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Ubiquitin carboxyl-terminal hydrolase MINDY-1 (EC 3.4.19.12) (Deubiquitinating enzyme MINDY-1) (Protein FAM63A)

 MINY1_HUMAN             Reviewed;         469 AA.
Q8N5J2; B3KWP4; B3KWV8; B4DXF2; B4E1S4; D3DV09; J3KP53; Q5SZF0;
Q9NUL9; Q9P2F7;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 2.
27-SEP-2017, entry version 119.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-1 {ECO:0000303|PubMed:27292798};
EC=3.4.19.12 {ECO:0000269|PubMed:27292798};
AltName: Full=Deubiquitinating enzyme MINDY-1 {ECO:0000303|PubMed:27292798};
AltName: Full=Protein FAM63A;
Name=MINDY1 {ECO:0000312|HGNC:HGNC:25648}; Synonyms=FAM63A, KIAA1390;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LYS-385.
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
VARIANT LYS-385.
TISSUE=Placenta, Testis, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-385.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LYS-385.
TISSUE=Brain;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-441, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 110-384, X-RAY
CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 110-384 IN COMPLEX WITH UBIQUITIN,
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-131; CYS-137;
ASP-209; VAL-210; TRP-240; TYR-258; GLU-263; PHE-315; HIS-319 AND
415-LEU-ALA-416, AND GENE FAMILY.
PubMed=27292798; DOI=10.1016/j.molcel.2016.05.009;
Abdul Rehman S.A., Kristariyanto Y.A., Choi S.Y., Nkosi P.J.,
Weidlich S., Labib K., Hofmann K., Kulathu Y.;
"MINDY-1 is a member of an evolutionarily conserved and structurally
distinct new family of deubiquitinating enzymes.";
Mol. Cell 63:146-155(2016).
[10]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 388-426 IN COMPLEX WITH
UBIQUITIN, BINDING TO 'LYS-47' POLYUBIQUITIN CHAINS, AND MUTAGENESIS
OF ALA-396; LEU-408; THR-411; ASP-412; LEU-413; GLU-414; LEU-415;
ALA-416; GLN-418; LEU-419; GLN-420; GLN-421; GLU-422; GLU-423 AND
TYR-424.
PubMed=28082312; DOI=10.15252/embr.201643205;
Kristariyanto Y.A., Abdul Rehman S.A., Weidlich S., Knebel A.,
Kulathu Y.;
"A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin
chains.";
EMBO Rep. 18:392-402(2017).
-!- FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked
conjugated ubiquitin from proteins. Has exodeubiquitinase activity
and has a preference for long polyubiquitin chains. May play a
regulatory role at the level of protein turnover.
{ECO:0000269|PubMed:27292798, ECO:0000269|PubMed:28082312}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000269|PubMed:27292798}.
-!- INTERACTION:
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-372322, EBI-10172181;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8N5J2-1; Sequence=Displayed;
Name=2;
IsoId=Q8N5J2-2; Sequence=VSP_034715;
Name=3;
IsoId=Q8N5J2-3; Sequence=VSP_037077;
Note=Ref.2 (BAG63364) sequence is in conflict in position:
44:K->E. {ECO:0000305};
Name=4;
IsoId=Q8N5J2-4; Sequence=VSP_037076;
-!- SIMILARITY: Belongs to the peptidase MINDY family. FAM63
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA92628.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB037811; BAA92628.1; ALT_INIT; mRNA.
EMBL; AK002142; BAA92104.1; -; mRNA.
EMBL; AK125493; BAG54206.1; -; mRNA.
EMBL; AK125959; BAG54270.1; -; mRNA.
EMBL; AK301946; BAG63364.1; -; mRNA.
EMBL; AK303962; BAG64886.1; -; mRNA.
EMBL; AL590133; CAI13336.1; -; Genomic_DNA.
EMBL; CH471121; EAW53491.1; -; Genomic_DNA.
EMBL; CH471121; EAW53492.1; -; Genomic_DNA.
EMBL; CH471121; EAW53493.1; -; Genomic_DNA.
EMBL; CH471121; EAW53495.1; -; Genomic_DNA.
EMBL; BC032321; AAH32321.1; -; mRNA.
CCDS; CCDS30854.1; -. [Q8N5J2-2]
CCDS; CCDS53361.1; -. [Q8N5J2-3]
CCDS; CCDS55635.1; -. [Q8N5J2-4]
CCDS; CCDS976.1; -. [Q8N5J2-1]
RefSeq; NP_001035307.1; NM_001040217.2.
RefSeq; NP_001156730.1; NM_001163258.1.
RefSeq; NP_001156731.1; NM_001163259.1.
RefSeq; NP_001156732.1; NM_001163260.1.
RefSeq; NP_001306927.1; NM_001319998.1.
RefSeq; NP_060849.2; NM_018379.4.
RefSeq; XP_016857261.1; XM_017001772.1. [Q8N5J2-1]
RefSeq; XP_016857266.1; XM_017001777.1. [Q8N5J2-3]
UniGene; Hs.743952; -.
PDB; 5JKN; X-ray; 3.00 A; A=110-384.
PDB; 5JQS; X-ray; 2.65 A; A=110-384.
PDB; 5MN9; X-ray; 2.05 A; C=388-426.
PDBsum; 5JKN; -.
PDBsum; 5JQS; -.
PDBsum; 5MN9; -.
ProteinModelPortal; Q8N5J2; -.
SMR; Q8N5J2; -.
BioGrid; 120906; 21.
IntAct; Q8N5J2; 5.
STRING; 9606.ENSP00000354669; -.
iPTMnet; Q8N5J2; -.
PhosphoSitePlus; Q8N5J2; -.
BioMuta; FAM63A; -.
DMDM; 311033379; -.
EPD; Q8N5J2; -.
MaxQB; Q8N5J2; -.
PaxDb; Q8N5J2; -.
PeptideAtlas; Q8N5J2; -.
PRIDE; Q8N5J2; -.
TopDownProteomics; Q8N5J2-2; -. [Q8N5J2-2]
DNASU; 55793; -.
Ensembl; ENST00000312210; ENSP00000310923; ENSG00000143409. [Q8N5J2-2]
Ensembl; ENST00000361738; ENSP00000354669; ENSG00000143409. [Q8N5J2-3]
Ensembl; ENST00000361936; ENSP00000354814; ENSG00000143409. [Q8N5J2-1]
Ensembl; ENST00000493834; ENSP00000437174; ENSG00000143409. [Q8N5J2-4]
Ensembl; ENST00000622754; ENSP00000481304; ENSG00000143409. [Q8N5J2-1]
GeneID; 55793; -.
KEGG; hsa:55793; -.
UCSC; uc001ewd.4; human. [Q8N5J2-1]
CTD; 55793; -.
DisGeNET; 55793; -.
EuPathDB; HostDB:ENSG00000143409.15; -.
GeneCards; FAM63A; -.
H-InvDB; HIX0001041; -.
HGNC; HGNC:25648; MINDY1.
HPA; HPA028351; -.
HPA; HPA028358; -.
HPA; HPA061086; -.
neXtProt; NX_Q8N5J2; -.
OpenTargets; ENSG00000143409; -.
PharmGKB; PA142671872; -.
eggNOG; KOG2427; Eukaryota.
eggNOG; ENOG41102GM; LUCA.
GeneTree; ENSGT00390000016607; -.
HOVERGEN; HBG054318; -.
InParanoid; Q8N5J2; -.
OMA; VIPENHE; -.
OrthoDB; EOG091G0C4Y; -.
PhylomeDB; Q8N5J2; -.
TreeFam; TF314589; -.
ChiTaRS; FAM63A; human.
GenomeRNAi; 55793; -.
PRO; PR:Q8N5J2; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143409; -.
CleanEx; HS_FAM63A; -.
ExpressionAtlas; Q8N5J2; baseline and differential.
Genevisible; Q8N5J2; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IDA:UniProtKB.
GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:InterPro.
InterPro; IPR007518; MINDY.
InterPro; IPR033979; MINDY_domain.
PANTHER; PTHR18063; PTHR18063; 1.
Pfam; PF04424; MINDY_DUB; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Hydrolase;
Phosphoprotein; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway.
CHAIN 1 469 Ubiquitin carboxyl-terminal hydrolase
MINDY-1.
/FTId=PRO_0000344037.
REGION 388 426 Ubiquitin-binding domain (UBD).
{ECO:0000305|PubMed:27292798}.
COMPBIAS 386 431 Gln-rich.
ACT_SITE 137 137 Nucleophile.
{ECO:0000305|PubMed:27292798}.
ACT_SITE 319 319 Proton acceptor.
{ECO:0000305|PubMed:27292798}.
SITE 412 412 Ubiquitin-binding.
{ECO:0000269|PubMed:28082312}.
SITE 415 416 Ubiquitin-binding.
{ECO:0000269|PubMed:28082312}.
SITE 419 419 Ubiquitin-binding.
{ECO:0000269|PubMed:28082312}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 142 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_034715.
VAR_SEQ 1 95 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037076.
VAR_SEQ 1 1 M -> MLLGPPPFNESTKPSPSPCHSFASQAWLRQVPEVSK
HLQCPSAKSLLTM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037077.
VARIANT 385 385 T -> K (in dbSNP:rs2925741).
{ECO:0000269|PubMed:10718198,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_044541.
MUTAGEN 131 131 Q->A,E: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 137 137 C->A: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 209 209 D->A: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 210 210 V->A: Greatly impairs ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 240 240 W->A: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 258 258 Y->A: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 263 263 E->A: Greatly impairs ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 263 263 E->R: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 315 315 F->A: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 319 319 H->A: Abolishes ubiquitin hydrolase
activity. {ECO:0000269|PubMed:27292798}.
MUTAGEN 396 396 A->G: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 408 408 L->A: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 411 411 T->A: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 412 412 D->A: Loss of binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 413 413 L->A: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 414 414 E->A: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 415 416 LA->AG: Decreased association with 'Lys-
48'-linked conjugated ubiquitin.
{ECO:0000269|PubMed:27292798}.
MUTAGEN 415 415 L->A: Loss of binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 416 416 A->G,D: Loss of binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 416 416 A->S: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 418 418 Q->A,K: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 419 419 L->A: Loss of binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 420 420 Q->A: Loss of binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 421 421 Q->E,R: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 422 422 E->A: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 423 423 E->A: Loss of binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 423 423 E->EA,EAAA,EAAAAAA,EAAAAAAA: Loss of
binding to 'Lys-48' tetraubiquitin
chains. {ECO:0000269|PubMed:28082312}.
MUTAGEN 423 423 Missing: Loss of binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 424 424 Y->A,D,E: Decreased binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
MUTAGEN 424 424 Y->F,W: No effect on binding to 'Lys-48'
tetraubiquitin chains.
{ECO:0000269|PubMed:28082312}.
CONFLICT 287 287 L -> P (in Ref. 2; BAA92104).
{ECO:0000305}.
CONFLICT 367 367 S -> R (in Ref. 2; BAA92104).
{ECO:0000305}.
STRAND 113 121 {ECO:0000244|PDB:5JQS}.
STRAND 124 129 {ECO:0000244|PDB:5JQS}.
HELIX 137 148 {ECO:0000244|PDB:5JQS}.
STRAND 160 162 {ECO:0000244|PDB:5JQS}.
HELIX 163 174 {ECO:0000244|PDB:5JQS}.
HELIX 188 206 {ECO:0000244|PDB:5JQS}.
STRAND 208 210 {ECO:0000244|PDB:5JQS}.
HELIX 224 231 {ECO:0000244|PDB:5JQS}.
STRAND 236 239 {ECO:0000244|PDB:5JKN}.
HELIX 247 253 {ECO:0000244|PDB:5JQS}.
HELIX 258 270 {ECO:0000244|PDB:5JQS}.
HELIX 274 289 {ECO:0000244|PDB:5JQS}.
TURN 290 292 {ECO:0000244|PDB:5JQS}.
HELIX 296 305 {ECO:0000244|PDB:5JQS}.
STRAND 311 316 {ECO:0000244|PDB:5JQS}.
STRAND 319 326 {ECO:0000244|PDB:5JQS}.
STRAND 329 333 {ECO:0000244|PDB:5JQS}.
HELIX 337 339 {ECO:0000244|PDB:5JQS}.
STRAND 347 349 {ECO:0000244|PDB:5JQS}.
STRAND 353 355 {ECO:0000244|PDB:5JQS}.
HELIX 411 425 {ECO:0000244|PDB:5MN9}.
SEQUENCE 469 AA; 51778 MW; FEB658BAF8A878C6 CRC64;
MEYHQPEDPA PGKAGTAEAV IPENHEVLAG PDEHPQDTDA RDADGEARER EPADQALLPS
QCGDNLESPL PEASSAPPGP TLGTLPEVET IRACSMPQEL PQSPRTRQPE PDFYCVKWIP
WKGEQTPIIT QSTNGPCPLL AIMNILFLQW KVKLPPQKEV ITSDELMAHL GNCLLSIKPQ
EKSEGLQLNF QQNVDDAMTV LPKLATGLDV NVRFTGVSDF EYTPECSVFD LLGIPLYHGW
LVDPQSPEAV RAVGKLSYNQ LVERIITCKH SSDTNLVTEG LIAEQFLETT AAQLTYHGLC
ELTAAAKEGE LSVFFRNNHF STMTKHKSHL YLLVTDQGFL QEEQVVWESL HNVDGDSCFC
DSDFHLSHSL GKGPGAEGGS GSPETQLQVD QDYLIALSLQ QQQPRGPLGL TDLELAQQLQ
QEEYQQQQAA QPVRMRTRVL SLQGRGATSG RPAGERRQRP KHESDCILL


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