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Database: UniProt
Entry: F7ILP4_CALJA
LinkDB: F7ILP4_CALJA
Original site: F7ILP4_CALJA 
ID   F7ILP4_CALJA            Unreviewed;      1085 AA.
AC   F7ILP4; U3BWL4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=LATS2 {ECO:0000313|EMBL:JAB10877.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000043996.2};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000043996.2, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000043996.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB10877.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB10877.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000043996.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; GAMT01000984; JAB10877.1; -; mRNA.
DR   STRING; 9483.ENSCJAP00000043996; -.
DR   Ensembl; ENSCJAT00000063445.4; ENSCJAP00000043996.2; ENSCJAG00000005013.5.
DR   eggNOG; KOG0608; Eukaryota.
DR   GeneTree; ENSGT00940000159161; -.
DR   HOGENOM; CLU_004885_1_0_1; -.
DR   OMA; FNNHQQP; -.
DR   TreeFam; TF351549; -.
DR   Proteomes; UP000008225; Chromosome 5.
DR   Bgee; ENSCJAG00000005013; Expressed in heart and 6 other cell types or tissues.
DR   GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0035329; P:hippo signaling; IEA:Ensembl.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0001827; P:inner cell mass cell fate commitment; IEA:Ensembl.
DR   GO; GO:0001828; P:inner cell mass cellular morphogenesis; IEA:Ensembl.
DR   GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR   GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd21777; MobB_LATS2; 1.
DR   CDD; cd05626; STKc_LATS2; 1.
DR   CDD; cd14398; UBA_LATS2; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF149; SERINE_THREONINE-PROTEIN KINASE LATS2; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:JAB10877.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          98..139
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          665..970
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          971..1049
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1077
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         694
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1085 AA;  120290 MW;  0EF66CA16C565D6D CRC64;
     MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSAQGLSVG PNSDTSLDTK ILGSKDATRQ
     QQQMRATPKF GPYQKALREI RYSLLPFANE SGTSAAAEVN RQMLQELVNA GCDQEMAGRA
     LKQTGSRSIE AALEYISKMG YLDPRNEQIV RVIKQTSPGK GLMPTPVTRR PSFEGTRDSF
     ASYHQLSGGA PYEGPSFGAD GPAALEEVPR PYVDYLFPGV GPHGPGHQHQ HQHPPKGYGA
     SVEAAGAHFP LQGAHYGRPH LLVPAEPLGY GVQRSPSFQS KTPPETGGYA SLPAKAQGGP
     PGTSLAFPPP TSGIYVTHPH HKQASPAAHQ LHLLGSRSQV FTSDSPPQSL LTPSRNSLNV
     DLYELGSTPV QQWPAATLAR RDSLQKPGLE APPRAHGTFR PDCPVPSRTN SFNSHQPRSG
     APGKAEPSLP ASNTVTAVTA AHILHPVKSV RVLRPEPQTA VGPSHPAWVP APVPAPAPEG
     LDAKEEHALT LGGAGAYPLD MEYGGPDRRC PPPPYPKHLL LRSKSEQYDL DSLCAGVEQS
     LRGGPSEPDG GDKSRKSTKA DKGGKDKKQI QTSPVPVRKN SRDEEKRESR IKSYSPYAFK
     FFMEQHVENV IKTYQQKVNR RLQLEQEMAK AGLCEAEQEQ MRKILYQKES NYNRLKRAKM
     DKSMFVKIKT LGIGAFGEVC LACKVDTHAL YAMKTLRKKD VLNRNQVAHV KAERDILAEA
     DNEWVVKLYY SFQDKDSLYF VMDYIPGGDM MSLLIRMEVF PEHLARFYIA ELTLAIESVH
     KMGFIHRDIK PDNILIDLDG HIKLTDFGLC TGFRWTHNSK YYQKGNHVRQ DSMEPSDLWD
     DVSNCRCGDR LKTLEQRARK QHQRCLAHSL VGTPNYIAPE VLLRKGYTQL CDWWSVGVIL
     FEMLVGQPPF LAPTPTETQL KVINWENTLH IPAQVKLSPE ARDLITKLCC AADHRLGRNG
     ADDLKAHPFF STIDFSSDIR KQPAPYVPTI SHPMDTSNFD PVDEESPWND ASEGSAKAWD
     TLTSPSNKHP EHAFYEFTFR RFFDDNGYPF RCPKPSGAEA SQSENSNLET SDLMDQTEGC
     QPVYV
//
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