ID KI20A_MOUSE Reviewed; 887 AA. AC P97329; Q542M4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 02-SEP-2026, entry version 197. DE RecName: Full=Kinesin-like protein KIF20A; DE AltName: Full=Kinesin-like protein 174; DE AltName: Full=Rab6-interacting kinesin-like protein; DE AltName: Full=Rabkinesin-6; GN Name=Kif20a; Synonyms=Rab6kifl; 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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC STRAIN=BALB/cJ; TISSUE=Testis; RX PubMed=9438855; DOI=10.1126/science.279.5350.580; RA Echard A., Jollivet F., Martinez O., Lacapere J.-J., Rousselet A., RA Janoueix-Lerosey I., Goud B.; RT "Interaction of a Golgi-associated kinesin-like protein with Rab6."; RL Science 279:580-585(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart, and Lung; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; 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). CC -!- FUNCTION: Mitotic kinesin required for chromosome passenger complex CC (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved CC in recruitment of PLK1 to the central spindle (By similarity). CC Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and CC RAB6B. May act as a motor required for the retrograde RAB6 regulated CC transport of Golgi membranes and associated vesicles along CC microtubules. Has a microtubule plus end-directed motility. CC {ECO:0000250, ECO:0000269|PubMed:9438855}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000305|PubMed:9438855}. Note=Localizes to CC the spindle midzone during anaphase and telophase. CC {ECO:0000250|UniProtKB:O95235}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in CC spleen and testis. {ECO:0000269|PubMed:9438855}. CC -!- PTM: Phosphorylated by PLK1 at Ser-527 during mitosis, creating a CC docking site for PLK1 and recruiting PLK1 at central spindle. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}. 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; Y09632; CAA70845.1; -; mRNA. DR EMBL; AK083412; BAC38906.1; -; mRNA. DR EMBL; AK084732; BAC39267.1; -; mRNA. DR EMBL; AK144844; BAE26095.1; -; mRNA. DR EMBL; BC060608; AAH60608.1; -; mRNA. DR CCDS; CCDS29131.1; -. DR RefSeq; NP_001159878.1; NM_001166406.1. DR RefSeq; NP_001159879.1; NM_001166407.1. DR RefSeq; NP_033030.1; NM_009004.4. DR PDB; 5LEF; X-ray; 2.09 A; C/D=603-665. DR PDB; 5ND2; EM; 5.80 A; C=21-521. DR PDB; 5ND3; EM; 6.10 A; C=21-521. DR PDB; 5ND4; EM; 4.40 A; C=21-521. DR PDB; 5ND7; EM; 7.90 A; C=21-521. DR PDB; 8BJS; X-ray; 2.73 A; A=55-513. DR PDB; 8F18; EM; 3.20 A; K=1-565. DR PDB; 8F1A; EM; 3.10 A; K=1-565. DR AlphaFoldDB; P97329; -. DR EMDB; EMD-28787; -. DR EMDB; EMD-28789; -. DR EMDB; EMD-3620; -. DR EMDB; EMD-3621; -. DR EMDB; EMD-3622; -. DR EMDB; EMD-3623; -. DR SMR; P97329; -. DR BioGRID; 202552; 13. DR FunCoup; P97329; 1208. DR IntAct; P97329; 10. DR STRING; 10090.ENSMUSP00000157839; -. DR iPTMnet; P97329; -. DR PhosphoSitePlus; P97329; -. DR SwissPalm; P97329; -. DR jPOST; P97329; -. DR PaxDb; 10090-ENSMUSP00000157839; -. DR PeptideAtlas; P97329; -. DR ProteomicsDB; 263437; -. DR Pumba; P97329; -. DR Antibodypedia; 26611; 317 antibodies from 30 providers. DR DNASU; 19348; -. DR Ensembl; ENSMUST00000166044.3; ENSMUSP00000132659.2; ENSMUSG00000003779.17. DR Ensembl; ENSMUST00000167161.9; ENSMUSP00000130045.2; ENSMUSG00000003779.17. DR Ensembl; ENSMUST00000237407.2; ENSMUSP00000157839.2; ENSMUSG00000003779.17. DR GeneID; 19348; -. DR KEGG; mmu:19348; -. DR UCSC; uc008ela.2; mouse. DR AGR; MGI:1201682; -. DR CTD; 10112; -. DR MGI; MGI:1201682; Kif20a. DR VEuPathDB; HostDB:ENSMUSG00000003779; -. DR eggNOG; KOG0247; Eukaryota. DR GeneTree; ENSGT00940000156931; -. DR HOGENOM; CLU_001485_2_5_1; -. DR InParanoid; P97329; -. DR OMA; NRHPQKA; -. DR OrthoDB; 2403182at2759; -. DR PhylomeDB; P97329; -. DR BRENDA; 5.6.1.3; 3474. 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-68884; Mitotic Telophase/Cytokinesis. DR Reactome; R-MMU-983189; Kinesins. DR BioGRID-ORCS; 19348; 18 hits in 81 CRISPR screens. DR PRO; PR:P97329; -. DR Proteomes; UP000000589; Chromosome 18. DR RNAct; P97329; protein. DR Bgee; ENSMUSG00000003779; Expressed in undifferentiated genital tubercle and 182 other cell types or tissues. DR ExpressionAtlas; P97329; baseline and differential. DR GO; GO:0032154; C:cleavage furrow; ISO:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0045171; C:intercellular bridge; ISO:GO_Central. DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; ISO:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005819; C:spindle; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008017; F:microtubule binding; IEA:InterPro. DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro. DR GO; GO:0019901; F:protein kinase binding; ISO:GO_Central. DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro. DR GO; GO:0061952; P:midbody abscission; ISS:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB. DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB. DR CDD; cd01368; KISc_KIF23_like; 1. DR CDD; cd21787; RBD_KIF20A; 1. DR FunFam; 3.40.850.10:FF:000094; Kinesin-like protein; 1. DR FunFam; 3.40.850.10:FF:000095; Kinesin-like protein; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR InterPro; IPR047149; KIF11-like. 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; PTHR47970:SF29; KINESIN FAMILY MEMBER 20B; 1. DR PANTHER; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 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 PDBsum; 5LEF; -. DR PDBsum; 5ND2; -. DR PDBsum; 5ND3; -. DR PDBsum; 5ND4; -. DR PDBsum; 5ND7; -. DR PDBsum; 8BJS; -. DR PDBsum; 8F18; -. DR PDBsum; 8F1A; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Coiled coil; Cytoplasm; KW Cytoskeleton; Golgi apparatus; Microtubule; Motor protein; KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:O95235" FT CHAIN 2..887 FT /note="Kinesin-like protein KIF20A" FT /id="PRO_0000125461" FT DOMAIN 63..506 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT REGION 527..553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 805..887 FT /note="Globular" FT /evidence="ECO:0000255" FT REGION 826..875 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 559..804 FT /evidence="ECO:0000255" FT COMPBIAS 543..553 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 856..865 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 159..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 527 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 683 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 823 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 855 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 865 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 876 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT MOD_RES 881 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95235" FT STRAND 64..70 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 71..74 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 75..79 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:8F18" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 123..126 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 132..138 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 140..149 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 153..158 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 165..169 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 178..190 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 213..227 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 287..291 FT /evidence="ECO:0007829|PDB:8BJS" FT TURN 293..295 FT /evidence="ECO:0007829|PDB:8F1A" FT STRAND 296..308 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 311..317 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 346..350 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 351..367 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:8F1A" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:8F1A" FT STRAND 380..395 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 397..407 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 408..411 FT /evidence="ECO:0007829|PDB:8F1A" FT HELIX 432..445 FT /evidence="ECO:0007829|PDB:8BJS" FT TURN 446..449 FT /evidence="ECO:0007829|PDB:8F1A" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 462..466 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:8BJS" FT TURN 471..473 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 474..483 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 487..489 FT /evidence="ECO:0007829|PDB:8F1A" FT HELIX 490..500 FT /evidence="ECO:0007829|PDB:8BJS" FT STRAND 502..506 FT /evidence="ECO:0007829|PDB:8BJS" FT HELIX 603..644 FT /evidence="ECO:0007829|PDB:5LEF" SQ SEQUENCE 887 AA; 99876 MW; 7143CCB261A4EA15 CRC64; MSHRILSPPA GLLSDEDVVD SPILESTAAD LRSVVRKDLL SDCSVISASL EDKQALLEDT SEKVKVYLRI RPFLTSELDR QEDQGCVCIE NTETLVLQAP KDSFALKSNE RGVGQATHKF TFSQIFGPEV GQVAFFNLTM KEMVKDVLKG QNWLIYTYGV TNSGKTYTIQ GTSKDAGILP QSLALIFNSL QGQLHPTPDL KPLLSNEVIW LDSKQIRQEE MKKLSLLIGG LQEEELSTSV KKRVHTESRI GASNSFDSGV AGLSSTSQFT SSSQLDETSQ LWAQPDTVPV SVPADIRFSV WISFFEIYNE LLYDLLEPPS HQHKRQTLRL CEDQNGNPYV KDLNWIHVRD VEEAWKLLKV GRKNQSFAST HMNQQSSRSH SIFSIRILHL QGEGDIVPKI SELSLCDLAG SERCKHQKSG ERLKEAGNIN TSLHTLGRCI AALRQNQQNR SKQNLIPFRD SKLTRVFQGF FTGRGRSCMI VNVNPCASTY DETLHAAKFS ALASQLVHAP PVHLGIPSLH SFIKKHSPQV GPGLEKEDKA DSDLEDSPED EADVSVYGKE ELLQVVEAMK ALLLKERQEK LQLEIQLREE ICNEMVEQMQ QREQWCSERL DNQKELMEEL YEEKLKILKE SLTTFYQEQI QERDEKIEEL ETLLQEAKQQ PAAQQSGGLS LLRRSQRLAA SASTQQFQEV KAELEQCKTE LSSTTAELHK YQQVLKPPPP AKPFTIDVDK KLEEGQKNIR LLRTELQKLG QSLQSAERAC CHSTGAGKLR QALTNCDDIL IKQNQTLAEL QNNMVLVKLD LQKKAACIAE QYHTVLKLQG QASAKKRLGA NQENQQPNHQ PPGKKPFLRN LLPRTPTCQS STDSSPYARI LRSRHSPLLK SPFGKKY //