O60828 (PQBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PQBP1
Synonyms:	NPW38
ORF Names:	JM26

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: Co-localized with POU3F2. Co-localized 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Mental retardation
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Traceable author statement Ref.2. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA cytoplasmic stress granule Inferred from electronic annotation. Source: Compara neuronal ribonucleoprotein granule Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Traceable author statement Ref.8. Source: ProtInc transcription coactivator activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 265	264	Polyglutamine-binding protein 1		PRO_0000076089
Regions
	Domain	46 – 80	35	WW
	Repeat	104 – 110	7	1-1
	Repeat	111 – 117	7	1-2
	Repeat	118 – 124	7	1-3
	Repeat	125 – 131	7	1-4
	Repeat	132 – 138	7	1-5
	Repeat	139 – 140	2	2-1
	Repeat	141 – 142	2	2-2
	Repeat	143 – 144	2	2-3
	Repeat	150 – 151	2	3-1
	Repeat	152 – 153	2	3-2
	Repeat	154 – 155	2	3-3
	Repeat	156 – 157	2	3-4
	Repeat	158 – 159	2	3-5
	Repeat	160 – 161	2	3-6
	Repeat	162 – 163	2	3-7
	Region	104 – 138	35	5 X 7 AA approximate tandem repeats of D-R-[SG]-H-D-K-S
	Region	139 – 144	6	3 X 2 AA tandem repeats of [DE]-R
	Region	150 – 163	14	7 X 2 AA tandem repeats of [DE]-R
	Coiled coil	84 – 109	26	Potential
	Compositional bias	140 – 181	42	Arg-rich
Sites
	Site	2	1	Not acetylated
Amino acid modifications
	Modified residue	94	1	Phosphoserine Ref.14
	Modified residue	247	1	Phosphoserine Ref.13
Natural variations
	Alternative sequence	55 – 73	19	VFDPS…DTDLV → RAPLLLECRHRPCILALPT in isoform 8.		VSP_015896
	Alternative sequence	60	1	C → W in isoform 10.		VSP_015897
	Alternative sequence	61 – 265	205	Missing in isoform 10.		VSP_015898
	Alternative sequence	61 – 67	7	GLPYYWN → PGWSAMV in isoform 9.		VSP_015899
	Alternative sequence	68 – 265	198	Missing in isoform 9.		VSP_015901
	Alternative sequence	68 – 167	100	Missing in isoform 5.		VSP_015900
	Alternative sequence	74 – 265	192	Missing in isoform 8.		VSP_015902
	Alternative sequence	98 – 192	95	Missing in isoform 4.		VSP_015903
	Alternative sequence	99 – 128	30	AEEKL…LDRGH → LCPQMLKKSWTGAMTSRTGA MTSRTAAMRN in isoform 7.		VSP_015904
	Alternative sequence	129 – 265	137	Missing in isoform 7.		VSP_015905
	Alternative sequence	149	1	V → Q in isoform 6.		VSP_015906
	Alternative sequence	150 – 265	116	Missing in isoform 6.		VSP_015907
	Alternative sequence	193 – 224	32	AVSRK…GLPKR → GKLGRMGLGETNKVQGALRE EAFPQKDAWTWG in isoform 3.		VSP_015908
	Alternative sequence	193	1	Missing in isoform 2.		VSP_015909
	Alternative sequence	225 – 265	41	Missing in isoform 3.		VSP_015910
	Natural variant	224	1	R → W in a colorectal cancer sample; somatic mutation. Ref.16		VAR_036357
Experimental info
	Mutagenesis	52	1	W → 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
	Mutagenesis	64	1	Y → 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
	Mutagenesis	65	1	Y → 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
	Mutagenesis	66	1	W → 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
	Mutagenesis	75	1	W → 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
	Mutagenesis	78	1	P → G: No effect on activity. Ref.2
	Sequence conflict	8	1	Q → L in CAJ00539. Ref.4
	Sequence conflict	57	1	D → N in CAJ00548. Ref.4
	Sequence conflict	107 – 113	7	Missing in CAJ00538. Ref.4
	Sequence conflict	107 – 113	7	Missing in CAJ00539. Ref.4
	Sequence conflict	107 – 113	7	Missing in CAJ00540. Ref.4
	Sequence conflict	107 – 113	7	Missing in CAJ00541. Ref.4
	Sequence conflict	107	1	H → Q in CAJ00549. Ref.4
	Sequence conflict	147	1	D → G in CAJ00549. Ref.4
	Sequence conflict	198	1	D → G in CAJ00549. Ref.4
	Sequence conflict	236	1	A → V in CAJ00548. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PQBP-1) [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 98C3BEF18CFF0297	FASTA	265	30,472
	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
	Isoform 2 [UniParc]. Checksum: 56BBC35A4CFB41C0	FASTA	264	30,401
	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 KKVSRKDEEL DPMDPSSYSD APRGTWSTGL PKRNEAKTGA DTTAAGPLFQ 250 260 QRPYPSPGAV LRANAEASRT KQQD
	Isoform 3 (PQBP-1b/c) [UniParc]. Checksum: 7DAC3C07D84492F0	FASTA	224	26,158
	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 REELAPYPKS KKGKLGRMGL GETNKVQGAL REEAFPQKDA WTWG
	Isoform 4 (PQBP-1d) [UniParc]. Checksum: D01C0EAB17B61307	FASTA	170	18,827
	10 20 30 40 50 60 MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKVFDPSC 70 80 90 100 110 120 GLPYYWNADT DLVSWLSPHD PNSVVTKSAK KLRSSNAAVS RKDEELDPMD PSSYSDAPRG 130 140 150 160 170 TWSTGLPKRN EAKTGADTTA AGPLFQQRPY PSPGAVLRAN AEASRTKQQD
	Isoform 5 [UniParc]. Checksum: A32760CAAEFE5751	FASTA	165	18,706
	10 20 30 40 50 60 MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKVFDPSC 70 80 90 100 110 120 GLPYYWNADR EEGKERRHHR REELAPYPKS KKAVSRKDEE LDPMDPSSYS DAPRGTWSTG 130 140 150 160 LPKRNEAKTG ADTTAAGPLF QQRPYPSPGA VLRANAEASR TKQQD
	Isoform 6 [UniParc]. Checksum: 88C7259FF95C0501	FASTA	149	17,183
	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 HEKLDRGHDK SDRGHDKSDR DRERGYDKQ
	Isoform 7 [UniParc]. Checksum: 1000C586B57B3758	FASTA	128	14,383
	10 20 30 40 50 60 MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKVFDPSC 70 80 90 100 110 120 GLPYYWNADT DLVSWLSPHD PNSVVTKSAK KLRSSNADLC PQMLKKSWTG AMTSRTGAMT SRTAAMRN
	Isoform 8 (PQBP-1a) [UniParc]. Checksum: EF932C61145DC023	FASTA	73	8,404
	10 20 30 40 50 60 MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKRAPLLL 70 ECRHRPCILA LPT
	Isoform 9 [UniParc]. Checksum: F7FA61EC5E06DE6D	FASTA	67	7,627
	10 20 30 40 50 60 MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKVFDPSC PGWSAMV
	Isoform 10 [UniParc]. Checksum: 1025785C46650A62	FASTA	60	6,981
	10 20 30 40 50 60 MPLPVALQTR LAKRGILKHL EPEPEEEIIA EDYDDDPVDY EATRLEGLPP SWYKVFDPSW

References

	« Hide 'large scale' referencesShow '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, LACK OF N-TERMINAL ACETYLATION, 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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. , 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.

Web resources

GeneReviews

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.
IPI	IPI00024698. IPI00030216. IPI00386483. IPI00386509. IPI00607789. IPI00607805. IPI00607824. IPI00644888. IPI00654565. IPI00654698.
RefSeq	NP_001027553.1. NM_001032381.1. NP_001027554.1. NM_001032382.1. NP_001027555.1. NM_001032383.1. NP_001027556.1. NM_001032384.1. NP_001161461.1. NM_001167989.1. NP_001161462.1. NM_001167990.1. NP_001161464.1. NM_001167992.1. NP_005701.1. NM_005710.2. NP_652766.1. NM_144495.2.
UniGene	Hs.534384.
3D structure databases
ProteinModelPortal	O60828.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60828. 8 interactions.
MINT	MINT-112545.
PTM databases
PhosphoSite	O60828.
Proteomic databases
PaxDb	O60828.
PRIDE	O60828.
Protocols and materials databases
DNASU	10084.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000218224; ENSP00000218224; ENSG00000102103. ENST00000247140; ENSP00000247140; ENSG00000102103. ENST00000376548; ENSP00000365731; ENSG00000102103. ENST00000376563; ENSP00000365747; ENSG00000102103. ENST00000376566; ENSP00000365750; ENSG00000102103. ENST00000396763; ENSP00000379985; ENSG00000102103. ENST00000447146; ENSP00000391759; ENSG00000102103. ENST00000593464; ENSP00000472506; ENSG00000268142. ENST00000594868; ENSP00000469772; ENSG00000268142. ENST00000597699; ENSP00000472009; ENSG00000268142. ENST00000597809; ENSP00000470666; ENSG00000268142. ENST00000600107; ENSP00000471461; ENSG00000268142. ENST00000600640; ENSP00000469504; ENSG00000268142. ENST00000601234; ENSP00000472437; ENSG00000268142.
GeneID	10084.
KEGG	hsa:10084.
UCSC	uc004dle.3. human. uc004dlj.1. human. uc004dlk.3. human. uc004dln.3. human. uc010nij.3. human.
Organism-specific databases
CTD	10084.
GeneCards	GC0XP048755.
HGNC	HGNC:9330. PQBP1.
HPA	HPA001880.
MIM	300463. gene. 309500. phenotype.
neXtProt	NX_O60828.
Orphanet	93946. Hamel cerebro-palato-cardiac syndrome. 93947. X-linked intellectual deficit, Golabi-Ito-Hall type. 93945. X-linked intellectual deficit, Porteous type. 93950. X-linked intellectual deficit, Sutherland-Haan type.
PharmGKB	PA33693.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG265480.
HOVERGEN	HBG053064.
InParanoid	O60828.
KO	K12865.
OMA	SHEKSDR.
OrthoDB	EOG4NCMF0.
PhylomeDB	O60828.
Enzyme and pathway databases
SignaLink	O60828.
Gene expression databases
ArrayExpress	O60828.
Bgee	O60828.
Genevestigator	O60828.
GermOnline	ENSG00000102103. Homo sapiens.
Family and domain databases
InterPro	IPR001202. WW_dom. [Graphical view]
Pfam	PF00397. WW. 1 hit. [Graphical view]
SMART	SM00456. WW. 1 hit. [Graphical view]
SUPFAM	SSF51045. WW_Rsp5_WWP. 1 hit.
PROSITE	PS01159. WW_DOMAIN_1. False negative. PS50020. WW_DOMAIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PQBP1. human.
GenomeRNAi	10084.
NextBio	38125.
PMAP-CutDB	O60828.
SOURCE	Search...

Entry information

Entry name

PQBP1_HUMAN

Accession

Primary (citable) accession number: O60828
Secondary accession number(s): Q4VY25 , 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:	May 29, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.