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Protein

Ubiquilin-1

Gene

UBQLN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors. Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation.

GO - Molecular functioni

  1. kinase binding Source: UniProtKB

GO - Biological processi

  1. cellular response to hypoxia Source: BHF-UCL
  2. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  3. regulation of protein ubiquitination Source: HGNC
  4. response to endoplasmic reticulum stress Source: BHF-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquilin-1
Alternative name(s):
Protein linking IAP with cytoskeleton 1
Short name:
PLIC-1
Short name:
hPLIC-1
Gene namesi
Name:UBQLN1
Synonyms:DA41, PLIC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12508. UBQLN1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Detected in neuronal processes and at synapses (By similarity). Detected in cytosolic puncta that may correspond to autophagosomes.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: HGNC
  3. nucleoplasm Source: HPA
  4. perinuclear region of cytoplasm Source: UniProtKB
  5. proteasome complex Source: UniProtKB-KW
  6. protein complex Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 589588Ubiquilin-1PRO_0000211008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UMX0.
PaxDbiQ9UMX0.
PRIDEiQ9UMX0.

2D gel databases

REPRODUCTION-2DPAGEIPI00071180.

PTM databases

PhosphoSiteiQ9UMX0.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed throughout the brain; detected in neurons and in neuropathological lesions, such as neurofibrillary tangles and Lewy bodies. Highly expressed in heart, placenta, pancreas, lung, liver, skeletal muscle and kidney.2 Publications

Gene expression databases

BgeeiQ9UMX0.
CleanExiHS_UBQLN1.
ExpressionAtlasiQ9UMX0. baseline and differential.
GenevestigatoriQ9UMX0.

Organism-specific databases

HPAiCAB037256.
HPA054143.

Interactioni

Subunit structurei

Binds CD47, NBL1, GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3. Binds UBE3A, BTRC, P4HB, MTOR, PSEN1 and PSEN2. Interacts with the proteasome 19S subunit. Interacts (via ubiquitin-like domain) with TREX1; the interaction is direct and may control TREX1 subcellular location.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRM1Q161864EBI-741480,EBI-954387
EPS15P425665EBI-741480,EBI-396684
PSMD4P550366EBI-741480,EBI-359318
RIC8AQ9NPQ83EBI-741480,EBI-717509
SERPINI2O758303EBI-741480,EBI-750144
UBCP0CG483EBI-741480,EBI-3390054
UBQLN4Q9NRR58EBI-741480,EBI-711226

Protein-protein interaction databases

BioGridi119007. 405 interactions.
DIPiDIP-41629N.
IntActiQ9UMX0. 51 interactions.
MINTiMINT-150317.
STRINGi9606.ENSP00000365576.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 426Combined sources
Beta strandi47 – 526Combined sources
Helixi58 – 6912Combined sources
Helixi73 – 753Combined sources
Beta strandi76 – 805Combined sources
Beta strandi83 – 853Combined sources
Helixi92 – 943Combined sources
Beta strandi101 – 1066Combined sources
Turni543 – 5475Combined sources
Helixi548 – 5569Combined sources
Helixi562 – 57211Combined sources
Helixi576 – 5838Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JY5NMR-A541-586[»]
2JY6NMR-B541-586[»]
2KLCNMR-A34-112[»]
ProteinModelPortaliQ9UMX0.
SMRiQ9UMX0. Positions 1-112, 537-586.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UMX0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 11175Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini546 – 58641UBAPROSITE-ProRule annotationAdd
BLAST

Domaini

The UBA domain mediates binding to PSEN1 and PSEN2. It also binds ubiquitin with micromolar affinity, independently of polyubiquitin linkage type.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOVERGENiHBG064537.
InParanoidiQ9UMX0.
KOiK04523.
OMAiTTEPGNQ.
OrthoDBiEOG7HF1J8.
PhylomeDBiQ9UMX0.
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.
IPR028799. UBQLN1.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PTHR10677:SF16. PTHR10677:SF16. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UMX0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAESGESGGP PGSQDSAAGA EGAGAPAAAA SAEPKIMKVT VKTPKEKEEF
60 70 80 90 100
AVPENSSVQQ FKEEISKRFK SHTDQLVLIF AGKILKDQDT LSQHGIHDGL
110 120 130 140 150
TVHLVIKTQN RPQDHSAQQT NTAGSNVTTS STPNSNSTSG SATSNPFGLG
160 170 180 190 200
GLGGLAGLSS LGLNTTNFSE LQSQMQRQLL SNPEMMVQIM ENPFVQSMLS
210 220 230 240 250
NPDLMRQLIM ANPQMQQLIQ RNPEISHMLN NPDIMRQTLE LARNPAMMQE
260 270 280 290 300
MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMLSAAQEQ FGGNPFASLV
310 320 330 340 350
SNTSSGEGSQ PSRTENRDPL PNPWAPQTSQ SSSASSGTAS TVGGTTGSTA
360 370 380 390 400
SGTSGQSTTA PNLVPGVGAS MFNTPGMQSL LQQITENPQL MQNMLSAPYM
410 420 430 440 450
RSMMQSLSQN PDLAAQMMLN NPLFAGNPQL QEQMRQQLPT FLQQMQNPDT
460 470 480 490 500
LSAMSNPRAM QALLQIQQGL QTLATEAPGL IPGFTPGLGA LGSTGGSSGT
510 520 530 540 550
NGSNATPSEN TSPTAGTTEP GHQQFIQQML QALAGVNPQL QNPEVRFQQQ
560 570 580
LEQLSAMGFL NREANLQALI ATGGDINAAI ERLLGSQPS
Length:589
Mass (Da):62,519
Last modified:March 1, 2002 - v2
Checksum:i8B4756B6113B7025
GO
Isoform 2 (identifier: Q9UMX0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-443: Missing.

Note: No experimental confirmation available.

Show »
Length:561
Mass (Da):59,220
Checksum:i1E0BC42EC5BA4DA6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → T in AAH39294 (PubMed:15489334).Curated
Sequence conflicti41 – 411V → A in BAB20436 (PubMed:10807547).Curated
Sequence conflicti61 – 611F → S in BAB20436 (PubMed:10807547).Curated
Sequence conflicti91 – 911L → S in BAB20436 (PubMed:10807547).Curated
Sequence conflicti125 – 1251S → G in CAB66578 (PubMed:11230166).Curated
Sequence conflicti202 – 2021P → H in AAH39294 (PubMed:15489334).Curated
Sequence conflicti537 – 5382NP → YS in BAB20436 (PubMed:10807547).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei416 – 44328Missing in isoform 2. 1 PublicationVSP_009787Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176069 mRNA. Translation: AAD49751.3.
AF293384 mRNA. Translation: AAG02473.1.
AB035275 mRNA. Translation: BAB20436.1.
AL136643 mRNA. Translation: CAB66578.1.
AL354920 Genomic DNA. Translation: CAI15100.1.
AL354920 Genomic DNA. Translation: CAI15101.1.
CH471089 Genomic DNA. Translation: EAW62659.1.
CH471089 Genomic DNA. Translation: EAW62661.1.
BC010066 mRNA. Translation: AAH10066.1.
BC039294 mRNA. Translation: AAH39294.1.
AK074535 mRNA. No translation available.
CCDSiCCDS6663.1. [Q9UMX0-1]
CCDS6664.1. [Q9UMX0-2]
RefSeqiNP_038466.2. NM_013438.4. [Q9UMX0-1]
NP_444295.1. NM_053067.2. [Q9UMX0-2]
UniGeneiHs.9589.

Genome annotation databases

EnsembliENST00000257468; ENSP00000257468; ENSG00000135018. [Q9UMX0-2]
ENST00000376395; ENSP00000365576; ENSG00000135018. [Q9UMX0-1]
GeneIDi29979.
KEGGihsa:29979.
UCSCiuc004amv.3. human. [Q9UMX0-1]
uc004amw.3. human. [Q9UMX0-2]

Polymorphism databases

DMDMi48475013.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176069 mRNA. Translation: AAD49751.3.
AF293384 mRNA. Translation: AAG02473.1.
AB035275 mRNA. Translation: BAB20436.1.
AL136643 mRNA. Translation: CAB66578.1.
AL354920 Genomic DNA. Translation: CAI15100.1.
AL354920 Genomic DNA. Translation: CAI15101.1.
CH471089 Genomic DNA. Translation: EAW62659.1.
CH471089 Genomic DNA. Translation: EAW62661.1.
BC010066 mRNA. Translation: AAH10066.1.
BC039294 mRNA. Translation: AAH39294.1.
AK074535 mRNA. No translation available.
CCDSiCCDS6663.1. [Q9UMX0-1]
CCDS6664.1. [Q9UMX0-2]
RefSeqiNP_038466.2. NM_013438.4. [Q9UMX0-1]
NP_444295.1. NM_053067.2. [Q9UMX0-2]
UniGeneiHs.9589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JY5NMR-A541-586[»]
2JY6NMR-B541-586[»]
2KLCNMR-A34-112[»]
ProteinModelPortaliQ9UMX0.
SMRiQ9UMX0. Positions 1-112, 537-586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119007. 405 interactions.
DIPiDIP-41629N.
IntActiQ9UMX0. 51 interactions.
MINTiMINT-150317.
STRINGi9606.ENSP00000365576.

PTM databases

PhosphoSiteiQ9UMX0.

Polymorphism databases

DMDMi48475013.

2D gel databases

REPRODUCTION-2DPAGEIPI00071180.

Proteomic databases

MaxQBiQ9UMX0.
PaxDbiQ9UMX0.
PRIDEiQ9UMX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257468; ENSP00000257468; ENSG00000135018. [Q9UMX0-2]
ENST00000376395; ENSP00000365576; ENSG00000135018. [Q9UMX0-1]
GeneIDi29979.
KEGGihsa:29979.
UCSCiuc004amv.3. human. [Q9UMX0-1]
uc004amw.3. human. [Q9UMX0-2]

Organism-specific databases

CTDi29979.
GeneCardsiGC09M086274.
HGNCiHGNC:12508. UBQLN1.
HPAiCAB037256.
HPA054143.
MIMi605046. gene.
neXtProtiNX_Q9UMX0.
PharmGKBiPA37155.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000005720.
HOVERGENiHBG064537.
InParanoidiQ9UMX0.
KOiK04523.
OMAiTTEPGNQ.
OrthoDBiEOG7HF1J8.
PhylomeDBiQ9UMX0.
TreeFamiTF314412.

Miscellaneous databases

ChiTaRSiUBQLN1. human.
EvolutionaryTraceiQ9UMX0.
GeneWikiiUBQLN1.
GenomeRNAii29979.
NextBioi52732.
PROiQ9UMX0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UMX0.
CleanExiHS_UBQLN1.
ExpressionAtlasiQ9UMX0. baseline and differential.
GenevestigatoriQ9UMX0.

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.
IPR028799. UBQLN1.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PTHR10677:SF16. PTHR10677:SF16. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation."
    Mah A.L., Perry G., Smith M.A., Monteiro M.J.
    J. Cell Biol. 151:847-862(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PSEN1 AND PSEN2, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. Mah A.L., Monteiro M.J.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UBE3A; BTRC AND THE PROTEASOME.
    Tissue: B-cell.
  4. "Molecular cloning and expression analysis of the human DA41 gene and its mapping to chromosome 9q21.2-q21.3."
    Hanaoka E., Ozaki T., Ohira M., Nakamura Y., Suzuki M., Takahashi E., Moriya H., Nakagawara A., Sakiyama S.
    J. Hum. Genet. 45:188-191(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Muscle.
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316.
    Tissue: Embryo.
  10. Lubec G., Chen W.-Q., Sun Y.
    Submitted (NOV-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-83; 207-236; 244-253 AND 547-582, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  11. "Characterization of ubiquilin 1, an mTOR-interacting protein."
    Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.
    Biochim. Biophys. Acta 1542:41-56(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH MTOR, TISSUE SPECIFICITY.
  12. "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death."
    Ko H.S., Uehara T., Nomura Y.
    J. Biol. Chem. 277:35386-35392(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH P4HB.
  13. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. "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(2008) [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].
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(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].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [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].
  18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [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].
  19. "The TREX1 C-terminal region controls cellular localization through ubiquitination."
    Orebaugh C.D., Fye J.M., Harvey S., Hollis T., Wilkinson J.C., Perrino F.W.
    J. Biol. Chem. 288:28881-28892(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TREX1, SUBCELLULAR LOCATION.
  20. "Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains."
    Zhang D., Raasi S., Fushman D.
    J. Mol. Biol. 377:162-180(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 541-586 ALONE AND IN COMPLEX WITH UBIQUITIN.

Entry informationi

Entry nameiUBQL1_HUMAN
AccessioniPrimary (citable) accession number: Q9UMX0
Secondary accession number(s): Q5T6J5
, Q5T6J9, Q8IXS9, Q8N2Q3, Q9H0T8, Q9H3R4, Q9HAZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2002
Last modified: April 1, 2015
This is version 139 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.