STK33_MOUSE
ID STK33_MOUSE Reviewed; 491 AA.
AC Q924X7; Q4A1D4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine/threonine-protein kinase 33;
DE EC=2.7.11.1;
GN Name=Stk33;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378.
RX PubMed=11528127; DOI=10.1159/000056999;
RA Amid C., Bahr A., Mujica A., Sampson N., Bikar S.E., Winterpacht A.,
RA Zabel B., Hankeln T., Schmidt E.R.;
RT "Comparative genomic sequencing reveals a strikingly similar architecture
RT of a conserved syntenic region on human chromosome 11p15.3 (including gene
RT ST5) and mouse chromosome 7.";
RL Cytogenet. Cell Genet. 93:284-290(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-423.
RC STRAIN=BALB/cJ;
RX PubMed=11738831; DOI=10.1016/s0378-1119(01)00780-6;
RA Mujica A.O., Hankeln T., Schmidt E.R.;
RT "A novel serine/threonine kinase gene, STK33, on human chromosome
RT 11p15.3.";
RL Gene 280:175-181(2001).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16176263; DOI=10.1111/j.1742-4658.2005.04900.x;
RA Mujica A.O., Brauksiepe B., Saaler-Reinhardt S., Reuss S., Schmidt E.R.;
RT "Differential expression pattern of the novel serine/threonine kinase,
RT STK33, in mice and men.";
RL FEBS J. 272:4884-4898(2005).
RN [5]
RP FUNCTION, INTERACTION WITH VIME, AND AUTOPHOSPHORYLATION.
RX PubMed=18811945; DOI=10.1186/1471-2091-9-25;
RA Brauksiepe B., Mujica A.O., Herrmann H., Schmidt E.R.;
RT "The serine/threonine kinase Stk33 exhibits autophosphorylation and
RT phosphorylates the intermediate filament protein Vimentin.";
RL BMC Biochem. 9:25-25(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serine/threonine protein kinase which phosphorylates VIME.
CC May play a specific role in the dynamic behavior of the intermediate
CC filament cytoskeleton by phosphorylation of VIME.
CC {ECO:0000269|PubMed:18811945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with VIME. {ECO:0000269|PubMed:18811945}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16176263}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, particularly in cells
CC from the spermatogenic epithelia. Significant expression is detected in
CC lung epithelia, alveolar macrophages, horizontal cells in the retina
CC and in embryonic organs such as heart, brain and spinal cord. Also
CC expressed in pituitary gland, kidney, pancreas, trachea and thyroid
CC gland. {ECO:0000269|PubMed:16176263}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AK014819; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ307671; CAC39171.1; -; Genomic_DNA.
DR EMBL; AM056057; CAJ20841.1; -; mRNA.
DR CCDS; CCDS52358.1; -.
DR RefSeq; NP_473444.1; NM_054103.1.
DR RefSeq; XP_006507287.1; XM_006507224.1.
DR RefSeq; XP_006507288.1; XM_006507225.3.
DR RefSeq; XP_006507289.1; XM_006507226.3.
DR RefSeq; XP_011239951.1; XM_011241649.2.
DR RefSeq; XP_011239952.1; XM_011241650.2.
DR RefSeq; XP_011239954.1; XM_011241652.1.
DR RefSeq; XP_017177428.1; XM_017321939.1.
DR RefSeq; XP_017177429.1; XM_017321940.1.
DR RefSeq; XP_017177430.1; XM_017321941.1.
DR AlphaFoldDB; Q924X7; -.
DR SMR; Q924X7; -.
DR BioGRID; 228210; 1.
DR STRING; 10090.ENSMUSP00000102356; -.
DR iPTMnet; Q924X7; -.
DR PhosphoSitePlus; Q924X7; -.
DR MaxQB; Q924X7; -.
DR PaxDb; Q924X7; -.
DR PeptideAtlas; Q924X7; -.
DR PRIDE; Q924X7; -.
DR ProteomicsDB; 254762; -.
DR Antibodypedia; 11459; 449 antibodies from 35 providers.
DR DNASU; 117229; -.
DR Ensembl; ENSMUST00000090414; ENSMUSP00000087897; ENSMUSG00000031027.
DR Ensembl; ENSMUST00000106745; ENSMUSP00000102356; ENSMUSG00000031027.
DR Ensembl; ENSMUST00000121748; ENSMUSP00000112515; ENSMUSG00000031027.
DR GeneID; 117229; -.
DR KEGG; mmu:117229; -.
DR UCSC; uc009jdm.2; mouse.
DR CTD; 65975; -.
DR MGI; MGI:2152419; Stk33.
DR VEuPathDB; HostDB:ENSMUSG00000031027; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000159050; -.
DR InParanoid; Q924X7; -.
DR OMA; CGEPPFM; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q924X7; -.
DR TreeFam; TF314166; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 117229; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Stk33; mouse.
DR PRO; PR:Q924X7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q924X7; protein.
DR Bgee; ENSMUSG00000031027; Expressed in spermatid and 54 other tissues.
DR ExpressionAtlas; Q924X7; baseline and differential.
DR Genevisible; Q924X7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..491
FT /note="Serine/threonine-protein kinase 33"
FT /id="PRO_0000278477"
FT DOMAIN 111..377
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 51..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 117..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 92
FT /note="Missing (in Ref. 1; AK014819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 54459 MW; 10F2490ACC4394B8 CRC64;
MADPSLNDNP TACPHCASSQ AGLLCVCPAG KSPVLVVEMS QTSSIGSTEF FASQERKKER
NTSRESSLKD LSIRTSNVER KPQAQWSRSN VTVGKIPHIR MDDGAGIEEF YTFGRILGQG
SFGMVFEAID KETGAKWAIK KVNKEKAGSS AMKLLEREVS ILKTVNHQHI IHLEQVFESP
QKMYLVMELC EDGELKAVMD QRGHFSENET RLIIQSLASA IAYLHNKDIV HRDLKLENIM
VKSSFIDDNN EMNLNIKVTD FGLSVQKHGS RSEGMMQTTC GTPIYMAPEV INAHDYSQQC
DIWSIGVIMF ILLCGEPPFL ANSEEKLYEL IKKGELRFEN PVWESVSDSA KNTLKQLMKV
DPAHRITAKE LLDNQWLTGN TLSSARPTNV LEMMKEWKNN PESDEETNTD EETEQSAVYS
PSANTAKQPT NAAKKPAAES VGMTSSNSSS SKLLSAESKA EPEKSSETVG HASVAKTTLK
STTLFRGKKR L
