RIPK2_MOUSE
ID RIPK2_MOUSE Reviewed; 539 AA.
AC P58801;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Receptor-interacting serine/threonine-protein kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=Tyrosine-protein kinase RIPK2;
DE EC=2.7.10.2;
GN Name=Ripk2;
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;
RX PubMed=11894097; DOI=10.1038/416190a;
RA Chin A.I., Dempsey P.W., Bruhn K., Miller J.F., Xu Y., Cheng G.;
RT "Involvement of receptor-interacting protein 2 in innate and adaptive
RT immune responses.";
RL Nature 416:190-194(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
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 [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17277144; DOI=10.4049/jimmunol.178.4.2380;
RA Park J.H., Kim Y.G., McDonald C., Kanneganti T.D., Hasegawa M.,
RA Body-Malapel M., Inohara N., Nunez G.;
RT "RICK/RIP2 mediates innate immune responses induced through Nod1 and Nod2
RT but not TLRs.";
RL J. Immunol. 178:2380-2386(2007).
RN [4]
RP INTERACTION WITH CARD9.
RX PubMed=17187069; DOI=10.1038/ni1426;
RA Hsu Y.M., Zhang Y., You Y., Wang D., Li H., Duramad O., Qin X.F., Dong C.,
RA Lin X.;
RT "The adaptor protein CARD9 is required for innate immune responses to
RT intracellular pathogens.";
RL Nat. Immunol. 8:198-205(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21469090; DOI=10.1002/eji.201040827;
RA Magalhaes J.G., Lee J., Geddes K., Rubino S., Philpott D.J., Girardin S.E.;
RT "Essential role of Rip2 in the modulation of innate and adaptive immunity
RT triggered by Nod1 and Nod2 ligands.";
RL Eur. J. Immunol. 41:1445-1455(2011).
RN [7]
RP FUNCTION.
RX PubMed=26646181; DOI=10.7554/elife.11692;
RA Lin Z., Tann J.Y., Goh E.T., Kelly C., Lim K.B., Gao J.F., Ibanez C.F.;
RT "Structural basis of death domain signaling in the p75 neurotrophin
RT receptor.";
RL Elife 4:e11692-e11692(2015).
RN [8]
RP FUNCTION, AND DEUBIQUITINATION BY MYSM1.
RX PubMed=30405132; DOI=10.1038/s41467-018-07016-0;
RA Panda S., Gekara N.O.;
RT "The deubiquitinase MYSM1 dampens NOD2-mediated inflammation and tissue
RT damage by inactivating the RIP2 complex.";
RL Nat. Commun. 9:4654-4654(2018).
CC -!- FUNCTION: Serine/threonine/tyrosine kinase that plays an essential role
CC in modulation of innate and adaptive immune responses. Upon stimulation
CC by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize
CC and recruit RIPK2 through CARD-CARD domains. Once recruited,
CC autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by
CC E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated
CC protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and
CC induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent
CC activation of IKBKB/IKKB. In turn, NF-kappa-B is release from NF-kappa-
CC B inhibitors and translocates into the nucleus where it activates the
CC transcription of hundreds of genes involved in immune response, growth
CC control, or protection against apoptosis. Also plays a role during
CC engagement of the T-cell receptor (TCR) in promoting BCL10
CC phosphorylation and subsequent NF-kappa-B activation. Plays a role in
CC the inactivation of RHOA in response to NGFR signaling
CC (PubMed:26646181). {ECO:0000250|UniProtKB:O43353,
CC ECO:0000269|PubMed:17277144, ECO:0000269|PubMed:21469090,
CC ECO:0000269|PubMed:26646181, ECO:0000269|PubMed:30405132}.
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=2.7.11.1;
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=2.7.11.1;
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=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- SUBUNIT: Found in a signaling complex consisting of at least ARHGEF2,
CC NOD2 and RIPK2. Interacts with ARHGEF2; the interaction mediates
CC tyrosine phosphorylation of RIPK2 by Src kinase CSK. Binds to
CC CFLAR/CLARP and CASP1 via their CARD domains. Binds to BIRC3/c-IAP1 and
CC BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6. May be a component of both
CC the TNFRSF1A and TNRFSF5/CD40 receptor complex. Interacts with NOD1.
CC Interacts (via CARD domain) with NOD2 (via CARD domain). Interacts with
CC MAP3K4; this interaction sequesters RIPK2 from the NOD2 signaling
CC pathway. Interacts with IKBKG/NEMO. The polyubiquitinated protein
CC interacts with MAP3K7/TAK1. Interacts with XIAP/BIRC4. Interacts with
CC NLRP10 (By similarity). Interacts with CARD9 (PubMed:17187069).
CC Interacts with INAVA; the interaction takes place upon PRR stimulation.
CC Interacts (via CARD domain) with NGFR (via death domain) (By
CC similarity). {ECO:0000250|UniProtKB:O43353,
CC ECO:0000269|PubMed:17187069}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: Contains an N-terminal kinase domain and a C-terminal caspase
CC activation and recruitment domain (CARD) that mediates the recruitment
CC of CARD-containing proteins. {ECO:0000250|UniProtKB:P51617}.
CC -!- PTM: Autophosphorylated. Autophosphorylation at Tyr-473 is necessary
CC for effective NOD2 signaling. {ECO:0000250|UniProtKB:P51617}.
CC -!- PTM: Ubiquitinated on Lys-209; undergoes 'Lys-63'-linked
CC polyubiquitination catalyzed by ITCH. Polyubiquitinated with 'Lys-48'
CC and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to
CC activation of NF-kappa-B. Also undergoes 'Met-1'-linked
CC polyubiquitination; the head-to-tail linear polyubiquitination is
CC mediated by the LUBAC complex in response to NOD2 stimulation. Linear
CC polyubiquitination is restricted by FAM105B/otulin, probably to limit
CC NOD2-dependent pro-inflammatory signaling activation of NF-kappa-B (By
CC similarity). Undergoes 'Lys-63'-linked deubiquitination by MYSM1 to
CC attenuate NOD2-mediated inflammation and tissue damage
CC (PubMed:30405132). Ubiquitination at Lys-502 by ZNRF4 via 'Lys-48'-
CC linked polyubiquitination promotes RIPK2 degradation by the proteasome;
CC ubiquitination by ZNRF4 takes place during both acute and NOD2
CC tolerance conditions (By similarity). {ECO:0000250|UniProtKB:O43353,
CC ECO:0000269|PubMed:30405132}.
CC -!- DISRUPTION PHENOTYPE: Mice show a lack of chemokine production induced
CC by bacterial peptidoglycans. RIPK2 deficiency affects cellular
CC signaling and cytokine responses triggered by NOD1 and NOD2 ligands,
CC but not TLR ligands. {ECO:0000269|PubMed:17277144,
CC ECO:0000269|PubMed:21469090}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF461040; AAL96436.1; -; mRNA.
DR EMBL; BC069878; AAH69878.1; -; mRNA.
DR CCDS; CCDS17988.1; -.
DR RefSeq; NP_620402.1; NM_138952.4.
DR AlphaFoldDB; P58801; -.
DR SMR; P58801; -.
DR BioGRID; 228697; 7.
DR CORUM; P58801; -.
DR IntAct; P58801; 2.
DR STRING; 10090.ENSMUSP00000038833; -.
DR BindingDB; P58801; -.
DR ChEMBL; CHEMBL4296021; -.
DR iPTMnet; P58801; -.
DR PhosphoSitePlus; P58801; -.
DR EPD; P58801; -.
DR jPOST; P58801; -.
DR PaxDb; P58801; -.
DR PeptideAtlas; P58801; -.
DR PRIDE; P58801; -.
DR ProteomicsDB; 254886; -.
DR Antibodypedia; 12695; 678 antibodies from 45 providers.
DR DNASU; 192656; -.
DR Ensembl; ENSMUST00000037035; ENSMUSP00000038833; ENSMUSG00000041135.
DR GeneID; 192656; -.
DR KEGG; mmu:192656; -.
DR UCSC; uc008sbr.1; mouse.
DR CTD; 8767; -.
DR MGI; MGI:1891456; Ripk2.
DR VEuPathDB; HostDB:ENSMUSG00000041135; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000156113; -.
DR InParanoid; P58801; -.
DR OMA; CPVNHSW; -.
DR OrthoDB; 436531at2759; -.
DR PhylomeDB; P58801; -.
DR TreeFam; TF106506; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR BioGRID-ORCS; 192656; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Ripk2; mouse.
DR PRO; PR:P58801; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P58801; protein.
DR Bgee; ENSMUSG00000041135; Expressed in animal zygote and 153 other tissues.
DR ExpressionAtlas; P58801; baseline and differential.
DR Genevisible; P58801; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050700; F:CARD domain binding; ISO:MGI.
DR GO; GO:0089720; F:caspase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0030274; F:LIM domain binding; ISO:MGI.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IMP:MGI.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IMP:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0033080; P:immature T cell proliferation in thymus; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IMP:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI.
DR GO; GO:0070427; P:nucleotide-binding oligomerization domain containing 1 signaling pathway; IMP:MGI.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:MGI.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:MGI.
DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IMP:MGI.
DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IMP:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
DR GO; GO:1904417; P:positive regulation of xenophagy; IMP:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0070555; P:response to interleukin-1; IMP:MGI.
DR GO; GO:0070671; P:response to interleukin-12; IMP:MGI.
DR GO; GO:0070673; P:response to interleukin-18; IMP:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; ISO:MGI.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IMP:MGI.
DR GO; GO:0098792; P:xenophagy; IMP:MGI.
DR CDD; cd08786; CARD_RIP2_CARD3; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR042149; CARD_RIP2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017322; Rcpt-int_Ser/Thr_kinase-2.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF037921; STPK_RIP2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Apoptosis; ATP-binding; Cytoplasm; Immunity;
KW Innate immunity; Isopeptide bond; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..539
FT /note="Receptor-interacting serine/threonine-protein kinase
FT 2"
FT /id="PRO_0000086609"
FT DOMAIN 18..294
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 431..523
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 335..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT MOD_RES 176
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O43353"
FT CROSSLNK 502
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O43353"
SQ SEQUENCE 539 AA; 60400 MW; 42951BF97CA15DFA CRC64;
MNGDAICSAL PPIPYHKLAD LHYLSRGASG TVSSARHADW RVRVAVKHLH IHTPLLDSER
NDILREAEIL HKARFSYILP ILGICNEPEF LGIVTEYMPN GSLNELLHRK TEYPDIAWPL
RFRILHEIAL GVNYLHNMNP PLLHHDLKTQ NILLDNEFHV KIADFGLSKW RMMSLSQSRS
YKSAPEGGTI IYMPPENYEP GQKSRASVKH DIYSYAVIMW EVLSRKQPFE EVTNPLQIMY
SVSQGHRPDT SEENLPFDIP HRGLMISLIQ SGWAQNPDER PSFLKCLIEL EPVLRTFEDI
TFLEAVIQLK KAKIQSSSST IHLCDKKMDL SLNIPANHPP QEESCGSSLL SRNTGSPGPS
RSLSAPQDKG FLSGAPQDCS SLKAHHCPGN HSWDGIVSVP PGAAFCDRRA SSCSLAVISP
FLVEKGSERP PIGIAQQWIQ SKREAIVSQM TEACLNQSLD ALLSRDLIMK EDYELISTKP
TRTSKVRQLL DTSDIQGEEF AKVVVQKLKD NKQLGLQPYP EVPVLSKAPP SNFPQNKSL
