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O60828 (PQBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PQBP1
Synonyms:NPW38
ORF Names:JM26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.10

Subunit structure

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. Ref.1 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus. Note: Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies. Ref.1 Ref.2 Ref.10

Tissue specificity

Widely expressed with high level in heart, skeletal muscle, pancreas, spleen, thymus, prostate, ovary, small intestine and peripheral blood leukocytes. Ref.1 Ref.2

Domain

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 C-terminal domain of RNA polymerase II large subunit.

Involvement in disease

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. Ref.12

Sequence similarities

Contains 1 WW domain.

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60828-1)

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.
Isoform 2 (identifier: O60828-2)

The sequence of this isoform differs from the canonical sequence as follows:
     193-193: Missing.
Isoform 3 (identifier: O60828-3)

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.
Isoform 4 (identifier: O60828-4)

Also known as: PQBP-1d;

The sequence of this isoform differs from the canonical sequence as follows:
     98-192: Missing.
Isoform 5 (identifier: O60828-5)

The sequence of this isoform differs from the canonical sequence as follows:
     68-167: Missing.
Isoform 6 (identifier: O60828-6)

The sequence of this isoform differs from the canonical sequence as follows:
     149-149: V → Q
     150-265: Missing.
Isoform 7 (identifier: O60828-7)

The sequence of this isoform differs from the canonical sequence as follows:
     99-128: AEEKLDRSHDKSDRGHDKSDRSHEKLDRGH → LCPQMLKKSWTGAMTSRTGAMTSRTAAMRN
     129-265: Missing.
Isoform 8 (identifier: O60828-8)

Also known as: PQBP-1a;

The sequence of this isoform differs from the canonical sequence as follows:
     55-73: VFDPSCGLPYYWNADTDLV → RAPLLLECRHRPCILALPT
     74-265: Missing.
Isoform 9 (identifier: O60828-9)

The sequence of this isoform differs from the canonical sequence as follows:
     61-67: GLPYYWN → PGWSAMV
     68-265: Missing.
Isoform 10 (identifier: O60828-10)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 265264Polyglutamine-binding protein 1
PRO_0000076089

Regions

Domain46 – 8035WW
Repeat104 – 11071-1
Repeat111 – 11771-2
Repeat118 – 12471-3
Repeat125 – 13171-4
Repeat132 – 13871-5
Repeat139 – 14022-1
Repeat141 – 14222-2
Repeat143 – 14422-3
Repeat150 – 15123-1
Repeat152 – 15323-2
Repeat154 – 15523-3
Repeat156 – 15723-4
Repeat158 – 15923-5
Repeat160 – 16123-6
Repeat162 – 16323-7
Region104 – 138355 X 7 AA approximate tandem repeats of D-R-[SG]-H-D-K-S
Region139 – 14463 X 2 AA tandem repeats of [DE]-R
Region150 – 163147 X 2 AA tandem repeats of [DE]-R
Coiled coil84 – 10926 Potential
Compositional bias140 – 18142Arg-rich

Amino acid modifications

Modified residue941Phosphoserine Ref.14
Modified residue2471Phosphoserine Ref.13

Natural variations

Alternative sequence55 – 7319VFDPS…DTDLV → RAPLLLECRHRPCILALPT in isoform 8.
VSP_015896
Alternative sequence601C → W in isoform 10.
VSP_015897
Alternative sequence61 – 265205Missing in isoform 10.
VSP_015898
Alternative sequence61 – 677GLPYYWN → PGWSAMV in isoform 9.
VSP_015899
Alternative sequence68 – 265198Missing in isoform 9.
VSP_015901
Alternative sequence68 – 167100Missing in isoform 5.
VSP_015900
Alternative sequence74 – 265192Missing in isoform 8.
VSP_015902
Alternative sequence98 – 19295Missing in isoform 4.
VSP_015903
Alternative sequence99 – 12830AEEKL…LDRGH → LCPQMLKKSWTGAMTSRTGA MTSRTAAMRN in isoform 7.
VSP_015904
Alternative sequence129 – 265137Missing in isoform 7.
VSP_015905
Alternative sequence1491V → Q in isoform 6.
VSP_015906
Alternative sequence150 – 265116Missing in isoform 6.
VSP_015907
Alternative sequence193 – 22432AVSRK…GLPKR → GKLGRMGLGETNKVQGALRE EAFPQKDAWTWG in isoform 3.
VSP_015908
Alternative sequence1931Missing in isoform 2.
VSP_015909
Alternative sequence225 – 26541Missing in isoform 3.
VSP_015910
Natural variant2241R → W in a colorectal cancer sample; somatic mutation. Ref.17
VAR_036357

Experimental info

Mutagenesis521W → A: Enhances activity. Reduces activity; when associated with A-75. Markedly reduced activity; when associated with A-64; A-65 and A-66. Abolishes activity; when associated with A-64; A-65; A-66 and A-75. Ref.2
Mutagenesis641Y → A: No effect on activity; when associated with A-65 and A-66. Markedly reduced activity; when associated with A-52; A-65 and A-66. Abolishes activity; when associated with A-52; A-65; A-66 and A-75. Ref.2
Mutagenesis651Y → A: No effect on activity; when associated with A-64 and A-66. Markedly reduced activity; when associated with A-52; A-64 and A-66. Abolishes activity; when associated with A-52; A-64; A-66 and A-75. Ref.2
Mutagenesis661W → A: No effect on activity; when associated with A-64 and A-65. Markedly reduced activity; when associated with A-52; A-64 and A-65. Abolishes activity; when associated with A-52; A-64; A-65 and A-75. Ref.2
Mutagenesis751W → A: No effect on activity. Reduces activity; when associated with A-52. Abolishes activity; when associated with A-52; A-64; A-65 and A-66. Ref.2
Mutagenesis781P → G: No effect on activity. Ref.2
Sequence conflict81Q → L in CAJ00539. Ref.4
Sequence conflict571D → N in CAJ00548. Ref.4
Sequence conflict107 – 1137Missing in CAJ00538. Ref.4
Sequence conflict107 – 1137Missing in CAJ00539. Ref.4
Sequence conflict107 – 1137Missing in CAJ00540. Ref.4
Sequence conflict107 – 1137Missing in CAJ00541. Ref.4
Sequence conflict1071H → Q in CAJ00549. Ref.4
Sequence conflict1471D → G in CAJ00549. Ref.4
Sequence conflict1981D → G in CAJ00549. Ref.4
Sequence conflict2361A → V in CAJ00548. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PQBP-1) [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 98C3BEF18CFF0297

FASTA26530,472
        10         20         30         40         50         60 
MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKVFDPSC 

        70         80         90        100        110        120 
GLPYYWNADT DLVSWLSPHD PNSVVTKSAK KLRSSNADAE EKLDRSHDKS DRGHDKSDRS 

       130        140        150        160        170        180 
HEKLDRGHDK SDRGHDKSDR DRERGYDKVD RERERDRERD RDRGYDKADR EEGKERRHHR 

       190        200        210        220        230        240 
REELAPYPKS KKAVSRKDEE LDPMDPSSYS DAPRGTWSTG LPKRNEAKTG ADTTAAGPLF 

       250        260 
QQRPYPSPGA VLRANAEASR TKQQD 

« Hide

Isoform 2 [UniParc].

Checksum: 56BBC35A4CFB41C0
Show »

FASTA26430,401
Isoform 3 (PQBP-1b/c) [UniParc].

Checksum: 7DAC3C07D84492F0
Show »

FASTA22426,158
Isoform 4 (PQBP-1d) [UniParc].

Checksum: D01C0EAB17B61307
Show »

FASTA17018,827
Isoform 5 [UniParc].

Checksum: A32760CAAEFE5751
Show »

FASTA16518,706
Isoform 6 [UniParc].

Checksum: 88C7259FF95C0501
Show »

FASTA14917,183
Isoform 7 [UniParc].

Checksum: 1000C586B57B3758
Show »

FASTA12814,383
Isoform 8 (PQBP-1a) [UniParc].

Checksum: EF932C61145DC023
Show »

FASTA738,404
Isoform 9 [UniParc].

Checksum: F7FA61EC5E06DE6D
Show »

FASTA677,627
Isoform 10 [UniParc].

Checksum: 1025785C46650A62
Show »

FASTA606,981

References

« Hide 'large scale' references
[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]"Polar amino acid-rich sequences bind to polyglutamine tracts."
Imafuku I., Waragai M., Takeuchi S., Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.
Biochem. Biophys. Res. Commun. 253:16-20(1998) [PubMed] [Europe PMC] [Abstract]
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]"Renpenning syndrome comes into focus."
Stevenson R.E., Bennett C.W., Abidi F., Kleefstra T., Porteous M., Simensen R.J., Lubs H.A., Hamel B.C.J., Schwartz C.E.
Am. J. Med. Genet. A 134:415-421(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON RENS1.
[12]"Mutations in the polyglutamine binding protein 1 gene cause X-linked mental retardation."
Kalscheuer V.M., Freude K., Musante L., Jensen L.R., Yntema H.G., Gecz J., Sefiani A., Hoffmann K., Moser B., Haas S., Gurok U., Haesler S., Aranda B., Nshedjan A., Tzschach A., Hartmann N., Roloff T.C., Shoichet S. expand/collapse author list , Hagens O., Tao J., Van Bokhoven H., Turner G., Chelly J., Moraine C., Fryns J.-P., Nuber U., Hoeltzenbein M., Scharff C., Scherthan H., Lenzner S., Hamel B.C.J., Schweiger S., Ropers H.-H.
Nat. Genet. 35:313-315(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RENS1.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-224.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14309.1. [O60828-1]
CCDS55412.1. [O60828-4]
RefSeqNP_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]
UniGeneHs.534384.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BWQX-ray2.10B/D/F/H223-265[»]
4BWSX-ray2.50B/E229-265[»]
4CDOX-ray2.50A/C223-265[»]
ProteinModelPortalO60828.
SMRO60828. Positions 46-79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115393. 36 interactions.
IntActO60828. 12 interactions.
MINTMINT-112545.

PTM databases

PhosphoSiteO60828.

Proteomic databases

MaxQBO60828.
PaxDbO60828.
PRIDEO60828.

Protocols and materials databases

DNASU10084.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218224; 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]
GeneID10084.
KEGGhsa:10084.
UCSCuc004dle.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

CTD10084.
GeneCardsGC0XP048755.
HGNCHGNC:9330. PQBP1.
HPAHPA001880.
MIM300463. gene.
309500. phenotype.
neXtProtNX_O60828.
Orphanet93946. 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.
PharmGKBPA33693.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265480.
HOVERGENHBG053064.
InParanoidO60828.
KOK12865.
OMASHEKSDR.
PhylomeDBO60828.
TreeFamTF320689.

Enzyme and pathway databases

SignaLinkO60828.

Gene expression databases

ArrayExpressO60828.
BgeeO60828.
GenevestigatorO60828.

Family and domain databases

InterProIPR001202. WW_dom.
[Graphical view]
PfamPF00397. WW. 1 hit.
[Graphical view]
SMARTSM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPQBP1. human.
GeneWikiPQBP1.
GenomeRNAi10084.
NextBio38125.
PMAP-CutDBO60828.
PROO60828.
SOURCESearch...

Entry information

Entry namePQBP1_HUMAN
AccessionPrimary (citable) accession number: O60828
Secondary accession number(s): Q4VY25 expand/collapse secondary AC list , Q4VY26, Q4VY27, Q4VY29, Q4VY30, Q4VY34, Q4VY35, Q4VY36, Q4VY37, Q4VY38, Q9GZP2, Q9GZU4, Q9GZZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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