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Database: UniProt
Entry: A0A2K6MVS3_RHIBE
LinkDB: A0A2K6MVS3_RHIBE
Original site: A0A2K6MVS3_RHIBE 
ID   A0A2K6MVS3_RHIBE        Unreviewed;      1083 AA.
AC   A0A2K6MVS3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
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|Ensembl:ENSRBIP00000039871.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000039871.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000039871.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000039871.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_017714624.1; XM_017859135.1.
DR   RefSeq; XP_017714632.1; XM_017859143.1.
DR   AlphaFoldDB; A0A2K6MVS3; -.
DR   STRING; 61621.ENSRBIP00000039871; -.
DR   Ensembl; ENSRBIT00000063900.1; ENSRBIP00000039871.1; ENSRBIG00000043386.1.
DR   GeneID; 108519857; -.
DR   KEGG; rbb:108519857; -.
DR   CTD; 26524; -.
DR   GeneTree; ENSGT00940000159161; -.
DR   OMA; FNNHQQP; -.
DR   OrthoDB; 5348633at2759; -.
DR   Proteomes; UP000233180; Unplaced.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
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          663..968
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          969..1047
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          23..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         692
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1083 AA;  119808 MW;  D32E927406101058 CRC64;
     MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSAQGLPVG PNSDTSLDAK VLGSKDAARQ
     QQQMRATPKF GPYQKALREI RYSLLPFANE SGTSAAAEVN RQMLQELVNA GCDQEMAGRA
     LKQTGSRSIE AALEYISKMG YLDPRNEQIV RVIKQTSPGR GLMPAPVTRR PSFEGTSDSF
     ASYHQLSGAP YEGPSFGADG PTALEEVPRP YVDYLFPGVG PHGPSHQHQH QHPPKGYGAS
     VEAAGAHFPL QGAHYGRPHL LVHGEPLGYG VQRSPSFQSK TPPETGGYAT KGQGGPPGAG
     LAFPPPTAGL YVPHPHHKQA GPTAHQLHVL GSRSQVFASD SPPQSLLTPS RNSLNVDLYD
     LGSTSVQQWP AATLARRDSL QKPGLEAPPR AHVAFRPDCP VPSRTNSFNS HQPRPGAPGK
     AEPSLPAPNT VTAVTAAHIL HPVKSVRVLR PEPQTAVGPS HPAWVPAPAP APAPATEGLD
     AKEEHALALG GAGAYPLDVE YGGPDRRCPP PPYPRHLLLR SKSEQYDLDS LCAGVEQSLR
     AGPSEPEGGE KSRKSAKGDK GGKDKKQIQT SPVPVRKNSR DEEKRESRIK SYSPYAFKFF
     MEQHVENVIK TYQQKVNRRL QLEQEMAKAG LCEAEQEQMR KILYQKESNY NRLKRAKMDK
     SMFVKIKTLG IGAFGEVCLA CKVDTHALYA MKTLRKKDVL NRNQVAHVKA ERDILAEADN
     EWVVKLYYSF QDKDSLYFVM DYIPGGDMMS LLIRMEVFPE HLARFYIAEL TLAIESVHKM
     GFIHRDIKPD NILIDLDGHI KLTDFGLCTG FRWTHNSKYY QKGSHVRQDS MEPSDLWDDV
     SNCRCGDRLK TLEQRARKQH QRCLAHSLVG TPNYIAPEVL LRKGYTQLCD WWSVGVILFE
     MLVGQPPFLA PTPTETQLKV INWENTLHIP AQVKLSPEAR DLITKLCCSA DHRLGRNGAE
     DLKAHPFFSA MDFSSDIRKQ PAPYVPTISH PMDTSNFDPV DEESPWNDAS EGSAKAWDTL
     TSPSNKHPEH AFYEFTFRRF FDDNGYPFRC PKPSGAEASQ SENADLEASD LVDQTEGCQP
     VYV
//
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