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Database: UniProt/SWISS-PROT
Entry: MK06_PONAB
LinkDB: MK06_PONAB
Original site: 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   23-MAY-2018, entry version 81.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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-
CC       associated protein 2 (MAP2) and MAPKAPK5. The precise role of the
CC       complex formed with MAPKAPK5 is still unclear, but the complex
CC       follows a complex set of phosphorylation events: upon interaction
CC       with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189
CC       and then mediates phosphorylation and activation of MAPKAPK5,
CC       which in turn phosphorylates ERK3/MAPK6. May promote entry in the
CC       cell cycle (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ENZYME REGULATION: Activated by phosphorylation at Ser-189.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE
CC       motif) MAPKAPK5 (By similarity). Interacts with UBE3A; this
CC       interaction may be indirect and mediated by HERC2, possibly via
CC       HERC2 interaction with NEURL4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Translocates to the cytoplasm following
CC       interaction with MAPKAPK5. {ECO:0000250}.
CC   -!- DOMAIN: In contrast to classical MAPKs, the TXY motif within the
CC       activation loop is replaced by the SEG motif, whose
CC       phosphorylation 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
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitination at Met-1 leads to degradation by the
CC       proteasome pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC       {ECO:0000305}.
DR   EMBL; CR860018; CAH92169.1; -; mRNA.
DR   RefSeq; NP_001126270.1; NM_001132798.1.
DR   RefSeq; XP_009248112.1; XM_009249837.1.
DR   ProteinModelPortal; Q5R7U1; -.
DR   SMR; Q5R7U1; -.
DR   PRIDE; Q5R7U1; -.
DR   GeneID; 100173242; -.
DR   KEGG; pon:100173242; -.
DR   CTD; 5597; -.
DR   HOVERGEN; HBG104376; -.
DR   InParanoid; Q5R7U1; -.
DR   KO; K06855; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT   CHAIN         1    721       Mitogen-activated protein kinase 6.
FT                                /FTId=PRO_0000249009.
FT   DOMAIN       20    316       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      26     34       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOTIF       189    191       SEG motif.
FT   MOTIF       332    337       FRIEDE motif.
FT   ACT_SITE    152    152       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      49     49       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     189    189       Phosphoserine; by PAK1, PAK2 and PAK3.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     386    386       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     452    452       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     556    556       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     558    558       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     665    665       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   MOD_RES     684    684       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q16659}.
FT   CROSSLNK      1      1       Peptide (Met-Gly) (interchain with G-Cter
FT                                in ubiquitin). {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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