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Protein

Ubiquilin-2

Gene

UBQLN2

Organism
Homo sapiens (Human)
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 (PubMed:10983987). 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 (PubMed:24215460, PubMed:18307982). 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 (PubMed:19148225, PubMed:20529957). 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) (PubMed:18199683).6 Publications

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of clathrin-mediated endocytosis Source: UniProtKB
  • negative regulation of G-protein coupled receptor internalization Source: UniProtKB
  • positive regulation of ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • regulation of autophagosome assembly Source: UniProtKB
  • regulation of macroautophagy Source: UniProtKB
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
Short name:
hPLIC-2
Ubiquitin-like product Chap1/Dsk2
Gene namesi
Name:UBQLN2
Synonyms:N4BP4, PLIC2
ORF Names:HRIHFB2157
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12509. UBQLN2.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB-KW
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia (ALS15)6 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS15 may develop frontotemporal dementia.

See also OMIM:300857
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551S → N in ALS15; uncertain pathological significance. 1 Publication
VAR_068892
Natural varianti189 – 1891P → T in ALS15; uncertain pathological significance. 1 Publication
VAR_068893
Natural varianti283 – 2831A → T in ALS15. 1 Publication
VAR_068895
Natural varianti425 – 4251Q → R in ALS15. 1 Publication
VAR_068896
Natural varianti487 – 4871T → I in ALS15. 1 Publication
VAR_068897
Natural varianti497 – 4971P → H in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1 and FAF2; increases translocation of HNRNPA1 to the cytoplasm; adversely affects ERAD. 3 Publications
VAR_066562
Natural varianti497 – 4971P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066563
Natural varianti506 – 5061P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066564
Natural varianti509 – 5091P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066565
Natural varianti525 – 5251P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066566

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

MIMi300857. phenotype.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA37156.

Polymorphism and mutation databases

BioMutaiUBQLN2.
DMDMi124056593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 624623Ubiquilin-2PRO_0000211011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Post-translational modificationi

Degraded during macroautophagy.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UHD9.
PaxDbiQ9UHD9.
PeptideAtlasiQ9UHD9.
PRIDEiQ9UHD9.

PTM databases

PhosphoSiteiQ9UHD9.

Expressioni

Inductioni

Highly expressed in mitotic cells from metaphase to telophase. Expression in non-mitotic cells is very low.

Gene expression databases

BgeeiQ9UHD9.
CleanExiHS_UBQLN2.
GenevisibleiQ9UHD9. HS.

Organism-specific databases

HPAiCAB013481.
HPA006431.

Interactioni

Subunit structurei

Homodimer. Forms heterodimer with UBQLN1. Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72. 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. Binds CD47 (By similarity).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRM1Q161864EBI-947187,EBI-954387
PSMD4P550363EBI-947187,EBI-359318
RAD23AP547253EBI-947187,EBI-746453
RPN13O487264EBI-947187,EBI-7710745From a different organism.

Protein-protein interaction databases

BioGridi119006. 65 interactions.
DIPiDIP-42116N.
IntActiQ9UHD9. 13 interactions.
MINTiMINT-1192483.
STRINGi9606.ENSP00000345195.

Structurei

Secondary structure

1
624
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253Combined sources
Beta strandi33 – 386Combined sources
Beta strandi43 – 486Combined sources
Helixi54 – 6512Combined sources
Beta strandi69 – 768Combined sources
Beta strandi79 – 824Combined sources
Helixi87 – 915Combined sources
Beta strandi93 – 10210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J8CNMR-A1-103[»]
ProteinModelPortaliQ9UHD9.
SMRiQ9UHD9. Positions 1-103, 578-624.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHD9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 10775Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini178 – 20629STI1 1Sequence AnalysisAdd
BLAST
Domaini208 – 24740STI1 2Sequence AnalysisAdd
BLAST
Domaini379 – 42648STI1 3Sequence AnalysisAdd
BLAST
Domaini430 – 46233STI1 4Sequence AnalysisAdd
BLAST
Repeati491 – 49331
Repeati494 – 49632
Repeati497 – 49933
Repeati500 – 50234
Repeati503 – 50535
Repeati506 – 50836
Repeati509 – 51137
Repeati512 – 51438
Repeati515 – 51739
Repeati518 – 520310
Repeati521 – 523311
Repeati524 – 526312
Domaini581 – 62141UBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni491 – 5263612 X 3 AA tandem repeats of P-X-XAdd
BLAST

Domaini

The ubiquitin-like domain is essential for its inhibitory effect on GPCR endocytosis. Mediates its association with the subunits of the proteasome.1 Publication1 Publication
The UBA domain is essential for its association with microtubule-associated protein 1 light chain 3 (MAP1LC3). Mediates its association with ubiquitinated substrates.1 Publication1 Publication
Dimerization is dependent upon the central region of the protein containing the STI1 domains and is independent of its ubiquitin-like and UBA domains.1 Publication

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.
InParanoidiQ9UHD9.
KOiK04523.
OMAiNRPQGQS.
OrthoDBiEOG7HF1J8.
PhylomeDBiQ9UHD9.
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.

Q9UHD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENGESSGP PRPSRGPAAA QGSAAAPAEP KIIKVTVKTP KEKEEFAVPE
60 70 80 90 100
NSSVQQFKEA ISKRFKSQTD QLVLIFAGKI LKDQDTLIQH GIHDGLTVHL
110 120 130 140 150
VIKSQNRPQG QSTQPSNAAG TNTTSASTPR SNSTPISTNS NPFGLGSLGG
160 170 180 190 200
LAGLSSLGLS STNFSELQSQ MQQQLMASPE MMIQIMENPF VQSMLSNPDL
210 220 230 240 250
MRQLIMANPQ MQQLIQRNPE ISHLLNNPDI MRQTLEIARN PAMMQEMMRN
260 270 280 290 300
QDLALSNLES IPGGYNALRR MYTDIQEPML NAAQEQFGGN PFASVGSSSS
310 320 330 340 350
SGEGTQPSRT ENRDPLPNPW APPPATQSSA TTSTTTSTGS GSGNSSSNAT
360 370 380 390 400
GNTVAAANYV ASIFSTPGMQ SLLQQITENP QLIQNMLSAP YMRSMMQSLS
410 420 430 440 450
QNPDLAAQMM LNSPLFTANP QLQEQMRPQL PAFLQQMQNP DTLSAMSNPR
460 470 480 490 500
AMQALMQIQQ GLQTLATEAP GLIPSFTPGV GVGVLGTAIG PVGPVTPIGP
510 520 530 540 550
IGPIVPFTPI GPIGPIGPTG PAAPPGSTGS GGPTGPTVSS AAPSETTSPT
560 570 580 590 600
SESGPNQQFI QQMVQALAGA NAPQLPNPEV RFQQQLEQLN AMGFLNREAN
610 620
LQALIATGGD INAAIERLLG SQPS
Length:624
Mass (Da):65,696
Last modified:January 23, 2007 - v2
Checksum:iDF7DF8C4D7B71AC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti544 – 5441S → R in AAF17237 (PubMed:10675567).Curated
Sequence conflicti544 – 5441S → R in BAA34801 (PubMed:9853615).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551S → N in ALS15; uncertain pathological significance. 1 Publication
VAR_068892
Natural varianti189 – 1891P → T in ALS15; uncertain pathological significance. 1 Publication
VAR_068893
Natural varianti235 – 2351L → H.
Corresponds to variant rs17002693 [ dbSNP | Ensembl ].
VAR_052680
Natural varianti282 – 2821A → V Probable disease-associated mutation found in a patient with frontotemporal dementia. 1 Publication
VAR_068894
Natural varianti283 – 2831A → T in ALS15. 1 Publication
VAR_068895
Natural varianti425 – 4251Q → R in ALS15. 1 Publication
VAR_068896
Natural varianti487 – 4871T → I in ALS15. 1 Publication
VAR_068897
Natural varianti497 – 4971P → H in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1 and FAF2; increases translocation of HNRNPA1 to the cytoplasm; adversely affects ERAD. 3 Publications
VAR_066562
Natural varianti497 – 4971P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066563
Natural varianti506 – 5061P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066564
Natural varianti509 – 5091P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066565
Natural varianti525 – 5251P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 Publications
VAR_066566

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF189009 mRNA. Translation: AAF17237.1.
AF293385 mRNA. Translation: AAG02474.1.
AL354793 Genomic DNA. Translation: CAD13519.1.
CH471154 Genomic DNA. Translation: EAW93233.1.
BC069237 mRNA. Translation: AAH69237.1.
AL442081 mRNA. Translation: CAC09446.1.
AB015344 mRNA. Translation: BAA34801.1.
CCDSiCCDS14374.1.
RefSeqiNP_038472.2. NM_013444.3.
UniGeneiHs.179309.

Genome annotation databases

EnsembliENST00000338222; ENSP00000345195; ENSG00000188021.
GeneIDi29978.
KEGGihsa:29978.
UCSCiuc004dus.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF189009 mRNA. Translation: AAF17237.1.
AF293385 mRNA. Translation: AAG02474.1.
AL354793 Genomic DNA. Translation: CAD13519.1.
CH471154 Genomic DNA. Translation: EAW93233.1.
BC069237 mRNA. Translation: AAH69237.1.
AL442081 mRNA. Translation: CAC09446.1.
AB015344 mRNA. Translation: BAA34801.1.
CCDSiCCDS14374.1.
RefSeqiNP_038472.2. NM_013444.3.
UniGeneiHs.179309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J8CNMR-A1-103[»]
ProteinModelPortaliQ9UHD9.
SMRiQ9UHD9. Positions 1-103, 578-624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119006. 65 interactions.
DIPiDIP-42116N.
IntActiQ9UHD9. 13 interactions.
MINTiMINT-1192483.
STRINGi9606.ENSP00000345195.

PTM databases

PhosphoSiteiQ9UHD9.

Polymorphism and mutation databases

BioMutaiUBQLN2.
DMDMi124056593.

Proteomic databases

MaxQBiQ9UHD9.
PaxDbiQ9UHD9.
PeptideAtlasiQ9UHD9.
PRIDEiQ9UHD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338222; ENSP00000345195; ENSG00000188021.
GeneIDi29978.
KEGGihsa:29978.
UCSCiuc004dus.3. human.

Organism-specific databases

CTDi29978.
GeneCardsiGC0XP056606.
GeneReviewsiUBQLN2.
HGNCiHGNC:12509. UBQLN2.
HPAiCAB013481.
HPA006431.
MIMi300264. gene.
300857. phenotype.
neXtProtiNX_Q9UHD9.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA37156.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ9UHD9.
KOiK04523.
OMAiNRPQGQS.
OrthoDBiEOG7HF1J8.
PhylomeDBiQ9UHD9.
TreeFamiTF314412.

Miscellaneous databases

ChiTaRSiUBQLN2. human.
EvolutionaryTraceiQ9UHD9.
GeneWikiiUBQLN2.
GenomeRNAii29978.
NextBioi52728.
PROiQ9UHD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHD9.
CleanExiHS_UBQLN2.
GenevisibleiQ9UHD9. HS.

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. "A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch."
    Kaye F.J., Modi S., Ivanovska I., Koonin E.V., Thress K., Kubo A., Kornbluth S., Rose M.D.
    FEBS Lett. 467:348-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STCH.
    Tissue: Lung.
  2. "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome."
    Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L., Gill G., Howley P.M.
    Mol. Cell 6:409-419(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PROTEASOME AND UBE3A.
    Tissue: B-cell.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Placenta.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-624.
    Tissue: Amygdala.
  7. "Selection system for genes encoding nuclear-targeted proteins."
    Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
    Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-624, SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  8. "Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins."
    Ford D.L., Monteiro M.J.
    Biochem. J. 399:397-404(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, HETERODIMERIZATION WITH UBQLN1.
  9. "Ubiquitin receptor proteins hHR23a and hPLIC2 interact."
    Kang Y., Zhang N., Koepp D.M., Walters K.J.
    J. Mol. Biol. 365:1093-1101(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD23A.
  10. "Herp enhances ER-associated protein degradation by recruiting ubiquilins."
    Kim T.Y., Kim E., Yoon S.K., Yoon J.B.
    Biochem. Biophys. Res. Commun. 369:741-746(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HERPUD1.
  11. "The ubiquitin-like protein PLIC-2 is a negative regulator of G protein-coupled receptor endocytosis."
    N'Diaye E.N., Hanyaloglu A.C., Kajihara K.K., Puthenveedu M.A., Wu P., von Zastrow M., Brown E.J.
    Mol. Biol. Cell 19:1252-1260(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN UBIQUITIN-LIKE, INTERACTION WITH EPS15; EPN1 AND EPN2.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation."
    N'Diaye E.N., Kajihara K.K., Hsieh I., Morisaki H., Debnath J., Brown E.J.
    EMBO Rep. 10:173-179(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN UBA.
  14. "Ubiquilin at a crossroads in protein degradation pathways."
    Rothenberg C., Monteiro M.J.
    Autophagy 6:979-980(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  15. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH UBQLN1 AND MAP1LC3A/B/C, PROTEOLYTIC DEGRADATION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Ubiquilins in the crosstalk among proteolytic pathways."
    Lee D.Y., Brown E.J.
    Biol. Chem. 393:441-447(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "Ubiquilin-2 (UBQLN2) binds with high affinity to the C-terminal region of TDP-43 and modulates TDP-43 levels in H4 cells: characterization of inhibition by nucleic acids and 4-aminoquinolines."
    Cassel J.A., Reitz A.B.
    Biochim. Biophys. Acta 1834:964-971(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TARDBP.
  20. "Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery."
    Lee D.Y., Arnott D., Brown E.J.
    EMBO Rep. 14:373-381(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBQLN4.
  21. "The ubiquilin gene family: evolutionary patterns and functional insights."
    Marin I.
    BMC Evol. Biol. 14:63-63(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  22. "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking."
    Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A., Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E., Atkin J.D.
    Hum. Mol. Genet. 23:3579-3595(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C9ORF72.
  23. "Ubiquilin 2: a component of the ubiquitin-proteasome system with an emerging role in neurodegeneration."
    Zhang K.Y., Yang S., Warraich S.T., Blair I.P.
    Int. J. Biochem. Cell Biol. 50:123-126(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  24. "Pathogenic mutation of UBQLN2 impairs its interaction with UBXD8 and disrupts endoplasmic reticulum-associated protein degradation."
    Xia Y., Yan L.H., Huang B., Liu M., Liu X., Huang C.
    J. Neurochem. 129:99-106(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FAF2, CHARACTERIZATION OF VARIANT ALS15 HIS-497.
  25. "Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a."
    Walters K.J., Kleijnen M.F., Goh A.M., Wagner G., Howley P.M.
    Biochemistry 41:1767-1777(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-103.
  26. Cited for: VARIANTS ALS15 HIS-497; SER-497; THR-506; SER-509 AND SER-525, CHARACTERIZATION OF VARIANTS ALS15 HIS-497 AND THR-506.
  27. "Screening in ALS and FTD patients reveals 3 novel UBQLN2 mutations outside the PXX domain and a pure FTD phenotype."
    Synofzik M., Maetzler W., Grehl T., Prudlo J., Vom Hagen J.M., Haack T., Rebassoo P., Munz M., Schols L., Biskup S.
    Neurobiol. Aging 33:E13-E17(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALS15 THR-283 AND ARG-425, VARIANT VAL-282.
  28. "UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis."
    Williams K.L., Warraich S.T., Yang S., Solski J.A., Fernando R., Rouleau G.A., Nicholson G.A., Blair I.P.
    Neurobiol. Aging 33:E3-E10(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALS15 ILE-487.
  29. "UBQLN2 mutations are rare in French and French-Canadian amyotrophic lateral sclerosis."
    Daoud H., Suhail H., Szuto A., Camu W., Salachas F., Meininger V., Bouchard J.P., Dupre N., Dion P.A., Rouleau G.A.
    Neurobiol. Aging 33:E1-E5(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALS15 ASN-155 AND THR-189.
  30. "ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1."
    Gilpin K.M., Chang L., Monteiro M.J.
    Hum. Mol. Genet. 24:2565-2577(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRNPA1 AND HNRNPU, CHARACTERIZATION OF VARIANTS ALS15 HIS-497; SER-497; THR-506; SER-509 AND SER-525.

Entry informationi

Entry nameiUBQL2_HUMAN
AccessioniPrimary (citable) accession number: Q9UHD9
Secondary accession number(s): O94798
, Q5D027, Q9H3W6, Q9HAZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.