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Protein

Ubiquilin-4

Gene

Ubqln4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (PubMed:18079109, PubMed:20940304). 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 (By similarity).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Autophagy

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ubqln4
Synonyms:Cip75, Ubin
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2150152. Ubqln4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 596595Ubiquilin-4PRO_0000211016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ99NB8.
PaxDbiQ99NB8.
PRIDEiQ99NB8.

PTM databases

PhosphoSiteiQ99NB8.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ99NB8.
CleanExiMM_UBQLN4.
GenevisibleiQ99NB8. MM.

Interactioni

Subunit structurei

Homooligomer. Binds ATXN1/SCA1. Interaction with ATXN1 inhibits polyubiquitination of UBQLN4 and interferes with PSMD4 binding (By similarity). Interacts (via ubiquitin-like domain) with PSMD2 and PSMD4, regulatory subunits of the proteasome (PubMed:18079109). Binds signal sequences of proteins that are targeted to the endoplasmic reticulum (PubMed:11162551). Interacts (via UBA domain) with GJA1 (not ubiquitinated) and with ubiquitin; both compete for the same binding site (PubMed:18079109, PubMed:20940304, PubMed:20127391). Interacts (via UBA domain) with polyubiquitin chains and polyubiquitinated proteins (PubMed:20940304). 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 (By similarity).By similarity4 Publications

Protein-protein interaction databases

BioGridi220488. 1 interaction.
IntActiQ99NB8. 4 interactions.
MINTiMINT-4139382.
STRINGi10090.ENSMUSP00000008748.

Structurei

Secondary structure

1
596
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi551 – 56212Combined sources
Turni563 – 5653Combined sources
Helixi569 – 57911Combined sources
Helixi583 – 59210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KNZNMR-A549-596[»]
ProteinModelPortaliQ99NB8.
SMRiQ99NB8. Positions 13-83, 549-596.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99NB8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 8775Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini187 – 22438STI1 1Sequence AnalysisAdd
BLAST
Domaini225 – 25632STI1 2Sequence AnalysisAdd
BLAST
Domaini388 – 43548STI1 3Sequence AnalysisAdd
BLAST
Domaini439 – 47133STI1 4Sequence AnalysisAdd
BLAST
Domaini548 – 59346UBAPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi174 – 25784Met-richAdd
BLAST

Sequence similaritiesi

Contains 4 STI1 domains.Sequence Analysis
Contains 1 UBA domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ99NB8.
KOiK04523.
OMAiNRNTAGQ.
OrthoDBiEOG7HF1J8.
PhylomeDBiQ99NB8.
TreeFamiTF314412.

Family and domain databases

InterProiIPR006636. 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]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99NB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPSGAETR PQIRVTVKTP KDKEEIVICD QASVKEFKEE ISRRFKAQQD
60 70 80 90 100
QLVLIFAGKI LKDGDTLSQH GIKDGLTVHL VIKTPQKAQD PVTAAASPPS
110 120 130 140 150
TPDSASAPST TPASPAAAPV QPCSSGNTTS DAGSGGGPSP VAAEGPSSAT
160 170 180 190 200
ASILSGFGGI LGLGSLGLGS ANFMELQQQM QRQLMSNPEM LSQIMENPLV
210 220 230 240 250
QDMMSNPDLM RHMIMANPQM QQLMERNPEI SHMLNNPELM RQTMELARNP
260 270 280 290 300
AMMQEMMRNQ DRALSNLESV PGGYNALRRM YTDIQEPMFT AAREQFGNNP
310 320 330 340 350
FSSLAGNSDN SSSQPLRTEN REPLPNPWSP SPPTSQAPGS GGEGTGGSGT
360 370 380 390 400
SQVHPTVSNP FGINAASLGS GMFNSPEMQA LLQQISENPQ LMQNVISAPY
410 420 430 440 450
MRTMMQTLAQ NPDFAAQMMV NVPLFAGNPQ LQEQLRLQLP VFLQQMQNPE
460 470 480 490 500
SLSILTNPRA MQALLQIQQG LQTLQTEAPG LVPSLGSFGT PRTSVPLAGS
510 520 530 540 550
NSGSSAEAPT SSPGVPATSP PSAGSNAQQQ LMQQMIQLLS GSGNSQVPMP
560 570 580 590
EVRFQQQLEQ LNSMGFINRE ANLQALIATG GDINAAIERL LGSQLS
Length:596
Mass (Da):63,506
Last modified:June 1, 2001 - v1
Checksum:i77CC85B49FD083C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040050 mRNA. Translation: BAB40326.1.
BC017686 mRNA. Translation: AAH17686.1.
AK077511 mRNA. Translation: BAC36837.1.
CCDSiCCDS17479.1.
RefSeqiNP_277068.1. NM_033526.2.
UniGeneiMm.303059.

Genome annotation databases

EnsembliENSMUST00000008748; ENSMUSP00000008748; ENSMUSG00000008604.
GeneIDi94232.
KEGGimmu:94232.
UCSCiuc008pvq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040050 mRNA. Translation: BAB40326.1.
BC017686 mRNA. Translation: AAH17686.1.
AK077511 mRNA. Translation: BAC36837.1.
CCDSiCCDS17479.1.
RefSeqiNP_277068.1. NM_033526.2.
UniGeneiMm.303059.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KNZNMR-A549-596[»]
ProteinModelPortaliQ99NB8.
SMRiQ99NB8. Positions 13-83, 549-596.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220488. 1 interaction.
IntActiQ99NB8. 4 interactions.
MINTiMINT-4139382.
STRINGi10090.ENSMUSP00000008748.

PTM databases

PhosphoSiteiQ99NB8.

Proteomic databases

MaxQBiQ99NB8.
PaxDbiQ99NB8.
PRIDEiQ99NB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000008748; ENSMUSP00000008748; ENSMUSG00000008604.
GeneIDi94232.
KEGGimmu:94232.
UCSCiuc008pvq.1. mouse.

Organism-specific databases

CTDi56893.
MGIiMGI:2150152. Ubqln4.

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ99NB8.
KOiK04523.
OMAiNRNTAGQ.
OrthoDBiEOG7HF1J8.
PhylomeDBiQ99NB8.
TreeFamiTF314412.

Miscellaneous databases

EvolutionaryTraceiQ99NB8.
NextBioi352243.
PROiQ99NB8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99NB8.
CleanExiMM_UBQLN4.
GenevisibleiQ99NB8. MM.

Family and domain databases

InterProiIPR006636. 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]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 PSMD2; 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. Cited for: STRUCTURE BY NMR OF 549-596, INTERACTION WITH GJA1.

Entry informationi

Entry nameiUBQL4_MOUSE
AccessioniPrimary (citable) accession number: Q99NB8
Secondary accession number(s): Q8BP88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.