STK35_HUMAN
ID STK35_HUMAN Reviewed; 534 AA.
AC Q8TDR2; B2RBM3; C7ENV8; Q2NKW6; Q5T3R1; Q5T3R2; Q96AB4; Q9BZ06;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Serine/threonine-protein kinase 35;
DE EC=2.7.11.1;
DE AltName: Full=CLP-36-interacting kinase 1;
DE Short=CLIK-1;
DE AltName: Full=PDLIM1-interacting kinase 1;
DE AltName: Full=Serine/threonine-protein kinase 35 L1;
GN Name=STK35; Synonyms=CLIK1, PDIK1, STK35L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=19756140; DOI=10.1371/journal.pone.0006981;
RA Goyal P., Behring A., Kumar A., Siess W.;
RT "Identifying and characterizing a novel protein kinase STK35L1 and
RT deciphering its orthologs and close-homologs in vertebrates.";
RL PLoS ONE 4:E6981-E6981(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX 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., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., 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., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-534.
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-534.
RC TISSUE=Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 134-534, MUTAGENESIS OF LYS-231, SUBCELLULAR
RP LOCATION, AND AUTOPHOSPHORYLATION.
RX PubMed=11973348; DOI=10.1242/jcs.115.10.2067;
RA Vallenius T., Maekelae T.P.;
RT "Clik1: a novel kinase targeted to actin stress fibers by the CLP-36 PDZ-
RT LIM protein.";
RL J. Cell Sci. 115:2067-2073(2002).
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.
CC -!- INTERACTION:
CC Q8TDR2; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-18986091, EBI-1051317;
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 (PubMed:11973348). However, PubMed:19756140
CC detected STK35 only in the nucleus, and the presence of PDLIM1 had no
CC influence on its location. {ECO:0000269|PubMed:11973348}.
CC -!- TISSUE SPECIFICITY: Expressed in testis.
CC -!- PTM: Autophosphorylated.
CC -!- MISCELLANEOUS: Association with PDLIM1 is controversial.
CC {ECO:0000305|PubMed:11973348}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40884.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI40885.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37270.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GQ281297; ACU33925.1; -; mRNA.
DR EMBL; AL359916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK314728; BAG37270.1; ALT_INIT; mRNA.
DR EMBL; BC017340; AAH17340.2; -; mRNA.
DR EMBL; BC111573; AAI11574.1; -; mRNA.
DR EMBL; BC140883; AAI40884.1; ALT_INIT; mRNA.
DR EMBL; BC140884; AAI40885.1; ALT_INIT; mRNA.
DR EMBL; AF195026; AAL99353.1; -; mRNA.
DR CCDS; CCDS13024.2; -.
DR RefSeq; NP_543026.2; NM_080836.3.
DR AlphaFoldDB; Q8TDR2; -.
DR BioGRID; 126760; 25.
DR IntAct; Q8TDR2; 18.
DR STRING; 9606.ENSP00000370891; -.
DR BindingDB; Q8TDR2; -.
DR ChEMBL; CHEMBL5651; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8TDR2; -.
DR iPTMnet; Q8TDR2; -.
DR PhosphoSitePlus; Q8TDR2; -.
DR BioMuta; STK35; -.
DR DMDM; 292495039; -.
DR EPD; Q8TDR2; -.
DR jPOST; Q8TDR2; -.
DR MassIVE; Q8TDR2; -.
DR MaxQB; Q8TDR2; -.
DR PaxDb; Q8TDR2; -.
DR PeptideAtlas; Q8TDR2; -.
DR PRIDE; Q8TDR2; -.
DR ProteomicsDB; 74332; -.
DR Antibodypedia; 23148; 190 antibodies from 27 providers.
DR DNASU; 140901; -.
DR Ensembl; ENST00000381482.8; ENSP00000370891.3; ENSG00000125834.13.
DR GeneID; 140901; -.
DR KEGG; hsa:140901; -.
DR MANE-Select; ENST00000381482.8; ENSP00000370891.3; NM_080836.4; NP_543026.2.
DR UCSC; uc002wfw.5; human.
DR CTD; 140901; -.
DR DisGeNET; 140901; -.
DR GeneCards; STK35; -.
DR HGNC; HGNC:16254; STK35.
DR HPA; ENSG00000125834; Tissue enriched (retina).
DR MIM; 609370; gene.
DR neXtProt; NX_Q8TDR2; -.
DR OpenTargets; ENSG00000125834; -.
DR PharmGKB; PA38097; -.
DR VEuPathDB; HostDB:ENSG00000125834; -.
DR eggNOG; KOG0595; Eukaryota.
DR GeneTree; ENSGT00940000158197; -.
DR HOGENOM; CLU_026714_1_0_1; -.
DR InParanoid; Q8TDR2; -.
DR OMA; WPGADHP; -.
DR OrthoDB; 813266at2759; -.
DR PhylomeDB; Q8TDR2; -.
DR TreeFam; TF105336; -.
DR PathwayCommons; Q8TDR2; -.
DR SignaLink; Q8TDR2; -.
DR BioGRID-ORCS; 140901; 19 hits in 1113 CRISPR screens.
DR ChiTaRS; STK35; human.
DR GeneWiki; Serine/threonine_kinase_35; -.
DR GeneWiki; STK35L1; -.
DR GenomeRNAi; 140901; -.
DR Pharos; Q8TDR2; Tchem.
DR PRO; PR:Q8TDR2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8TDR2; protein.
DR Bgee; ENSG00000125834; Expressed in secondary oocyte and 187 other tissues.
DR ExpressionAtlas; Q8TDR2; baseline and differential.
DR Genevisible; Q8TDR2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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..534
FT /note="Serine/threonine-protein kinase 35"
FT /id="PRO_0000086717"
FT DOMAIN 202..530
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 32..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 360
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 208..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 231
FT /note="K->M: No autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11973348"
FT CONFLICT 69
FT /note="R -> G (in Ref. 3; BAG37270)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="D -> G (in Ref. 3; BAG37270)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..307
FT /note="YLRLVETSLKGERILGYAEE -> GNGEGRRPQRYTKPGAEKAK (in
FT Ref. 4; AAI11574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 58051 MW; CA1A99D26829C9AF CRC64;
MGHQESPLAR APAGGAAYVK RLCKGLSWRE HVESHGSLGA QASPASAAAA EGSATRRARA
ATSRAARSRR QPGPGADHPQ AGAPGGKRAA RKWRCAGQVT IQGPAPPRPR AGRRDEAGGA
RAAPLLLPPP PAAMETGKDG ARRGTQSPER KRRSPVPRAP STKLRPAAAA RAMDPVAAEA
PGEAFLARRR PEGGGGSARP RYSLLAEIGR GSYGVVYEAV AGRSGARVAV KKIRCDAPEN
VELALAEFWA LTSLKRRHQN VVQFEECVLQ RNGLAQRMSH GNKSSQLYLR LVETSLKGER
ILGYAEEPCY LWFVMEFCEG GDLNQYVLSR RPDPATNKSF MLQLTSAIAF LHKNHIVHRD
LKPDNILITE RSGTPILKVA DFGLSKVCAG LAPRGKEGNQ DNKNVNVNKY WLSSACGSDF
YMAPEVWEGH YTAKADIFAL GIIIWAMIER ITFIDSETKK ELLGTYIKQG TEIVPVGEAL
LENPKMELHI PQKRRTSMSE GIKQLLKDML AANPQDRPDA FELETRMDQV TCAA
