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Q9BRQ0

- PYGO2_HUMAN

UniProt

Q9BRQ0 - PYGO2_HUMAN

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Protein

Pygopus homolog 2

Gene

PYGO2

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

Functioni

Involved in signal transduction through the Wnt pathway.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri327 – 38559PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. histone acetyltransferase regulator activity Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. brain development Source: Ensembl
  2. canonical Wnt signaling pathway Source: Ensembl
  3. developmental growth Source: Ensembl
  4. in utero embryonic development Source: Ensembl
  5. kidney development Source: Ensembl
  6. lens development in camera-type eye Source: Ensembl
  7. mammary gland development Source: Ensembl
  8. palate development Source: Ensembl
  9. positive regulation of chromatin binding Source: Ensembl
  10. post-embryonic development Source: Ensembl
  11. regulation of histone H3-K4 methylation Source: Ensembl
  12. regulation of mammary gland epithelial cell proliferation Source: Ensembl
  13. spermatid nucleus differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Pygopus homolog 2
Gene namesi
Name:PYGO2
ORF Names:PP7910
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30257. PYGO2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134881185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 406405Pygopus homolog 2PRO_0000097123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei302 – 3021Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BRQ0.
PaxDbiQ9BRQ0.
PRIDEiQ9BRQ0.

PTM databases

PhosphoSiteiQ9BRQ0.

Expressioni

Gene expression databases

BgeeiQ9BRQ0.
CleanExiHS_PYGO2.
ExpressionAtlasiQ9BRQ0. baseline and differential.
GenevestigatoriQ9BRQ0.

Organism-specific databases

HPAiHPA023689.

Interactioni

Subunit structurei

Binds to BCL9 via the PHD-type zinc finger motif, and thereby becomes part of the nuclear beta-catenin/TCF complex.

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL9O005122EBI-932471,EBI-533127

Protein-protein interaction databases

BioGridi124760. 13 interactions.
IntActiQ9BRQ0. 3 interactions.
MINTiMINT-8177751.
STRINGi9606.ENSP00000357442.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni331 – 3333Combined sources
Beta strandi343 – 3453Combined sources
Turni347 – 3504Combined sources
Beta strandi353 – 3553Combined sources
Helixi356 – 3583Combined sources
Helixi363 – 3719Combined sources
Beta strandi375 – 3773Combined sources
Helixi380 – 3845Combined sources
Turni385 – 3873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XB1X-ray1.90A/C325-387[»]
ProteinModelPortaliQ9BRQ0.
SMRiQ9BRQ0. Positions 325-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi41 – 477Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 329324Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri327 – 38559PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG72798.
GeneTreeiENSGT00530000063948.
HOGENOMiHOG000001580.
HOVERGENiHBG053774.
InParanoidiQ9BRQ0.
OMAiPGLVYPC.
OrthoDBiEOG79W952.
PhylomeDBiQ9BRQ0.
TreeFamiTF333020.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BRQ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASAPPPPD KLEGGGGPAP PPAPPSTGRK QGKAGLQMKS PEKKRRKSNT
60 70 80 90 100
QGPAYSHLTE FAPPPTPMVD HLVASNPFED DFGAPKVGVA APPFLGSPVP
110 120 130 140 150
FGGFRVQGGM AGQVPPGYST GGGGGPQPLR RQPPPFPPNP MGPAFNMPPQ
160 170 180 190 200
GPGYPPPGNM NFPSQPFNQP LGQNFSPPSG QMMPGPVGGF GPMISPTMGQ
210 220 230 240 250
PPRAELGPPS LSQRFAQPGA PFGPSPLQRP GQGLPSLPPN TSPFPGPDPG
260 270 280 290 300
FPGPGGEDGG KPLNPPASTA FPQEPHSGSP AAAVNGNQPS FPPNSSGRGG
310 320 330 340 350
GTPDANSLAP PGKAGGGSGP QPPPGLVYPC GACRSEVNDD QDAILCEASC
360 370 380 390 400
QKWFHRECTG MTESAYGLLT TEASAVWACD LCLKTKEIQS VYIREGMGQL

VAANDG
Length:406
Mass (Da):41,244
Last modified:September 19, 2002 - v2
Checksum:iCA002A5447767CD9
GO

Sequence cautioni

The sequence AAL55782.1 differs from that shown. Reason: Sequencing errors.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571P → Q in AAL55782. (PubMed:15498874)Curated
Sequence conflicti170 – 1701P → L in AAL55782. (PubMed:15498874)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF457208 mRNA. Translation: AAL91371.1.
BC006132 mRNA. Translation: AAH06132.2.
BC013725 mRNA. Translation: AAH13725.1.
BC032099 mRNA. Translation: AAH32099.1.
AF289598 mRNA. Translation: AAL55782.1. Sequence problems.
CCDSiCCDS1075.1.
RefSeqiNP_612157.1. NM_138300.3.
UniGeneiHs.533597.

Genome annotation databases

EnsembliENST00000368457; ENSP00000357442; ENSG00000163348.
GeneIDi90780.
KEGGihsa:90780.
UCSCiuc001fft.3. human.

Polymorphism databases

DMDMi23396825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF457208 mRNA. Translation: AAL91371.1 .
BC006132 mRNA. Translation: AAH06132.2 .
BC013725 mRNA. Translation: AAH13725.1 .
BC032099 mRNA. Translation: AAH32099.1 .
AF289598 mRNA. Translation: AAL55782.1 . Sequence problems.
CCDSi CCDS1075.1.
RefSeqi NP_612157.1. NM_138300.3.
UniGenei Hs.533597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XB1 X-ray 1.90 A/C 325-387 [» ]
ProteinModelPortali Q9BRQ0.
SMRi Q9BRQ0. Positions 325-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124760. 13 interactions.
IntActi Q9BRQ0. 3 interactions.
MINTi MINT-8177751.
STRINGi 9606.ENSP00000357442.

PTM databases

PhosphoSitei Q9BRQ0.

Polymorphism databases

DMDMi 23396825.

Proteomic databases

MaxQBi Q9BRQ0.
PaxDbi Q9BRQ0.
PRIDEi Q9BRQ0.

Protocols and materials databases

DNASUi 90780.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368457 ; ENSP00000357442 ; ENSG00000163348 .
GeneIDi 90780.
KEGGi hsa:90780.
UCSCi uc001fft.3. human.

Organism-specific databases

CTDi 90780.
GeneCardsi GC01M154929.
HGNCi HGNC:30257. PYGO2.
HPAi HPA023689.
MIMi 606903. gene.
neXtProti NX_Q9BRQ0.
PharmGKBi PA134881185.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG72798.
GeneTreei ENSGT00530000063948.
HOGENOMi HOG000001580.
HOVERGENi HBG053774.
InParanoidi Q9BRQ0.
OMAi PGLVYPC.
OrthoDBi EOG79W952.
PhylomeDBi Q9BRQ0.
TreeFami TF333020.

Enzyme and pathway databases

Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.

Miscellaneous databases

ChiTaRSi PYGO2. human.
GeneWikii PYGO2.
GenomeRNAii 90780.
NextBioi 76956.
PROi Q9BRQ0.
SOURCEi Search...

Gene expression databases

Bgeei Q9BRQ0.
CleanExi HS_PYGO2.
ExpressionAtlasi Q9BRQ0. baseline and differential.
Genevestigatori Q9BRQ0.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of pygopus to the nuclear beta-catenin-TCF complex."
    Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S., Murone M., Zuellig S., Basler K.
    Cell 109:47-60(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Brain and Ovary.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-406.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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].
  6. "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 THR-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYGO2_HUMAN
AccessioniPrimary (citable) accession number: Q9BRQ0
Secondary accession number(s): Q8WYZ4, Q96CY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: November 26, 2014
This is version 115 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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