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Q9UHD9

- UBQL2_HUMAN

UniProt

Q9UHD9 - UBQL2_HUMAN

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Protein

Ubiquilin-2

Gene
UBQLN2, N4BP4, PLIC2, HRIHFB2157
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Increases the half-life of proteins destined to be degraded by the proteasome; may modulate proteasome-mediated protein degradation.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. cell death Source: UniProtKB-KW
Complete GO annotation...

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: Chromosome X

Organism-specific databases

HGNCiHGNC:12509. UBQLN2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Where it colocalizes with the proteasome. Associated with fibers in mitotic cells.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB-SubCell
  3. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia (ALS15) [MIM:300857]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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. 1 Publication
VAR_066562
Natural varianti497 – 4971P → S in ALS15. 1 Publication
VAR_066563
Natural varianti506 – 5061P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. 1 Publication
VAR_066564
Natural varianti509 – 5091P → S in ALS15. 1 Publication
VAR_066565
Natural varianti525 – 5251P → S in ALS15. 1 Publication
VAR_066566

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 624623Ubiquilin-2PRO_0000211011Add
BLAST

Amino acid modifications

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

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.
GenevestigatoriQ9UHD9.

Organism-specific databases

HPAiCAB013481.
HPA006431.

Interactioni

Subunit structurei

Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRM1Q161863EBI-947187,EBI-954387
PSMD4P550363EBI-947187,EBI-359318
RAD23AP547253EBI-947187,EBI-746453
RPN13O487264EBI-947187,EBI-7710745From a different organism.

Protein-protein interaction databases

BioGridi119006. 60 interactions.
DIPiDIP-42116N.
IntActiQ9UHD9. 12 interactions.
MINTiMINT-1192483.
STRINGi9606.ENSP00000345195.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J8CNMR-A1-103[»]
ProteinModelPortaliQ9UHD9.
SMRiQ9UHD9. Positions 1-103, 578-624.

Miscellaneous databases

EvolutionaryTraceiQ9UHD9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 10775Ubiquitin-likeAdd
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 – 62141UBAAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 UBA domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5272.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ9UHD9.
KOiK04523.
OMAiLMASPEM.
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

MAENGESSGP PRPSRGPAAA QGSAAAPAEP KIIKVTVKTP KEKEEFAVPE    50
NSSVQQFKEA ISKRFKSQTD QLVLIFAGKI LKDQDTLIQH GIHDGLTVHL 100
VIKSQNRPQG QSTQPSNAAG TNTTSASTPR SNSTPISTNS NPFGLGSLGG 150
LAGLSSLGLS STNFSELQSQ MQQQLMASPE MMIQIMENPF VQSMLSNPDL 200
MRQLIMANPQ MQQLIQRNPE ISHLLNNPDI MRQTLEIARN PAMMQEMMRN 250
QDLALSNLES IPGGYNALRR MYTDIQEPML NAAQEQFGGN PFASVGSSSS 300
SGEGTQPSRT ENRDPLPNPW APPPATQSSA TTSTTTSTGS GSGNSSSNAT 350
GNTVAAANYV ASIFSTPGMQ SLLQQITENP QLIQNMLSAP YMRSMMQSLS 400
QNPDLAAQMM LNSPLFTANP QLQEQMRPQL PAFLQQMQNP DTLSAMSNPR 450
AMQALMQIQQ GLQTLATEAP GLIPSFTPGV GVGVLGTAIG PVGPVTPIGP 500
IGPIVPFTPI GPIGPIGPTG PAAPPGSTGS GGPTGPTVSS AAPSETTSPT 550
SESGPNQQFI QQMVQALAGA NAPQLPNPEV RFQQQLEQLN AMGFLNREAN 600
LQALIATGGD INAAIERLLG SQPS 624
Length:624
Mass (Da):65,696
Last modified:January 23, 2007 - v2
Checksum:iDF7DF8C4D7B71AC3
GO

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. 1 Publication
VAR_066562
Natural varianti497 – 4971P → S in ALS15. 1 Publication
VAR_066563
Natural varianti506 – 5061P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. 1 Publication
VAR_066564
Natural varianti509 – 5091P → S in ALS15. 1 Publication
VAR_066565
Natural varianti525 – 5251P → S in ALS15. 1 Publication
VAR_066566

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti544 – 5441S → R1 Publication
Sequence conflicti544 – 5441S → R1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi124056593.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14374.1.
RefSeqi NP_038472.2. NM_013444.3.
UniGenei Hs.179309.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J8C NMR - A 1-103 [» ]
ProteinModelPortali Q9UHD9.
SMRi Q9UHD9. Positions 1-103, 578-624.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119006. 60 interactions.
DIPi DIP-42116N.
IntActi Q9UHD9. 12 interactions.
MINTi MINT-1192483.
STRINGi 9606.ENSP00000345195.

PTM databases

PhosphoSitei Q9UHD9.

Polymorphism databases

DMDMi 124056593.

Proteomic databases

MaxQBi Q9UHD9.
PaxDbi Q9UHD9.
PeptideAtlasi Q9UHD9.
PRIDEi Q9UHD9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338222 ; ENSP00000345195 ; ENSG00000188021 .
GeneIDi 29978.
KEGGi hsa:29978.
UCSCi uc004dus.3. human.

Organism-specific databases

CTDi 29978.
GeneCardsi GC0XP056606.
GeneReviewsi UBQLN2.
HGNCi HGNC:12509. UBQLN2.
HPAi CAB013481.
HPA006431.
MIMi 300264. gene.
300857. phenotype.
neXtProti NX_Q9UHD9.
Orphaneti 803. Amyotrophic lateral sclerosis.
PharmGKBi PA37156.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5272.
HOGENOMi HOG000234878.
HOVERGENi HBG064537.
InParanoidi Q9UHD9.
KOi K04523.
OMAi LMASPEM.
OrthoDBi EOG7HF1J8.
PhylomeDBi Q9UHD9.
TreeFami TF314412.

Miscellaneous databases

EvolutionaryTracei Q9UHD9.
GeneWikii UBQLN2.
GenomeRNAii 29978.
NextBioi 52728.
PROi Q9UHD9.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHD9.
CleanExi HS_UBQLN2.
Genevestigatori Q9UHD9.

Family and domain databases

InterProi IPR016024. 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 ]
PANTHERi PTHR10677. PTHR10677. 1 hit.
PTHR10677:SF5. PTHR10677:SF5. 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.
SSF48371. SSF48371. 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. "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. "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].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.
  12. "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.
  13. Cited for: VARIANTS ALS15 HIS-497; SER-497; THR-506; SER-509 AND SER-525, CHARACTERIZATION OF VARIANTS ALS15 HIS-497 AND THR-506.
  14. "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.
  15. "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.
  16. "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.

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: September 3, 2014
This is version 121 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

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