ID STK6_HUMAN STANDARD; PRT; 403 AA. AC O14965; O60445; O75873; Q9BQD6; Q9UPG5; DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JAN-2003, sequence version 2. DT 27-JUN-2006, entry version 66. DE Serine/threonine-protein kinase 6 (EC 2.7.11.1) (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; Euarchontoglires; Primates; Haplorrhini; OC 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 [LARGE SCALE MRNA]. 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). RN [9] RP INTERACTION WITH TACC1. RX PubMed=14603251; DOI=10.1038/sj.onc.1206972; RA Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D., RA Larroque C., Prigent C., Seraphin B., Jacquemier J., Birnbaum D.; RT "TACC1-chTOG-Aurora A protein complex in breast cancer."; RL Oncogene 22:8102-8116(2003). 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 -!- SUBUNIT: Interacts with TACC1. CC -!- INTERACTION: CC Q9NWT8:AURKAIP1; NbExp=2; IntAct=EBI-448680, EBI-448665; CC O75410-1:TACC1; NbExp=1; IntAct=EBI-448680, EBI-624252; CC -!- SUBCELLULAR LOCATION: Centrosome. Spindle. Localizes on CC centrosomes in interphase cells and at each spindle pole in CC 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 -!- SIMILARITY: Contains 1 protein kinase domain. 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; mRNA. DR EMBL; AF008551; AAC12708.1; -; mRNA. DR EMBL; AF011467; AAC23448.1; -; Genomic_DNA. DR EMBL; AF011468; AAC63902.1; -; mRNA. DR EMBL; AF195947; AAF29508.1; -; Genomic_DNA. DR EMBL; AF195942; AAF29508.1; JOINED; Genomic_DNA. DR EMBL; AF195943; AAF29508.1; JOINED; Genomic_DNA. DR EMBL; AF195944; AAF29508.1; JOINED; Genomic_DNA. DR EMBL; AF195945; AAF29508.1; JOINED; Genomic_DNA. DR EMBL; AF195946; AAF29508.1; JOINED; Genomic_DNA. DR EMBL; AL121914; CAC12717.1; -; Genomic_DNA. DR EMBL; BC001280; AAH01280.1; -; mRNA. DR EMBL; BC002499; AAH02499.1; -; mRNA. DR EMBL; BC006423; AAH06423.1; -; mRNA. DR EMBL; BC027464; AAH27464.1; -; mRNA. DR PDB; 1MQ4; X-ray; A=125-391. DR PDB; 1MUO; X-ray; A=107-403. DR PDB; 1OL5; X-ray; A=122-403. DR PDB; 1OL6; X-ray; A=122-403. DR PDB; 1OL7; X-ray; A=122-403. DR PDB; 2BMC; X-ray; A/B/C/D/E/F=100-403. DR PDB; 2C6D; X-ray; A=124-398. DR PDB; 2C6E; X-ray; A/B=123-401. DR IntAct; O14965; -. DR Ensembl; ENSG00000087586; Homo sapiens. DR H-InvDB; HIX0015930; -. DR HGNC; HGNC:11393; STK15. DR HGNC; HGNC:11409; STK6. DR MIM; 602687; gene. DR MIM; 603072; gene. DR LinkHub; O14965; -. DR RZPD-ProtExp; IOH21165; -. DR RZPD-ProtExp; Q0008; -. DR RZPD-ProtExp; Z0617; -. 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:0007049; P:cell cycle; NAS. DR GO; GO:0007067; P:mitosis; TAS. DR GO; GO:0048015; P:phosphoinositide-mediated signaling; NAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS. DR GO; GO:0031647; P:regulation of protein stability; IMP. DR GO; GO:0007051; P:spindle organization and biogenesis; NAS. 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; Kinase; Nucleotide-binding; KW Phosphorylation; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 403 Serine/threonine-protein kinase 6. FT /FTId=PRO_0000086692. FT DOMAIN 133 383 Protein kinase. FT NP_BIND 139 147 ATP (By similarity). FT ACT_SITE 256 256 Proton acceptor (By similarity). FT BINDING 162 162 ATP (By similarity). FT CONFLICT 31 31 F -> I (in Ref. 3). FT CONFLICT 57 57 V -> I (in Ref. 2). FT HELIX 130 132 FT STRAND 133 141 FT STRAND 143 152 FT TURN 153 155 FT STRAND 158 165 FT HELIX 166 172 FT TURN 173 173 FT HELIX 175 187 FT TURN 191 192 FT STRAND 193 193 FT STRAND 196 201 FT STRAND 203 210 FT TURN 214 215 FT STRAND 217 217 FT HELIX 218 225 FT STRAND 226 227 FT HELIX 230 249 FT TURN 250 251 FT STRAND 252 253 FT HELIX 259 261 FT STRAND 262 264 FT TURN 266 267 FT STRAND 270 272 FT HELIX 275 277 FT STRAND 279 283 FT TURN 294 295 FT HELIX 298 301 FT TURN 302 303 FT STRAND 306 306 FT TURN 308 308 FT HELIX 309 324 FT STRAND 325 326 FT TURN 328 329 FT STRAND 332 333 FT HELIX 334 343 FT TURN 344 344 FT TURN 350 351 FT STRAND 352 352 FT HELIX 354 363 FT STRAND 366 367 FT HELIX 368 370 FT STRAND 371 371 FT HELIX 374 378 FT TURN 379 379 FT HELIX 381 386 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 //