Full text data of UBQLN4
UBQLN4
(C1orf6, CIP75, UBIN)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein; A1Up; Ataxin-1 ubiquitin-like-interacting protein A1U; Connexin43-interacting protein of 75 kDa; CIP75)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein; A1Up; Ataxin-1 ubiquitin-like-interacting protein A1U; Connexin43-interacting protein of 75 kDa; CIP75)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NRR5
ID UBQL4_HUMAN Reviewed; 601 AA.
AC Q9NRR5; A6ND44; B2RAY7; Q5VYA0; Q5VYA1; Q9BR98; Q9UHX4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Ubiquilin-4;
DE AltName: Full=Ataxin-1 interacting ubiquitin-like protein;
DE Short=A1Up;
DE AltName: Full=Ataxin-1 ubiquitin-like-interacting protein A1U;
DE AltName: Full=Connexin43-interacting protein of 75 kDa;
DE Short=CIP75;
GN Name=UBQLN4; Synonyms=C1orf6, CIP75, UBIN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP INTERACTION WITH ATXN1/SCA1, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11001934;
RA Davidson J.D., Riley B., Burright E.N., Duvick L.A., Zoghbi H.Y.,
RA Orr H.T.;
RT "Identification and characterization of an ataxin-1-interacting
RT protein: A1Up, a ubiquitin-like nuclear protein.";
RL Hum. Mol. Genet. 9:2305-2312(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP MET-495.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Colon, and PNS;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-601 (ISOFORM 1), AND VARIANT
RP MET-495.
RX PubMed=10575211;
RA Fogli A., Giglio S., Lo Nigro C., Zollo M., Viggiano L., Rocchi M.,
RA Archidiacono N., Zuffardi O., Carrozzo R.;
RT "Identification of two paralogous regions mapping to the short and
RT long arms of human chromosome 2 comprising LIS1 pseudogenes.";
RL Cytogenet. Cell Genet. 86:225-232(1999).
RN [6]
RP FUNCTION, INTERACTION WITH UBIQUITIN; ATXN1 AND PSMD4, SUBUNIT,
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=15280365; DOI=10.1074/jbc.M406284200;
RA Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.;
RT "The effects of the polyglutamine repeat protein ataxin-1 on the UbL-
RT UBA protein A1Up.";
RL J. Biol. Chem. 279:42290-42301(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role in the regulation of proteasomal protein
CC degradation. Depending on the case, may promote or inhibit
CC proteasomal protein degradation.
CC -!- SUBUNIT: Binds signal sequences of proteins that are targeted to
CC the endoplasmic reticulum. Interacts (via UBA domain) with GJA1
CC (not ubiquitinated) and with ubiquitin; both compete for the same
CC binding site (By similarity). Homodimer. Interacts (via UBA
CC domain) with ubiquitin and with polyubiquitin chains. Interacts
CC (via ubiquitin-like domain) with PSMD4, a regulatory subunit of
CC the 26S proteasome. Interacts with ATXN1/SCA1. Interaction with
CC ATXN1 inhibits polyubiquitination of UBQLN4 and interferes with
CC PSMD4 binding.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-711226, EBI-711226;
CC P54253:ATXN1; NbExp=6; IntAct=EBI-711226, EBI-930964;
CC P26885:FKBP2; NbExp=2; IntAct=EBI-711226, EBI-719873;
CC Q9H492:MAP1LC3A; NbExp=3; IntAct=EBI-711226, EBI-720768;
CC P55198:MLLT6; NbExp=2; IntAct=EBI-711226, EBI-740216;
CC Q9NR12:PDLIM7; NbExp=2; IntAct=EBI-711226, EBI-350517;
CC Q9Y5P3:RAI2; NbExp=3; IntAct=EBI-711226, EBI-746228;
CC Q13049:TRIM32; NbExp=3; IntAct=EBI-711226, EBI-742790;
CC Q9UMX0:UBQLN1; NbExp=8; IntAct=EBI-711226, EBI-741480;
CC O95201:ZNF205; NbExp=2; IntAct=EBI-711226, EBI-747343;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum
CC (Probable). Cytoplasm, perinuclear region (By similarity).
CC Note=Colocalizes with the proteasome, both in nucleus and
CC cytoplasm. May associate with the endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRR5-2; Sequence=VSP_041187, VSP_041188;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, kidney, skeletal
CC muscle, heart and throughout the brain, and at lower levels in
CC placenta, lung and liver.
CC -!- PTM: Ubiquitinated; this does not lead to proteasomal degradation.
CC May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19084.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=AAH06410.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF188240; AAF80171.1; -; mRNA.
DR EMBL; AK098368; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK314413; BAG37034.1; -; mRNA.
DR EMBL; AL355388; CAH72633.1; -; Genomic_DNA.
DR EMBL; AL355388; CAH72634.1; -; Genomic_DNA.
DR EMBL; BC006410; AAH06410.1; ALT_INIT; mRNA.
DR EMBL; BC018403; AAH18403.1; -; mRNA.
DR EMBL; BC063841; AAH63841.1; -; mRNA.
DR EMBL; AF113544; AAF19084.1; ALT_INIT; mRNA.
DR RefSeq; NP_064516.2; NM_020131.3.
DR UniGene; Hs.283739; -.
DR ProteinModelPortal; Q9NRR5; -.
DR SMR; Q9NRR5; 13-83, 555-601.
DR IntAct; Q9NRR5; 150.
DR MINT; MINT-1373057; -.
DR STRING; 9606.ENSP00000357292; -.
DR PhosphoSite; Q9NRR5; -.
DR DMDM; 45476982; -.
DR PaxDb; Q9NRR5; -.
DR PRIDE; Q9NRR5; -.
DR Ensembl; ENST00000368307; ENSP00000357290; ENSG00000160803.
DR Ensembl; ENST00000368309; ENSP00000357292; ENSG00000160803.
DR GeneID; 56893; -.
DR KEGG; hsa:56893; -.
DR UCSC; uc001fna.3; human.
DR CTD; 56893; -.
DR GeneCards; GC01M156005; -.
DR HGNC; HGNC:1237; UBQLN4.
DR HPA; HPA027920; -.
DR MIM; 605440; gene.
DR neXtProt; NX_Q9NRR5; -.
DR PharmGKB; PA25619; -.
DR eggNOG; COG5272; -.
DR HOVERGEN; HBG064537; -.
DR InParanoid; Q9NRR5; -.
DR KO; K04523; -.
DR OMA; FGMSRTT; -.
DR OrthoDB; EOG7HF1J8; -.
DR PhylomeDB; Q9NRR5; -.
DR ChiTaRS; UBQLN4; human.
DR GenomeRNAi; 56893; -.
DR NextBio; 62315; -.
DR PRO; PR:Q9NRR5; -.
DR Bgee; Q9NRR5; -.
DR CleanEx; HS_UBQLN4; -.
DR Genevestigator; Q9NRR5; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR015496; Ubiquilin.
DR InterPro; IPR000626; Ubiquitin_dom.
DR PANTHER; PTHR10677; PTHR10677; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 4.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Endoplasmic reticulum; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 601 Ubiquilin-4.
FT /FTId=PRO_0000211015.
FT DOMAIN 13 87 Ubiquitin-like.
FT DOMAIN 553 598 UBA.
FT MOD_RES 98 98 Phosphoserine.
FT VAR_SEQ 93 226 AATASSPSTPDPASAPSTTPASPATPAQPSTSGSASSDAGS
FT GSRRSSGGGPSPGAGEGSPSATASILSGFGGILGLGSLGLG
FT SANFMELQQQMQRQLMSNPEMLSQIMENPLVQDMMSNPDLM
FT RHMIMANPQMQ -> PPAAPSLPAADAEPRVTLHPYQSPSH
FT AGIAADPAGTTDLADRGPWAGTQPWLLWDIPDPSTLSRQQR
FT RVYARGPHFLTSHASHIFSNRGFQRPAATHAADDPAFGWKW
FT KLTGADARSEISAAAGAAQLHGLHQS (in isoform
FT 2).
FT /FTId=VSP_041187.
FT VAR_SEQ 227 601 Missing (in isoform 2).
FT /FTId=VSP_041188.
FT VARIANT 495 495 I -> M (in dbSNP:rs2297792).
FT /FTId=VAR_052685.
FT CONFLICT 188 189 QL -> HV (in Ref. 1; AAF80171).
FT CONFLICT 298 298 R -> Q (in Ref. 1; AAF80171).
SQ 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
//
ID UBQL4_HUMAN Reviewed; 601 AA.
AC Q9NRR5; A6ND44; B2RAY7; Q5VYA0; Q5VYA1; Q9BR98; Q9UHX4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Ubiquilin-4;
DE AltName: Full=Ataxin-1 interacting ubiquitin-like protein;
DE Short=A1Up;
DE AltName: Full=Ataxin-1 ubiquitin-like-interacting protein A1U;
DE AltName: Full=Connexin43-interacting protein of 75 kDa;
DE Short=CIP75;
GN Name=UBQLN4; Synonyms=C1orf6, CIP75, UBIN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP INTERACTION WITH ATXN1/SCA1, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11001934;
RA Davidson J.D., Riley B., Burright E.N., Duvick L.A., Zoghbi H.Y.,
RA Orr H.T.;
RT "Identification and characterization of an ataxin-1-interacting
RT protein: A1Up, a ubiquitin-like nuclear protein.";
RL Hum. Mol. Genet. 9:2305-2312(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP MET-495.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Colon, and PNS;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-601 (ISOFORM 1), AND VARIANT
RP MET-495.
RX PubMed=10575211;
RA Fogli A., Giglio S., Lo Nigro C., Zollo M., Viggiano L., Rocchi M.,
RA Archidiacono N., Zuffardi O., Carrozzo R.;
RT "Identification of two paralogous regions mapping to the short and
RT long arms of human chromosome 2 comprising LIS1 pseudogenes.";
RL Cytogenet. Cell Genet. 86:225-232(1999).
RN [6]
RP FUNCTION, INTERACTION WITH UBIQUITIN; ATXN1 AND PSMD4, SUBUNIT,
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=15280365; DOI=10.1074/jbc.M406284200;
RA Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.;
RT "The effects of the polyglutamine repeat protein ataxin-1 on the UbL-
RT UBA protein A1Up.";
RL J. Biol. Chem. 279:42290-42301(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role in the regulation of proteasomal protein
CC degradation. Depending on the case, may promote or inhibit
CC proteasomal protein degradation.
CC -!- SUBUNIT: Binds signal sequences of proteins that are targeted to
CC the endoplasmic reticulum. Interacts (via UBA domain) with GJA1
CC (not ubiquitinated) and with ubiquitin; both compete for the same
CC binding site (By similarity). Homodimer. Interacts (via UBA
CC domain) with ubiquitin and with polyubiquitin chains. Interacts
CC (via ubiquitin-like domain) with PSMD4, a regulatory subunit of
CC the 26S proteasome. Interacts with ATXN1/SCA1. Interaction with
CC ATXN1 inhibits polyubiquitination of UBQLN4 and interferes with
CC PSMD4 binding.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-711226, EBI-711226;
CC P54253:ATXN1; NbExp=6; IntAct=EBI-711226, EBI-930964;
CC P26885:FKBP2; NbExp=2; IntAct=EBI-711226, EBI-719873;
CC Q9H492:MAP1LC3A; NbExp=3; IntAct=EBI-711226, EBI-720768;
CC P55198:MLLT6; NbExp=2; IntAct=EBI-711226, EBI-740216;
CC Q9NR12:PDLIM7; NbExp=2; IntAct=EBI-711226, EBI-350517;
CC Q9Y5P3:RAI2; NbExp=3; IntAct=EBI-711226, EBI-746228;
CC Q13049:TRIM32; NbExp=3; IntAct=EBI-711226, EBI-742790;
CC Q9UMX0:UBQLN1; NbExp=8; IntAct=EBI-711226, EBI-741480;
CC O95201:ZNF205; NbExp=2; IntAct=EBI-711226, EBI-747343;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum
CC (Probable). Cytoplasm, perinuclear region (By similarity).
CC Note=Colocalizes with the proteasome, both in nucleus and
CC cytoplasm. May associate with the endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRR5-2; Sequence=VSP_041187, VSP_041188;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, kidney, skeletal
CC muscle, heart and throughout the brain, and at lower levels in
CC placenta, lung and liver.
CC -!- PTM: Ubiquitinated; this does not lead to proteasomal degradation.
CC May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19084.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=AAH06410.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF188240; AAF80171.1; -; mRNA.
DR EMBL; AK098368; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK314413; BAG37034.1; -; mRNA.
DR EMBL; AL355388; CAH72633.1; -; Genomic_DNA.
DR EMBL; AL355388; CAH72634.1; -; Genomic_DNA.
DR EMBL; BC006410; AAH06410.1; ALT_INIT; mRNA.
DR EMBL; BC018403; AAH18403.1; -; mRNA.
DR EMBL; BC063841; AAH63841.1; -; mRNA.
DR EMBL; AF113544; AAF19084.1; ALT_INIT; mRNA.
DR RefSeq; NP_064516.2; NM_020131.3.
DR UniGene; Hs.283739; -.
DR ProteinModelPortal; Q9NRR5; -.
DR SMR; Q9NRR5; 13-83, 555-601.
DR IntAct; Q9NRR5; 150.
DR MINT; MINT-1373057; -.
DR STRING; 9606.ENSP00000357292; -.
DR PhosphoSite; Q9NRR5; -.
DR DMDM; 45476982; -.
DR PaxDb; Q9NRR5; -.
DR PRIDE; Q9NRR5; -.
DR Ensembl; ENST00000368307; ENSP00000357290; ENSG00000160803.
DR Ensembl; ENST00000368309; ENSP00000357292; ENSG00000160803.
DR GeneID; 56893; -.
DR KEGG; hsa:56893; -.
DR UCSC; uc001fna.3; human.
DR CTD; 56893; -.
DR GeneCards; GC01M156005; -.
DR HGNC; HGNC:1237; UBQLN4.
DR HPA; HPA027920; -.
DR MIM; 605440; gene.
DR neXtProt; NX_Q9NRR5; -.
DR PharmGKB; PA25619; -.
DR eggNOG; COG5272; -.
DR HOVERGEN; HBG064537; -.
DR InParanoid; Q9NRR5; -.
DR KO; K04523; -.
DR OMA; FGMSRTT; -.
DR OrthoDB; EOG7HF1J8; -.
DR PhylomeDB; Q9NRR5; -.
DR ChiTaRS; UBQLN4; human.
DR GenomeRNAi; 56893; -.
DR NextBio; 62315; -.
DR PRO; PR:Q9NRR5; -.
DR Bgee; Q9NRR5; -.
DR CleanEx; HS_UBQLN4; -.
DR Genevestigator; Q9NRR5; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR015496; Ubiquilin.
DR InterPro; IPR000626; Ubiquitin_dom.
DR PANTHER; PTHR10677; PTHR10677; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 4.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Endoplasmic reticulum; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 601 Ubiquilin-4.
FT /FTId=PRO_0000211015.
FT DOMAIN 13 87 Ubiquitin-like.
FT DOMAIN 553 598 UBA.
FT MOD_RES 98 98 Phosphoserine.
FT VAR_SEQ 93 226 AATASSPSTPDPASAPSTTPASPATPAQPSTSGSASSDAGS
FT GSRRSSGGGPSPGAGEGSPSATASILSGFGGILGLGSLGLG
FT SANFMELQQQMQRQLMSNPEMLSQIMENPLVQDMMSNPDLM
FT RHMIMANPQMQ -> PPAAPSLPAADAEPRVTLHPYQSPSH
FT AGIAADPAGTTDLADRGPWAGTQPWLLWDIPDPSTLSRQQR
FT RVYARGPHFLTSHASHIFSNRGFQRPAATHAADDPAFGWKW
FT KLTGADARSEISAAAGAAQLHGLHQS (in isoform
FT 2).
FT /FTId=VSP_041187.
FT VAR_SEQ 227 601 Missing (in isoform 2).
FT /FTId=VSP_041188.
FT VARIANT 495 495 I -> M (in dbSNP:rs2297792).
FT /FTId=VAR_052685.
FT CONFLICT 188 189 QL -> HV (in Ref. 1; AAF80171).
FT CONFLICT 298 298 R -> Q (in Ref. 1; AAF80171).
SQ 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
//
MIM
605440
*RECORD*
*FIELD* NO
605440
*FIELD* TI
*605440 UBIQUILIN 4; UBQLN4
;;ATAXIN-1 UBIQUITIN-LIKE INTERACTING PROTEIN; A1U;;
C1ORF6;;
read moreCONNEXIN 43-INTERACTING PROTEIN, 75-KD; CIP75
*FIELD* TX
CLONING
By a yeast 2-hybrid screen of an adult human brain cDNA library,
Davidson et al. (2000) isolated cDNA clones which they used to assemble
a complete cDNA encoding the 601-amino acid ataxin-1 ubiquitin-like
interacting protein (A1U). Sequence comparison revealed that A1U
contains an N-terminal ubiquitin-like region, placing it within a large
family of similar proteins. In addition, A1U shows substantial homology
to human UBQLN2 (300264), a protein that binds the ATPase domain of the
HSP70-like STCH protein (601100). Expression analyses demonstrated that
A1U mRNA is widely expressed as a 4.0-kb transcript and is present in
Purkinje cells, the primary site of spinocerebellar ataxia-1 (SCA1;
164400) cerebellar pathology. The A1U protein localized to the nucleus
and cytoplasm of transfected COS-1 cells. Sequences important for the
transport of A1U into the nucleus appeared to lie within the C terminus.
In the nucleus, A1U colocalized with mutant ataxin-1 (ATX1; 601556),
further demonstrating that A1U interacts with ataxin-1.
Using Northern and Western blot analyses, Su et al. (2010) detected
variable Cip75 mRNA and protein expression in all mouse tissues
examined.
GENE FUNCTION
Davidson et al. (2000) suggested that A1U may link ataxin-1 with the
chaperone and ubiquitin/proteasome pathways and that ataxin-1 may
function in the formation and regulation of multimeric protein complexes
within the nucleus.
Monoubiquitination usually marks proteins for endocytosis, whereas
lys48-linked tetraubiquitination typically marks proteins for
proteasomal degradation. Su et al. (2010) showed that mouse Cip75
interacted with both synthetic monoubiquitinated and tetraubiquitinated
proteins in vitro and with a host of endogenous ubiquitinated proteins
in HeLa cell lysates. Cip75 also interacted with nonubiquitinated Cx43
(GJA1; 121014) in the endoplasmic reticulum. Even in the absence of Cx43
ubiquitination, Cip75 stimulated Cx43 proteasomal degradation.
MAPPING
Davidson et al. (2000) found that AIU (UBQLN4) is the same as C1orf6,
which was mapped by FISH to chromosome 1q21 by Fogli et al. (1999).
*FIELD* RF
1. 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. Molec. Genet. 9:
2305-2312, 2000.
2. Fogli, A.; Giglio, S.; Arrigo, G.; 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.
3. Su, V.; Nakagawa, R.; Koval, M.; Lau, A. F.: Ubiquitin-independent
proteasomal degradation of endoplasmic reticulum-localized connexin43
mediated by CIP75. J. Biol. Chem. 285: 40979-40990, 2010.
*FIELD* CN
Patricia A. Hartz - updated: 10/21/2011
*FIELD* CD
George E. Tiller: 11/30/2000
*FIELD* ED
mgross: 10/27/2011
terry: 10/21/2011
alopez: 5/6/2008
carol: 4/25/2002
joanna: 12/1/2000
carol: 11/30/2000
*RECORD*
*FIELD* NO
605440
*FIELD* TI
*605440 UBIQUILIN 4; UBQLN4
;;ATAXIN-1 UBIQUITIN-LIKE INTERACTING PROTEIN; A1U;;
C1ORF6;;
read moreCONNEXIN 43-INTERACTING PROTEIN, 75-KD; CIP75
*FIELD* TX
CLONING
By a yeast 2-hybrid screen of an adult human brain cDNA library,
Davidson et al. (2000) isolated cDNA clones which they used to assemble
a complete cDNA encoding the 601-amino acid ataxin-1 ubiquitin-like
interacting protein (A1U). Sequence comparison revealed that A1U
contains an N-terminal ubiquitin-like region, placing it within a large
family of similar proteins. In addition, A1U shows substantial homology
to human UBQLN2 (300264), a protein that binds the ATPase domain of the
HSP70-like STCH protein (601100). Expression analyses demonstrated that
A1U mRNA is widely expressed as a 4.0-kb transcript and is present in
Purkinje cells, the primary site of spinocerebellar ataxia-1 (SCA1;
164400) cerebellar pathology. The A1U protein localized to the nucleus
and cytoplasm of transfected COS-1 cells. Sequences important for the
transport of A1U into the nucleus appeared to lie within the C terminus.
In the nucleus, A1U colocalized with mutant ataxin-1 (ATX1; 601556),
further demonstrating that A1U interacts with ataxin-1.
Using Northern and Western blot analyses, Su et al. (2010) detected
variable Cip75 mRNA and protein expression in all mouse tissues
examined.
GENE FUNCTION
Davidson et al. (2000) suggested that A1U may link ataxin-1 with the
chaperone and ubiquitin/proteasome pathways and that ataxin-1 may
function in the formation and regulation of multimeric protein complexes
within the nucleus.
Monoubiquitination usually marks proteins for endocytosis, whereas
lys48-linked tetraubiquitination typically marks proteins for
proteasomal degradation. Su et al. (2010) showed that mouse Cip75
interacted with both synthetic monoubiquitinated and tetraubiquitinated
proteins in vitro and with a host of endogenous ubiquitinated proteins
in HeLa cell lysates. Cip75 also interacted with nonubiquitinated Cx43
(GJA1; 121014) in the endoplasmic reticulum. Even in the absence of Cx43
ubiquitination, Cip75 stimulated Cx43 proteasomal degradation.
MAPPING
Davidson et al. (2000) found that AIU (UBQLN4) is the same as C1orf6,
which was mapped by FISH to chromosome 1q21 by Fogli et al. (1999).
*FIELD* RF
1. 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. Molec. Genet. 9:
2305-2312, 2000.
2. Fogli, A.; Giglio, S.; Arrigo, G.; 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.
3. Su, V.; Nakagawa, R.; Koval, M.; Lau, A. F.: Ubiquitin-independent
proteasomal degradation of endoplasmic reticulum-localized connexin43
mediated by CIP75. J. Biol. Chem. 285: 40979-40990, 2010.
*FIELD* CN
Patricia A. Hartz - updated: 10/21/2011
*FIELD* CD
George E. Tiller: 11/30/2000
*FIELD* ED
mgross: 10/27/2011
terry: 10/21/2011
alopez: 5/6/2008
carol: 4/25/2002
joanna: 12/1/2000
carol: 11/30/2000