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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

Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and 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:15147878). Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:19822669, PubMed:18307982). Isoform 1, isoform 2 and isoform 3 play a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress (PubMed:18953672). 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, PubMed:23459205). Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway (PubMed:21695056). Isoform 1 and isoform 3 play a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis (PubMed:21143716). Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently downregulating the ORAI1-mediated Ca2+ mobilization (PubMed:23307288). Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (By similarity).1 PublicationBy similarity9 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • kinase binding Source: UniProtKB
  • polyubiquitin binding Source: UniProtKB

GO - Biological processi

  • aggrephagy Source: UniProtKB
  • cellular response to hypoxia Source: BHF-UCL
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of autophagic vacuole fusion Source: UniProtKB
  • negative regulation of store-operated calcium channel activity Source: UniProtKB
  • positive regulation of ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • positive regulation of protein ubiquitination Source: UniProtKB
  • regulation of autophagic vacuole assembly Source: UniProtKB
  • regulation of macroautophagy Source: UniProtKB
  • regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • regulation of protein ubiquitination Source: HGNC
  • response to endoplasmic reticulum stress Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Autophagy

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

GO - Cellular componenti

  • aggresome Source: UniProtKB
  • autophagic vacuole Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • nucleoplasm Source: HPA
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • proteasome complex Source: UniProtKB-KW
  • protein complex Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37155.

Polymorphism and mutation databases

BioMutaiUBQLN1.
DMDMi48475013.

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

Degraded during both macroautophagy and during chaperone-mediated autophagy (CMA).1 Publication
Phosphorylated.1 Publication
Ubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UMX0.
PaxDbiQ9UMX0.
PRIDEiQ9UMX0.

2D gel databases

REPRODUCTION-2DPAGEIPI00071180.

PTM databases

PhosphoSiteiQ9UMX0.

Expressioni

Tissue specificityi

Brain (at protein level) (PubMed:18953672). 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.3 Publications

Gene expression databases

BgeeiQ9UMX0.
CleanExiHS_UBQLN1.
ExpressionAtlasiQ9UMX0. baseline and differential.
GenevisibleiQ9UMX0. HS.

Organism-specific databases

HPAiCAB037256.
HPA054143.

Interactioni

Subunit structurei

Monomer and homodimer. Heterodimer with UBQLN2 (PubMed:16813565). Binds CD47, NBL1, GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3 (By similarity). Binds UBE3A, BTRC, P4HB and MTOR. Interacts with the proteasome 19S subunit. Interacts (via ubiquitin-like domain) with TREX1; the interaction is direct and may control TREX1 subcellular location. Forms a complex with UBXN4 and VCP. Interacts (via UBA domain) with UBQLN4 (via ubiquitin-like domain). Found in a complex with UBQLN2 and MAP1LC3A/B/C. The monomeric form interacts with PSEN2 and the monomeric forms of isoform 1 and isoform 3 interact with PSEN1. Interacts with ORAI1. Interacts (via UBA domain) with TICAM1. Interacts with EPS15. Interacts (via UBA domain) with UBA52 and (via ubiquitin-like domain) with PSMD3 and PSMD4. Interacts with HERPUD1. Interacts with MAP1LC3A/B/C in the presence of UBQLN4. Interacts (via ubiquitin-like domain) with EPS15 (via UIM domains) and both the ubiquitinated and non-ubiquitinated forms can interact with EPS15. Interacts (via ubiquitin-like domain) with EPS15L1, HGS (via UIM domain) and STAM2 (via UIM domain).By similarity17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-741480,EBI-741480
Q8WU023EBI-741480,EBI-747182
Q96FB23EBI-10173939,EBI-2857623
ACOT7O001543EBI-10173939,EBI-948905
ADRM1Q161864EBI-741480,EBI-954387
AGPAT5Q9NUQ23EBI-741480,EBI-6916385
AGR2O959943EBI-741480,EBI-712648
AGR3Q8TD063EBI-10173939,EBI-3925742
BPIFA1Q9NP553EBI-10173939,EBI-953896
C1QTNF2Q9BXJ53EBI-10173939,EBI-2817707
CALUO438523EBI-10173939,EBI-1171069
CARKDQ8IW453EBI-10173939,EBI-8650724
CCL7P800983EBI-10173939,EBI-718759
CD99L2Q8TCZ23EBI-10173939,EBI-2824782
COL10A1Q036923EBI-741480,EBI-2528309
COL1A2P081233EBI-741480,EBI-983038
COLGALT2Q8IYK43EBI-10173939,EBI-10263496
COMTD1Q86VU53EBI-10173939,EBI-2836030
CSTF2P332404EBI-741480,EBI-711360
CSTF2TQ9H0L44EBI-741480,EBI-747012
CTAG1BP783583EBI-741480,EBI-1188472
CTAG2O756383EBI-10173939,EBI-10188927
CYB5R1Q9UHQ93EBI-10173939,EBI-953870
DEFA6Q015243EBI-741480,EBI-10222451
EFEMP2O959673EBI-10173939,EBI-743414
EPS15P425665EBI-741480,EBI-396684
ERP27Q96DN03EBI-10173939,EBI-953772
ETNK1Q9HBU63EBI-10173939,EBI-2834493
FAM127AA6ZKI33EBI-741480,EBI-10174072
FAM127BQ9BWD34EBI-741480,EBI-741643
FAM127CQ17RB03EBI-10173939,EBI-10238588
FCGR2AP123183EBI-10173939,EBI-1395970
FKBP2P268853EBI-741480,EBI-719873
FN1P027513EBI-741480,EBI-1220319
GABRDO147644EBI-741480,EBI-744352
GHRLQ9UBU33EBI-741480,EBI-10319458
GPX3P223523EBI-10173939,EBI-2832946
GRM2Q144163EBI-10173939,EBI-10232876
GYPBP060283EBI-10173939,EBI-10194756
HK2P527894EBI-741480,EBI-741469
HSD17B12Q53GQ03EBI-10173939,EBI-2963255
HSPA13P487235EBI-741480,EBI-750892
IGL@Q6PIK13EBI-10173939,EBI-10253735
IGL@Q6PIQ73EBI-10173939,EBI-6677651
IGL@Q8N3554EBI-741480,EBI-748681
IL6STQ17RA03EBI-10173939,EBI-10238517
IST1P539903EBI-741480,EBI-945994
ITPRIPL1Q6GPH63EBI-741480,EBI-953819
KLHL42Q9P2K63EBI-10173939,EBI-739890
LITAFQ997324EBI-741480,EBI-725647
MANBALQ9NQG13EBI-10173939,EBI-3867271
MCM7P339933EBI-10173939,EBI-355924
MIEF1Q9NQG63EBI-10173939,EBI-740987
MIEF2Q96C034EBI-741480,EBI-750153
MLLT6P551983EBI-10173939,EBI-740216
NBL1P412713EBI-10173939,EBI-10208650
NGLY1Q96IV03EBI-10173939,EBI-6165879
NME3Q132323EBI-10173939,EBI-713684
NPPAP011603EBI-741480,EBI-953859
NUPL1Q9BVL23EBI-10173939,EBI-2811583
PAUFC3PTT63EBI-10173939,EBI-3505892
PBXIP1Q96AQ63EBI-10173939,EBI-740845
PIK3IP1Q96FE73EBI-741480,EBI-10285708
PLA2G16P538164EBI-741480,EBI-746318
PNMA1Q8ND904EBI-741480,EBI-302345
PPIBP232843EBI-741480,EBI-359252
PPICP458773EBI-10173939,EBI-953909
PRAP1Q96NZ93EBI-741480,EBI-2116102
PRB1A5D9033EBI-10173939,EBI-10173935
PSMD4P550366EBI-741480,EBI-359318
PSMD6Q150083EBI-10173939,EBI-359701
RIC8AQ9NPQ83EBI-741480,EBI-717509
RIC8AQ9NPQ8-43EBI-10173939,EBI-9091816
RNF208Q9H0X63EBI-741480,EBI-751555
RPN1P048433EBI-10173939,EBI-355963
RSRC2Q7L4I2-23EBI-741480,EBI-10256202
SCG5P054083EBI-10173939,EBI-722635
SCMH1Q96GD33EBI-741480,EBI-713793
SERPINE1P051213EBI-741480,EBI-953978
SERPINI2O758306EBI-741480,EBI-750144
SIL1Q9H1733EBI-741480,EBI-2840325
SMIM2Q9BVW63EBI-10173939,EBI-10300146
SMR3BP028143EBI-741480,EBI-738612
SRGNP101243EBI-10173939,EBI-744915
TMCO6Q96DC7-23EBI-741480,EBI-10284552
TMEM31Q5JXX73EBI-10173939,EBI-10244617
TMUB2Q71RG43EBI-10173939,EBI-2820477
TRIM32Q130494EBI-741480,EBI-742790
TXNDC12O958813EBI-10173939,EBI-2564581
UBBQ5U5U63EBI-741480,EBI-1642104
UBCP0CG483EBI-741480,EBI-3390054
UBCQ96C323EBI-741480,EBI-745483
UBE2V1Q134043EBI-741480,EBI-1050671
UBQLN4Q9NRR58EBI-741480,EBI-711226
UBXN1Q043233EBI-10173939,EBI-1058647
UBXN4Q925753EBI-10173939,EBI-723441
XPO4Q0VG753EBI-10173939,EBI-10226948
ZFAND2BQ8WV993EBI-10173939,EBI-747823
ZG16O608444EBI-741480,EBI-746479
ZMYM4Q5VZL53EBI-10173939,EBI-2514659
ZNF343Q6P1L63EBI-741480,EBI-10252492

Protein-protein interaction databases

BioGridi119007. 402 interactions.
DIPiDIP-41629N.
IntActiQ9UMX0. 127 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
Domaini182 – 21029STI1 1Sequence AnalysisAdd
BLAST
Domaini212 – 25140STI1 2Sequence AnalysisAdd
BLAST
Domaini387 – 43448STI1 3Sequence AnalysisAdd
BLAST
Domaini438 – 47033STI1 4Sequence AnalysisAdd
BLAST
Domaini546 – 58641UBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 428251Interaction with UBXN41 PublicationAdd
BLAST

Domaini

The UBA domain mediates binding to PSEN1 and PSEN2. It also binds ubiquitin with micromolar affinity, independently of polyubiquitin linkage type. Essential for its association with microtubule-associated protein 1 light chain 3 (MAP1LC3).3 Publications
The ubiquitin-like domain mediates its association with the subunits of the proteasome.1 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

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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 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:
     417-444: Missing.

Note: No experimental confirmation available.
Show »
Length:561
Mass (Da):59,220
Checksum:i1E0BC42EC5BA4DA6
GO
Isoform 3 (identifier: Q9UMX0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-237: Missing.

Show »
Length:412
Mass (Da):43,038
Checksum:i61264678FFCAA699
GO
Isoform 4 (identifier: Q9UMX0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-181: GGLGGLAGLSSLGLNTTNFSELQSQMQRQLLS → DVGTCQESSNDAGDDEEPGPSFEQPRKHPRGI
     182-589: Missing.

Show »
Length:181
Mass (Da):18,910
Checksum:i92A3D97BF619E306
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 sequencei61 – 237177Missing in isoform 3. 1 PublicationVSP_057689Add
BLAST
Alternative sequencei150 – 18132GGLGG…RQLLS → DVGTCQESSNDAGDDEEPGP SFEQPRKHPRGI in isoform 4. 1 PublicationVSP_057690Add
BLAST
Alternative sequencei182 – 589408Missing in isoform 4. 1 PublicationVSP_057691Add
BLAST
Alternative sequencei417 – 44428Missing in isoform 2. 2 PublicationsVSP_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]

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. 402 interactions.
DIPiDIP-41629N.
IntActiQ9UMX0. 127 interactions.
MINTiMINT-150317.
STRINGi9606.ENSP00000365576.

PTM databases

PhosphoSiteiQ9UMX0.

Polymorphism and mutation databases

BioMutaiUBQLN1.
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.
GenevisibleiQ9UMX0. HS.

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(2000) [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 (JAN-2002) 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(2000) [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(2000) [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(2004) [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(2004) [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(2004) [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 (DEC-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(2002) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH P4HB.
  13. "Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains."
    Ko H.S., Uehara T., Tsuruma K., Nomura Y.
    FEBS Lett. 566:110-114(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN UBIQUITIN-LIKE, DOMAIN UBA, INTERACTION WITH UBA52; PSMD3 AND PSMD4.
  14. Cited for: INTERACTION WITH EPS15; EPS15L1; HGS AND STAM2, SUBCELLULAR LOCATION, UBIQUITINATION.
  15. "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 UBQLN2, INTERACTION WITH PSEN1 AND PSEN2.
  16. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  17. "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.
  18. "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: INTERACTION WITH EPS15.
  19. "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].
  20. "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.
  21. Cited for: FUNCTION, INTERACTION WITH UBXN4, IDENTIFICATION IN A COMPLEX WITH UBXN4 AND VCP, SUBCELLULAR LOCATION.
  22. Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4), FUNCTION, TISSUE SPECIFICITY.
  23. "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.
  24. Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH UBQLN2 AND MAP1LC3A/B/C, PROTEOLYTIC DEGRADATION.
  25. "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(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].
    Tissue: Cervix carcinoma.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Involvement of ubiquilin-1 transcript variants in protein degradation and accumulation."
    Haapasalo A., Viswanathan J., Kurkinen K.M., Bertram L., Soininen H., Dantuma N.P., Tanzi R.E., Hiltunen M.
    Commun. Integr. Biol. 4:428-432(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  28. "The ubiquitin-like protein PLIC-1 or ubiquilin 1 inhibits TLR3-Trif signaling."
    Biswas N., Liu S., Ronni T., Aussenberg S.E., Liu W., Fujita T., Wang T.
    PLoS ONE 6:E21153-E21153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TICAM1.
  29. "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(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].
  30. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PSEN1.
  31. "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.
  32. "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(2012) [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].
  33. "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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBQLN4 AND MAP1LC3A/B/C.
  34. Cited for: REVIEW.
  35. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TREX1, SUBCELLULAR LOCATION.
  36. "Ubiquilin 1 interacts with Orai1 to regulate calcium mobilization."
    Lee J.E., Jeon I.S., Han N.E., Song H.J., Kim E.G., Choi J.W., Song K.D., Lee H.K., Choi J.K.
    Mol. Cells 35:41-46(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ORAI1, SUBCELLULAR LOCATION.
  37. "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.
  38. "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(2008) [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: June 24, 2015
This is version 142 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.