M3K7_RAT
ID M3K7_RAT Reviewed; 606 AA.
AC P0C8E4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 7;
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:O43318};
GN Name=Map3k7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-331.
RC TISSUE=Hypothalamus, and Prostate;
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-606.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Serine/threonine kinase which acts as an essential component
CC of the MAP kinase signal transduction pathway. Plays an important role
CC in the cascades of cellular responses evoked by changes in the
CC environment. Mediates signal transduction of TRAF6, various cytokines
CC including interleukin-1 (IL-1), transforming growth factor-beta (TGFB),
CC TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR),
CC tumor necrosis factor receptor CD40 and B-cell receptor (BCR).
CC Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts
CC as an upstream activator of the MKK/JNK signal transduction cascade and
CC the p38 MAPK signal transduction cascade through the phosphorylation
CC and activation of several MAP kinase kinases like MAP2K1/MEK1,
CC MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate
CC p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex
CC (IKK). Both p38 MAPK and JNK pathways control the transcription factors
CC activator protein-1 (AP-1), while nuclear factor-kappa B is activated
CC by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6
CC signaling and mediates BMP2-induced apoptosis. In osmotic stress
CC signaling, plays a major role in the activation of MAPK8/JNK1, but not
CC that of NF-kappa-B (By similarity). Promotes TRIM5 capsid-specific
CC restriction activity (By similarity). Phosphorylates RIPK1 at 'Ser-321'
CC which positively regulates RIPK1 interaction with RIPK3 to promote
CC necroptosis but negatively regulates RIPK1 kinase activity and its
CC interaction with FADD to mediate apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:O43318, ECO:0000250|UniProtKB:Q62073}.
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 Evidence={ECO:0000250|UniProtKB:O43318};
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; Evidence={ECO:0000250|UniProtKB:O43318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by pro-inflammatory cytokines and in
CC response to physical and chemical stresses, including osmotic stress,
CC oxidative stress, arsenic and ultraviolet light irradiation. Activated
CC by 'Lys-63'-linked polyubiquitination and by autophosphorylation.
CC Association with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 promotes activation
CC through autophosphorylation, whereas PPM1B/PP2CB, PP2A and PPP6C
CC dephosphorylation leads to inactivation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form homodimer. Binds both upstream activators and
CC downstream substrates in multimolecular complexes. Interacts with
CC TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3. Identified in the
CC TRIKA2 complex composed of MAP3K7/TAK1, TAB1/MAP3K7IP1 and
CC TAB2/MAP3K7IP2. Interacts with PPM1L and PPM1B/PP2CB. Interaction with
CC PP2A and PPP6C leads to its repressed activity. Interacts with TRAF6
CC and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with TAOK1 and
CC TAOK2; interaction with TAOK2 interferes with MAP3K7 interaction with
CC IKKA, thus preventing NF-kappa-B activation. Interacts with DYNC2I2
CC (via WD domains). Interacts with CYLD and RBCK1. Interacts with TGFBR1;
CC induces MAP3K7/TAK1 activation by TRAF6. Interacts with MAPK8IP1 and
CC SMAD6. Interacts with isoform 1 of VRK2. Interacts with DAB2; the
CC interaction is induced by TGF-beta stimulation and may mediate TGF-beta
CC stimulated JNK activation. Interacts with TRIM5. Part of a complex
CC containing ITCH, NDFIP1 and MAP3K7. Interacts with PLEKHM1 (via N- and
CC C-terminus). Found in a complex with SH3RF1, RAC2, MAP2K7/MKK7,
CC MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2. Interacts with SASH1 (By
CC similarity). Interacts with RIPK1 (By similarity).
CC {ECO:0000250|UniProtKB:O43318, ECO:0000250|UniProtKB:Q62073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Although the majority of MAP3K7/TAK1 is found
CC in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2,
CC it is also localized at the cell membrane. {ECO:0000250}.
CC -!- PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation at
CC Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2,
CC itself associated with free unanchored Lys-63 polyubiquitin chain,
CC promotes autophosphorylation and subsequent activation of MAP3K7.
CC Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and
CC PPP6C leads to inactivation (By similarity). {ECO:0000250}.
CC -!- PTM: 'Lys-48'-linked polyubiquitination at Lys-72 is induced by
CC TNFalpha, and leads to proteasomal degradation. Undergoes 'Lys-48'-
CC linked polyubiquitination catalyzed by ITCH. 'Lys-63'-linked
CC polyubiquitination at Lys-158 by TRIM8 does not lead to proteasomal
CC degradation but contributes to autophosphorylation and activation.
CC Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-
CC linked ubiquitin chains. {ECO:0000250|UniProtKB:O43318,
CC ECO:0000250|UniProtKB:Q62073}.
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; AABR03040223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CB583299; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB771642; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CK481792; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DN936104; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001101390.2; NM_001107920.2.
DR RefSeq; XP_003750801.1; XM_003750753.4.
DR AlphaFoldDB; P0C8E4; -.
DR SMR; P0C8E4; -.
DR BioGRID; 260325; 2.
DR IntAct; P0C8E4; 1.
DR STRING; 10116.ENSRNOP00000007654; -.
DR iPTMnet; P0C8E4; -.
DR PhosphoSitePlus; P0C8E4; -.
DR jPOST; P0C8E4; -.
DR PaxDb; P0C8E4; -.
DR PRIDE; P0C8E4; -.
DR Ensembl; ENSRNOT00000007654; ENSRNOP00000007654; ENSRNOG00000005724.
DR GeneID; 313121; -.
DR KEGG; rno:313121; -.
DR UCSC; RGD:1309438; rat.
DR CTD; 6885; -.
DR RGD; 1309438; Map3k7.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000157785; -.
DR HOGENOM; CLU_000288_7_41_1; -.
DR InParanoid; P0C8E4; -.
DR OMA; PARTQCF; -.
DR OrthoDB; 635654at2759; -.
DR PhylomeDB; P0C8E4; -.
DR TreeFam; TF105116; -.
DR Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-RNO-202424; Downstream TCR signaling.
DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-RNO-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR Reactome; R-RNO-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-RNO-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-RNO-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR PRO; PR:P0C8E4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000005724; Expressed in ovary and 19 other tissues.
DR Genevisible; P0C8E4; RN.
DR GO; GO:0140672; C:ATAC complex; ISO:RGD.
DR GO; GO:0008385; C:IkappaB kinase complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004707; F:MAP kinase activity; ISO:RGD.
DR GO; GO:0004708; F:MAP kinase kinase activity; ISO:RGD.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:RGD.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; ISO:RGD.
DR GO; GO:0019211; F:phosphatase activator activity; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0043276; P:anoikis; ISO:RGD.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0007252; P:I-kappaB phosphorylation; ISS:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IDA:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0060546; P:negative regulation of necroptotic process; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:1902443; P:negative regulation of ripoptosome assembly involved in necroptotic process; ISO:RGD.
DR GO; GO:0001841; P:neural tube formation; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:RGD.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
DR GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017421; MAPKKK7.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46716; PTHR46716; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF038168; MAPKKK7; 1.
DR PRINTS; PR00109; TYRKINASE.
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;
KW Apoptosis; ATP-binding; Cell membrane; Cytoplasm; Isopeptide bond; Kinase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT CHAIN 1..606
FT /note="Mitogen-activated protein kinase kinase kinase 7"
FT /id="PRO_0000353138"
FT DOMAIN 36..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..300
FT /note="Interaction with MAPK8IP1"
FT /evidence="ECO:0000250"
FT REGION 301..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 184
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O43318"
FT MOD_RES 187
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O43318"
FT MOD_RES 192
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O43318"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43318"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43318"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O43318"
FT CROSSLNK 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q62073"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q62073"
SQ SEQUENCE 606 AA; 67200 MW; E24987277A616DCD CRC64;
MSTASAASSS SSSSASEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV
AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE
PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC
DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM
WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY
PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ
SDSGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIV ATTAYTKPKR GHRKTASFGN
ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP GQVSSRSSSP SVRMITTSGP TSEKPARSLP
WTPDDSTDTN GSDNSIPMAY LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI
ALLLQRKQEL VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ
KRQGTS
