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MK06_PONAB
ID   MK06_PONAB              Reviewed;         721 AA.
AC   Q5R7U1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Mitogen-activated protein kinase 6;
DE            Short=MAP kinase 6;
DE            Short=MAPK 6;
DE            EC=2.7.11.24;
GN   Name=MAPK6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Atypical MAPK protein. Phosphorylates microtubule-associated
CC       protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed
CC       with MAPKAPK5 is still unclear, but the complex follows a complex set
CC       of phosphorylation events: upon interaction with atypical MAPKAPK5,
CC       ERK3/MAPK6 is phosphorylated at Ser-189 and then mediates
CC       phosphorylation and activation of MAPKAPK5, which in turn
CC       phosphorylates ERK3/MAPK6. May promote entry in the cell cycle (By
CC       similarity). {ECO:0000250}.
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=2.7.11.24;
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=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation at Ser-189.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE motif)
CC       MAPKAPK5 (By similarity). Interacts with UBE3A; this interaction may be
CC       indirect and mediated by HERC2, possibly via HERC2 interaction with
CC       NEURL4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Translocates to the cytoplasm following interaction with MAPKAPK5.
CC       {ECO:0000250}.
CC   -!- DOMAIN: In contrast to classical MAPKs, the TXY motif within the
CC       activation loop is replaced by the SEG motif, whose phosphorylation
CC       activates the MAP kinases. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in
CC       catalytic activation. Phosphorylated by MAPKAPK5 at other sites (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitination at Met-1 leads to degradation by the proteasome
CC       pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; CR860018; CAH92169.1; -; mRNA.
DR   RefSeq; NP_001126270.1; NM_001132798.1.
DR   RefSeq; XP_009248112.1; XM_009249837.1.
DR   AlphaFoldDB; Q5R7U1; -.
DR   SMR; Q5R7U1; -.
DR   STRING; 9601.ENSPPYP00000007346; -.
DR   Ensembl; ENSPPYT00000007648; ENSPPYP00000007346; ENSPPYG00000006482.
DR   GeneID; 100173242; -.
DR   KEGG; pon:100173242; -.
DR   CTD; 5597; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   GeneTree; ENSGT00940000154351; -.
DR   InParanoid; Q5R7U1; -.
DR   OrthoDB; 741207at2759; -.
DR   Proteomes; UP000001595; Chromosome 15.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR008350; MAPK_ERK3/4.
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   PRINTS; PR01771; ERK3ERK4MAPK.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..721
FT                   /note="Mitogen-activated protein kinase 6"
FT                   /id="PRO_0000249009"
FT   DOMAIN          20..316
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          701..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           189..191
FT                   /note="SEG motif"
FT   MOTIF           332..337
FT                   /note="FRIEDE motif"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         26..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         189
FT                   /note="Phosphoserine; by PAK1, PAK2 and PAK3"
FT                   /evidence="ECO:0000250|UniProtKB:Q16659"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16659"
FT   MOD_RES         452
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16659"
FT   MOD_RES         556
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16659"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16659"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16659"
FT   MOD_RES         684
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16659"
FT   CROSSLNK        1
FT                   /note="Peptide (Met-Gly) (interchain with G-Cter in
FT                   ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   721 AA;  82678 MW;  CE43B75DADD726DF CRC64;
     MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK IVLTDPQSVK
     HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE LNSVYIVQEY METDLANVLE
     QGPLLEEHAR LFMYQLLRGL KYIHSANVLH RDLKPANLFI NTEDLVLKIG DFGLARIMDP
     HYSHKGHLSE GLVTKWYRSP RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ
     MQLILESIPV VHEEDRQELL SVIPVYIRND MTEPHKPLTQ LLPGISREAL DFLEQILTFS
     PMDRLTAEEA LSHPYMSIYS FPMDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC
     QFSEHDWPVH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTNYS
     TEPCWQYSDH HENKYCDLEC GHTCNYKTRS SSYLDNLVWR ESEVNHYYEP KLIIDLSNWK
     EQSKEKSDKK GKSKCERNGL VKAQIALEEA SQQLAGKERE KNQGFDFDSF IAGTIQLSSQ
     HEPTDVVDKL NDLNSSVSQL ELKSLISKSV SQEKQEKGMA NLAQLEALYQ SSWDSQFVNG
     GEDCFFINQF CEVRKDEQVE KENTYTSYLD KFFSRKEDTE MLETEPVEDG KLGERGHEEG
     FLNNSGEFLF NKQLESIGIP QFHSPVGSPL KSIQATLTPS AMKSSPQIPH QTYSSILKHL
     N
 
 
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