KIF4A_HUMAN
ID KIF4A_HUMAN Reviewed; 1232 AA.
AC O95239; B2R7V5; D3DVU4; Q86TN3; Q86XX7; Q9NNY6; Q9NY24; Q9UMW3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Chromosome-associated kinesin KIF4A;
DE AltName: Full=Chromokinesin-A;
GN Name=KIF4A; Synonyms=KIF4;
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).
RC TISSUE=Lymphocyte;
RA Villard L.;
RT "Human KIF4 mRNA, complete coding sequence.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP TRP-422.
RX PubMed=10978527; DOI=10.1016/s0167-4781(00)00151-2;
RA Oh S.J., Hahn H., Torrey T.A., Shin H., Choi W., Lee Y.M., Morse H.C. III,
RA Kim W.;
RT "Identification of the human homologue of mouse KIF4, a kinesin superfamily
RT motor protein.";
RL Biochim. Biophys. Acta 1493:219-224(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retinoblastoma;
RA Rentsch A., Neumann T., Rommerskirch W.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-668 (ISOFORM 1), AND VARIANT TRP-422.
RC TISSUE=Lymph, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 128-1232.
RC TISSUE=Retinoblastoma;
RX PubMed=9168136; DOI=10.1016/s0378-1119(96)00860-8;
RA Yan R.-T., Wang S.-Z.;
RT "Increased chromokinesin immunoreactivity in retinoblastoma cells.";
RL Gene 189:263-267(1997).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11736643; DOI=10.1042/0264-6021:3600549;
RA Lee Y.M., Lee S., Lee E., Shin H., Hahn H., Choi W., Kim W.;
RT "Human kinesin superfamily member 4 is dominantly localized in the nuclear
RT matrix and is associated with chromosomes during mitosis.";
RL Biochem. J. 360:549-556(2001).
RN [10]
RP FUNCTION, INTERACTION WITH PRC1, AND SUBCELLULAR LOCATION.
RX PubMed=15297875; DOI=10.1038/sj.emboj.7600347;
RA Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.;
RT "Essential roles of KIF4 and its binding partner PRC1 in organized central
RT spindle midzone formation.";
RL EMBO J. 23:3237-3248(2004).
RN [11]
RP FUNCTION, INTERACTION WITH PRC1, AND SUBCELLULAR LOCATION.
RX PubMed=15625105; DOI=10.1073/pnas.0408438102;
RA Zhu C., Jiang W.;
RT "Cell cycle-dependent translocation of PRC1 on the spindle by Kif4 is
RT essential for midzone formation and cytokinesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:343-348(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-799; SER-801; SER-951;
RP SER-1001; SER-1013; SER-1017 AND SER-1028, AND IDENTIFICATION BY MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-995 AND SER-1001, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-799; SER-801; SER-1001;
RP THR-1181 AND SER-1186, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-799; SER-801; SER-815;
RP SER-1126 AND THR-1181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP INVOLVEMENT IN XLID100.
RX PubMed=24812067; DOI=10.1136/jmedgenet-2013-102182;
RA Willemsen M.H., Ba W., Wissink-Lindhout W.M., de Brouwer A.P., Haas S.A.,
RA Bienek M., Hu H., Vissers L.E., van Bokhoven H., Kalscheuer V.,
RA Nadif Kasri N., Kleefstra T.;
RT "Involvement of the kinesin family members KIF4A and KIF5C in intellectual
RT disability and synaptic function.";
RL J. Med. Genet. 51:487-494(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1194, 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 [22]
RP FUNCTION, COFACTOR, INTERACTION WITH CIAO2B; MMS19 AND PRC1, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF 1086-CYS--ASP-1144; CYS-1106; CYS-1110 AND
RP CYS-1112, AND REGION.
RX PubMed=29848660; DOI=10.1242/jcs.211433;
RA Ben-Shimon L., Paul V.D., David-Kadoch G., Volpe M., Stuempfig M., Bill E.,
RA Muehlenhoff U., Lill R., Ben-Aroya S.;
RT "Fe-S cluster coordination of the chromokinesin KIF4A alters its
RT subcellular localization during mitosis.";
RL J. Cell Sci. 131:0-0(2018).
CC -!- FUNCTION: Iron-sulfur (Fe-S) cluster binding motor protein that has a
CC role in chromosome segregation during mitosis (PubMed:29848660).
CC Translocates PRC1 to the plus ends of interdigitating spindle
CC microtubules during the metaphase to anaphase transition, an essential
CC step for the formation of an organized central spindle midzone and
CC midbody and for successful cytokinesis (PubMed:15297875,
CC PubMed:15625105). May play a role in mitotic chromosomal positioning
CC and bipolar spindle stabilization (By similarity).
CC {ECO:0000250|UniProtKB:P33174, ECO:0000269|PubMed:15297875,
CC ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:29848660}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:29848660};
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:29848660};
CC Note=Binds 1 [4Fe-4S] cluster (PubMed:29848660). In the presence of
CC oxygen, the [4Fe-4S] cluster may be converted to [2Fe-2S]
CC (PubMed:29848660). {ECO:0000269|PubMed:29848660};
CC -!- SUBUNIT: Interacts with the cytosolic iron-sulfur protein assembly
CC (CIA) complex components CIAO2B and MMS19; the interactions facilitate
CC the transfer of Fe-S clusters to KIF4A to ensure proper localization of
CC KIF4A to mitotic machinery components (PubMed:29848660). Interacts (via
CC C-terminus) with unphosphorylated PRC1 (via N-terminus); the
CC interaction is required for the progression of mitosis
CC (PubMed:15297875, PubMed:15625105, PubMed:29848660).
CC {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105,
CC ECO:0000269|PubMed:29848660}.
CC -!- INTERACTION:
CC O95239; O94880: PHF14; NbExp=4; IntAct=EBI-1057516, EBI-2680164;
CC O95239; O94880-1: PHF14; NbExp=3; IntAct=EBI-1057516, EBI-16716857;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:11736643}.
CC Cytoplasm {ECO:0000269|PubMed:11736643}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:29848660}.
CC Midbody {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:29848660}.
CC Chromosome {ECO:0000269|PubMed:11736643, ECO:0000269|PubMed:15297875,
CC ECO:0000269|PubMed:29848660}. Note=Associates with chromosomes at all
CC stage of mitosis (PubMed:11736643, PubMed:15297875, PubMed:15625105).
CC Chromatin localization is dependent on iron-sulfur cluster binding
CC (PubMed:29848660). In anaphase, associates with the mitotic spindle
CC midzone (PubMed:15297875). In telophase and cytokinesis, co-localizes
CC with CIAO2B at the spindle midzone and midbody (PubMed:29848660,
CC PubMed:15297875). Co-localizes with PRC1 in early mitosis and at the
CC spindle midzone from anaphase B to telophase (PubMed:15297875,
CC PubMed:15625105). Does not localize to the nucleolus (PubMed:11736643).
CC {ECO:0000269|PubMed:11736643, ECO:0000269|PubMed:15297875,
CC ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:29848660}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95239-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95239-2; Sequence=VSP_013375, VSP_013376;
CC -!- TISSUE SPECIFICITY: Highly expressed in hematopoietic tissues, fetal
CC liver, spleen, thymus and adult thymus and bone marrow. Lower levels
CC are found in heart, testis, kidney, colon and lung.
CC {ECO:0000269|PubMed:10978527}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 100 (XLID100)
CC [MIM:300923]: A disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Intellectual deficiency is the only primary symptom of non-syndromic X-
CC linked forms, while syndromic forms present with associated physical,
CC neurological and/or psychiatric manifestations. XLID100 clinical
CC features include intellectual disability, epilepsy, microcephaly and
CC cortical malformations. {ECO:0000269|PubMed:24812067}. Note=The disease
CC may be caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Chromokinesin subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49218.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF179308; AAD51855.1; -; mRNA.
DR EMBL; AF071592; AAD05492.2; -; mRNA.
DR EMBL; AJ271784; CAB75427.1; -; mRNA.
DR EMBL; AK313133; BAG35952.1; -; mRNA.
DR EMBL; AL139398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05341.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05342.1; -; Genomic_DNA.
DR EMBL; BC049218; AAH49218.1; ALT_SEQ; mRNA.
DR EMBL; BC050548; AAH50548.1; -; mRNA.
DR EMBL; AF277375; AAF86334.1; -; mRNA.
DR CCDS; CCDS14401.1; -. [O95239-1]
DR RefSeq; NP_036442.3; NM_012310.4. [O95239-1]
DR PDB; 6OYL; X-ray; 3.15 A; B=1192-1232.
DR PDBsum; 6OYL; -.
DR AlphaFoldDB; O95239; -.
DR SMR; O95239; -.
DR BioGRID; 117288; 72.
DR CORUM; O95239; -.
DR ELM; O95239; -.
DR IntAct; O95239; 21.
DR MINT; O95239; -.
DR STRING; 9606.ENSP00000363524; -.
DR ChEMBL; CHEMBL6163; -.
DR GlyGen; O95239; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95239; -.
DR MetOSite; O95239; -.
DR PhosphoSitePlus; O95239; -.
DR BioMuta; KIF4A; -.
DR CPTAC; CPTAC-971; -.
DR EPD; O95239; -.
DR jPOST; O95239; -.
DR MassIVE; O95239; -.
DR MaxQB; O95239; -.
DR PaxDb; O95239; -.
DR PeptideAtlas; O95239; -.
DR PRIDE; O95239; -.
DR ProteomicsDB; 50738; -. [O95239-1]
DR ProteomicsDB; 50739; -. [O95239-2]
DR Antibodypedia; 27394; 228 antibodies from 32 providers.
DR DNASU; 24137; -.
DR Ensembl; ENST00000374403.4; ENSP00000363524.3; ENSG00000090889.12. [O95239-1]
DR GeneID; 24137; -.
DR KEGG; hsa:24137; -.
DR MANE-Select; ENST00000374403.4; ENSP00000363524.3; NM_012310.5; NP_036442.3.
DR UCSC; uc004dyg.4; human. [O95239-1]
DR CTD; 24137; -.
DR DisGeNET; 24137; -.
DR GeneCards; KIF4A; -.
DR HGNC; HGNC:13339; KIF4A.
DR HPA; ENSG00000090889; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; KIF4A; -.
DR MIM; 300521; gene.
DR MIM; 300923; phenotype.
DR neXtProt; NX_O95239; -.
DR OpenTargets; ENSG00000090889; -.
DR PharmGKB; PA30105; -.
DR VEuPathDB; HostDB:ENSG00000090889; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000158195; -.
DR HOGENOM; CLU_001485_4_1_1; -.
DR InParanoid; O95239; -.
DR OMA; PAFNKQH; -.
DR PhylomeDB; O95239; -.
DR TreeFam; TF105224; -.
DR PathwayCommons; O95239; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; O95239; -.
DR SIGNOR; O95239; -.
DR BioGRID-ORCS; 24137; 252 hits in 706 CRISPR screens.
DR ChiTaRS; KIF4A; human.
DR GeneWiki; KIF4A; -.
DR GenomeRNAi; 24137; -.
DR Pharos; O95239; Tbio.
DR PRO; PR:O95239; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O95239; protein.
DR Bgee; ENSG00000090889; Expressed in oocyte and 123 other tissues.
DR Genevisible; O95239; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005876; C:spindle microtubule; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008089; P:anterograde axonal transport; TAS:ProtInc.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0006996; P:organelle organization; TAS:ProtInc.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
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 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 3D-structure; Alternative splicing; ATP-binding; Chromosome; Coiled coil;
KW Cytoplasm; Cytoskeleton; DNA-binding; Intellectual disability; Iron;
KW Iron-sulfur; Isopeptide bond; Metal-binding; Microtubule; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1232
FT /note="Chromosome-associated kinesin KIF4A"
FT /id="PRO_0000125437"
FT DOMAIN 9..336
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..1232
FT /note="Required for the interaction with PRC1"
FT /evidence="ECO:0000269|PubMed:15297875"
FT REGION 1000..1232
FT /note="Globular"
FT REGION 1086..1144
FT /note="CRD; required for [4Fe-4S] cluster binding and
FT localization to the spindle midzone and midbody during
FT anaphase and telophase"
FT /evidence="ECO:0000269|PubMed:29848660"
FT REGION 1122..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..999
FT /evidence="ECO:0000255"
FT MOTIF 793..798
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:11736643"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33174"
FT MOD_RES 799
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33174"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 995
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18318008"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1181
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33174"
FT CROSSLNK 1194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1086..1127
FT /note="CSCKGWCGNKQCGCRKQKSDCGVDCCCDPTKCRNRQQGKDSL -> VLLLTP
FT VISALWEAEARGLLEARSSRPAWATWRDPVSTKPKN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013375"
FT VAR_SEQ 1128..1232
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013376"
FT VARIANT 422
FT /note="L -> W (in dbSNP:rs1199457)"
FT /evidence="ECO:0000269|PubMed:10978527,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_021828"
FT VARIANT 491
FT /note="A -> V (in dbSNP:rs2297871)"
FT /id="VAR_049693"
FT VARIANT 1193
FT /note="L -> S (in dbSNP:rs1046485)"
FT /id="VAR_049694"
FT MUTAGEN 1086..1144
FT /note="Missing: Diffuse localization and does not localize
FT to the spindle midzone or midbody during anaphase and
FT telophase. Does not affect the interaction with PRC1."
FT /evidence="ECO:0000269|PubMed:29848660"
FT MUTAGEN 1106
FT /note="C->A: Abolishes chromatin localization; in
FT association with A-1110 and A-1112."
FT /evidence="ECO:0000269|PubMed:29848660"
FT MUTAGEN 1110
FT /note="C->A: Abolishes chromatin localization; in
FT association with A-1106 and A-1112."
FT /evidence="ECO:0000269|PubMed:29848660"
FT MUTAGEN 1112
FT /note="C->A: Abolishes chromatin localization; in
FT association with A-1106 and A-1110."
FT /evidence="ECO:0000269|PubMed:29848660"
FT CONFLICT 223
FT /note="R -> G (in Ref. 2; AAD05492)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="S -> T (in Ref. 8; AAF86334)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="V -> A (in Ref. 2; AAD05492)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="L -> H (in Ref. 8; AAF86334)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="L -> P (in Ref. 2; AAD05492)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="K -> E (in Ref. 3; CAB75427)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="K -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="Q -> P (in Ref. 1; AAD51855)"
FT /evidence="ECO:0000305"
FT CONFLICT 958
FT /note="Q -> R (in Ref. 3; CAB75427)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="L -> Q (in Ref. 1; AAD51855)"
FT /evidence="ECO:0000305"
FT CONFLICT 996..997
FT /note="LL -> S (in Ref. 8; AAF86334)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003..1014
FT /note="QKHLPKDTLLSP -> RTLPRIPFYLQ (in Ref. 8; AAF86334)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="P -> Q (in Ref. 2; AAD05492)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="K -> N (in Ref. 2; AAD05492)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138
FT /note="G -> S (in Ref. 2; AAD05492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1232 AA; 139881 MW; AD1B7C2A10AB24DB CRC64;
MKEEVKGIPV RVALRCRPLV PKEISEGCQM CLSFVPGEPQ VVVGTDKSFT YDFVFDPSTE
QEEVFNTAVA PLIKGVFKGY NATVLAYGQT GSGKTYSMGG AYTAEQENEP TVGVIPRVIQ
LLFKEIDKKS DFEFTLKVSY LEIYNEEILD LLCPSREKAQ INIREDPKEG IKIVGLTEKT
VLVALDTVSC LEQGNNSRTV ASTAMNSQSS RSHAIFTISL EQRKKSDKNS SFRSKLHLVD
LAGSERQKKT KAEGDRLKEG ININRGLLCL GNVISALGDD KKGGFVPYRD SKLTRLLQDS
LGGNSHTLMI ACVSPADSNL EETLNTLRYA DRARKIKNKP IVNIDPQTAE LNHLKQQVQQ
LQVLLLQAHG GTLPGSITVE PSENLQSLME KNQSLVEENE KLSRGLSEAA GQTAQMLERI
ILTEQANEKM NAKLEELRQH AACKLDLQKL VETLEDQELK ENVEIICNLQ QLITQLSDET
VACMAAAIDT AVEQEAQVET SPETSRSSDA FTTQHALRQA QMSKELVELN KALALKEALA
RKMTQNDSQL QPIQYQYQDN IKELELEVIN LQKEKEELVL ELQTAKKDAN QAKLSERRRK
RLQELEGQIA DLKKKLNEQS KLLKLKESTE RTVSKLNQEI RMMKNQRVQL MRQMKEDAEK
FRQWKQKKDK EVIQLKERDR KRQYELLKLE RNFQKQSNVL RRKTEEAAAA NKRLKDALQK
QREVADKRKE TQSRGMEGTA ARVKNWLGNE IEVMVSTEEA KRHLNDLLED RKILAQDVAQ
LKEKKESGEN PPPKLRRRTF SLTEVRGQVS ESEDSITKQI ESLETEMEFR SAQIADLQQK
LLDAESEDRP KQRWENIATI LEAKCALKYL IGELVSSKIQ VSKLESSLKQ SKTSCADMQK
MLFEERNHFA EIETELQAEL VRMEQQHQEK VLYLLSQLQQ SQMAEKQLEE SVSEKEQQLL
STLKCQDEEL EKMREVCEQN QQLLRENEII KQKLTLLQVA SRQKHLPKDT LLSPDSSFEY
VPPKPKPSRV KEKFLEQSMD IEDLKYCSEH SVNEHEDGDG DDDEGDDEEW KPTKLVKVSR
KNIQGCSCKG WCGNKQCGCR KQKSDCGVDC CCDPTKCRNR QQGKDSLGTV ERTQDSEGSF
KLEDPTEVTP GLSFFNPVCA TPNSKILKEM CDVEQVLSKK TPPAPSPFDL PELKHVATEY
QENKAPGKKK KRALASNTSF FSGCSPIEEE AH
