEKENHCPT MLRPLSHRTV TGAKPLKKAV VMPLQLIQEQ
AASPNAEIHI LKNKGRKRKL ESLDALEPEE KAEDCWELQI SPELLAHGRQ KILDLLNEGS
ARDLRSLQRI GPKKAQLIVG WRELHGPFSQ VEDLERVEGI TGKQMESFLK ANILGLAAGQ
RCGAS
