(data stored in ACNUC8465 zone)

SWISSPROT: MP2K4_MOUSE

ID   MP2K4_MOUSE             Reviewed;         397 AA.
AC   P47809;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   11-DEC-2019, entry version 166.
DE   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 4;
DE            Short=MAP kinase kinase 4;
DE            Short=MAPKK 4;
DE            EC=2.7.12.2;
DE   AltName: Full=C-JUN N-terminal kinase kinase 1;
DE            Short=JNK kinase 1;
DE            Short=JNKK 1;
DE   AltName: Full=JNK-activating kinase 1;
DE   AltName: Full=MAPK/ERK kinase 4;
DE            Short=MEK 4;
DE   AltName: Full=SAPK/ERK kinase 1;
DE            Short=SEK1;
GN   Name=Map2k4; Synonyms=Jnkk1, Mek4, Mkk4, Prkmk4, Sek1, Serk1, Skk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LYS-129.
RC   TISSUE=Embryo;
RX   PubMed=7997269; DOI=10.1038/372794a0;
RA   Sanchez I., Hughes R.T., Mayer B.J., Yee K., Woodgett J.R., Avruch J.,
RA   Kyriakis J.M., Zon L.I.;
RT   "Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating
RT   transcription factor c-Jun.";
RL   Nature 372:794-798(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Zon L.I.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=9620683; DOI=10.1016/s1074-7613(00)80567-1;
RA   Swat W., Fujikawa K., Ganiatsas S., Yang D., Xavier R.J., Harris N.L.,
RA   Davidson L., Ferrini R., Davis R.J., Labow M.A., Flavell R.A., Zon L.I.,
RA   Alt F.W.;
RT   "SEK1/MKK4 is required for maintenance of a normal peripheral lymphoid
RT   compartment but not for lymphocyte development.";
RL   Immunity 8:625-634(1998).
RN   [4]
RP   ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND FUNCTION OF THE MKK/JNK
RP   PATHWAY.
RX   PubMed=9891090; DOI=10.1128/mcb.19.2.1569;
RA   Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
RT   "The MKK7 gene encodes a group of c-Jun NH2-terminal kinase kinases.";
RL   Mol. Cell. Biol. 19:1569-1581(1999).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=10095085; DOI=10.1016/s0169-328x(99)00035-2;
RA   Lee J.K., Hwang W.S., Lee Y.D., Han P.L.;
RT   "Dynamic expression of SEK1 suggests multiple roles of the gene during
RT   embryogenesis and in adult brain of mice.";
RL   Brain Res. Mol. Brain Res. 66:133-140(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=11390361; DOI=10.1101/gad.888501;
RA   Tournier C., Dong C., Turner T.K., Jones S.N., Flavell R.A., Davis R.J.;
RT   "MKK7 is an essential component of the JNK signal transduction pathway
RT   activated by proinflammatory cytokines.";
RL   Genes Dev. 15:1419-1426(2001).
RN   [7]
RP   PHOSPHORYLATION, AND INTERACTION WITH MAP3K1/MEKK1.
RX   PubMed=12401521; DOI=10.1016/s0898-6568(02)00056-6;
RA   Tu Z., Mooney S.M., Lee F.S.;
RT   "A subdomain of MEKK1 that is critical for binding to MKK4.";
RL   Cell. Signal. 15:65-77(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=12624093; DOI=10.1074/jbc.m213182200;
RA   Kishimoto H., Nakagawa K., Watanabe T., Kitagawa D., Momose H., Seo J.,
RA   Nishitai G., Shimizu N., Ohata S., Tanemura S., Asaka S., Goto T.,
RA   Fukushi H., Yoshida H., Suzuki A., Sasaki T., Wada T., Penninger J.M.,
RA   Nishina H., Katada T.;
RT   "Different properties of SEK1 and MKK7 in dual phosphorylation of stress-
RT   induced activated protein kinase SAPK/JNK in embryonic stem cells.";
RL   J. Biol. Chem. 278:16595-16601(2003).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17875933; DOI=10.1128/mcb.00226-07;
RA   Wang X., Nadarajah B., Robinson A.C., McColl B.W., Jin J.W.,
RA   Dajas-Bailador F., Boot-Handford R.P., Tournier C.;
RT   "Targeted deletion of the mitogen-activated protein kinase kinase 4 gene in
RT   the nervous system causes severe brain developmental defects and premature
RT   death.";
RL   Mol. Cell. Biol. 27:7935-7946(2007).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19265040; DOI=10.1161/circresaha.108.188292;
RA   Liu W., Zi M., Jin J., Prehar S., Oceandy D., Kimura T.E., Lei M.,
RA   Neyses L., Weston A.H., Cartwright E.J., Wang X.;
RT   "Cardiac-specific deletion of mkk4 reveals its role in pathological
RT   hypertrophic remodeling but not in physiological cardiac growth.";
RL   Circ. Res. 104:905-914(2009).
RN   [11]
RP   REVIEW ON ACTIVITY REGULATION.
RX   PubMed=17496909; DOI=10.1038/sj.onc.1210392;
RA   Raman M., Chen W., Cobb M.H.;
RT   "Differential regulation and properties of MAPKs.";
RL   Oncogene 26:3100-3112(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-255 AND THR-259, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [13]
RP   REVIEW ON FUNCTION.
RX   PubMed=20801953; DOI=10.1093/jb/mvq098;
RA   Asaoka Y., Nishina H.;
RT   "Diverse physiological functions of MKK4 and MKK7 during early
RT   embryogenesis.";
RL   J. Biochem. 148:393-401(2010).
RN   [14]
RP   REVIEW ON REGULATION, AND REVIEW ON FUNCTION.
RX   PubMed=21333379; DOI=10.1016/j.ejcb.2010.11.008;
RA   Haeusgen W., Herdegen T., Waetzig V.;
RT   "The bottleneck of JNK signaling: molecular and functional characteristics
RT   of MKK4 and MKK7.";
RL   Eur. J. Cell Biol. 90:536-544(2011).
RN   [15]
RP   INTERACTION WITH SPAG9.
RX   PubMed=12391307; DOI=10.1073/pnas.232310199;
RA   Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT   "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and
RT   transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN   [16]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-56, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Dual specificity protein kinase which acts as an essential
CC       component of the MAP kinase signal transduction pathway. Essential
CC       component of the stress-activated protein kinase/c-Jun N-terminal
CC       kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the
CC       only known kinase to directly activate the stress-activated protein
CC       kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3.
CC       MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation,
CC       but they differ in their preference for the phosphorylation site in the
CC       Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the
CC       Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of
CC       the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK
CC       activation at least in response to proinflammatory cytokines, while
CC       other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which
CC       synergistically phosphorylate JNKs. MAP2K4 is required for maintaining
CC       peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also
CC       involved in mitochondrial death signaling pathway, including the
CC       release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7
CC       exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38
CC       MAPKs MAPK11, MAPK12, MAPK13 and MAPK14. {ECO:0000269|PubMed:11390361,
CC       ECO:0000269|PubMed:12624093, ECO:0000269|PubMed:7997269,
CC       ECO:0000269|PubMed:9620683, ECO:0000269|PubMed:9891090}.
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=2.7.12.2;
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=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- ACTIVITY REGULATION: Activated in response to a variety of cellular
CC       stresses, including UV and gamma-irradiation, heat shock,
CC       hyperosmolarity, T-cell receptor stimulation, peroxide and inflammatory
CC       cytokines. Also activated by developmental cues. MAP2K4/MKK4 is
CC       activated by the majority of MKKKs, such as MAP3K5/ASK1, MAP3K1/MEKK1,
CC       MAP3K7/TAK1, MAP3K10/MLK2, MAP3K11/MLK3, MAP3K12/DLK and MAP3K13/LZK.
CC       {ECO:0000269|PubMed:9891090}.
CC   -!- SUBUNIT: Interacts with SPAG9. Interacts (via its D domain) with its
CC       substrates MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAPK11 and MAPK14 (By
CC       similarity). Interacts (via its DVD domain) with MAP3Ks activators like
CC       MAP3K1/MEKK1 and MAP3K11/MLK3. Interacts with ARRB1, ARRB2 and
CC       MAPK8IP3/JIP3 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P53349:Map3k1; NbExp=2; IntAct=EBI-447934, EBI-447913;
CC       Q9ESN9-2:Mapk8ip3; NbExp=3; IntAct=EBI-447934, EBI-9549291;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9891090}. Nucleus
CC       {ECO:0000269|PubMed:9891090}.
CC   -!- TISSUE SPECIFICITY: Strong expression is detected in most of the
CC       central nervous system and in liver and thymus during early stages of
CC       development. While expression in nervous system increases over time,
CC       expression in fetal liver and thymus gradually decreases as
CC       embryogenesis proceeds. High level of expression in the central nervous
CC       system persists throughout postnatal development and remained at a
CC       stable level in adult brain. {ECO:0000269|PubMed:10095085}.
CC   -!- DOMAIN: The DVD domain (residues 362-385) contains a conserved docking
CC       site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD
CC       sites bind to their specific upstream MAP kinase kinase kinases
CC       (MAP3Ks) and are essential for activation (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The D domain (residues 35-50) contains a conserved docking site
CC       and is required for the binding to MAPk substrates.
CC   -!- PTM: Activated by phosphorylation on Ser-255 and Thr-259 by MAP kinase
CC       kinase kinases (MAP3Ks). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Causes irregular alignment of Purkinje cells in
CC       the cerebellum and delayed radial migration in the cortex during brain
CC       development. The cardiac-specific deletion prevents pathological
CC       cardiac hypertrophy. {ECO:0000269|PubMed:17875933,
CC       ECO:0000269|PubMed:19265040}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
DR   EMBL; U18310; AAB81554.1; -; mRNA.
DR   CCDS; CCDS24844.1; -.
DR   PIR; S52423; S52423.
DR   RefSeq; NP_033183.1; NM_009157.5.
DR   SMR; P47809; -.
DR   BioGrid; 204952; 8.
DR   CORUM; P47809; -.
DR   DIP; DIP-869N; -.
DR   IntAct; P47809; 5.
DR   MINT; P47809; -.
DR   STRING; 10090.ENSMUSP00000041282; -.
DR   ChEMBL; CHEMBL2201; -.
DR   iPTMnet; P47809; -.
DR   PhosphoSitePlus; P47809; -.
DR   EPD; P47809; -.
DR   jPOST; P47809; -.
DR   PaxDb; P47809; -.
DR   PeptideAtlas; P47809; -.
DR   PRIDE; P47809; -.
DR   DNASU; 26398; -.
DR   Ensembl; ENSMUST00000046963; ENSMUSP00000041282; ENSMUSG00000033352.
DR   GeneID; 26398; -.
DR   KEGG; mmu:26398; -.
DR   UCSC; uc007jlb.1; mouse.
DR   CTD; 6416; -.
DR   MGI; MGI:1346869; Map2k4.
DR   eggNOG; KOG0984; Eukaryota.
DR   eggNOG; ENOG410XT3F; LUCA.
DR   GeneTree; ENSGT00940000154744; -.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; P47809; -.
DR   KO; K04430; -.
DR   OMA; MKSNDCN; -.
DR   OrthoDB; 688282at2759; -.
DR   PhylomeDB; P47809; -.
DR   TreeFam; TF350701; -.
DR   BRENDA; 2.7.12.2; 3474.
DR   Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   ChiTaRS; Map2k4; mouse.
DR   PRO; PR:P47809; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P47809; protein.
DR   Bgee; ENSMUSG00000033352; Expressed in 312 organ(s), highest expression level in secondary oocyte.
DR   ExpressionAtlas; P47809; baseline and differential.
DR   Genevisible; P47809; MM.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0008545; F:JUN kinase kinase activity; ISO:MGI.
DR   GO; GO:0004708; F:MAP kinase kinase activity; ISO:MGI.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007257; P:activation of JUN kinase activity; ISO:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; IBA:GO_Central.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0072709; P:cellular response to sorbitol; IEA:Ensembl.
DR   GO; GO:0007254; P:JNK cascade; ISO:MGI.
DR   GO; GO:0000165; P:MAPK cascade; IPI:MGI.
DR   GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR   GO; GO:0009611; P:response to wounding; IMP:MGI.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
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   Pfam; PF00069; Pkinase; 1.
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   1: Evidence at protein level;
DR   PRODOM; P47809.
DR   SWISS-2DPAGE; P47809.
KW   Acetylation; Apoptosis; ATP-binding; Cytoplasm; Kinase; Methylation;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Stress response; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P45985"
FT   CHAIN           2..397
FT                   /note="Dual specificity mitogen-activated protein kinase
FT                   kinase 4"
FT                   /id="PRO_0000086382"
FT   DOMAIN          100..366
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         106..114
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          35..50
FT                   /note="D domain"
FT                   /evidence="ECO:0000250"
FT   REGION          362..385
FT                   /note="DVD domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        5..17
FT                   /note="Gly/Ser-rich"
FT   ACT_SITE        227
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         129
FT                   /note="ATP"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P45985"
FT   MOD_RES         56
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         56
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P45985"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MOD_RES         259
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MUTAGEN         129
FT                   /note="K->R: Loss of ATP-binding."
FT                   /evidence="ECO:0000269|PubMed:7997269"
SQ   SEQUENCE   397 AA;  44114 MW;  B99C6688184E5B3D CRC64;
     MAAPSPSGGG GSGGGGGTPG PIGPPASGHP AVSSMQGKRK ALKLNFANPP VKSTARFTLN
     PNTTGVQNPH IERLRTHSIE SSGKLKISPE QHWDFTAEDL KDLGEIGRGA YGSVNKMVHK
     PSGQIMAVKR IRSTVDEKEQ KQLLMDLDVV MRSSDCPYIV QFYGALFREG DCWICMELMS
     TSFDKFYKYV YSVLDDVIPE EILGKITLAT VKALNHLKEN LKIIHRDIKP SNILLDRSGN
     IKLCDFGISG QLVDSIAKTR DAGCRPYMAP ERIDPSASRQ GYDVRSDVWS LGITLYELAT
     GRFPYPKWNS VFDQLTQVVK GDPPQLSNSE EREFSPSFIN FVNLCLTKDE SKRPKYKELL
     KHPFILMYEE RTVEVACYVC KILDQMPATP SSPMYVD
//

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