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Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein) (A1Up) (Ataxin-1 ubiquitin-like-interacting protein A1U) (Connexin43-interacting protein of 75 kDa) (CIP75)

 UBQL4_HUMAN             Reviewed;         601 AA.
Q9NRR5; A6ND44; B2RAY7; Q5VYA0; Q5VYA1; Q9BR98; Q9UHX4;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 2.
22-NOV-2017, entry version 150.
RecName: Full=Ubiquilin-4;
AltName: Full=Ataxin-1 interacting ubiquitin-like protein;
Short=A1Up;
AltName: Full=Ataxin-1 ubiquitin-like-interacting protein A1U;
AltName: Full=Connexin43-interacting protein of 75 kDa;
Short=CIP75;
Name=UBQLN4; Synonyms=C1orf6, CIP75, UBIN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
INTERACTION WITH ATXN1/SCA1, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11001934; DOI=10.1093/oxfordjournals.hmg.a018922;
Davidson J.D., Riley B., Burright E.N., Duvick L.A., Zoghbi H.Y.,
Orr H.T.;
"Identification and characterization of an ataxin-1-interacting
protein: A1Up, a ubiquitin-like nuclear protein.";
Hum. Mol. Genet. 9:2305-2312(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
MET-495.
TISSUE=Brain;
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 MRNA] (ISOFORM 1).
TISSUE=Brain, Colon, and PNS;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 161-601 (ISOFORM 1), AND VARIANT
MET-495.
PubMed=10575211;
Fogli A., Giglio S., Lo Nigro C., Zollo M., Viggiano L., Rocchi M.,
Archidiacono N., Zuffardi O., Carrozzo R.;
"Identification of two paralogous regions mapping to the short and
long arms of human chromosome 2 comprising LIS1 pseudogenes.";
Cytogenet. Cell Genet. 86:225-232(1999).
[6]
FUNCTION, INTERACTION WITH UBIQUITIN; ATXN1 AND PSMD4, SUBUNIT,
SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=15280365; DOI=10.1074/jbc.M406284200;
Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.;
"The effects of the polyglutamine repeat protein ataxin-1 on the UbL-
UBA protein A1Up.";
J. Biol. Chem. 279:42290-42301(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[8]
INTERACTION WITH HERPUD1.
PubMed=18307982; DOI=10.1016/j.bbrc.2008.02.086;
Kim T.Y., Kim E., Yoon S.K., Yoon J.B.;
"Herp enhances ER-associated protein degradation by recruiting
ubiquilins.";
Biochem. Biophys. Res. Commun. 369:741-746(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
INTERACTION WITH UBQLN1; UBQLN2 AND MAP1LC3A/B/C, AND MUTAGENESIS OF
ILE-55.
PubMed=23459205; DOI=10.1038/embor.2013.22;
Lee D.Y., Arnott D., Brown E.J.;
"Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the
autophagy machinery.";
EMBO Rep. 14:373-381(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, 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).
[13]
REVIEW.
PubMed=24674348; DOI=10.1186/1471-2148-14-63;
Marin I.;
"The ubiquilin gene family: evolutionary patterns and functional
insights.";
BMC Evol. Biol. 14:63-63(2014).
[14]
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).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-23 AND LYS-62, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Plays a role in the regulation of protein degradation
via the ubiquitin-proteasome system (UPS). Mediates the
proteasomal targeting of misfolded or accumulated proteins for
degradation by binding (via UBA domain) to their polyubiquitin
chains and by interacting (via ubiquitin-like domain) with the
subunits of the proteasome (Ref. 6). Plays a role in the
regulation of the proteasomal degradation of non-ubiquitinated
GJA1 (By similarity). Acts as an adapter protein that recruits
UBQLN1 to the autophagy machinery. Mediates the association of
UBQLN1 with autophagosomes and the autophagy-related protein LC3
(MAP1LC3A/B/C) and may assist in the maturation of autophagosomes
to autolysosomes by mediating autophagosome-lysosome fusion
(PubMed:23459205). {ECO:0000250|UniProtKB:Q99NB8,
ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:23459205}.
-!- SUBUNIT: Homooligomer (Ref. 6). Binds signal sequences of proteins
that are targeted to the endoplasmic reticulum. Interacts (via UBA
domain) with GJA1 (not ubiquitinated) and with ubiquitin; both
compete for the same binding site. Interacts (via UBA domain) with
ubiquitin and with polyubiquitin chains. Interacts with PSMD2 (By
similarity). Interacts (via ubiquitin-like domain) with PSMD4, a
regulatory subunit of the 26S proteasome. Interacts with
ATXN1/SCA1. Interaction with ATXN1 inhibits polyubiquitination of
UBQLN4 and interferes with PSMD4 binding. Interacts with HERPUD1.
Interacts (via ubiquitin-like domain) with UBQLN1 (via UBA
domain). Interacts (via STI1 1 and 2 domains) with MAP1LC3A/B/C.
Interacts with UBQLN2. {ECO:0000250|UniProtKB:Q99NB8,
ECO:0000269|PubMed:11001934, ECO:0000269|PubMed:15280365,
ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:23459205}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-711226, EBI-711226;
P54253:ATXN1; NbExp=6; IntAct=EBI-711226, EBI-930964;
P26885:FKBP2; NbExp=2; IntAct=EBI-711226, EBI-719873;
P08050:Gja1 (xeno); NbExp=2; IntAct=EBI-711226, EBI-476947;
Q9H492:MAP1LC3A; NbExp=3; IntAct=EBI-711226, EBI-720768;
P55198:MLLT6; NbExp=2; IntAct=EBI-711226, EBI-740216;
Q9NR12:PDLIM7; NbExp=2; IntAct=EBI-711226, EBI-350517;
Q9Y5P3:RAI2; NbExp=3; IntAct=EBI-711226, EBI-746228;
Q13049:TRIM32; NbExp=3; IntAct=EBI-711226, EBI-742790;
Q9UMX0:UBQLN1; NbExp=8; IntAct=EBI-711226, EBI-741480;
O95201:ZNF205; NbExp=2; IntAct=EBI-711226, EBI-747343;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11001934,
ECO:0000269|PubMed:15280365}. Cytoplasm
{ECO:0000269|PubMed:15280365}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q99NB8}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q99NB8}. Cytoplasmic vesicle, autophagosome
{ECO:0000269|PubMed:23459205}. Note=Colocalizes with the
proteasome, both in nucleus and cytoplasm.
{ECO:0000269|PubMed:15280365}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NRR5-1; Sequence=Displayed;
Name=2;
IsoId=Q9NRR5-2; Sequence=VSP_041187, VSP_041188;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas, kidney, skeletal
muscle, heart and throughout the brain, and at lower levels in
placenta, lung and liver. {ECO:0000269|PubMed:11001934}.
-!- PTM: Ubiquitinated; this does not lead to proteasomal degradation.
May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
{ECO:0000269|PubMed:15280365}.
-!- SEQUENCE CAUTION:
Sequence=AAF19084.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH06410.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF188240; AAF80171.1; -; mRNA.
EMBL; AK098368; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK314413; BAG37034.1; -; mRNA.
EMBL; AL355388; CAH72633.1; -; Genomic_DNA.
EMBL; AL355388; CAH72634.1; -; Genomic_DNA.
EMBL; BC006410; AAH06410.1; ALT_INIT; mRNA.
EMBL; BC018403; AAH18403.1; -; mRNA.
EMBL; BC063841; AAH63841.1; -; mRNA.
EMBL; AF113544; AAF19084.1; ALT_INIT; mRNA.
CCDS; CCDS1127.1; -. [Q9NRR5-1]
RefSeq; NP_001291271.1; NM_001304342.1.
RefSeq; NP_064516.2; NM_020131.4. [Q9NRR5-1]
UniGene; Hs.283739; -.
ProteinModelPortal; Q9NRR5; -.
SMR; Q9NRR5; -.
BioGrid; 121223; 191.
IntAct; Q9NRR5; 159.
MINT; MINT-1373057; -.
STRING; 9606.ENSP00000357292; -.
TCDB; 8.A.52.1.1; the ubiquitin-related protein degradation (upd) family.
iPTMnet; Q9NRR5; -.
PhosphoSitePlus; Q9NRR5; -.
BioMuta; UBQLN4; -.
DMDM; 45476982; -.
EPD; Q9NRR5; -.
MaxQB; Q9NRR5; -.
PaxDb; Q9NRR5; -.
PeptideAtlas; Q9NRR5; -.
PRIDE; Q9NRR5; -.
TopDownProteomics; Q9NRR5-2; -. [Q9NRR5-2]
Ensembl; ENST00000368309; ENSP00000357292; ENSG00000160803. [Q9NRR5-1]
GeneID; 56893; -.
KEGG; hsa:56893; -.
UCSC; uc001fna.4; human. [Q9NRR5-1]
CTD; 56893; -.
DisGeNET; 56893; -.
EuPathDB; HostDB:ENSG00000160803.7; -.
GeneCards; UBQLN4; -.
HGNC; HGNC:1237; UBQLN4.
HPA; HPA061797; -.
MIM; 605440; gene.
neXtProt; NX_Q9NRR5; -.
OpenTargets; ENSG00000160803; -.
PharmGKB; PA25619; -.
eggNOG; KOG0010; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00390000005720; -.
HOVERGEN; HBG064537; -.
InParanoid; Q9NRR5; -.
KO; K04523; -.
OMA; MISAPYM; -.
OrthoDB; EOG091G08WB; -.
PhylomeDB; Q9NRR5; -.
TreeFam; TF314412; -.
ChiTaRS; UBQLN4; human.
GenomeRNAi; 56893; -.
PRO; PR:Q9NRR5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160803; -.
CleanEx; HS_UBQLN4; -.
Genevisible; Q9NRR5; HS.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:1901097; P:negative regulation of autophagosome maturation; IMP:UniProtKB.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
InterPro; IPR006636; STI1_HS-bd.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR015496; Ubiquilin.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
PANTHER; PTHR10677; PTHR10677; 1.
Pfam; PF00627; UBA; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00727; STI1; 4.
SMART; SM00165; UBA; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50030; UBA; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
Alternative splicing; Autophagy; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Endoplasmic reticulum; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 601 Ubiquilin-4.
/FTId=PRO_0000211015.
DOMAIN 13 87 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 192 229 STI1 1. {ECO:0000255}.
DOMAIN 230 261 STI1 2. {ECO:0000255}.
DOMAIN 393 440 STI1 3. {ECO:0000255}.
DOMAIN 444 476 STI1 4. {ECO:0000255}.
DOMAIN 553 598 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 287 287 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 62 62 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 93 226 AATASSPSTPDPASAPSTTPASPATPAQPSTSGSASSDAGS
GSRRSSGGGPSPGAGEGSPSATASILSGFGGILGLGSLGLG
SANFMELQQQMQRQLMSNPEMLSQIMENPLVQDMMSNPDLM
RHMIMANPQMQ -> PPAAPSLPAADAEPRVTLHPYQSPSH
AGIAADPAGTTDLADRGPWAGTQPWLLWDIPDPSTLSRQQR
RVYARGPHFLTSHASHIFSNRGFQRPAATHAADDPAFGWKW
KLTGADARSEISAAAGAAQLHGLHQS (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_041187.
VAR_SEQ 227 601 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041188.
VARIANT 495 495 I -> M (in dbSNP:rs2297792).
{ECO:0000269|PubMed:10575211,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_052685.
MUTAGEN 55 55 I->A: Loss of interaction with UBQLN1.
CONFLICT 188 189 QL -> HV (in Ref. 1; AAF80171).
{ECO:0000305}.
CONFLICT 298 298 R -> Q (in Ref. 1; AAF80171).
{ECO:0000305}.
SEQUENCE 601 AA; 63853 MW; E57B9FFEF90793FE CRC64;
MAEPSGAETR PPIRVTVKTP KDKEEIVICD RASVKEFKEE ISRRFKAQQD QLVLIFAGKI
LKDGDTLNQH GIKDGLTVHL VIKTPQKAQD PAAATASSPS TPDPASAPST TPASPATPAQ
PSTSGSASSD AGSGSRRSSG GGPSPGAGEG SPSATASILS GFGGILGLGS LGLGSANFME
LQQQMQRQLM SNPEMLSQIM ENPLVQDMMS NPDLMRHMIM ANPQMQQLME RNPEISHMLN
NPELMRQTME LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMFSAAREQ
FGNNPFSSLA GNSDSSSSQP LRTENREPLP NPWSPSPPTS QAPGSGGEGT GGSGTSQVHP
TVSNPFGINA ASLGSGMFNS PEMQALLQQI SENPQLMQNV ISAPYMRSMM QTLAQNPDFA
AQMMVNVPLF AGNPQLQEQL RLQLPVFLQQ MQNPESLSIL TNPRAMQALL QIQQGLQTLQ
TEAPGLVPSL GSFGISRTPA PSAGSNAGST PEAPTSSPAT PATSSPTGAS SAQQQLMQQM
IQLLAGSGNS QVQTPEVRFQ QQLEQLNSMG FINREANLQA LIATGGDINA AIERLLGSQL
S


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