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Q9NRR5 (UBQL4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquilin-4
Alternative name(s):
Ataxin-1 interacting ubiquitin-like protein
Short name=A1Up
Ataxin-1 ubiquitin-like-interacting protein A1U
Connexin43-interacting protein of 75 kDa
Short name=CIP75
Gene names
Name:UBQLN4
Synonyms:C1orf6, CIP75, UBIN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the regulation of proteasomal protein degradation. Depending on the case, may promote or inhibit proteasomal protein degradation. Ref.6

Subunit structure

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 By similarity. Homodimer. Interacts (via UBA domain) with ubiquitin and with polyubiquitin chains. 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. Ref.1 Ref.6

Subcellular location

Nucleus. Cytoplasm. Endoplasmic reticulum Probable. Cytoplasmperinuclear region By similarity. Note: Colocalizes with the proteasome, both in nucleus and cytoplasm. May associate with the endoplasmic reticulum. Ref.1 Ref.6

Tissue specificity

Highly expressed in pancreas, kidney, skeletal muscle, heart and throughout the brain, and at lower levels in placenta, lung and liver. Ref.1

Post-translational modification

Ubiquitinated; this does not lead to proteasomal degradation. May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Ref.6

Sequence similarities

Contains 1 UBA domain.

Contains 1 ubiquitin-like domain.

Sequence caution

The sequence AAF19084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH06410.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRR5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NRR5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     93-226: AATASSPSTP...HMIMANPQMQ → PPAAPSLPAA...AAQLHGLHQS
     227-601: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Ubiquilin-4
PRO_0000211015

Regions

Domain13 – 8775Ubiquitin-like
Domain553 – 59846UBA

Amino acid modifications

Modified residue981Phosphoserine Ref.8

Natural variations

Alternative sequence93 – 226134AATAS…NPQMQ → PPAAPSLPAADAEPRVTLHP YQSPSHAGIAADPAGTTDLA DRGPWAGTQPWLLWDIPDPS TLSRQQRRVYARGPHFLTSH ASHIFSNRGFQRPAATHAAD DPAFGWKWKLTGADARSEIS AAAGAAQLHGLHQS in isoform 2.
VSP_041187
Alternative sequence227 – 601375Missing in isoform 2.
VSP_041188
Natural variant4951I → M. Ref.2 Ref.5
Corresponds to variant rs2297792 [ dbSNP | Ensembl ].
VAR_052685

Experimental info

Sequence conflict188 – 1892QL → HV in AAF80171. Ref.1
Sequence conflict2981R → Q in AAF80171. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: E57B9FFEF90793FE

FASTA60163,853
        10         20         30         40         50         60 
MAEPSGAETR PPIRVTVKTP KDKEEIVICD RASVKEFKEE ISRRFKAQQD QLVLIFAGKI 

        70         80         90        100        110        120 
LKDGDTLNQH GIKDGLTVHL VIKTPQKAQD PAAATASSPS TPDPASAPST TPASPATPAQ 

       130        140        150        160        170        180 
PSTSGSASSD AGSGSRRSSG GGPSPGAGEG SPSATASILS GFGGILGLGS LGLGSANFME 

       190        200        210        220        230        240 
LQQQMQRQLM SNPEMLSQIM ENPLVQDMMS NPDLMRHMIM ANPQMQQLME RNPEISHMLN 

       250        260        270        280        290        300 
NPELMRQTME LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMFSAAREQ 

       310        320        330        340        350        360 
FGNNPFSSLA GNSDSSSSQP LRTENREPLP NPWSPSPPTS QAPGSGGEGT GGSGTSQVHP 

       370        380        390        400        410        420 
TVSNPFGINA ASLGSGMFNS PEMQALLQQI SENPQLMQNV ISAPYMRSMM QTLAQNPDFA 

       430        440        450        460        470        480 
AQMMVNVPLF AGNPQLQEQL RLQLPVFLQQ MQNPESLSIL TNPRAMQALL QIQQGLQTLQ 

       490        500        510        520        530        540 
TEAPGLVPSL GSFGISRTPA PSAGSNAGST PEAPTSSPAT PATSSPTGAS SAQQQLMQQM 

       550        560        570        580        590        600 
IQLLAGSGNS QVQTPEVRFQ QQLEQLNSMG FINREANLQA LIATGGDINA AIERLLGSQL 


S 

« Hide

Isoform 2 [UniParc].

Checksum: 69101551F1551A93
Show »

FASTA22624,527

References

« Hide 'large scale' references
[1]"Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein."
Davidson J.D., Riley B., Burright E.N., Duvick L.A., Zoghbi H.Y., Orr H.T.
Hum. Mol. Genet. 9:2305-2312(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH ATXN1/SCA1, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT MET-495.
Tissue: Brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain, Colon and PNS.
[5]"Identification of two paralogous regions mapping to the short and long arms of human chromosome 2 comprising LIS1 pseudogenes."
Fogli A., Giglio S., Lo Nigro C., Zollo M., Viggiano L., Rocchi M., Archidiacono N., Zuffardi O., Carrozzo R.
Cytogenet. Cell Genet. 86:225-232(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-601 (ISOFORM 1), VARIANT MET-495.
[6]"The effects of the polyglutamine repeat protein ataxin-1 on the UbL-UBA protein A1Up."
Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.
J. Biol. Chem. 279:42290-42301(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBIQUITIN; ATXN1 AND PSMD4, SUBUNIT, SUBCELLULAR LOCATION, UBIQUITINATION.
[7]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF188240 mRNA. Translation: AAF80171.1.
AK098368 mRNA. No translation available.
AK314413 mRNA. Translation: BAG37034.1.
AL355388 Genomic DNA. Translation: CAH72633.1.
AL355388 Genomic DNA. Translation: CAH72634.1.
BC006410 mRNA. Translation: AAH06410.1. Different initiation.
BC018403 mRNA. Translation: AAH18403.1.
BC063841 mRNA. Translation: AAH63841.1.
AF113544 mRNA. Translation: AAF19084.1. Different initiation.
CCDSCCDS1127.1. [Q9NRR5-1]
RefSeqNP_064516.2. NM_020131.3. [Q9NRR5-1]
UniGeneHs.283739.

3D structure databases

ProteinModelPortalQ9NRR5.
SMRQ9NRR5. Positions 13-83, 555-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121223. 179 interactions.
IntActQ9NRR5. 151 interactions.
MINTMINT-1373057.
STRING9606.ENSP00000357292.

PTM databases

PhosphoSiteQ9NRR5.

Polymorphism databases

DMDM45476982.

Proteomic databases

MaxQBQ9NRR5.
PaxDbQ9NRR5.
PRIDEQ9NRR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368309; ENSP00000357292; ENSG00000160803. [Q9NRR5-1]
GeneID56893.
KEGGhsa:56893.
UCSCuc001fna.3. human. [Q9NRR5-1]

Organism-specific databases

CTD56893.
GeneCardsGC01M156005.
HGNCHGNC:1237. UBQLN4.
HPAHPA027920.
MIM605440. gene.
neXtProtNX_Q9NRR5.
PharmGKBPA25619.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5272.
HOVERGENHBG064537.
InParanoidQ9NRR5.
KOK04523.
OMAFGMSRTT.
OrthoDBEOG7HF1J8.
PhylomeDBQ9NRR5.
TreeFamTF314412.

Gene expression databases

BgeeQ9NRR5.
CleanExHS_UBQLN4.
GenevestigatorQ9NRR5.

Family and domain databases

InterProIPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR015496. Ubiquilin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10677. PTHR10677. 1 hit.
PfamPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBQLN4. human.
GenomeRNAi56893.
NextBio62315.
PROQ9NRR5.
SOURCESearch...

Entry information

Entry nameUBQL4_HUMAN
AccessionPrimary (citable) accession number: Q9NRR5
Secondary accession number(s): A6ND44 expand/collapse secondary AC list , B2RAY7, Q5VYA0, Q5VYA1, Q9BR98, Q9UHX4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM