M3K13_MOUSE
ID M3K13_MOUSE Reviewed; 959 AA.
AC Q1HKZ5; Q8BKN0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 13;
DE EC=2.7.11.25;
GN Name=Map3k13;
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].
RC STRAIN=C57BL/6J;
RA Itoh A., Itoh T.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 690-959.
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
CC -!- FUNCTION: Activates the JUN N-terminal pathway through activation of
CC the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to
CC regulate the activation of NF-kappa-B in the cytosol. This activation
CC is kinase-dependent and involves activating the IKK complex, the IKBKB-
CC containing complex that phosphorylates inhibitors of NF-kappa-B (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=2.7.11.25;
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=2.7.11.25;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation and
CC homodimerization. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; forms dimers through the leucine-zipper motif.
CC Interacts with the C-terminus of MAPK8IP1 through the kinase catalytic
CC domain. Binds PRDX3. Associates with the IKK complex through the kinase
CC domain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ480427; ABF19581.1; -; mRNA.
DR EMBL; AK051378; BAC34618.1; -; mRNA.
DR CCDS; CCDS37294.1; -.
DR RefSeq; NP_766409.2; NM_172821.3.
DR RefSeq; XP_006522645.1; XM_006522582.3.
DR RefSeq; XP_006522646.1; XM_006522583.3.
DR RefSeq; XP_006522647.1; XM_006522584.3.
DR RefSeq; XP_011244317.1; XM_011246015.2.
DR RefSeq; XP_011244318.1; XM_011246016.2.
DR AlphaFoldDB; Q1HKZ5; -.
DR SMR; Q1HKZ5; -.
DR BioGRID; 214899; 4.
DR STRING; 10090.ENSMUSP00000047388; -.
DR iPTMnet; Q1HKZ5; -.
DR PhosphoSitePlus; Q1HKZ5; -.
DR MaxQB; Q1HKZ5; -.
DR PaxDb; Q1HKZ5; -.
DR PeptideAtlas; Q1HKZ5; -.
DR PRIDE; Q1HKZ5; -.
DR ProteomicsDB; 295747; -.
DR Antibodypedia; 33834; 306 antibodies from 27 providers.
DR DNASU; 71751; -.
DR Ensembl; ENSMUST00000042065; ENSMUSP00000047388; ENSMUSG00000033618.
DR Ensembl; ENSMUST00000231988; ENSMUSP00000156075; ENSMUSG00000033618.
DR Ensembl; ENSMUST00000232240; ENSMUSP00000156202; ENSMUSG00000033618.
DR GeneID; 71751; -.
DR KEGG; mmu:71751; -.
DR UCSC; uc007yrr.2; mouse.
DR CTD; 9175; -.
DR MGI; MGI:2444243; Map3k13.
DR VEuPathDB; HostDB:ENSMUSG00000033618; -.
DR eggNOG; KOG4721; Eukaryota.
DR GeneTree; ENSGT00940000158216; -.
DR HOGENOM; CLU_009311_2_1_1; -.
DR InParanoid; Q1HKZ5; -.
DR OMA; KYPGTCK; -.
DR OrthoDB; 938929at2759; -.
DR PhylomeDB; Q1HKZ5; -.
DR TreeFam; TF105119; -.
DR BioGRID-ORCS; 71751; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Map3k13; mouse.
DR PRO; PR:Q1HKZ5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q1HKZ5; protein.
DR Bgee; ENSMUSG00000033618; Expressed in ureter and 67 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0106137; F:IkappaB kinase complex binding; ISO:MGI.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:ARUK-UCL.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:ARUK-UCL.
DR GO; GO:0007254; P:JNK cascade; IMP:ARUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:ARUK-UCL.
DR GO; GO:1905492; P:positive regulation of branching morphogenesis of a nerve; IMP:ARUK-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:ARUK-UCL.
DR GO; GO:0014042; P:positive regulation of neuron maturation; IMP:ARUK-UCL.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IMP:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:ARUK-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017419; MAP3K12_MAP3K13.
DR InterPro; IPR027258; MAPKKK13.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR PIRSF; PIRSF500742; MAPKKK13; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..959
FT /note="Mitogen-activated protein kinase kinase kinase 13"
FT /id="PRO_0000277591"
FT DOMAIN 167..408
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..453
FT /note="Leucine-zipper 1"
FT REGION 485..506
FT /note="Leucine-zipper 2"
FT REGION 533..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 173..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 959 AA; 106987 MW; 18424BA1695DEDAE CRC64;
MANPQEHLSC SSLPHLPLTE NKTSGGRNEL AAMGNHPSPK LPEDPQERGA IQSELMEITG
SPISTTVLTS VSEDSRGQFE NSVLQLREQD ESEMTLSLGN SNTVDGENTN GPEDIKIQFS
RSGSGSGGFL EGLFGCLRPV WNIIGKAYST DYKLQQQDTW EVPFEEISEL QWLGSGAQGA
VFLGKFRAEE VAIKKVREQN ETDIKHLRKL KHPNIIAFKG VCTQAPCYCI IMEYCAHGQL
YEVLRAGRKI TPRLLVDWST GIASGMNYLH LHKIIHRDLK SPNVLVTHTD AVKISDFGTS
KELSDKSTKM SFAGTVAWMA PEVIRNEPVS EKVDIWSFGV VLWELLTGEI PYKDVDSSAI
IWGVGSNSLH LPVPSTCPDG FKILMKQTWQ SKPRNRPSFR QTLMHLDIAS ADVLATPQET
YFKSQAEWRE EVKKHFEKIK SEGTCIHRLD EELIRRRREE LRHALDIREH YERKLERANN
LYMELSAIML QLEMREKELL KREQAVEKKY PGTYKRHPVR PIIHPNAMEK LMKRKGVPHK
AGVQTKRPDL LRSEGIPSTE AVPTASPLSG SPKMSTASSR SRYRSKPRHR RGNSRGSHSD
FAAILKTQPA QENSPHPTYM HHTQAQCASV HQHNPLQQQY QQIPPAQPQS RHPRLNAHGQ
DIATCANNLR YFGPAAALRS PLSNHAQRQM PGSSPDLIST AMAADWRNSE LDQDQVGPWG
CCQAEPYDPC FQCRPEHSGS LDVPTTEPVG RSPDLSSSPA HNPLSGNAQG SERTGANGFS
GCQSGISHQF TPPMLPQKTR PLQKSGDDSS EEEGEVDSEV EFPRRQRPHR CISSYQSYST
FSSENFSVSD GEEGNTSDHS NSPDESANRR QDRLAETLDD LLSQTPEAPI EISSHSDGLS
DKECAVRRVK TQMSLGKLCA EERGYENPVQ FGDSDCDSSE GECSDATVRT SKNYSSATW
