ID STK6_HUMAN STANDARD; PRT; 403 AA. AC O14965; O60445; O75873; Q9BQD6; Q9UPG5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Serine/threonine-protein kinase 6 (EC 2.7.1.37) (Serine/threonine DE kinase 15) (Aurora/IPL1-related kinase 1) (Aurora-related kinase 1) DE (hARK1) (Aurora-A) (Breast-tumor-amplified kinase). GN Name=STK6; Synonyms=AIK, ARK1, AURA, BTAK, STK15; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood; RX MEDLINE=97298083; PubMed=9153231; DOI=10.1074/jbc.272.21.13766; RA Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., RA Okano Y.; RT "Cell cycle-dependent expression and spindle pole localization of a RT novel human protein kinase, Aik, related to Aurora of Drosophila and RT yeast Ipl1."; RL J. Biol. Chem. 272:13766-13771(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=98183439; PubMed=9514916; DOI=10.1006/bbrc.1998.8250; RA Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., RA Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.; RT "cDNA cloning, expression, subcellular localization, and chromosomal RT assignment of mammalian aurora homologues, aurora-related kinase (ARK) RT 1 and 2."; RL Biochem. Biophys. Res. Commun. 244:285-292(1998). RN [3] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Mammary gland; RX MEDLINE=98442657; PubMed=9771714; DOI=10.1038/2496; RA Zhou H., Kuang J., Zhong L., Kuo W.-L., Gray J.W., Sahin A., RA Brinkley B.R., Sen S.; RT "Tumour amplified kinase STK15/BTAK induces centrosome amplification, RT aneuploidy and transformation."; RL Nat. Genet. 20:189-193(1998). RN [4] RP NUCLEOTIDE SEQUENCE. RA Wang L., Thibodeau S.N.; RT "Mutational analysis of the STK15 gene in human tumors."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Cervix, Colon, Kidney, and Muscle; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [7] RP CELL-CYCLE REGULATION. RX MEDLINE=21895866; PubMed=11790771; DOI=10.1074/jbc.M108252200; RA Tanaka M., Ueda A., Kanamori H., Ideguchi H., Yang J., Kitajima S., RA Ishigatsubo Y.; RT "Cell-cycle-dependent regulation of human aurora A transcription is RT mediated by periodic repression of E4TF1."; RL J. Biol. Chem. 277:10719-10726(2002). RN [8] RP REVIEW. RX MEDLINE=21306577; PubMed=11413462; DOI=10.1038/35048096; RA Nigg E.A.; RT "Mitotic kinases as regulators of cell division and its checkpoints."; RL Nat. Rev. Mol. Cell Biol. 2:21-32(2001). CC -!- FUNCTION: May play a role in cell cycle regulation during anaphase CC and/or telophase, in relation to the function of the CC centrosome/spindle pole region during chromosome segregation. CC Maybe involved in microtubule formation and/or stabilization. May CC play a key role during tumor development and progression. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Localizes on centrosomes in interphase cells CC and at each spindle pole in mitosis. CC -!- TISSUE SPECIFICITY: Highly expressed in testis and weakly in CC skeletal muscle, thymus and spleen. Also highly expressed in CC colon, ovarian, prostate, neuroblastoma, breast and cervical CC cancer cell lines. Expression is cell-cycle regulated, low in CC G1/S, accumulates during G2/M, and decreases rapidly after. CC -!- PTM: Phosphorylated. CC -!- DISEASE: Defects in STK6 are responsible for numerical centrosome CC aberrations including aneuploidy. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. Aurora CC subfamily. CC -!- CAUTION: Ref.1 sequence differs from that shown due to frameshifts CC in positions 105, 125, 129, 235 and 241. CC -!- CAUTION: Although authors have considered STK6 and STK15 as two CC different proteins, it is clear that they are the same protein. 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; D84212; BAA23592.1; ALT_FRAME. DR EMBL; AF008551; AAC12708.1; -. DR EMBL; AF011467; AAC23448.1; -. DR EMBL; AF011468; AAC63902.1; -. DR EMBL; AF195947; AAF29508.1; -. DR EMBL; AF195942; AAF29508.1; JOINED. DR EMBL; AF195943; AAF29508.1; JOINED. DR EMBL; AF195944; AAF29508.1; JOINED. DR EMBL; AF195945; AAF29508.1; JOINED. DR EMBL; AF195946; AAF29508.1; JOINED. DR EMBL; AL121914; CAC12717.1; -. DR EMBL; BC001280; AAH01280.1; -. DR EMBL; BC002499; AAH02499.1; -. DR EMBL; BC006423; AAH06423.1; -. DR EMBL; BC027464; AAH27464.1; -. DR PDB; 1MQ4; X-ray; A=120-391. DR PDB; 1MUO; X-ray; A=107-403. DR PDB; 1OL6; X-ray; A=122-403. DR PDB; 1OL7; X-ray; A=122-403. DR IntAct; O14965; -. DR Genew; HGNC:11393; STK15. DR Genew; HGNC:11409; STK6. DR H-InvDB; HIX0015930; -. DR MIM; 602687; -. DR MIM; 603072; -. DR GO; GO:0005634; C:nucleus; TAS. DR GO; GO:0005819; C:spindle; TAS. DR GO; GO:0005515; F:protein binding; IDA. DR GO; GO:0004672; F:protein kinase activity; TAS. DR GO; GO:0007067; P:mitosis; TAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW 3D-structure; ATP-binding; Cell cycle; Phosphorylation; KW Serine/threonine-protein kinase; Transferase. FT DOMAIN 133 383 Protein kinase. FT NP_BIND 139 147 ATP (By similarity). FT BINDING 162 162 ATP (By similarity). FT ACT_SITE 256 256 Proton acceptor (By similarity). FT CONFLICT 31 31 F -> I (in Ref. 3). FT CONFLICT 57 57 V -> I (in Ref. 2). SQ SEQUENCE 403 AA; 45809 MW; 125F3594834CD157 CRC64; MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP SNSSQRVPLQ AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ PLPSAPENNP EEELASKQKN EESKKRQWAL EDFEIGRPLG KGKFGNVYLA REKQSKFILA LKVLFKAQLE KAGVEHQLRR EVEIQSHLRH PNILRLYGYF HDATRVYLIL EYAPLGTVYR ELQKLSKFDE QRTATYITEL ANALSYCHSK RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD FVTEGARDLI SRLLKHNPSQ RPMLREVLEH PWITANSSKP SNCQNKESAS KQS //