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Database: UniProt
Entry: A0A2I3SNK3_PANTR
LinkDB: A0A2I3SNK3_PANTR
Original site: A0A2I3SNK3_PANTR 
ID   A0A2I3SNK3_PANTR        Unreviewed;      1215 AA.
AC   A0A2I3SNK3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=MAP4K4 {ECO:0000313|Ensembl:ENSPTRP00000078540.1,
GN   ECO:0000313|VGNC:VGNC:299};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000078540.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000078540.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000078540.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   EMBL; AACZ04057778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3SNK3; -.
DR   Ensembl; ENSPTRT00000084097.1; ENSPTRP00000078540.1; ENSPTRG00000012294.5.
DR   VGNC; VGNC:299; MAP4K4.
DR   GeneTree; ENSGT00940000155063; -.
DR   Proteomes; UP000002277; Chromosome 2A.
DR   Bgee; ENSPTRG00000012294; Expressed in fibroblast and 21 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001180; CNH_dom.
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   PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          25..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          902..1189
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          302..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..333
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..701
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1215 AA;  138429 MW;  5C516D8872FCD6F2 CRC64;
     MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
     DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT
     KGNTLKEDWI AYISREILRG LAHLHIHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDLWSCG ITAIEMAEGA PRNSLVTCDL
     NPSQDFKKNS SAPWIKKFFS FIEGCLVKNY MQRPSTEQLL KHPFIRDQPN ERQVRIQLKD
     HIDRTRKKRG EKDETEYEYS GSEEEEEEVP EQEGEPSSIV NVPGESTLRR DFLRLQQENK
     ERSEALRRQQ LLQEQQLREQ EEYKRQLLAE RQKRIEQQKE QRRRLEEQQR REREARRQQE
     REQRRREQEE KRRLEELERR RKEEEERRRA EEEKRRVERE QEYIRRQLEE EQRHLEVLQQ
     QLLQEQAMLL HDHRRPHPQH SQQPPPPQQE RSKPSFHAPE PKAHYEPADR AREVPVRTTS
     RSPVLSRRDS PLQGSGQQNS QAGQRNSTSS IEPRLLWERV EKLVPRPGSG SSSGSSNSGS
     QPGSHPGSQS GSGERFRVRS SSKSEGSPSQ RLENAVKKPE DKKEVFRPLK PADLTALAKE
     LRAVEDVRPP HKVTDYSSSS EESGTTDEED DDVEQEGADE STSGPEDTRA ASSLNLSNGE
     TESVKTMIVH DDVESEPAMT PSKEGTLIVR QSTVDQKRAS HHESNGFAGR IHLLPDLLQQ
     SHSSSTSSTS SSPSSSQPTP TMSPQTPQDK LTANETQSAS STLQKHKSSS SFTPFIDPRL
     LQISPSSGTT VTSVVGFSCD GMRPEAIRQD PTRKGSVVNV NPTNTRPQSD TPEIRKYKKR
     FNSEILCAAL WGVNLLVGTE SGLMLLDRSG QGKVYPLINR RRFQQMDVLE GLNVLVTISG
     KKDKLRVYYL SWLRNKILHN DPEVEKKQGW TTVGDLEGCV HYKVVKYERI KFLVIALKSS
     VEVYAWAPKP YHKFMAFKSF GELVHKPLLV DLTVEEGQRL KVIYGSCAGF HAVDVDSGSV
     YDIYLPTHIQ CSIKPHAIII LPNTDGMELL VCYEDEGVYV NTYGRITKDV VLQWGEMPTS
     VAYIRSNQTM GWGEKAIEIR SVETGHLDGV FMHKRAQRLK FLCERNDKVF FASVRSGGSS
     QVYFMTLGRT SLLSW
//
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