ARI5A_MOUSE
ID ARI5A_MOUSE Reviewed; 590 AA.
AC Q3U108; Q3TZS4; Q3U0F0; Q3U0S2; Q3UDA3; Q3UDZ6; Q8BI45; Q8BYB5; Q8R2W1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=AT-rich interactive domain-containing protein 5A;
DE Short=ARID domain-containing protein 5A;
GN Name=Arid5a;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryonic lung, Spleen, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-283, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 [4]
RP FUNCTION, INTERACTION WITH SOX9, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RX PubMed=21346191; DOI=10.1091/mbc.e10-07-0566;
RA Amano K., Hata K., Muramatsu S., Wakabayashi M., Takigawa Y., Ono K.,
RA Nakanishi M., Takashima R., Kogo M., Matsuda A., Nishimura R., Yoneda T.;
RT "Arid5a cooperates with Sox9 to stimulate chondrocyte-specific
RT transcription.";
RL Mol. Biol. Cell 22:1300-1311(2011).
RN [5]
RP FUNCTION.
RX PubMed=23676272; DOI=10.1073/pnas.1307419110;
RA Masuda K., Ripley B., Nishimura R., Mino T., Takeuchi O., Shioi G.,
RA Kiyonari H., Kishimoto T.;
RT "Arid5a controls IL-6 mRNA stability, which contributes to elevation of IL-
RT 6 level in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9409-9414(2013).
RN [6]
RP FUNCTION, INTERACTION WITH RORC, AND INDUCTION.
RX PubMed=24782182; DOI=10.1002/art.38324;
RA Saito Y., Kagami S., Sanayama Y., Ikeda K., Suto A., Kashiwakuma D.,
RA Furuta S., Iwamoto I., Nonaka K., Ohara O., Nakajima H.;
RT "AT-rich-interactive domain-containing protein 5A functions as a negative
RT regulator of retinoic acid receptor-related orphan nuclear receptor gammat-
RT induced Th17 cell differentiation.";
RL Arthritis Rheum. 66:1185-1194(2014).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ARG-128.
RX PubMed=27022145; DOI=10.1084/jem.20151289;
RA Masuda K., Ripley B., Nyati K.K., Dubey P.K., Zaman M.M., Hanieh H.,
RA Higa M., Yamashita K., Standley D.M., Mashima T., Katahira M., Okamoto T.,
RA Matsuura Y., Takeuchi O., Kishimoto T.;
RT "Arid5a regulates naive CD4+ T cell fate through selective stabilization of
RT Stat3 mRNA.";
RL J. Exp. Med. 213:605-619(2016).
RN [8]
RP FUNCTION.
RX PubMed=27671645; DOI=10.1073/pnas.1613307113;
RA Zaman M.M., Masuda K., Nyati K.K., Dubey P.K., Ripley B., Wang K.,
RA Chalise J.P., Higa M., Hanieh H., Kishimoto T.;
RT "Arid5a exacerbates IFN-gamma-mediated septic shock by stabilizing T-bet
RT mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:11543-11548(2016).
RN [9]
RP PHOSPHORYLATION AT SER-253; SER-433 AND SER-458, UBIQUITINATION AT LYS-80
RP AND LYS-89, AND MUTAGENESIS OF SER-253; SER-433 AND SER-458.
RX PubMed=28168301; DOI=10.1093/nar/gkx064;
RA Nyati K.K., Masuda K., Zaman M.M., Dubey P.K., Millrine D., Chalise J.P.,
RA Higa M., Li S., Standley D.M., Saito K., Hanieh H., Kishimoto T.;
RT "TLR4-induced NF-kappaB and MAPK signaling regulate the IL-6 mRNA
RT stabilizing protein Arid5a.";
RL Nucleic Acids Res. 45:2687-2703(2017).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ARG-128.
RX PubMed=29244194; DOI=10.1002/eji.201747109;
RA Hanieh H., Masuda K., Metwally H., Chalise J.P., Mohamed M., Nyati K.K.,
RA Standley D.M., Li S., Higa M., Zaman M.M., Kishimoto T.;
RT "Arid5a stabilizes OX40 mRNA in murine CD4+ T cells by recognizing a stem-
RT loop structure in its 3'UTR.";
RL Eur. J. Immunol. 48:593-604(2018).
CC -!- FUNCTION: DNA-binding protein that may regulate transcription and act
CC as a repressor by binding to AT-rich stretches in the promoter region
CC of target genes (By similarity). May positively regulate chondrocyte-
CC specific transcription such as of COL2A1 in collaboration with SOX9 and
CC positively regulate histone H3 acetylation at chondrocyte-specific
CC genes. May stimulate early-stage chondrocyte differentiation and
CC inhibit later stage differention (PubMed:21346191). Can repress ESR1-
CC mediated transcriptional activation; proposed to act as corepressor for
CC selective nuclear hormone receptors (By similarity). As RNA-binding
CC protein involved in the regulation of inflammatory response by
CC stabilizing selective inflammation-related mRNAs, such as IL6, STAT3
CC and TBX21. Binds to stem loop structures located in the 3'UTRs of IL6,
CC STAT3 and TBX21 mRNAs; at least for STAT3 prevents binding of ZC3H12A
CC to the mRNA stem loop structure thus inhibiting its degradation
CC activity. Contributes to elevated IL6 levels possibly implicated in
CC autoimmunity processes. IL6-dependent stabilization of STAT3 mRNA may
CC promote differentiation of naive CD4+ T-cells into T-helper Th17 cells
CC (PubMed:23676272, PubMed:27022145). In CD4+ T-cells may also inhibit
CC RORC-induced Th17 cell differentiation independently of IL6 signaling
CC (PubMed:24782182). Stabilization of TBX21 mRNA contributes to elevated
CC interferon-gamma secretion in Th1 cells possibly implicated in the
CC establishment of septic shock (PubMed:27671645). Stabilizes
CC TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in
CC its 3'UTR; thereby competing with the mRNA-destabilizing functions of
CC RC3H1 and endoribonuclease ZC3H12A (PubMed:29244194).
CC {ECO:0000250|UniProtKB:Q03989, ECO:0000269|PubMed:21346191,
CC ECO:0000269|PubMed:23676272, ECO:0000269|PubMed:24782182,
CC ECO:0000269|PubMed:27022145, ECO:0000269|PubMed:27671645,
CC ECO:0000269|PubMed:29244194}.
CC -!- SUBUNIT: Interacts with SOX9 (PubMed:21346191). Interacts with ESR1 (By
CC similarity). Interacts with RORC (PubMed:24782182).
CC {ECO:0000250|UniProtKB:Q03989, ECO:0000269|PubMed:21346191,
CC ECO:0000269|PubMed:24782182}.
CC -!- INTERACTION:
CC Q3U108; P48436: SOX9; Xeno; NbExp=3; IntAct=EBI-14022639, EBI-3920028;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:21346191}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q3U108-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U108-2; Sequence=VSP_025839;
CC Name=3;
CC IsoId=Q3U108-3; Sequence=VSP_025840, VSP_025842;
CC Name=4;
CC IsoId=Q3U108-4; Sequence=VSP_025841;
CC Name=5;
CC IsoId=Q3U108-5; Sequence=VSP_025838;
CC -!- TISSUE SPECIFICITY: Expressed in T cells (at protein level)
CC (PubMed:29244194). Expressed at high levels in cartilage, heart, testis
CC and bone (PubMed:21346191). {ECO:0000269|PubMed:21346191,
CC ECO:0000269|PubMed:29244194}.
CC -!- INDUCTION: In macrophages by LPS, IL1B and IL6 (PubMed:21346191). By
CC IL6/STAT3 signaling in T-helper Th17 cells (PubMed:24782182,
CC PubMed:29244194). {ECO:0000269|PubMed:21346191,
CC ECO:0000269|PubMed:24782182, ECO:0000269|PubMed:29244194}.
CC -!- PTM: Phosphorylated by MAPK14 on serine residues involving a TLR4
CC signaling pathway upon lipopolysaccharide (LPS) stimulation leading to
CC its ubiquitination and proteasomal degradation.
CC {ECO:0000269|PubMed:28168301}.
CC -!- PTM: Ubiquitinated leading to proteasomal degradation; involving WWP1
CC linked to MAPK14-mediated phosphorylation upon LPS stimulation.
CC {ECO:0000269|PubMed:28168301}.
CC -!- DISRUPTION PHENOTYPE: Mice are resistant to experimental autoimmune
CC encephalomyelitis (EAE), a T-cell-mediated autoimmune model
CC (PubMed:29244194). The expression of pro-inflammatory mediators is
CC severely reduced in EAE (PubMed:29244194).
CC {ECO:0000269|PubMed:29244194}.
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DR EMBL; AK041344; BAC30913.1; -; mRNA.
DR EMBL; AK085015; BAC39338.1; -; mRNA.
DR EMBL; AK149839; BAE29115.1; -; mRNA.
DR EMBL; AK150170; BAE29358.1; -; mRNA.
DR EMBL; AK156376; BAE33692.1; -; mRNA.
DR EMBL; AK156622; BAE33779.1; -; mRNA.
DR EMBL; AK156934; BAE33904.1; -; mRNA.
DR EMBL; AK157607; BAE34133.1; -; mRNA.
DR EMBL; BC027152; AAH27152.1; -; mRNA.
DR CCDS; CCDS14876.1; -. [Q3U108-4]
DR CCDS; CCDS48239.1; -. [Q3U108-1]
DR CCDS; CCDS69878.1; -. [Q3U108-5]
DR CCDS; CCDS78560.1; -. [Q3U108-2]
DR RefSeq; NP_001165676.1; NM_001172205.1. [Q3U108-1]
DR RefSeq; NP_001165677.1; NM_001172206.1.
DR RefSeq; NP_001277655.1; NM_001290726.1.
DR RefSeq; NP_001277656.1; NM_001290727.1. [Q3U108-5]
DR RefSeq; NP_666108.2; NM_145996.4. [Q3U108-4]
DR AlphaFoldDB; Q3U108; -.
DR SMR; Q3U108; -.
DR BioGRID; 229569; 14.
DR IntAct; Q3U108; 2.
DR STRING; 10090.ENSMUSP00000110684; -.
DR iPTMnet; Q3U108; -.
DR PhosphoSitePlus; Q3U108; -.
DR CPTAC; non-CPTAC-3309; -.
DR EPD; Q3U108; -.
DR MaxQB; Q3U108; -.
DR PaxDb; Q3U108; -.
DR PRIDE; Q3U108; -.
DR ProteomicsDB; 273940; -. [Q3U108-1]
DR ProteomicsDB; 273941; -. [Q3U108-2]
DR ProteomicsDB; 273942; -. [Q3U108-3]
DR ProteomicsDB; 273943; -. [Q3U108-4]
DR ProteomicsDB; 274968; -. [Q3U108-5]
DR Antibodypedia; 1050; 219 antibodies from 18 providers.
DR DNASU; 214855; -.
DR Ensembl; ENSMUST00000115029; ENSMUSP00000110681; ENSMUSG00000037447. [Q3U108-5]
DR Ensembl; ENSMUST00000115031; ENSMUSP00000110683; ENSMUSG00000037447. [Q3U108-3]
DR Ensembl; ENSMUST00000115032; ENSMUSP00000110684; ENSMUSG00000037447. [Q3U108-1]
DR Ensembl; ENSMUST00000137906; ENSMUSP00000117810; ENSMUSG00000037447. [Q3U108-4]
DR GeneID; 214855; -.
DR KEGG; mmu:214855; -.
DR UCSC; uc007apu.2; mouse. [Q3U108-4]
DR UCSC; uc007apv.2; mouse. [Q3U108-1]
DR UCSC; uc007apy.2; mouse. [Q3U108-3]
DR CTD; 10865; -.
DR MGI; MGI:2443039; Arid5a.
DR VEuPathDB; HostDB:ENSMUSG00000037447; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000161253; -.
DR HOGENOM; CLU_032275_0_0_1; -.
DR InParanoid; Q3U108; -.
DR OMA; ECGAKSM; -.
DR TreeFam; TF324725; -.
DR BioGRID-ORCS; 214855; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q3U108; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3U108; protein.
DR Bgee; ENSMUSG00000037447; Expressed in granulocyte and 94 other tissues.
DR ExpressionAtlas; Q3U108; baseline and differential.
DR Genevisible; Q3U108; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IDA:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IMP:UniProtKB.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Immunity; Innate immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..590
FT /note="AT-rich interactive domain-containing protein 5A"
FT /id="PRO_0000288931"
FT DOMAIN 50..142
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 1..294
FT /note="Interaction with SOX9"
FT /evidence="ECO:0000269|PubMed:21346191"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28168301"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28168301"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28168301"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28168301"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28168301"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025838"
FT VAR_SEQ 1..2
FT /note="MA -> MLKGGRPDLCVVNSLIKLQKLKLHVDAEHQT (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025839"
FT VAR_SEQ 2
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025840"
FT VAR_SEQ 42..99
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025841"
FT VAR_SEQ 81..82
FT /note="QI -> QSASLGGGGWCSGRVSVGGQQPGDVPRQDNRQGTSAKGDPGCRQPV
FT GVACEDGASLKARGGVGFSSSWAACPVHNSGPAWECGVTEPDRLPCLFPSV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025842"
FT MUTAGEN 128
FT /note="R->A: Abolishes binding to STAT3 3'UTR stem loop
FT structure. Abolishes binding to TNFRSF4/OX40 mRNA."
FT /evidence="ECO:0000269|PubMed:27022145,
FT ECO:0000269|PubMed:29244194"
FT MUTAGEN 253
FT /note="S->A: Abolishes ubiquitination; largely impairs
FT proteasomal degradation; results in overproduction of IL-6
FT upon overexpression; in association with A-433 and A-458."
FT /evidence="ECO:0000269|PubMed:28168301"
FT MUTAGEN 433
FT /note="S->A: Abolishes ubiquitination; largely impairs
FT proteasomal degradation; results in overproduction of IL-6
FT upon overexpression; in association with A-253 and A-458."
FT /evidence="ECO:0000269|PubMed:28168301"
FT MUTAGEN 458
FT /note="S->A: Abolishes ubiquitination; largely impairs
FT proteasomal degradation; results in overproduction of IL-6
FT upon overexpression; in association with A-253 and A-433."
FT /evidence="ECO:0000269|PubMed:28168301"
FT CONFLICT 51
FT /note="E -> K (in Ref. 1; BAE34133)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="L -> Q (in Ref. 1; BAE29358)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="S -> P (in Ref. 2; AAH27152)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="H -> R (in Ref. 1; BAE29115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 63898 MW; D4C00C2F1DEBDCC3 CRC64;
MAAPPAKGNT EQSEEGDLPQ LPVSPKPDDE QSRSQSPTQL QDSPEAGGEQ EEEQAFLVSL
YKFMKERHTP IERVPHLGFK QINLWKIYKA VEKLGAYELV TGRRLWKNVY DELGGSPGST
SAATCTRRHY ERLVLPYVRH LKGEDDKPLP PTKPRKQYKM AKELRGDDGT TEKLKKAKDS
EERRVEQTTP GKTKSDATGQ TQLPCQGSSR DSTEQLGPVS GPSPPLTGAS SCPEAYKRLL
SSFYCKGAHG IMSPLAKKKL LAQVSKAEAL QCQEEGCRHG ARSPNKDIQD SPQNLRGPAE
NSEHQLTPRE GLQAPGGSTR MEAQVGPCPT APMFSGCFHA YPTEVLKPVS QHPRDFFSGL
KDRVLLGPPG KEEGPTTKES HLVWGGDANH PSAFHKGSTR KRSFYPKPKA CWVSPMAKVP
TERPGAPSPH PSSPGLGSKR GLEEEGFAHG GKKLRAVSPF LKEVDSKETG GKPAAPGLAV
SCLLGPTPGP TPPEAYRGTM LRCPLNFTGS ADPLKGQASL PFSPLVIPAF PAHLLATTGS
SPMAASLMHF PPTPYDAVLR NRLGPASSAW HMPPVTTYAA PHFFHLNTKL
