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 27-MAR-2024, entry version 212. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 99. DR CORUM; O95239; -. DR ELM; O95239; -. DR IntAct; O95239; 23. 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 SwissPalm; O95239; -. DR BioMuta; KIF4A; -. DR CPTAC; CPTAC-971; -. DR EPD; O95239; -. DR jPOST; O95239; -. DR MassIVE; O95239; -. DR MaxQB; O95239; -. DR PaxDb; 9606-ENSP00000363524; -. DR PeptideAtlas; O95239; -. DR ProteomicsDB; 50738; -. [O95239-1] DR ProteomicsDB; 50739; -. [O95239-2] DR Pumba; O95239; -. DR Antibodypedia; 27394; 269 antibodies from 33 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 AGR; HGNC:13339; -. 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 OrthoDB; 602895at2759; -. 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; 259 hits in 779 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 124 other cell types or tissues. 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 CDD; cd01372; KISc_KIF4; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. 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 PANTHER; PTHR47969:SF23; CHROMOSOME-ASSOCIATED KINESIN KIF4A; 1. DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1. DR Pfam; PF00225; Kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR Genevisible; O95239; HS. 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 //