KI20A_MOUSE
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 03-AUG-2022, entry version 178.
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}.
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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 PDBsum; 5LEF; -.
DR PDBsum; 5ND2; -.
DR PDBsum; 5ND3; -.
DR PDBsum; 5ND4; -.
DR PDBsum; 5ND7; -.
DR AlphaFoldDB; P97329; -.
DR SMR; P97329; -.
DR BioGRID; 202552; 12.
DR IntAct; P97329; 10.
DR STRING; 10090.ENSMUSP00000132659; -.
DR iPTMnet; P97329; -.
DR PhosphoSitePlus; P97329; -.
DR EPD; P97329; -.
DR jPOST; P97329; -.
DR MaxQB; P97329; -.
DR PaxDb; P97329; -.
DR PeptideAtlas; P97329; -.
DR PRIDE; P97329; -.
DR ProteomicsDB; 263437; -.
DR Antibodypedia; 26611; 322 antibodies from 28 providers.
DR DNASU; 19348; -.
DR Ensembl; ENSMUST00000166044; ENSMUSP00000132659; ENSMUSG00000003779.
DR Ensembl; ENSMUST00000167161; ENSMUSP00000130045; ENSMUSG00000003779.
DR Ensembl; ENSMUST00000237407; ENSMUSP00000157839; ENSMUSG00000003779.
DR GeneID; 19348; -.
DR KEGG; mmu:19348; -.
DR UCSC; uc008ela.2; mouse.
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; DVREECW; -.
DR OrthoDB; 314538at2759; -.
DR PhylomeDB; P97329; -.
DR TreeFam; TF105232; -.
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 76 CRISPR screens.
DR ChiTaRS; Kif20a; mouse.
DR PRO; PR:P97329; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P97329; protein.
DR Bgee; ENSMUSG00000003779; Expressed in undifferentiated genital tubercle and 179 other tissues.
DR ExpressionAtlas; P97329; baseline and differential.
DR Genevisible; P97329; MM.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0061952; P:midbody abscission; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027326; KIF20A.
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; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF352; PTHR24115:SF352; 1.
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; 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 826..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..869
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 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
