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Q99NB8 (UBQL4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:Cip75, Ubin
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length596 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.4 Ref.5

Subunit structure

Homodimer. Binds ATXN1/SCA1. Interaction with ATXN1 inhibits polyubiquitination of UBQLN4 and interferes with PSMD4 binding By similarity. Interacts (via ubiquitin-like domain) with PSMD4, a regulatory subunit of the proteasome. 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 polyubiquitin chains and polyubiquitinated proteins. Ref.1 Ref.4 Ref.5 Ref.6

Subcellular location

Nucleus By similarity. Cytoplasm. Endoplasmic reticulum Probable. Cytoplasmperinuclear region. Note: Colocalizes with the proteasome, both in nucleus and cytoplasm By similarity. May associate with the endoplasmic reticulum. Ref.1 Ref.4 Ref.5

Tissue specificity

Detected in testis, ovary, thyroid, kidney, thymus, heart, liver, lung and spleen (at protein level). Highly expressed in heart, skeletal muscle, kidney, liver and brain. Detected at lower levels in testis, lung and spleen. Ref.1 Ref.5

Post-translational modification

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

Sequence similarities

Contains 1 UBA domain.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 596596Ubiquilin-4
PRO_0000211016

Regions

Domain13 – 8775Ubiquitin-like
Domain548 – 59346UBA
Compositional bias174 – 25784Met-rich

Secondary structure

........ 596
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99NB8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 77CC85B49FD083C4

FASTA59663,506
        10         20         30         40         50         60 
MAEPSGAETR PQIRVTVKTP KDKEEIVICD QASVKEFKEE ISRRFKAQQD QLVLIFAGKI 

        70         80         90        100        110        120 
LKDGDTLSQH GIKDGLTVHL VIKTPQKAQD PVTAAASPPS TPDSASAPST TPASPAAAPV 

       130        140        150        160        170        180 
QPCSSGNTTS DAGSGGGPSP VAAEGPSSAT ASILSGFGGI LGLGSLGLGS ANFMELQQQM 

       190        200        210        220        230        240 
QRQLMSNPEM LSQIMENPLV QDMMSNPDLM RHMIMANPQM QQLMERNPEI SHMLNNPELM 

       250        260        270        280        290        300 
RQTMELARNP AMMQEMMRNQ DRALSNLESV PGGYNALRRM YTDIQEPMFT AAREQFGNNP 

       310        320        330        340        350        360 
FSSLAGNSDN SSSQPLRTEN REPLPNPWSP SPPTSQAPGS GGEGTGGSGT SQVHPTVSNP 

       370        380        390        400        410        420 
FGINAASLGS GMFNSPEMQA LLQQISENPQ LMQNVISAPY MRTMMQTLAQ NPDFAAQMMV 

       430        440        450        460        470        480 
NVPLFAGNPQ LQEQLRLQLP VFLQQMQNPE SLSILTNPRA MQALLQIQQG LQTLQTEAPG 

       490        500        510        520        530        540 
LVPSLGSFGT PRTSVPLAGS NSGSSAEAPT SSPGVPATSP PSAGSNAQQQ LMQQMIQLLS 

       550        560        570        580        590 
GSGNSQVPMP EVRFQQQLEQ LNSMGFINRE ANLQALIATG GDINAAIERL LGSQLS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a novel ubiquitin-like protein, UBIN, that binds to ER targeting signal sequences."
Matsuda M., Koide T., Yorihuzi T., Hosokawa N., Nagata K.
Biochem. Biophys. Res. Commun. 280:535-540(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SIGNAL SEQUENCES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Embryo.
[2]"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].
Tissue: Kidney.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 549-596.
Strain: C57BL/6J.
Tissue: Embryo.
[4]"A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43."
Li X., Su V., Kurata W.E., Jin C., Lau A.F.
J. Biol. Chem. 283:5748-5759(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PSMD4 AND GJA1.
[5]"Ubiquitin-independent proteasomal degradation of endoplasmic reticulum-localized connexin43 mediated by CIP75."
Su V., Nakagawa R., Koval M., Lau A.F.
J. Biol. Chem. 285:40979-40990(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBIQUITIN AND GJA1, TISSUE SPECIFICITY.
[6]"NMR structure note: UBA domain of CIP75."
Kieken F., Spagnol G., Su V., Lau A.F., Sorgen P.L.
J. Biomol. NMR 46:245-250(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 549-596, INTERACTION WITH GJA1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB040050 mRNA. Translation: BAB40326.1.
BC017686 mRNA. Translation: AAH17686.1.
AK077511 mRNA. Translation: BAC36837.1.
CCDSCCDS17479.1.
RefSeqNP_277068.1. NM_033526.2.
UniGeneMm.303059.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KNZNMR-A549-596[»]
ProteinModelPortalQ99NB8.
SMRQ99NB8. Positions 13-83, 549-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220488. 1 interaction.
IntActQ99NB8. 4 interactions.
MINTMINT-4139382.

PTM databases

PhosphoSiteQ99NB8.

Proteomic databases

MaxQBQ99NB8.
PaxDbQ99NB8.
PRIDEQ99NB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000008748; ENSMUSP00000008748; ENSMUSG00000008604.
GeneID94232.
KEGGmmu:94232.
UCSCuc008pvq.1. mouse.

Organism-specific databases

CTD56893.
MGIMGI:2150152. Ubqln4.

Phylogenomic databases

eggNOGCOG5272.
GeneTreeENSGT00390000005720.
HOGENOMHOG000234878.
HOVERGENHBG064537.
InParanoidQ99NB8.
KOK04523.
OMAVAVNIRC.
OrthoDBEOG7HF1J8.
PhylomeDBQ99NB8.
TreeFamTF314412.

Gene expression databases

BgeeQ99NB8.
CleanExMM_UBQLN4.
GenevestigatorQ99NB8.

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

EvolutionaryTraceQ99NB8.
NextBio352243.
PROQ99NB8.
SOURCESearch...

Entry information

Entry nameUBQL4_MOUSE
AccessionPrimary (citable) accession number: Q99NB8
Secondary accession number(s): Q8BP88
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot