STK35_MOUSE
ID STK35_MOUSE Reviewed; 539 AA.
AC Q80ZW0; A2ANF2; Q3TMD8; Q8BIC2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase 35;
DE AltName: Full=Serine/threonine-protein kinase 35 L1;
DE EC=2.7.11.1;
GN Name=Stk35; Synonyms=Stk35l1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-539.
RC TISSUE=Olfactory epithelium;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-539.
RC STRAIN=C57BL/6J; TISSUE=Lung, and 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 [4]
RP IDENTIFICATION BY 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 -!- 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 PDLIM1/CLP-36. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Cytoplasm. Note=When
CC associated with PDLIM1, it is mostly found in cytoplasm, localized to
CC actin stress fibers. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI38905.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI38906.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25152.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25152.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE38504.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM22106.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL808137; CAM22106.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC047277; AAH47277.1; -; mRNA.
DR EMBL; BC138904; AAI38905.1; ALT_INIT; mRNA.
DR EMBL; BC138905; AAI38906.1; ALT_INIT; mRNA.
DR EMBL; AK006778; BAC25152.1; ALT_SEQ; mRNA.
DR EMBL; AK165988; BAE38504.1; ALT_INIT; mRNA.
DR CCDS; CCDS16732.2; -.
DR RefSeq; NP_899085.3; NM_183262.3.
DR AlphaFoldDB; Q80ZW0; -.
DR SMR; Q80ZW0; -.
DR BioGRID; 212113; 3.
DR STRING; 10090.ENSMUSP00000126541; -.
DR iPTMnet; Q80ZW0; -.
DR PhosphoSitePlus; Q80ZW0; -.
DR EPD; Q80ZW0; -.
DR MaxQB; Q80ZW0; -.
DR PaxDb; Q80ZW0; -.
DR PRIDE; Q80ZW0; -.
DR ProteomicsDB; 258757; -.
DR Antibodypedia; 23148; 190 antibodies from 27 providers.
DR DNASU; 67333; -.
DR Ensembl; ENSMUST00000165413; ENSMUSP00000126541; ENSMUSG00000037885.
DR GeneID; 67333; -.
DR KEGG; mmu:67333; -.
DR UCSC; uc008mie.2; mouse.
DR CTD; 140901; -.
DR MGI; MGI:1914583; Stk35.
DR VEuPathDB; HostDB:ENSMUSG00000037885; -.
DR eggNOG; KOG0595; Eukaryota.
DR GeneTree; ENSGT00940000158197; -.
DR HOGENOM; CLU_026714_1_0_1; -.
DR InParanoid; Q80ZW0; -.
DR OMA; WPGADHP; -.
DR OrthoDB; 813266at2759; -.
DR PhylomeDB; Q80ZW0; -.
DR TreeFam; TF105336; -.
DR BioGRID-ORCS; 67333; 5 hits in 76 CRISPR screens.
DR PRO; PR:Q80ZW0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80ZW0; protein.
DR Bgee; ENSMUSG00000037885; Expressed in retinal neural layer and 207 other tissues.
DR ExpressionAtlas; Q80ZW0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..539
FT /note="Serine/threonine-protein kinase 35"
FT /id="PRO_0000277618"
FT DOMAIN 207..535
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 103..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 365
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 213..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 28
FT /note="W -> G (in Ref. 3; BAE38504)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="R -> G (in Ref. 3; BAE38504/BAC25152)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="R -> S (in Ref. 3; BAC25152)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..327
FT /note="ERILGYAEEPCYLWFVMEYCEGGD -> RSFGTHSLIVSRTGWQRVQVVVIS
FT (in Ref. 3; BAE38504)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="P -> A (in Ref. 3; BAC25152)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="F -> V (in Ref. 3; BAC25152)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..377
FT /note="DLKPDNILITERS -> RPKARQHPDHRAV (in Ref. 3;
FT BAC25152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 59459 MW; 66959648E99458B3 CRC64;
MGHQESPLTR AAAGGAAYIK RLRKVLSWRE LGDGHGNLEA EASPGSVAVI TRAAPRRATR
SARLPASRPT RLCRQARLGT DHPPARAPRG NRFARKRNSA GQITIQGPAP PHLGARRRDE
ARGARAAPLL LPPPPAAMET GKENGARRGT KSPERKRRSP VQRVLCEKLR PAAQAMDPAG
AEVPGEAFLA RRRPDGGGGD VPARPRYSLL AEIGRGSYGV VYEAVAGRSG ARVAVKKIRC
DAPENVELAL AEFWALTSLK RRHQNIVQFE ECVLQRNGLA QRMSHGNKNS QLYLRLVETS
LKGERILGYA EEPCYLWFVM EYCEGGDLNQ YVLSRRPDPA TNKSFMLQLT SAIAFLHKNH
IVHRDLKPDN ILITERSGTP ILKVADFGLS KVCAGLAPRG KEGNQDNKNV NVNKYWLSSA
CGSDFYMAPE VWEGHYTAKA DIFALGIIIW AMIERITFID SETKKELLGT YIKQGTEIVP
VGEALLENPK MELHIPQKRR TSMSEGVKQL LKDMLAANPQ DRPDAFELET RMDQVTCAA
