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Protein

UBX domain-containing protein 4

Gene

Ubxn4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Unfolded protein response

Names & Taxonomyi

Protein namesi
Recommended name:
UBX domain-containing protein 4
Alternative name(s):
Erasin
UBX domain-containing protein 2
Gene namesi
Name:Ubxn4
Synonyms:Ubxd2, Ubxdc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1915062. Ubxn4.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
  • Nucleus envelope By similarity

  • Note: Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 411411CytoplasmicSequence analysisAdd
BLAST
Intramembranei412 – 43221Sequence analysisAdd
BLAST
Topological domaini433 – 50674CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 506506UBX domain-containing protein 4PRO_0000211028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei487 – 4871PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8VCH8.
MaxQBiQ8VCH8.
PaxDbiQ8VCH8.
PRIDEiQ8VCH8.

PTM databases

iPTMnetiQ8VCH8.
PhosphoSiteiQ8VCH8.
SwissPalmiQ8VCH8.

Expressioni

Tissue specificityi

Expressed in many tissues, including brain, heart, kidney, liver, muscle and spleen (at protein level).1 Publication

Gene expression databases

BgeeiQ8VCH8.

Interactioni

Subunit structurei

Directly interacts with VCP. Interacts with UBQLN1. Forms a complex with VCP and UBQLN1.By similarity

Protein-protein interaction databases

MINTiMINT-1863647.
STRINGi10090.ENSMUSP00000027592.

Structurei

Secondary structure

1
506
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi318 – 3236Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi329 – 3346Combined sources
Helixi340 – 35112Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi363 – 3653Combined sources
Turni371 – 3755Combined sources
Helixi379 – 3813Combined sources
Beta strandi384 – 3929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZKNMR-A312-409[»]
ProteinModelPortaliQ8VCH8.
SMRiQ8VCH8. Positions 312-409.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VCH8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini313 – 39179UBXPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 199199Interaction with UBQLN1By similarityAdd
BLAST

Domaini

The UBX domain is required for interaction with VCP.By similarity
The intramembrane domain also contains the signal for ER targeting.By similarity

Sequence similaritiesi

Contains 1 UBX domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2507. Eukaryota.
ENOG410ZR21. LUCA.
HOGENOMiHOG000007283.
HOVERGENiHBG056020.
InParanoidiQ8VCH8.
OrthoDBiEOG7DRJ3M.
PhylomeDBiQ8VCH8.
TreeFamiTF317466.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF00789. UBX. 1 hit.
[Graphical view]
SMARTiSM00166. UBX. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50033. UBX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VCH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWFQGAIPA AIASAKRSGA VFVVFVAGDD EQSIQMAASW EDEKVTQASS
60 70 80 90 100
NNFVAIKIDT KSEACLQFSQ IYPVVCVPSS FFIGDSGIPL EVIAGSVSAD
110 120 130 140 150
ELVTRIHKVQ QMHSSKGEAS VTNDNQSESS VSTPSASFEP DVCENPESKN
160 170 180 190 200
TELCETPATS DIKSDTATGG ECTGHDSHSQ EPHGCSNQRP AEDLTVRVER
210 220 230 240 250
LTKKLEERRE EKRKEEAQRE IKKEIERRKT GKEMLDYKRK QEEELTKRML
260 270 280 290 300
EERSREKAED RAARERIKQQ IALDRAERAA RFAKTKEAEA AKAAALLTKQ
310 320 330 340 350
AGTEVKREST ARDRSTIARI QFRLPDGSSF TNQFPSDAPL EEARQFAAQT
360 370 380 390 400
VGNTYGNFSL ATMFPRREFT REDYKRRLLD LELAPSASVV LLPAGRPATS
410 420 430 440 450
IVHSSSGDIW TLLGTVLYPF LAIWRLISNF LFSNPPPAQT SARATSTEPS
460 470 480 490 500
NSASSSKSEK REPVRKRMLE KRGEDFKKEG KIYRLRTQDD GEDENNTWNG

NSTQQM
Length:506
Mass (Da):56,472
Last modified:March 1, 2002 - v1
Checksum:iDD9CCC380F29C80F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651C → R in BAC35906 (PubMed:16141072).Curated
Sequence conflicti162 – 1621I → T in BAE28143 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075716 mRNA. Translation: BAC35906.1.
AK147795 mRNA. Translation: BAE28143.1.
BC019795 mRNA. Translation: AAH19795.1.
CCDSiCCDS15251.1.
RefSeqiNP_080666.2. NM_026390.2.
UniGeneiMm.293321.

Genome annotation databases

GeneIDi67812.
KEGGimmu:67812.
UCSCiuc007cll.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075716 mRNA. Translation: BAC35906.1.
AK147795 mRNA. Translation: BAE28143.1.
BC019795 mRNA. Translation: AAH19795.1.
CCDSiCCDS15251.1.
RefSeqiNP_080666.2. NM_026390.2.
UniGeneiMm.293321.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZKNMR-A312-409[»]
ProteinModelPortaliQ8VCH8.
SMRiQ8VCH8. Positions 312-409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1863647.
STRINGi10090.ENSMUSP00000027592.

PTM databases

iPTMnetiQ8VCH8.
PhosphoSiteiQ8VCH8.
SwissPalmiQ8VCH8.

Proteomic databases

EPDiQ8VCH8.
MaxQBiQ8VCH8.
PaxDbiQ8VCH8.
PRIDEiQ8VCH8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi67812.
KEGGimmu:67812.
UCSCiuc007cll.1. mouse.

Organism-specific databases

CTDi23190.
MGIiMGI:1915062. Ubxn4.

Phylogenomic databases

eggNOGiKOG2507. Eukaryota.
ENOG410ZR21. LUCA.
HOGENOMiHOG000007283.
HOVERGENiHBG056020.
InParanoidiQ8VCH8.
OrthoDBiEOG7DRJ3M.
PhylomeDBiQ8VCH8.
TreeFamiTF317466.

Miscellaneous databases

ChiTaRSiUbxn4. mouse.
EvolutionaryTraceiQ8VCH8.
PROiQ8VCH8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VCH8.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF00789. UBX. 1 hit.
[Graphical view]
SMARTiSM00166. UBX. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50033. UBX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Liver and Melanocyte.
  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: Liver.
  3. "Characterization of erasin (UBXD2): a new ER protein that promotes ER-associated protein degradation."
    Liang J., Yin C., Doong H., Fang S., Peterhoff C., Nixon R.A., Monteiro M.J.
    J. Cell Sci. 119:4011-4024(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "Structure of the UBX domain in mouse UBX domain-containing protein 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 309-409.

Entry informationi

Entry nameiUBXN4_MOUSE
AccessioniPrimary (citable) accession number: Q8VCH8
Secondary accession number(s): Q3UGR4, Q8BW17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 109 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

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 one 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.