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STIP1 homology and U box-containing protein 1 (EC 2.3.2.27) (Carboxy terminus of Hsp70-interacting protein) (E3 ubiquitin-protein ligase CHIP) (RING-type E3 ubiquitin transferase CHIP)

 CHIP_MOUSE              Reviewed;         304 AA.
Q9WUD1; Q9DCJ0;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 161.
RecName: Full=STIP1 homology and U box-containing protein 1 {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:21855799};
AltName: Full=Carboxy terminus of Hsp70-interacting protein {ECO:0000303|PubMed:10330192};
AltName: Full=E3 ubiquitin-protein ligase CHIP {ECO:0000305};
AltName: Full=RING-type E3 ubiquitin transferase CHIP {ECO:0000305};
Name=Stub1 {ECO:0000312|MGI:MGI:1891731};
Synonyms=Chip {ECO:0000303|PubMed:10330192};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10330192; DOI=10.1128/MCB.19.6.4535;
Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y.,
Patterson C.;
"Identification of CHIP, a novel tetratricopeptide repeat-containing
protein that interacts with heat shock proteins and negatively
regulates chaperone functions.";
Mol. Cell. Biol. 19:4535-4545(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Embryo, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DOMAIN,
AND MUTAGENESIS OF HIS-261 AND PRO-270.
PubMed=11435423; DOI=10.1074/jbc.M102755200;
Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
"U box proteins as a new family of ubiquitin-protein ligases.";
J. Biol. Chem. 276:33111-33120(2001).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-24, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND
ATXN3, UBIQUITINATION AT LYS-2, AND MUTAGENESIS OF LYS-2; LYS-4 AND
LYS-7.
PubMed=21855799; DOI=10.1016/j.molcel.2011.05.036;
Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P.,
Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J.,
Gestwicki J.E., Paulson H.L.;
"Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP.";
Mol. Cell 43:599-612(2011).
[10]
FUNCTION, INTERACTION WITH FOXP3, AND INDUCTION.
PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D.,
Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.;
"The ubiquitin ligase Stub1 negatively modulates regulatory T cell
suppressive activity by promoting degradation of the transcription
factor Foxp3.";
Immunity 39:272-285(2013).
[11]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N
AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN
COMPLEX WITH HSP90AA1, AND HOMODIMERIZATION.
PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
Pearl L.H.;
"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
Mol. Cell 20:525-538(2005).
-!- FUNCTION: E3 ubiquitin-protein ligase which targets misfolded
chaperone substrates towards proteasomal degradation. Collaborates
with ATXN3 in the degradation of misfolded chaperone substrates:
ATXN3 restricting the length of ubiquitin chain attached to
STUB1/CHIP substrates and preventing further chain extension.
Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the
activity of several chaperone complexes, including Hsp70, Hsc70
and Hsp90. Mediates transfer of non-canonical short ubiquitin
chains to HSPA8 that have no effect on HSPA8 degradation. Mediates
polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41',
'Lys-61' and 'Lys-81', thereby playing a role in base-excision
repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-
BP1-dependent monoubiquitination and leading to POLB-degradation
by the proteasome. Mediates polyubiquitination of CYP3A4.
Ubiquitinates EPHA2 and may regulate the receptor stability and
activity through proteasomal degradation. Negatively regulates the
suppressive function of regulatory T-cells (Treg) during
inflammation by mediating the ubiquitination and degradation of
FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Acts as a
co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes
ubiquitin-mediated protein degradation. Negatively regulates TGF-
beta signaling by modulating the basal level of SMAD3 via
ubiquitin-mediated degradation (By similarity).
{ECO:0000250|UniProtKB:Q9UNE7, ECO:0000269|PubMed:11435423,
ECO:0000269|PubMed:21855799, ECO:0000269|PubMed:23973223}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:11435423,
ECO:0000269|PubMed:21855799}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:21855799}.
-!- SUBUNIT: Homodimer (PubMed:16307917). Interacts with BAG2, and
with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and
UBE2D3. Detected in a ternary complex containing STUB1, HSPA1A and
HSPBP1. Interacts with MKKS. Interacts with DNAAF4 and POLB (By
similarity). Interacts (via the U-box domain) with the UBE2V2-
UBE2N heterodimer; the complex has a specific 'Lys-63'-linked
polyubiquitination activity (PubMed:16307917). Interacts (when
monoubiquitinated) with ATXN3 (PubMed:21855799). Interacts with
UBE2W (PubMed:21855799). Interacts with DNAJB6 (By similarity).
Interacts with FOXP3 (PubMed:23973223). Interacts with FLCN and
HSP90AA1. Interacts with HSP90. Interacts with UBE2N and UBE2V1.
Interacts (via TPR repeats) with the C-terminal domains of HSPA8
and HSPA1A. Interacts with the non-acetylated form of HSPA1A and
HSPA1B. Interacts with SMAD3 and HSP90AB1 (By similarity).
{ECO:0000250|UniProtKB:Q9UNE7, ECO:0000269|PubMed:16307917,
ECO:0000269|PubMed:21855799, ECO:0000269|PubMed:23973223}.
-!- INTERACTION:
O55222:Ilk; NbExp=7; IntAct=EBI-773027, EBI-6690138;
Q5S007:LRRK2 (xeno); NbExp=2; IntAct=EBI-773027, EBI-5323863;
P61088:UBE2N (xeno); NbExp=2; IntAct=EBI-773027, EBI-1052908;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11435423}.
Nucleus {ECO:0000250|UniProtKB:Q9UNE7}. Note=Translocates to the
nucleus in response to inflammatory signals in regulatory T-cells
(Treg). {ECO:0000250|UniProtKB:Q9UNE7}.
-!- INDUCTION: Up-regulated by inflammatory signals in Treg regulatory
T-cells (Treg). {ECO:0000269|PubMed:23973223}.
-!- DOMAIN: The U-box domain is required for the ubiquitin protein
ligase activity. {ECO:0000269|PubMed:11435423}.
-!- DOMAIN: The TPR domain is essential for ubiquitination mediated by
UBE2D1. {ECO:0000250|UniProtKB:Q9UNE7}.
-!- PTM: Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2.
Monoubiquitinated at Lys-2 following cell stress by UBE2W,
promoting the interaction with ATXN3.
{ECO:0000269|PubMed:21855799}.
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EMBL; AF129086; AAD33401.1; -; mRNA.
EMBL; AK002752; BAB22329.1; -; mRNA.
EMBL; AK004464; BAB23315.1; -; mRNA.
EMBL; AK045776; BAC32489.1; -; mRNA.
EMBL; AK166630; BAE38905.1; -; mRNA.
EMBL; BC027427; AAH27427.1; -; mRNA.
EMBL; BC038939; AAH38939.1; -; mRNA.
CCDS; CCDS28533.1; -.
RefSeq; NP_062693.1; NM_019719.3.
UniGene; Mm.277599; -.
UniGene; Mm.491120; -.
PDB; 2C2L; X-ray; 3.30 A; A/B/C/D=24-304.
PDB; 2C2V; X-ray; 2.90 A; S/T/U/V=227-304.
PDB; 3Q47; X-ray; 1.70 A; B=23-155.
PDB; 3Q49; X-ray; 1.54 A; B=23-155.
PDB; 3Q4A; X-ray; 1.54 A; B=23-155.
PDBsum; 2C2L; -.
PDBsum; 2C2V; -.
PDBsum; 3Q47; -.
PDBsum; 3Q49; -.
PDBsum; 3Q4A; -.
ProteinModelPortal; Q9WUD1; -.
SMR; Q9WUD1; -.
BioGrid; 207969; 44.
DIP; DIP-29751N; -.
IntAct; Q9WUD1; 16.
STRING; 10090.ENSMUSP00000040431; -.
iPTMnet; Q9WUD1; -.
PhosphoSitePlus; Q9WUD1; -.
EPD; Q9WUD1; -.
MaxQB; Q9WUD1; -.
PaxDb; Q9WUD1; -.
PeptideAtlas; Q9WUD1; -.
PRIDE; Q9WUD1; -.
Ensembl; ENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615.
GeneID; 56424; -.
KEGG; mmu:56424; -.
UCSC; uc008bcf.1; mouse.
CTD; 10273; -.
MGI; MGI:1891731; Stub1.
eggNOG; KOG4642; Eukaryota.
eggNOG; ENOG410ZC2R; LUCA.
GeneTree; ENSGT00730000111218; -.
HOGENOM; HOG000163725; -.
HOVERGEN; HBG053046; -.
InParanoid; Q9WUD1; -.
KO; K09561; -.
OMA; TNATYFT; -.
OrthoDB; EOG091G0FJB; -.
PhylomeDB; Q9WUD1; -.
TreeFam; TF313937; -.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q9WUD1; -.
PRO; PR:Q9WUD1; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000039615; -.
CleanEx; MM_STUB1; -.
Genevisible; Q9WUD1; MM.
GO; GO:0005737; C:cytoplasm; ISS:HGNC.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0042405; C:nuclear inclusion body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0031371; C:ubiquitin conjugating enzyme complex; TAS:HGNC.
GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0001664; F:G-protein coupled receptor binding; ISO:MGI.
GO; GO:0031072; F:heat shock protein binding; TAS:HGNC.
GO; GO:0030544; F:Hsp70 protein binding; ISS:HGNC.
GO; GO:0051879; F:Hsp90 protein binding; ISS:BHF-UCL.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
GO; GO:0030674; F:protein binding, bridging; TAS:HGNC.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0046332; F:SMAD binding; ISS:HGNC.
GO; GO:0030911; F:TPR domain binding; ISS:HGNC.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:1904264; F:ubiquitin protein ligase activity involved in ERAD pathway; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
GO; GO:0071218; P:cellular response to misfolded protein; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:ParkinsonsUK-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:HGNC.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:HGNC.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0051604; P:protein maturation; TAS:HGNC.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0031943; P:regulation of glucocorticoid metabolic process; ISS:HGNC.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; ISS:HGNC.
Gene3D; 1.25.40.10; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF04564; U-box; 1.
SMART; SM00028; TPR; 3.
SMART; SM00504; Ubox; 1.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 1.
PROSITE; PS51698; U_BOX; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
TPR repeat; Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 304 STIP1 homology and U box-containing
protein 1.
/FTId=PRO_0000106330.
REPEAT 27 60 TPR 1.
REPEAT 61 94 TPR 2.
REPEAT 96 128 TPR 3.
DOMAIN 227 301 U-box.
COMPBIAS 14 19 Poly-Gly.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNE7}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNE7}.
CROSSLNK 2 2 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21855799}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9UNE7}.
CROSSLNK 222 222 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9UNE7}.
CROSSLNK 256 256 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9UNE7}.
MUTAGEN 2 2 K->R: Impaired interaction with ATXN3;
when associated with R-4 and R-7.
{ECO:0000269|PubMed:21855799}.
MUTAGEN 4 4 K->R: Impaired interaction with ATXN3;
when associated with R-2 and R-7.
{ECO:0000269|PubMed:21855799}.
MUTAGEN 7 7 K->R: Impaired interaction with ATXN3;
when associated with R-2 and R-4.
{ECO:0000269|PubMed:21855799}.
MUTAGEN 261 261 H->A: Loss of E3 ubiquitin protein ligase
activity. {ECO:0000269|PubMed:11435423}.
MUTAGEN 270 270 P->A: Loss of E3 ubiquitin protein ligase
activity. {ECO:0000269|PubMed:11435423}.
CONFLICT 20 20 S -> T (in Ref. 2; BAB22329).
{ECO:0000305}.
HELIX 27 39 {ECO:0000244|PDB:3Q4A}.
HELIX 43 56 {ECO:0000244|PDB:3Q4A}.
HELIX 61 73 {ECO:0000244|PDB:3Q4A}.
HELIX 77 90 {ECO:0000244|PDB:3Q4A}.
HELIX 95 107 {ECO:0000244|PDB:3Q4A}.
HELIX 111 127 {ECO:0000244|PDB:3Q4A}.
HELIX 135 152 {ECO:0000244|PDB:3Q4A}.
HELIX 161 178 {ECO:0000244|PDB:2C2L}.
TURN 179 181 {ECO:0000244|PDB:2C2L}.
HELIX 183 185 {ECO:0000244|PDB:2C2L}.
TURN 186 188 {ECO:0000244|PDB:2C2L}.
HELIX 191 194 {ECO:0000244|PDB:2C2L}.
HELIX 196 218 {ECO:0000244|PDB:2C2L}.
HELIX 230 232 {ECO:0000244|PDB:2C2V}.
TURN 235 237 {ECO:0000244|PDB:2C2V}.
STRAND 242 246 {ECO:0000244|PDB:2C2V}.
STRAND 252 254 {ECO:0000244|PDB:2C2V}.
HELIX 255 264 {ECO:0000244|PDB:2C2V}.
TURN 270 272 {ECO:0000244|PDB:2C2V}.
HELIX 278 280 {ECO:0000244|PDB:2C2V}.
HELIX 285 298 {ECO:0000244|PDB:2C2V}.
SEQUENCE 304 AA; 34909 MW; 18BD2728908025A8 CRC64;
MKGKEEKEGG ARLGTGGGGS PDKSPSAQEL KEQGNRLFVG RKYPEAAACY GRAITRNPLV
AVYYTNRALC YLKMQQPEQA LADCRRALEL DGQSVKAHFF LGQCQLEMES YDEAIANLQR
AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS IEERRIHQES ELHSYLTRLI AAERERELEE
CQRNHEGHED DGHIRAQQAC IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL
MREPCITPSG ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW
VEDY


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