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Ubiquitin D (Diubiquitin) (Ubiquitin-like protein FAT10)

 UBD_HUMAN               Reviewed;         165 AA.
O15205; B0UZT6; Q5STL2; Q5SUK2; Q96EC7;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
28-FEB-2018, entry version 150.
RecName: Full=Ubiquitin D;
AltName: Full=Diubiquitin;
AltName: Full=Ubiquitin-like protein FAT10;
Name=UBD; Synonyms=FAT10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-160, AND TISSUE SPECIFICITY.
PubMed=9368598; DOI=10.1002/eji.1830271002;
Bates E.E.M., Ravel O., Dieu M.-C., Ho S., Guret C., Bridon J.-M.,
Ait-Yahia S., Briere F., Caux C., Banchereau J., Lebecque S.;
"Identification and analysis of a novel member of the ubiquitin family
expressed in dendritic cells and mature B cells.";
Eur. J. Immunol. 27:2471-2477(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAD2L1, AND VARIANT
SER-160.
TISSUE=Spleen;
PubMed=10200259; DOI=10.1073/pnas.96.8.4313;
Liu Y.-C., Pan J., Zhang C., Fan W., Collinge M., Bender J.R.,
Weissman S.M.;
"A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to
the spindle assembly checkpoint protein MAD2.";
Proc. Natl. Acad. Sci. U.S.A. 96:4313-4318(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-160.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-160.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
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).
[6]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION IN
HEPATOCELLULAR CARCINOMA.
PubMed=12730673; DOI=10.1038/sj.onc.1206337;
Lee C.G.L., Ren J., Cheong I.S.Y., Ban K.H.K., Ooi L.L.P.J.,
Yong Tan S., Kan A., Nuchprayoon I., Jin R., Lee K.-H., Choti M.,
Lee L.A.;
"Expression of the FAT10 gene is highly upregulated in hepatocellular
carcinoma and other gastrointestinal and gynecological cancers.";
Oncogene 22:2592-2603(2003).
[7]
INTERACTION WITH NUB1, AND INDUCTION BY NUB1.
PubMed=14757770; DOI=10.1074/jbc.M310114200;
Hipp M.S., Raasi S., Groettrup M., Schmidtke G.;
"NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein
FAT10 and accelerates its degradation.";
J. Biol. Chem. 279:16503-16510(2004).
[8]
FUNCTION.
PubMed=15831455; DOI=10.1128/MCB.25.9.3483-3491.2005;
Hipp M.S., Kalveram B., Raasi S., Groettrup M., Schmidtke G.;
"FAT10, a ubiquitin-independent signal for proteasomal degradation.";
Mol. Cell. Biol. 25:3483-3491(2005).
[9]
INDUCTION BY CELL CYCLE.
PubMed=16959044; DOI=10.1186/1747-1028-1-20;
Lim C.-B., Zhang D., Lee C.G.;
"FAT10, a gene up-regulated in various cancers, is cell-cycle
regulated.";
Cell Div. 1:20-20(2006).
[10]
FUNCTION, AND INDUCTION IN HIVAN.
PubMed=16495380; DOI=10.1681/ASN.2005070692;
Ross M.J., Wosnitzer M.S., Ross M.D., Granelli B., Gusella G.L.,
Husain M., Kaufman L., Vasievich M., D'Agati V.D., Wilson P.D.,
Klotman M.E., Klotman P.E.;
"Role of ubiquitin-like protein FAT10 in epithelial apoptosis in renal
disease.";
J. Am. Soc. Nephrol. 17:996-1004(2006).
[11]
FUNCTION, AND INTERACTION WITH MAD2L1.
PubMed=16495226; DOI=10.1074/jbc.M507218200;
Ren J., Kan A., Leong S.H., Ooi L.L.P.J., Jeang K.-T., Chong S.S.,
Kon O.L., Lee C.G.L.;
"FAT10 plays a role in the regulation of chromosomal stability.";
J. Biol. Chem. 281:11413-11421(2006).
[12]
INTERACTION WITH NUB1 AND PROTEASOME.
PubMed=16707496; DOI=10.1074/jbc.M603063200;
Schmidtke G., Kalveram B., Weber E., Bochtler P., Lukasiak S.,
Hipp M.S., Groettrup M.;
"The UBA domains of NUB1L are required for binding but not for
accelerated degradation of the ubiquitin-like modifier FAT10.";
J. Biol. Chem. 281:20045-20054(2006).
[13]
INDUCTION BY TP53.
PubMed=16501612; DOI=10.1038/sj.onc.1209220;
Zhang D.W., Jeang K.-T., Lee C.G.;
"p53 negatively regulates the expression of FAT10, a gene upregulated
in various cancers.";
Oncogene 25:2318-2327(2006).
[14]
FUNCTION, INTERACTION WITH UBA6, THIOESTER FORMATION, INDUCTION BY TNF
AND IFNG, AND MUTAGENESIS OF 164-GLY-GLY-165.
PubMed=17889673; DOI=10.1016/j.molcel.2007.08.020;
Chiu Y.-H., Sun Q., Chen Z.J.;
"E1-L2 activates both ubiquitin and FAT10.";
Mol. Cell 27:1014-1023(2007).
[15]
FUNCTION, INTERACTION WITH HDAC6, SUBCELLULAR LOCATION, AND
ACETYLATION.
PubMed=19033385; DOI=10.1242/jcs.035006;
Kalveram B., Schmidtke G., Groettrup M.;
"The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes
to aggresomes under proteasome inhibition.";
J. Cell Sci. 121:4079-4088(2008).
[16]
FUNCTION, AND INDUCTION BY CYTOKINES.
PubMed=18574467; DOI=10.1038/onc.2008.201;
Lukasiak S., Schiller C., Oehlschlaeger P., Schmidtke G., Krause P.,
Legler D.F., Autschbach F., Schirmacher P., Breuhahn K., Groettrup M.;
"Proinflammatory cytokines cause FAT10 upregulation in cancers of
liver and colon.";
Oncogene 27:6068-6074(2008).
[17]
FUNCTION.
PubMed=19166848; DOI=10.1016/j.febslet.2009.01.006;
Schmidtke G., Kalveram B., Groettrup M.;
"Degradation of FAT10 by the 26S proteasome is independent of
ubiquitylation but relies on NUB1L.";
FEBS Lett. 583:591-594(2009).
[18]
FUNCTION, AND INDUCTION.
PubMed=19028597; DOI=10.1016/j.biocel.2008.10.023;
Ebstein F., Lange N., Urban S., Seifert U., Krueger E.,
Kloetzel P.-M.;
"Maturation of human dendritic cells is accompanied by functional
remodelling of the ubiquitin-proteasome system.";
Int. J. Biochem. Cell Biol. 41:1205-1215(2009).
[19]
FUNCTION, AND INDUCTION.
PubMed=19726511; DOI=10.1128/JVI.00034-09;
Snyder A., Alsauskas Z., Gong P., Rosenstiel P.E., Klotman M.E.,
Klotman P.E., Ross M.J.;
"FAT10: a novel mediator of Vpr-induced apoptosis in human
immunodeficiency virus-associated nephropathy.";
J. Virol. 83:11983-11988(2009).
[20]
INDUCTION.
PubMed=19437562; DOI=10.3748/wjg.15.2228;
Ji F., Jin X., Jiao C.-H., Xu Q.-W., Wang Z.-W., Chen Y.-L.;
"FAT10 level in human gastric cancer and its relation with mutant p53
level, lymph node metastasis and TNM staging.";
World J. Gastroenterol. 15:2228-2233(2009).
[21]
FUNCTION, AND INDUCTION.
PubMed=19959714; DOI=10.1681/ASN.2009050479;
Gong P., Canaan A., Wang B., Leventhal J., Snyder A., Nair V.,
Cohen C.D., Kretzler M., D'Agati V., Weissman S., Ross M.J.;
"The ubiquitin-like protein FAT10 mediates NF-kappa-B activation.";
J. Am. Soc. Nephrol. 21:316-326(2010).
[22] {ECO:0000244|PDB:2MBE}
STRUCTURE BY NMR OF 8-82, INTERACTION WITH TP53; MAD2L1; HDAC6; UBA6;
NUB1 AND SQSTM1, AND MUTAGENESIS OF HIS-11; ARG-13; HIS-75; THR-77;
LYS-79 AND 164-GLY-GLY-165.
PubMed=25422469; DOI=10.1073/pnas.1403383111;
Theng S.S., Wang W., Mah W.C., Chan C., Zhuo J., Gao Y., Qin H.,
Lim L., Chong S.S., Song J., Lee C.G.;
"Disruption of FAT10-MAD2 binding inhibits tumor progression.";
Proc. Natl. Acad. Sci. U.S.A. 111:E5282-E5291(2014).
-!- FUNCTION: Ubiquitin-like protein modifier which can be covalently
attached to target protein and subsequently leads to their
degradation by the 26S proteasome, in a NUB1-dependent manner.
Probably functions as a survival factor. Conjugation ability
activated by UBA6. Promotes the expression of the proteasome
subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and
LPS-mediated activation of the central mediator of innate immunity
NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation
of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced
p65 nuclear translocation in renal tubular epithelial cells
(RTECs). May be involved in dendritic cell (DC) maturation, the
process by which immature dendritic cells differentiate into fully
competent antigen-presenting cells that initiate T-cell responses.
Mediates mitotic non-disjunction and chromosome instability, in
long-term in vitro culture and cancers, by abbreviating mitotic
phase and impairing the kinetochore localization of MAD2L1 during
the prometaphase stage of the cell cycle. May be involved in the
formation of aggresomes when proteasome is saturated or impaired.
Mediates apoptosis in a caspase-dependent manner, especially in
renal epithelium and tubular cells during renal diseases such as
polycystic kidney disease and Human immunodeficiency virus (HIV)-
associated nephropathy (HIVAN). {ECO:0000269|PubMed:15831455,
ECO:0000269|PubMed:16495226, ECO:0000269|PubMed:16495380,
ECO:0000269|PubMed:17889673, ECO:0000269|PubMed:18574467,
ECO:0000269|PubMed:19028597, ECO:0000269|PubMed:19033385,
ECO:0000269|PubMed:19166848, ECO:0000269|PubMed:19726511,
ECO:0000269|PubMed:19959714}.
-!- SUBUNIT: Interact directly with the 26S proteasome. The
interaction with NUB1 via the N-terminal ubiquitin domain
facilitates the linking of UBD-conjugated target protein to the
proteasome complex and accelerates its own degradation and that of
its conjugates. Interacts (via ubiquitin-like 1 domain) with the
spindle checkpoint protein MAD2L1 during mitosis. Present in
aggresomes of proteasome inhibited cells. Interacts with HDAC6
under proteasome impairment conditions. Forms a thioester with
UBA6 in cells stimulated with tumor necrosis factor-alpha (TNFa)
and interferon-gamma (IFNg). Interacts with SQSTM1 and TP53/p53
(PubMed:25422469). {ECO:0000269|PubMed:10200259,
ECO:0000269|PubMed:14757770, ECO:0000269|PubMed:16495226,
ECO:0000269|PubMed:16707496, ECO:0000269|PubMed:17889673,
ECO:0000269|PubMed:19033385, ECO:0000269|PubMed:25422469}.
-!- INTERACTION:
Q13387:MAPK8IP2; NbExp=3; IntAct=EBI-6657186, EBI-722813;
Q9H832:UBE2Z; NbExp=2; IntAct=EBI-6657186, EBI-720977;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12730673,
ECO:0000269|PubMed:19033385}. Cytoplasm {ECO:0000250}.
Note=Accumulates in aggresomes under proteasome inhibition
conditions.
-!- TISSUE SPECIFICITY: Constitutively expressed in mature dendritic
cells and B-cells. Mostly expressed in the reticuloendothelial
system (e.g. thymus, spleen), the gastrointestinal system, kidney,
lung and prostate gland. {ECO:0000269|PubMed:12730673,
ECO:0000269|PubMed:9368598}.
-!- INDUCTION: Rapidly degraded by the proteasome. Cell-cycle
regulation with highest expression during the S-phase (at protein
level). Induced during dendritic cell maturation. Negatively
regulated by p53/TP53. High levels in various gastrointestinal and
gynecological cancer cells. Induced in RTECs in common renal
diseases including diabetic nephropathy (DN), IgA nephropathy
(IgAN), and hypertensive nephrosclerosis (HN), as well as in
hepatocellular carcinoma (HCC) and during HIVAN. Inducible by the
proinflammatory cytokines IFNG/IFN-gamma and TNF in cancers of
liver and colon. Repressed by NUB1 (at protein level).
{ECO:0000269|PubMed:12730673, ECO:0000269|PubMed:14757770,
ECO:0000269|PubMed:16495380, ECO:0000269|PubMed:16501612,
ECO:0000269|PubMed:16959044, ECO:0000269|PubMed:17889673,
ECO:0000269|PubMed:18574467, ECO:0000269|PubMed:19028597,
ECO:0000269|PubMed:19437562, ECO:0000269|PubMed:19726511,
ECO:0000269|PubMed:19959714}.
-!- PTM: Can be acetylated. {ECO:0000269|PubMed:19033385}.
-!- MISCELLANEOUS: Common types of chronic kidney disease are
associated with tubulointerstitial up-regulation of FAT10. FAT10
may mediate NF-kappa-B activation and may promote
tubulointerstitial inflammation in chronic kidney diseases.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/UBDID43742ch6p22.html";
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EMBL; Y12653; CAA73200.1; -; mRNA.
EMBL; AF123050; AAD52982.1; -; mRNA.
EMBL; AL031983; CAA21458.1; -; Genomic_DNA.
EMBL; AL662826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL645936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR942274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03201.1; -; Genomic_DNA.
EMBL; BC012472; AAH12472.1; -; mRNA.
CCDS; CCDS4662.1; -.
RefSeq; NP_006389.2; NM_006398.3.
UniGene; Hs.44532; -.
PDB; 2MBE; NMR; -; A=8-82.
PDBsum; 2MBE; -.
ProteinModelPortal; O15205; -.
SMR; O15205; -.
BioGrid; 115791; 24.
IntAct; O15205; 6.
MINT; O15205; -.
STRING; 9606.ENSP00000366249; -.
iPTMnet; O15205; -.
PhosphoSitePlus; O15205; -.
BioMuta; UBD; -.
MaxQB; O15205; -.
PaxDb; O15205; -.
PeptideAtlas; O15205; -.
PRIDE; O15205; -.
DNASU; 10537; -.
Ensembl; ENST00000377050; ENSP00000366249; ENSG00000213886.
Ensembl; ENST00000383547; ENSP00000373039; ENSG00000206468.
Ensembl; ENST00000421519; ENSP00000396152; ENSG00000231968.
Ensembl; ENST00000432676; ENSP00000410416; ENSG00000228913.
GeneID; 10537; -.
KEGG; hsa:10537; -.
UCSC; uc003nmo.4; human.
CTD; 10537; -.
DisGeNET; 10537; -.
EuPathDB; HostDB:ENSG00000213886.3; -.
GeneCards; UBD; -.
HGNC; HGNC:18795; UBD.
HPA; HPA043710; -.
MIM; 606050; gene.
neXtProt; NX_O15205; -.
OpenTargets; ENSG00000213886; -.
PharmGKB; PA38682; -.
eggNOG; KOG0001; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00910000144359; -.
HOVERGEN; HBG101094; -.
InParanoid; O15205; -.
KO; K12157; -.
OMA; ETQIVTC; -.
OrthoDB; EOG091G178I; -.
PhylomeDB; O15205; -.
Reactome; R-HSA-8951664; Neddylation.
ChiTaRS; UBD; human.
GeneWiki; Ubiquitin_D; -.
GenomeRNAi; 10537; -.
PRO; PR:O15205; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000213886; -.
CleanEx; HS_UBD; -.
ExpressionAtlas; O15205; baseline and differential.
Genevisible; O15205; HS.
GO; GO:0016235; C:aggresome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
GO; GO:0070842; P:aggresome assembly; IDA:UniProtKB.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0032446; P:protein modification by small protein conjugation; NAS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
GO; GO:0034341; P:response to interferon-gamma; IEP:UniProtKB.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF00240; ubiquitin; 2.
PRINTS; PR00348; UBIQUITIN.
SMART; SM00213; UBQ; 2.
SUPFAM; SSF54236; SSF54236; 2.
PROSITE; PS50053; UBIQUITIN_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; Nucleus;
Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway.
CHAIN 1 165 Ubiquitin D.
/FTId=PRO_0000114893.
DOMAIN 6 81 Ubiquitin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 90 163 Ubiquitin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
SITE 164 165 Activation by thioester intermediate
formation with UBA6.
VARIANT 51 51 L -> S (in dbSNP:rs2076484).
/FTId=VAR_024273.
VARIANT 68 68 I -> T (in dbSNP:rs2076485).
/FTId=VAR_024274.
VARIANT 95 95 S -> P (in dbSNP:rs2076486).
/FTId=VAR_024275.
VARIANT 99 99 A -> G (in dbSNP:rs2076487).
/FTId=VAR_025401.
VARIANT 120 120 E -> K (in dbSNP:rs17184290).
/FTId=VAR_052693.
VARIANT 160 160 C -> S (in dbSNP:rs8337).
{ECO:0000269|PubMed:10200259,
ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:9368598,
ECO:0000269|Ref.4}.
/FTId=VAR_025402.
VARIANT 162 162 C -> F (in dbSNP:rs7757931).
/FTId=VAR_024276.
MUTAGEN 11 11 H->D: Decreases interaction with MAD2L1,
no effect on the interaction with HDAC6,
UBA6, NUB1 and SQSTM1 and moderately
attenuates UBD-induced tumor formation in
vivo; when associated with Q-13. Complete
loss of interaction with MAD2L1, no
effect on the interaction with TP53/p53,
HDAC6, UBA6, NUB1 and SQSTM1 and
significantly attenuates UBD-induced
tumor formation in vivo; when associated
with Q-13; D-75; D-77 and Q-79.
{ECO:0000269|PubMed:25422469}.
MUTAGEN 13 13 R->Q: Decreases interaction with MAD2L1,
no effect on the interaction with HDAC6,
UBA6, NUB1 and SQSTM1 and moderately
attenuates UBD-induced tumor formation in
vivo; when associated with D-11. Complete
loss of interaction with MAD2L1, no
effect on the interaction with TP53/p53,
HDAC6, UBA6, NUB1 and SQSTM1 and
significantly attenuates UBD-induced
tumor formation in vivo; when associated
with D-11; D-75; D-77 and Q-79.
{ECO:0000269|PubMed:25422469}.
MUTAGEN 75 75 H->D: Decreases interaction with MAD2L1,
no effect on the interaction with HDAC6,
UBA6, NUB1 and SQSTM1 and moderately
attenuates UBD-induced tumor formation in
vivo; when associated with D-77 and Q-79.
Complete loss of interaction with MAD2L1,
no effect on the interaction with
TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1
and significantly attenuates UBD-induced
tumor formation in vivo; when associated
with D-11; Q-13; D-77 and Q-79.
{ECO:0000269|PubMed:25422469}.
MUTAGEN 77 77 T->D: Decreases interaction with MAD2L1,
no effect on the interaction with HDAC6,
UBA6, NUB1 and SQSTM1 and moderately
attenuates UBD-induced tumor formation in
vivo; when associated with D-75 and Q-79.
Complete loss of interaction with MAD2L1,
no effect on the interaction with
TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1
and significantly attenuates UBD-induced
tumor formation in vivo; when associated
with D-11; Q-13; D-75 and Q-79.
{ECO:0000269|PubMed:25422469}.
MUTAGEN 79 79 K->Q: Decreases interaction with MAD2L1,
no effect on the interaction with HDAC6,
UBA6, NUB1 and SQSTM1 and moderately
attenuates UBD-induced tumor formation in
vivo; when associated with D-75 and D-77.
Complete loss of interaction with MAD2L1,
no effect on the interaction with
TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1
and significantly attenuates UBD-induced
tumor formation in vivo; when associated
with D-11; Q-13; D-75 and D-77.
{ECO:0000269|PubMed:25422469}.
MUTAGEN 164 165 GG->AA: Impaired thioester formation-
mediated activation by UBA6. Loss of
interaction with UBA6 and SQSTM1. No
effect on its interaction with MAD2L1,
HDAC6 and NUB1.
{ECO:0000269|PubMed:17889673,
ECO:0000269|PubMed:25422469}.
STRAND 9 15 {ECO:0000244|PDB:2MBE}.
HELIX 30 35 {ECO:0000244|PDB:2MBE}.
STRAND 38 44 {ECO:0000244|PDB:2MBE}.
STRAND 47 60 {ECO:0000244|PDB:2MBE}.
STRAND 74 79 {ECO:0000244|PDB:2MBE}.
SEQUENCE 165 AA; 18473 MW; 40BE415049920CC6 CRC64;
MAPNASCLCV HVRSEEWDLM TFDANPYDSV KKIKEHVRSK TKVPVQDQVL LLGSKILKPR
RSLSSYGIDK EKTIHLTLKV VKPSDEELPL FLVESGDEAK RHLLQVRRSS SVAQVKAMIE
TKTGIIPETQ IVTCNGKRLE DGKMMADYGI RKGNLLFLAC YCIGG


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