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 10-MAY-2017, entry version 145.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Mitotic kinesin required for chromosome passenger
CC complex (CPC)-mediated cytokinesis. Following phosphorylation by
CC PLK1, involved in recruitment of PLK1 to the central spindle (By
CC similarity). Interacts with guanosine triphosphate (GTP)-bound
CC forms of RAB6A and RAB6B. May act as a motor required for the
CC retrograde RAB6 regulated transport of Golgi membranes and
CC associated vesicles along microtubules. Has a microtubule plus
CC end-directed motility. {ECO:0000250, ECO:0000269|PubMed:9438855}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000305|PubMed:9438855}.
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-
CC 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 UniGene; Mm.258846; -.
DR ProteinModelPortal; P97329; -.
DR BioGrid; 202552; 11.
DR IntAct; P97329; 10.
DR STRING; 10090.ENSMUSP00000130045; -.
DR iPTMnet; P97329; -.
DR PhosphoSitePlus; P97329; -.
DR EPD; P97329; -.
DR MaxQB; P97329; -.
DR PaxDb; P97329; -.
DR PeptideAtlas; P97329; -.
DR PRIDE; P97329; -.
DR Ensembl; ENSMUST00000166044; ENSMUSP00000132659; ENSMUSG00000003779.
DR Ensembl; ENSMUST00000167161; ENSMUSP00000130045; ENSMUSG00000003779.
DR GeneID; 19348; -.
DR KEGG; mmu:19348; -.
DR UCSC; uc008ela.2; mouse.
DR CTD; 10112; -.
DR MGI; MGI:1201682; Kif20a.
DR eggNOG; KOG0247; Eukaryota.
DR eggNOG; COG5059; LUCA.
DR GeneTree; ENSGT00870000136438; -.
DR HOGENOM; HOG000054207; -.
DR HOVERGEN; HBG052246; -.
DR InParanoid; P97329; -.
DR KO; K10402; -.
DR OMA; PANIRFS; -.
DR OrthoDB; EOG091G00AY; -.
DR PhylomeDB; P97329; -.
DR TreeFam; TF105232; -.
DR Reactome; R-MMU-68884; Mitotic Telophase/Cytokinesis.
DR ChiTaRS; Kif20a; mouse.
DR PRO; PR:P97329; -.
DR Proteomes; UP000000589; Chromosome 18.
DR Bgee; ENSMUSG00000003779; -.
DR CleanEx; MM_KIF20A; -.
DR Genevisible; P97329; MM.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000920; P:cell separation after cytokinesis; ISS:UniProtKB.
DR GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027326; KIF20A.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115:SF589; PTHR24115:SF589; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O95235}.
FT CHAIN 2 887 Kinesin-like protein KIF20A.
FT /FTId=PRO_0000125461.
FT DOMAIN 63 506 Kinesin motor. {ECO:0000255|PROSITE-
FT ProRule:PRU00283}.
FT NP_BIND 159 166 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00283}.
FT REGION 805 887 Globular. {ECO:0000255}.
FT COILED 559 804 {ECO:0000255}.
FT MOD_RES 2 2 N-acetylserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 7 7 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 14 14 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 21 21 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 527 527 Phosphoserine; by PLK1. {ECO:0000250}.
FT MOD_RES 683 683 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 823 823 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 855 855 Phosphothreonine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 865 865 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 876 876 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
FT MOD_RES 881 881 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95235}.
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CC The following FT lines are automated annotations from the MyHits database.
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FT MYHIT 63 506 iprf:KINESIN_MOTOR_2 [T]
FT MYHIT 69 505 ipfam:Kinesin [T]
FT MYHIT 401 412 ipat:KINESIN_MOTOR_1 [T]
FT MYHIT 61 514 ismart:KISc [T]
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
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