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Protein

Ubiquilin-2

Gene

Ubqln2

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

Functioni

Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. 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. Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor-arrestin complexes concentrate in clathrin-coated pits (CCPs) (By similarity). Links CD47 to vimentin-containing intermediate filaments of the cytoskeleton (PubMed:10549293).By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Autophagy

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquilin-2
Alternative name(s):
Chap1
DSK2 homolog
Protein linking IAP with cytoskeleton 2
Short name:
PLIC-2
Ubiquitin-like product Chap1/Dsk2
Gene namesi
Name:Ubqln2
Synonyms:Plic2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1860283. Ubqln2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication
  • Membrane 1 Publication
  • Cytoplasmic vesicleautophagosome By similarity

  • Note: Colocalizes with a subset of proteasomes, namely those that are cytoskeleton associated or free in the cytosol. Associated with fibers in mitotic cells.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 638637Ubiquilin-2PRO_0000211012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei25 – 251Phosphoserine1 Publication

Post-translational modificationi

Degraded during macroautophagy.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9QZM0.
PaxDbiQ9QZM0.
PRIDEiQ9QZM0.

PTM databases

PhosphoSiteiQ9QZM0.

Expressioni

Tissue specificityi

Highly expressed in smooth muscle. Expression in other tissues is very low.1 Publication

Gene expression databases

BgeeiQ9QZM0.
CleanExiMM_UBQLN2.
GenevisibleiQ9QZM0. MM.

Interactioni

Subunit structurei

Homodimer. Forms heterodimer with UBQLN1. Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72 (By similarity). Binds CD47 (PubMed:10549293). Interacts with HNRNPA1 and HNRNPU. Found in a complex with UBQLN1 and MAP1LC3A/B/C. Interacts with EPS15, EPN1 and EPN2. Interacts with HERPUD1. Interacts with RAD23A. Interacts with TARDBP. Interacts (via C-terminus) with FAF2 (via N-terminus). Interacts with UBQLN4 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi207684. 3 interactions.
IntActiQ9QZM0. 1 interaction.
MINTiMINT-4139365.
STRINGi10090.ENSMUSP00000056888.

Structurei

3D structure databases

ProteinModelPortaliQ9QZM0.
SMRiQ9QZM0. Positions 1-103, 587-635.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 10775Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini189 – 21729STI1 1Sequence AnalysisAdd
BLAST
Domaini219 – 25840STI1 2Sequence AnalysisAdd
BLAST
Domaini393 – 44048STI1 3Sequence AnalysisAdd
BLAST
Domaini444 – 47633STI1 4Sequence AnalysisAdd
BLAST
Repeati505 – 50731
Repeati508 – 51032
Repeati511 – 51333
Repeati514 – 51634
Repeati517 – 51935
Repeati520 – 52236
Repeati523 – 52537
Repeati526 – 52838
Repeati529 – 53139
Repeati532 – 533210
Repeati535 – 537311
Domaini589 – 63547UBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni505 – 5373311 X 3 AA tandem repeats P-X-XAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 3021Pro-richAdd
BLAST
Compositional biasi113 – 15240Thr-richAdd
BLAST
Compositional biasi336 – 36126Ser/Thr-richAdd
BLAST

Domaini

The ubiquitin-like domain is essential for its inhibitory effect on GPCR endocytosis. Mediates its association with the subunits of the proteasome.By similarity
The UBA domain is essential for its association with microtubule-associated protein 1 light chain 3 (MAP1LC3). Mediates its association with ubiquitinated substrates.By similarity
Dimerization is dependent upon the central region of the protein containing the STI1 domains and is independent of its ubiquitin-like and UBA domains.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ9QZM0.
KOiK04523.
OMAiAPTRNNE.
OrthoDBiEOG7HF1J8.
TreeFamiTF314412.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR015496. Ubiquilin.
IPR028430. Ubiquilin-2.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PTHR10677:SF5. PTHR10677:SF5. 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.
SSF48371. SSF48371. 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.

Q9QZM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENGESSGP PRPSRGPAAA PGAASPPAEP KIIKVTVKTP KEKEEFAVPE
60 70 80 90 100
NSTVQQFKEA ISKRFKSQTD QLVLIFAGKI LKDQDTLMQH GIHDGLTVHL
110 120 130 140 150
VIKSQNRPQG QATTQPSTTA GTSTTTTTTT TAAAPAATTS SAPRSSSTPT
160 170 180 190 200
TTNSSSFGLG SLSSLSNLGL NSPNFTELQN QMQQQLLASP EMMIQIMENP
210 220 230 240 250
FVQSMLSNPD LMRQLIMANP QMQQLIQRNP EISHLLNNPD IMRQTLEIAR
260 270 280 290 300
NPAMMQEMMR NQDLALSNLE SIPGGYNALR RMYTDIQEPM LNAAQEQFGG
310 320 330 340 350
NPFATVGSSS TSGEGTQPSR TENRDPLPNP WAPPPTTQTA ATTTTTTTTS
360 370 380 390 400
SGSGSGSSSS STTAGNTMAA ANYVASIFST PGMQSLLQQI TENPQLIQNM
410 420 430 440 450
LSAPYMRSMM QSLSQNPDMA AQMMLSSPLF TSNPQLQEQM RPQLPNFLQQ
460 470 480 490 500
MQNPETIAAM SNPRAMQALM QIQQGLQTLA TEAPGLIPSF APGVGMGVLG
510 520 530 540 550
TAITPVGPVT PIGPIGPIVP FTPIGPIGPI GPTGPASSPG STGTGIPPAT
560 570 580 590 600
TVSSSAPTET ISPTSESGPN QQFIQQMVQA LTGGSPPQPP NPEVRFQQQL
610 620 630
EQLNAMGFLN REANLQALIA TGGDINAAIE RLLGSQPS
Length:638
Mass (Da):67,351
Last modified:July 27, 2011 - v2
Checksum:iA9E7350F978B8E2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791Q → R in AAF01366 (PubMed:10549293).Curated
Sequence conflicti362 – 3621Missing in AAH21824 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177346 mRNA. Translation: AAF01366.1.
AL844583 Genomic DNA. Translation: CAM18356.1.
CH466653 Genomic DNA. Translation: EDL31351.1.
BC021824 mRNA. Translation: AAH21824.1.
BC053022 mRNA. Translation: AAH53022.1.
CCDSiCCDS30482.1.
RefSeqiNP_061268.2. NM_018798.2.
UniGeneiMm.430772.

Genome annotation databases

EnsembliENSMUST00000060714; ENSMUSP00000056888; ENSMUSG00000050148.
GeneIDi54609.
KEGGimmu:54609.
UCSCiuc009uqw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177346 mRNA. Translation: AAF01366.1.
AL844583 Genomic DNA. Translation: CAM18356.1.
CH466653 Genomic DNA. Translation: EDL31351.1.
BC021824 mRNA. Translation: AAH21824.1.
BC053022 mRNA. Translation: AAH53022.1.
CCDSiCCDS30482.1.
RefSeqiNP_061268.2. NM_018798.2.
UniGeneiMm.430772.

3D structure databases

ProteinModelPortaliQ9QZM0.
SMRiQ9QZM0. Positions 1-103, 587-635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207684. 3 interactions.
IntActiQ9QZM0. 1 interaction.
MINTiMINT-4139365.
STRINGi10090.ENSMUSP00000056888.

PTM databases

PhosphoSiteiQ9QZM0.

Proteomic databases

MaxQBiQ9QZM0.
PaxDbiQ9QZM0.
PRIDEiQ9QZM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060714; ENSMUSP00000056888; ENSMUSG00000050148.
GeneIDi54609.
KEGGimmu:54609.
UCSCiuc009uqw.1. mouse.

Organism-specific databases

CTDi29978.
MGIiMGI:1860283. Ubqln2.

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ9QZM0.
KOiK04523.
OMAiAPTRNNE.
OrthoDBiEOG7HF1J8.
TreeFamiTF314412.

Miscellaneous databases

ChiTaRSiUbqln2. mouse.
NextBioi311408.
PROiQ9QZM0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZM0.
CleanExiMM_UBQLN2.
GenevisibleiQ9QZM0. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR015496. Ubiquilin.
IPR028430. Ubiquilin-2.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PTHR10677:SF5. PTHR10677:SF5. 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.
SSF48371. SSF48371. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane."
    Wu A.-L., Wang J., Zheleznyak A., Brown E.J.
    Mol. Cell 4:619-625(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CD47.
    Strain: Swiss Webster / NIH.
    Tissue: Embryo.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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].
    Strain: C57BL/6.
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.

Entry informationi

Entry nameiUBQL2_MOUSE
AccessioniPrimary (citable) accession number: Q9QZM0
Secondary accession number(s): B1AY62, Q7TSJ8, Q8VDH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.