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O60828

- PQBP1_HUMAN

UniProt

O60828 - PQBP1_HUMAN

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Protein
Polyglutamine-binding protein 1
Gene
PQBP1, NPW38, JM26
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probably functions as scaffold protein that is part of numerous complexes and thereby plays a role in pre-mRNA splicing, transcription regulation and neuron development. Required for normal alternative splicing of target pre-mRNA species (1 Publication). May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit.

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. ribonucleoprotein complex binding Source: MGI
  3. transcription coactivator activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. regulation of RNA splicing Source: MGI
  2. regulation of transcription, DNA-templated Source: ProtInc
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiO60828.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyglutamine-binding protein 1
Short name:
PQBP-1
Alternative name(s):
38 kDa nuclear protein containing a WW domain
Short name:
Npw38
Polyglutamine tract-binding protein 1
Gene namesi
Name:PQBP1
Synonyms:NPW38
ORF Names:JM26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9330. PQBP1.

Subcellular locationi

Nucleus. Nucleus speckle By similarity
Note: Colocalizes with SRSF2 in nuclear speckles By similarity. Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic stress granule Source: Ensembl
  3. neuronal ribonucleoprotein granule Source: Ensembl
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Renpenning syndrome 1 (RENS1) [MIM:309500]: A X-linked mental retardation syndrome characterized by mental retardation, microcephaly, short stature, and small testes. The craniofacies tends to be narrow and tall with upslanting palpebral fissures, abnormal nasal configuration, cupped ears, and short philtrum. The nose may appear long or bulbous, with overhanging columella. Less consistent manifestations include ocular colobomas, cardiac malformations, cleft palate, and anal anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651Y → C in RENS1; impairs interaction with WBP11, SF3B1 and ATN1.
VAR_071063

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521W → A: Enhances transcriptional activation. Reduces transcriptional activation; when associated with A-75. Markedly reduced transcriptional activation; when associated with A-64; A-65 and A-66. Abolishes transcriptional activation; when associated with A-64; A-65; A-66 and A-75.
Mutagenesisi64 – 641Y → A: No effect on transcriptional activation; when associated with A-65 and A-66. Markedly reduced transcriptional activation; when associated with A-52; A-65 and A-66. Abolishes transcriptional activation; when associated with A-52; A-65; A-66 and A-75.
Mutagenesisi65 – 651Y → A: No effect on transcriptional activation; when associated with A-64 and A-66. Markedly reduced transcriptional activation; when associated with A-52; A-64 and A-66. Abolishes transcriptional activation; when associated with A-52; A-64; A-66 and A-75.
Mutagenesisi66 – 661W → A: No effect on transcriptional activation; when associated with A-64 and A-65. Markedly reduced transcriptional activation; when associated with A-52; A-64 and A-65. Abolishes transcriptional activation; when associated with A-52; A-64; A-65 and A-75.
Mutagenesisi75 – 751W → A: No effect on transcriptional activation. Reduces transcriptional activation; when associated with A-52. Abolishes transcriptional activation; when associated with A-52; A-64; A-65 and A-66.
Mutagenesisi78 – 781P → G: No effect on transcriptional activation.
Mutagenesisi245 – 2451Y → D: Abolishes interaction with TXNL4A.
Mutagenesisi248 – 2481P → D: Abolishes interaction with TXNL4A.
Mutagenesisi251 – 2511V → D: Abolishes interaction with TXNL4A.
Mutagenesisi252 – 2521L → D: Abolishes interaction with TXNL4A.
Mutagenesisi253 – 2531R → D: Strongly reduces affinity for TXNL4A.
Mutagenesisi255 – 2551N → D: Strongly reduces affinity for TXNL4A.

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi309500. phenotype.
Orphaneti93946. Hamel cerebro-palato-cardiac syndrome.
93947. X-linked intellectual disability, Golabi-Ito-Hall type.
93945. X-linked intellectual disability, Porteous type.
93950. X-linked intellectual disability, Sutherland-Haan type.
PharmGKBiPA33693.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 265264Polyglutamine-binding protein 1
PRO_0000076089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60828.
PaxDbiO60828.
PRIDEiO60828.

PTM databases

PhosphoSiteiO60828.

Miscellaneous databases

PMAP-CutDBO60828.

Expressioni

Tissue specificityi

Widely expressed with high level in heart, skeletal muscle, pancreas, spleen, thymus, prostate, ovary, small intestine and peripheral blood leukocytes.2 Publications

Gene expression databases

ArrayExpressiO60828.
BgeeiO60828.
GenevestigatoriO60828.

Organism-specific databases

HPAiHPA001880.

Interactioni

Subunit structurei

Interacts with POU3F2/Brn-2, ATXN1, TXNL4A, HTT and AR. Interaction with ATXN1 correlates positively with the length of the polyglutamine tract. Interacts with RNA polymerase II large subunit in a phosphorylation-dependent manner. Forms a ternary complex with ATXN1 mutant and phosphorylated RNA polymerase II. Interacts (via C-terminus) with TXNL4A and CD2BP2. Interacts (via WW domain) with ATN1, WBP11 and SF3B1, and may interact with additional splice factors.4 Publications

Protein-protein interaction databases

BioGridi115393. 36 interactions.
IntActiO60828. 12 interactions.
MINTiMINT-112545.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi248 – 25811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BWQX-ray2.10B/D/F/H223-265[»]
4BWSX-ray2.50B/E229-265[»]
4CDOX-ray2.50A/C223-265[»]
ProteinModelPortaliO60828.
SMRiO60828. Positions 46-79.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 8035WW
Add
BLAST
Repeati104 – 11071-1
Repeati111 – 11771-2
Repeati118 – 12471-3
Repeati125 – 13171-4
Repeati132 – 13871-5
Repeati139 – 14022-1
Repeati141 – 14222-2
Repeati143 – 14422-3
Repeati150 – 15123-1
Repeati152 – 15323-2
Repeati154 – 15523-3
Repeati156 – 15723-4
Repeati158 – 15923-5
Repeati160 – 16123-6
Repeati162 – 16323-7

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 265172Intrinsically disordered
Add
BLAST
Regioni104 – 138355 X 7 AA approximate tandem repeats of D-R-[SG]-H-D-K-S
Add
BLAST
Regioni139 – 14463 X 2 AA tandem repeats of [DE]-R
Regioni150 – 163147 X 2 AA tandem repeats of [DE]-R
Add
BLAST
Regioni245 – 25511Important for interaction with TXNL4A
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi140 – 18142Arg-rich
Add
BLAST

Domaini

The WW domain may play a role as a transcriptional activator directly or via association with the transcription machinery. The WW domain mediates interaction with WBP11, ATN1, SF3B1 and the C-terminal domain of the RNA polymerase II large subunit.
Except for the WW domain, the protein is intrinsically disordered.

Sequence similaritiesi

Contains 1 WW domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG265480.
HOVERGENiHBG053064.
InParanoidiO60828.
KOiK12865.
OMAiSHEKSDR.
PhylomeDBiO60828.
TreeFamiTF320689.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

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

This entry describes 10 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60828-1) [UniParc]FASTAAdd to Basket

Also known as: PQBP-1

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

MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP    50
SWYKVFDPSC GLPYYWNADT DLVSWLSPHD PNSVVTKSAK KLRSSNADAE 100
EKLDRSHDKS DRGHDKSDRS HEKLDRGHDK SDRGHDKSDR DRERGYDKVD 150
RERERDRERD RDRGYDKADR EEGKERRHHR REELAPYPKS KKAVSRKDEE 200
LDPMDPSSYS DAPRGTWSTG LPKRNEAKTG ADTTAAGPLF QQRPYPSPGA 250
VLRANAEASR TKQQD 265
Length:265
Mass (Da):30,472
Last modified:August 1, 1998 - v1
Checksum:i98C3BEF18CFF0297
GO
Isoform 2 (identifier: O60828-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     193-193: Missing.

Show »
Length:264
Mass (Da):30,401
Checksum:i56BBC35A4CFB41C0
GO
Isoform 3 (identifier: O60828-3) [UniParc]FASTAAdd to Basket

Also known as: PQBP-1b/c

The sequence of this isoform differs from the canonical sequence as follows:
     193-224: AVSRKDEELDPMDPSSYSDAPRGTWSTGLPKR → GKLGRMGLGETNKVQGALREEAFPQKDAWTWG
     225-265: Missing.

Show »
Length:224
Mass (Da):26,158
Checksum:i7DAC3C07D84492F0
GO
Isoform 4 (identifier: O60828-4) [UniParc]FASTAAdd to Basket

Also known as: PQBP-1d

The sequence of this isoform differs from the canonical sequence as follows:
     98-192: Missing.

Show »
Length:170
Mass (Da):18,827
Checksum:iD01C0EAB17B61307
GO
Isoform 5 (identifier: O60828-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-167: Missing.

Show »
Length:165
Mass (Da):18,706
Checksum:iA32760CAAEFE5751
GO
Isoform 6 (identifier: O60828-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     149-149: V → Q
     150-265: Missing.

Show »
Length:149
Mass (Da):17,183
Checksum:i88C7259FF95C0501
GO
Isoform 7 (identifier: O60828-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     99-128: AEEKLDRSHDKSDRGHDKSDRSHEKLDRGH → LCPQMLKKSWTGAMTSRTGAMTSRTAAMRN
     129-265: Missing.

Show »
Length:128
Mass (Da):14,383
Checksum:i1000C586B57B3758
GO
Isoform 8 (identifier: O60828-8) [UniParc]FASTAAdd to Basket

Also known as: PQBP-1a

The sequence of this isoform differs from the canonical sequence as follows:
     55-73: VFDPSCGLPYYWNADTDLV → RAPLLLECRHRPCILALPT
     74-265: Missing.

Show »
Length:73
Mass (Da):8,404
Checksum:iEF932C61145DC023
GO
Isoform 9 (identifier: O60828-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-67: GLPYYWN → PGWSAMV
     68-265: Missing.

Show »
Length:67
Mass (Da):7,627
Checksum:iF7FA61EC5E06DE6D
GO
Isoform 10 (identifier: O60828-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-60: C → W
     61-265: Missing.

Show »
Length:60
Mass (Da):6,981
Checksum:i1025785C46650A62
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651Y → C in RENS1; impairs interaction with WBP11, SF3B1 and ATN1.
VAR_071063
Natural varianti224 – 2241R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036357

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 7319VFDPS…DTDLV → RAPLLLECRHRPCILALPT in isoform 8.
VSP_015896Add
BLAST
Alternative sequencei60 – 601C → W in isoform 10.
VSP_015897
Alternative sequencei61 – 265205Missing in isoform 10.
VSP_015898Add
BLAST
Alternative sequencei61 – 677GLPYYWN → PGWSAMV in isoform 9.
VSP_015899
Alternative sequencei68 – 265198Missing in isoform 9.
VSP_015901Add
BLAST
Alternative sequencei68 – 167100Missing in isoform 5.
VSP_015900Add
BLAST
Alternative sequencei74 – 265192Missing in isoform 8.
VSP_015902Add
BLAST
Alternative sequencei98 – 19295Missing in isoform 4.
VSP_015903Add
BLAST
Alternative sequencei99 – 12830AEEKL…LDRGH → LCPQMLKKSWTGAMTSRTGA MTSRTAAMRN in isoform 7.
VSP_015904Add
BLAST
Alternative sequencei129 – 265137Missing in isoform 7.
VSP_015905Add
BLAST
Alternative sequencei149 – 1491V → Q in isoform 6.
VSP_015906
Alternative sequencei150 – 265116Missing in isoform 6.
VSP_015907Add
BLAST
Alternative sequencei193 – 22432AVSRK…GLPKR → GKLGRMGLGETNKVQGALRE EAFPQKDAWTWG in isoform 3.
VSP_015908Add
BLAST
Alternative sequencei193 – 1931Missing in isoform 2.
VSP_015909
Alternative sequencei225 – 26541Missing in isoform 3.
VSP_015910Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81Q → L in CAJ00539. 1 Publication
Sequence conflicti57 – 571D → N in CAJ00548. 1 Publication
Sequence conflicti107 – 1137Missing in CAJ00538. 1 Publication
Sequence conflicti107 – 1137Missing in CAJ00539. 1 Publication
Sequence conflicti107 – 1137Missing in CAJ00540. 1 Publication
Sequence conflicti107 – 1137Missing in CAJ00541. 1 Publication
Sequence conflicti107 – 1071H → Q in CAJ00549. 1 Publication
Sequence conflicti147 – 1471D → G in CAJ00549. 1 Publication
Sequence conflicti198 – 1981D → G in CAJ00549. 1 Publication
Sequence conflicti236 – 2361A → V in CAJ00548. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ242829 mRNA. Translation: CAB44309.1.
AB016533 mRNA. Translation: BAA76400.1.
AB041832 Genomic DNA. Translation: BAB16702.1.
AB041832 Genomic DNA. Translation: BAB16703.1.
AB041832 Genomic DNA. Translation: BAB16704.1.
AB041832 Genomic DNA. Translation: BAB16705.1.
AB041833 mRNA. Translation: BAB16706.1.
AB041834 mRNA. Translation: BAB16707.1.
AB041835 mRNA. Translation: BAB16708.1.
AB041836 mRNA. Translation: BAB16709.1.
AJ973593 mRNA. Translation: CAJ00537.1.
AJ973594 mRNA. Translation: CAJ00538.1.
AJ973595 mRNA. Translation: CAJ00539.1.
AJ973596 mRNA. Translation: CAJ00540.1.
AJ973597 mRNA. Translation: CAJ00541.1.
AJ973598 mRNA. Translation: CAJ00542.1.
AJ973599 mRNA. Translation: CAJ00543.1.
AJ973600 mRNA. Translation: CAJ00544.1.
AJ973601 mRNA. Translation: CAJ00545.1.
AJ973602 mRNA. Translation: CAJ00546.1.
AJ973603 mRNA. Translation: CAJ00547.1.
AJ973605 mRNA. Translation: CAJ00548.1.
AJ973606 mRNA. Translation: CAJ00549.1.
AJ973607 mRNA. Translation: CAJ00550.1.
AJ005893 mRNA. Translation: CAA06750.1.
BC012358 mRNA. Translation: AAH12358.1.
CCDSiCCDS14309.1. [O60828-1]
CCDS55412.1. [O60828-4]
RefSeqiNP_001027553.1. NM_001032381.1. [O60828-1]
NP_001027554.1. NM_001032382.1. [O60828-1]
NP_001027555.1. NM_001032383.1. [O60828-1]
NP_001027556.1. NM_001032384.1. [O60828-1]
NP_001161461.1. NM_001167989.1. [O60828-2]
NP_001161462.1. NM_001167990.1.
NP_001161464.1. NM_001167992.1. [O60828-5]
NP_005701.1. NM_005710.2. [O60828-1]
NP_652766.1. NM_144495.2. [O60828-4]
XP_005272628.1. XM_005272571.2. [O60828-2]
XP_005272629.1. XM_005272572.2. [O60828-4]
UniGeneiHs.534384.

Genome annotation databases

EnsembliENST00000218224; ENSP00000218224; ENSG00000102103. [O60828-1]
ENST00000247140; ENSP00000247140; ENSG00000102103. [O60828-4]
ENST00000376548; ENSP00000365731; ENSG00000102103. [O60828-9]
ENST00000376563; ENSP00000365747; ENSG00000102103. [O60828-1]
ENST00000376566; ENSP00000365750; ENSG00000102103. [O60828-4]
ENST00000396763; ENSP00000379985; ENSG00000102103. [O60828-1]
ENST00000447146; ENSP00000391759; ENSG00000102103. [O60828-1]
ENST00000593464; ENSP00000472506; ENSG00000268142. [O60828-1]
ENST00000594868; ENSP00000469772; ENSG00000268142. [O60828-1]
ENST00000597699; ENSP00000472009; ENSG00000268142. [O60828-1]
ENST00000597809; ENSP00000470666; ENSG00000268142. [O60828-9]
ENST00000600107; ENSP00000471461; ENSG00000268142. [O60828-1]
ENST00000600640; ENSP00000469504; ENSG00000268142. [O60828-4]
ENST00000601234; ENSP00000472437; ENSG00000268142. [O60828-4]
GeneIDi10084.
KEGGihsa:10084.
UCSCiuc004dle.3. human. [O60828-1]
uc004dlj.1. human. [O60828-3]
uc004dlk.3. human. [O60828-4]
uc004dln.3. human. [O60828-2]
uc010nij.3. human. [O60828-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ242829 mRNA. Translation: CAB44309.1 .
AB016533 mRNA. Translation: BAA76400.1 .
AB041832 Genomic DNA. Translation: BAB16702.1 .
AB041832 Genomic DNA. Translation: BAB16703.1 .
AB041832 Genomic DNA. Translation: BAB16704.1 .
AB041832 Genomic DNA. Translation: BAB16705.1 .
AB041833 mRNA. Translation: BAB16706.1 .
AB041834 mRNA. Translation: BAB16707.1 .
AB041835 mRNA. Translation: BAB16708.1 .
AB041836 mRNA. Translation: BAB16709.1 .
AJ973593 mRNA. Translation: CAJ00537.1 .
AJ973594 mRNA. Translation: CAJ00538.1 .
AJ973595 mRNA. Translation: CAJ00539.1 .
AJ973596 mRNA. Translation: CAJ00540.1 .
AJ973597 mRNA. Translation: CAJ00541.1 .
AJ973598 mRNA. Translation: CAJ00542.1 .
AJ973599 mRNA. Translation: CAJ00543.1 .
AJ973600 mRNA. Translation: CAJ00544.1 .
AJ973601 mRNA. Translation: CAJ00545.1 .
AJ973602 mRNA. Translation: CAJ00546.1 .
AJ973603 mRNA. Translation: CAJ00547.1 .
AJ973605 mRNA. Translation: CAJ00548.1 .
AJ973606 mRNA. Translation: CAJ00549.1 .
AJ973607 mRNA. Translation: CAJ00550.1 .
AJ005893 mRNA. Translation: CAA06750.1 .
BC012358 mRNA. Translation: AAH12358.1 .
CCDSi CCDS14309.1. [O60828-1 ]
CCDS55412.1. [O60828-4 ]
RefSeqi NP_001027553.1. NM_001032381.1. [O60828-1 ]
NP_001027554.1. NM_001032382.1. [O60828-1 ]
NP_001027555.1. NM_001032383.1. [O60828-1 ]
NP_001027556.1. NM_001032384.1. [O60828-1 ]
NP_001161461.1. NM_001167989.1. [O60828-2 ]
NP_001161462.1. NM_001167990.1.
NP_001161464.1. NM_001167992.1. [O60828-5 ]
NP_005701.1. NM_005710.2. [O60828-1 ]
NP_652766.1. NM_144495.2. [O60828-4 ]
XP_005272628.1. XM_005272571.2. [O60828-2 ]
XP_005272629.1. XM_005272572.2. [O60828-4 ]
UniGenei Hs.534384.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BWQ X-ray 2.10 B/D/F/H 223-265 [» ]
4BWS X-ray 2.50 B/E 229-265 [» ]
4CDO X-ray 2.50 A/C 223-265 [» ]
ProteinModelPortali O60828.
SMRi O60828. Positions 46-79.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115393. 36 interactions.
IntActi O60828. 12 interactions.
MINTi MINT-112545.

PTM databases

PhosphoSitei O60828.

Proteomic databases

MaxQBi O60828.
PaxDbi O60828.
PRIDEi O60828.

Protocols and materials databases

DNASUi 10084.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000218224 ; ENSP00000218224 ; ENSG00000102103 . [O60828-1 ]
ENST00000247140 ; ENSP00000247140 ; ENSG00000102103 . [O60828-4 ]
ENST00000376548 ; ENSP00000365731 ; ENSG00000102103 . [O60828-9 ]
ENST00000376563 ; ENSP00000365747 ; ENSG00000102103 . [O60828-1 ]
ENST00000376566 ; ENSP00000365750 ; ENSG00000102103 . [O60828-4 ]
ENST00000396763 ; ENSP00000379985 ; ENSG00000102103 . [O60828-1 ]
ENST00000447146 ; ENSP00000391759 ; ENSG00000102103 . [O60828-1 ]
ENST00000593464 ; ENSP00000472506 ; ENSG00000268142 . [O60828-1 ]
ENST00000594868 ; ENSP00000469772 ; ENSG00000268142 . [O60828-1 ]
ENST00000597699 ; ENSP00000472009 ; ENSG00000268142 . [O60828-1 ]
ENST00000597809 ; ENSP00000470666 ; ENSG00000268142 . [O60828-9 ]
ENST00000600107 ; ENSP00000471461 ; ENSG00000268142 . [O60828-1 ]
ENST00000600640 ; ENSP00000469504 ; ENSG00000268142 . [O60828-4 ]
ENST00000601234 ; ENSP00000472437 ; ENSG00000268142 . [O60828-4 ]
GeneIDi 10084.
KEGGi hsa:10084.
UCSCi uc004dle.3. human. [O60828-1 ]
uc004dlj.1. human. [O60828-3 ]
uc004dlk.3. human. [O60828-4 ]
uc004dln.3. human. [O60828-2 ]
uc010nij.3. human. [O60828-5 ]

Organism-specific databases

CTDi 10084.
GeneCardsi GC0XP048755.
HGNCi HGNC:9330. PQBP1.
HPAi HPA001880.
MIMi 300463. gene.
309500. phenotype.
neXtProti NX_O60828.
Orphaneti 93946. Hamel cerebro-palato-cardiac syndrome.
93947. X-linked intellectual disability, Golabi-Ito-Hall type.
93945. X-linked intellectual disability, Porteous type.
93950. X-linked intellectual disability, Sutherland-Haan type.
PharmGKBi PA33693.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG265480.
HOVERGENi HBG053064.
InParanoidi O60828.
KOi K12865.
OMAi SHEKSDR.
PhylomeDBi O60828.
TreeFami TF320689.

Enzyme and pathway databases

SignaLinki O60828.

Miscellaneous databases

ChiTaRSi PQBP1. human.
GeneWikii PQBP1.
GenomeRNAii 10084.
NextBioi 38125.
PMAP-CutDB O60828.
PROi O60828.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60828.
Bgeei O60828.
Genevestigatori O60828.

Family and domain databases

InterProi IPR001202. WW_dom.
[Graphical view ]
Pfami PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "PQBP-1, a novel polyglutamine tract binding protein, inhibits transcription activation by Brn-2 and affects cell survival."
    Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y., Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.
    Hum. Mol. Genet. 8:977-987(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH POU3F2; HTT AND AR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Npw38, a novel nuclear protein possessing a WW domain capable of activating basal transcription."
    Komuro A., Saeki M., Kato S.
    Nucleic Acids Res. 27:1957-1965(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TRP-52; TYR-64; TYR-65; TRP-66; TRP-75 AND PRO-78.
    Tissue: Gastric adenocarcinoma.
  3. "Genomic organization and alternative transcripts of the human PQBP-1 gene."
    Iwamoto K., Huang Y.-T., Ueda S.
    Gene 259:69-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3; 4 AND 7).
  4. "Detailed sampling of cloned cDNA samples identifies additional PQBP1 transcript variants."
    Eades T.L., Huckle E.L., Ross M.T.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 8; 9 AND 10).
    Tissue: Adrenal gland, Kidney, Small intestine and Thymus.
  5. "Transcription map in Xp11.23."
    Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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] (ISOFORM 1).
    Tissue: Lung.
  7. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10 AND 229-243, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  8. Cited for: INTERACTION WITH POU3F2.
  9. "PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain."
    Waragai M., Junn E., Kajikawa M., Takeuchi S., Kanazawa I., Shibata M., Mouradian M.M., Okazawa H.
    Biochem. Biophys. Res. Commun. 273:592-595(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TXNL4A.
  10. "Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death."
    Okazawa H., Rich T., Chang A., Lin X., Waragai M., Kajikawa M., Enokido Y., Komuro A., Kato S., Shibata M., Hatanaka H., Mouradian M.M., Sudol M., Kanazawa I.
    Neuron 34:701-713(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATXN1 AND RNA POLYMERASE II LARGE SUBUNIT, SUBCELLULAR LOCATION.
  11. Cited for: REVIEW ON RENS1.
  12. Cited for: INVOLVEMENT IN RENS1.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Polyglutamine tract binding protein-1 is an intrinsically unstructured protein."
    Takahashi M., Mizuguchi M., Shinoda H., Aizawa T., Demura M., Okazawa H., Kawano K.
    Biochim. Biophys. Acta 1794:936-943(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, CIRCULAR DICHROISM, NMR, INTERACTION WITH TXNL4A.
  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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth."
    Wang Q., Moore M.J., Adelmant G., Marto J.A., Silver P.A.
    Genes Dev. 27:615-626(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SF3B1 AND WBP11, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT RENS1 CYS-65.
  19. "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD."
    Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y., Okazawa H.
    Nat. Commun. 5:3822-3822(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 223-265 IN COMPLEXES WITH TXNL4A AND CD2BP2, INTERACTION WITH TXNL4A AND CD2BP2, DOMAIN, MUTAGENESIS OF TYR-245; PRO-248; VAL-251; LEU-252; ARG-253 AND ASN-255.
  20. "Golabi-Ito-Hall syndrome results from a missense mutation in the WW domain of the PQBP1 gene."
    Lubs H., Abidi F.E., Echeverri R., Holloway L., Meindl A., Stevenson R.E., Schwartz C.E.
    J. Med. Genet. 43:E30-E30(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RENS1 CYS-65.
  21. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-224.
  22. "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing."
    Tapia V.E., Nicolaescu E., McDonald C.B., Musi V., Oka T., Inayoshi Y., Satteson A.C., Mazack V., Humbert J., Gaffney C.J., Beullens M., Schwartz C.E., Landgraf C., Volkmer R., Pastore A., Farooq A., Bollen M., Sudol M.
    J. Biol. Chem. 285:19391-19401(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT RENS1 CYS-65, INTERACTION WITH WBP11 AND ATN1, DOMAIN, FUNCTION.

Entry informationi

Entry nameiPQBP1_HUMAN
AccessioniPrimary (citable) accession number: O60828
Secondary accession number(s): Q4VY25
, Q4VY26, Q4VY27, Q4VY29, Q4VY30, Q4VY34, Q4VY35, Q4VY36, Q4VY37, Q4VY38, Q9GZP2, Q9GZU4, Q9GZZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 127 of the entry and version 1 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 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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