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Q99NB8

- UBQL4_MOUSE

UniProt

Q99NB8 - UBQL4_MOUSE

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Protein

Ubiquilin-4

Gene

Ubqln4

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

Functioni

Plays a role in the regulation of proteasomal protein degradation. Depending on the case, may promote or inhibit proteasomal protein degradation.2 Publications

GO - Molecular functioni

  1. polyubiquitin binding Source: UniProtKB

GO - Biological processi

  1. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

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: Chromosome 3

Organism-specific databases

MGIiMGI:2150152. Ubqln4.

Subcellular locationi

Nucleus By similarity. Cytoplasm. Endoplasmic reticulum Curated. Cytoplasmperinuclear region
Note: Colocalizes with the proteasome, both in nucleus and cytoplasm (By similarity). May associate with the endoplasmic reticulum.By similarity

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: MGI
  4. cytosolic proteasome complex Source: Ensembl
  5. endoplasmic reticulum membrane Source: MGI
  6. nuclear proteasome complex Source: Ensembl
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 596596Ubiquilin-4PRO_0000211016Add
BLAST

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

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.
GenevestigatoriQ99NB8.

Interactioni

Subunit structurei

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.By similarity4 Publications

Protein-protein interaction databases

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

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
Domaini548 – 59346UBAPROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 UBA domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ99NB8.
KOiK04523.
OMAiVAVNIRC.
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.

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 .
CCDSi CCDS17479.1.
RefSeqi NP_277068.1. NM_033526.2.
UniGenei Mm.303059.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KNZ NMR - A 549-596 [» ]
ProteinModelPortali Q99NB8.
SMRi Q99NB8. Positions 13-83, 549-596.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 220488. 1 interaction.
IntActi Q99NB8. 4 interactions.
MINTi MINT-4139382.

PTM databases

PhosphoSitei Q99NB8.

Proteomic databases

MaxQBi Q99NB8.
PaxDbi Q99NB8.
PRIDEi Q99NB8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000008748 ; ENSMUSP00000008748 ; ENSMUSG00000008604 .
GeneIDi 94232.
KEGGi mmu:94232.
UCSCi uc008pvq.1. mouse.

Organism-specific databases

CTDi 56893.
MGIi MGI:2150152. Ubqln4.

Phylogenomic databases

eggNOGi COG5272.
GeneTreei ENSGT00390000005720.
HOGENOMi HOG000234878.
HOVERGENi HBG064537.
InParanoidi Q99NB8.
KOi K04523.
OMAi VAVNIRC.
OrthoDBi EOG7HF1J8.
PhylomeDBi Q99NB8.
TreeFami TF314412.

Miscellaneous databases

EvolutionaryTracei Q99NB8.
NextBioi 352243.
PROi Q99NB8.
SOURCEi Search...

Gene expression databases

Bgeei Q99NB8.
CleanExi MM_UBQLN4.
Genevestigatori Q99NB8.

Family and domain databases

InterProi IPR006636. 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 ]
PANTHERi PTHR10677. PTHR10677. 1 hit.
Pfami PF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view ]
SMARTi SM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 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: November 26, 2014
This is version 113 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