GenomeNet

Database: UniProt
Entry: G3HP37_CRIGR
LinkDB: G3HP37_CRIGR
Original site: G3HP37_CRIGR 
ID   G3HP37_CRIGR            Unreviewed;      1008 AA.
AC   G3HP37;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=I79_012541 {ECO:0000313|EMBL:EGV99811.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV99811.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH000564; EGV99811.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3HP37; -.
DR   STRING; 10029.G3HP37; -.
DR   PaxDb; 10029-XP_007617150-1; -.
DR   eggNOG; KOG0584; Eukaryota.
DR   InParanoid; G3HP37; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14032; STKc_WNK2_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR   PANTHER; PTHR13902:SF10; SERINE_THREONINE-PROTEIN KINASE WNK2; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGV99811.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          196..454
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          924..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1008 AA;  108501 MW;  D4B903791636D060 CRC64;
     MDHDGGRRDA PGALMEAGRG AGSAGMAEPR ARAARLGPQR FLRRSVVESD QEEPPGLEAA
     ETPSSQPPQP LQRRVLLLCK TRRLIAERAR GRPAAPAPAA PAAPSDSPGA PSDPGPERAG
     TQEPSPDPTT ASAAAEPVPD GGPRQEEEAP APTREIAGAT EAKPEPGRAR KDEPEVEEDD
     EDDLKAVATS LDGRFLKFDI ELGRGSFKTV YKGLDTETWV EVAWCELQDR KLTKLERQRF
     KEEAEMLKGL QHPNIVRFYD FWESSAKGKR CIVLVTELMT SGTLKTYLKR FKVMKPKVLR
     SWCRQILKGL LFLHTRTPPI IHRDLKCDNI FITGPTGSVK IGDLGLATLK RASFAKSVIG
     TPEFMAPEMY EEHYDESVDV YAFGMCMLEM ATSEYPYSEC QNAAQIYRKV TCGIKPASFE
     KVHDPEIKEI IGECICKNKE ERYEIKDLLS HAFFAEDTGV RVELAEEDHG RKSTIALRLW
     VEDPKKLKGK PKDNGAIEFT FDLEKETPDE VAQEMIDSGF FHESDVKIVA KSIRDRVALI
     QWRRERIWPA LQSQEPKDSG SPDKAKGLPA PLQVQVTYHA QSGQPGLPEA EEPEADQHLL
     PPTLPASVTS LASDSTFDSG QGSTVYSDSQ SSQQSMVLSS LVDTTPTPAS CVCSPPVSEG
     PGLTHTLPAL GAFQQPAAVP GLSVGPVPPP ARPALIQQHF PEPSMSFTPV LPPPSTPVPT
     GPSQPAPPVQ QVLAPQPVGT VQPVGTVQPV PSHLPPYLPP TSQVVAPAQL KPLQMPQTPL
     QPLAQVPPQM PQMPVVPPIT PLAGLDGLPQ TLTDLPAANV APVPPPQYFS PAVILPSLTT
     PLPTSPALPL QAVKLPHPPG APLTVPCQTI VPNAPAAIPL LAVAPQGVAA LSIHPAVAQI
     PAQLPAQLPA QPVYPAAFPQ LAPGDIPPSP HHTVQSLRAT PPQLASPVPP QPVQPSVVHL
     PEQAAPVAAS GTQVIHLWEW TYYSLPGDPQ GQFQETLELF PSEGHGSC
//
DBGET integrated database retrieval system