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Protein

Pygopus homolog 1

Gene

PYGO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 fingeri340 – 39859PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
SIGNORiQ9Y3Y4.

Names & Taxonomyi

Protein namesi
Recommended name:
Pygopus homolog 1
Gene namesi
Name:PYGO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30256. PYGO1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi349 – 3491E → A: Reduces interaction with H3K4me2. 1 Publication
Mutagenesisi350 – 3501V → E: Almost complete loss of interaction with H3K4me2. 1 Publication
Mutagenesisi351 – 3511N → A: Reduces interaction with H3K4me2. 1 Publication
Mutagenesisi354 – 3541Q → A: Reduces interaction with H3K4me2. 1 Publication
Mutagenesisi356 – 3561A → E: Almost complete loss of interaction with H3K4me2. 1 Publication
Mutagenesisi357 – 3571I → R: Loss of interaction with H3K4me2. 1 Publication
Mutagenesisi360 – 3601E → A: Loss of interaction with H3K4me2. 1 Publication
Mutagenesisi366 – 3661W → E: Loss of interaction with H3K4me2. 1 Publication

Organism-specific databases

PharmGKBiPA134875127.

Polymorphism and mutation databases

DMDMi23396828.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419Pygopus homolog 1PRO_0000097121Add
BLAST

Proteomic databases

PaxDbiQ9Y3Y4.
PeptideAtlasiQ9Y3Y4.
PRIDEiQ9Y3Y4.

PTM databases

iPTMnetiQ9Y3Y4.
PhosphoSiteiQ9Y3Y4.

Expressioni

Gene expression databases

BgeeiQ9Y3Y4.
CleanExiHS_PYGO1.
GenevisibleiQ9Y3Y4. HS.

Organism-specific databases

HPAiHPA042248.

Interactioni

Subunit structurei

Interacts with BCL9 via The PHD-type zinc finger motiv, and thereby becomes part of the nuclear beta-catenin/TCF complex. Identified in a complex with BCL9L, CDC73, CTNNB1 and PYGO1. Interacts with histone H3 mono-, di- or tri-methylated at 'Lys4' (H3K4me1, H3K4me2, H3K4me3); the interaction is enhanced by the interaction with BCL9.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL9O005127EBI-3397474,EBI-533127

Protein-protein interaction databases

BioGridi117557. 6 interactions.
IntActiQ9Y3Y4. 7 interactions.
MINTiMINT-7969845.
STRINGi9606.ENSP00000302327.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi340 – 3423Combined sources
Turni344 – 3463Combined sources
Beta strandi356 – 3594Combined sources
Turni360 – 3634Combined sources
Beta strandi366 – 3683Combined sources
Helixi369 – 3724Combined sources
Helixi376 – 3849Combined sources
Beta strandi388 – 3903Combined sources
Helixi393 – 3964Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VP7X-ray1.65A333-402[»]
2VPBX-ray1.59A333-397[»]
2VPDX-ray2.77A/C333-398[»]
2VPEX-ray1.70A/C340-398[»]
2VPGX-ray1.60A/C340-398[»]
ProteinModelPortaliQ9Y3Y4.
SMRiQ9Y3Y4. Positions 341-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3Y4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 38848Interaction with H3K4me2Add
BLAST
Regioni373 – 39119Interaction with BCL9Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi35 – 417Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 13589Pro-richAdd
BLAST
Compositional biasi153 – 305153Asn-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri340 – 39859PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IDYF. Eukaryota.
ENOG4111FFC. LUCA.
GeneTreeiENSGT00530000063948.
HOGENOMiHOG000001580.
HOVERGENiHBG053774.
InParanoidiQ9Y3Y4.
OMAiSAVWGCD.
OrthoDBiEOG79W952.
PhylomeDBiQ9Y3Y4.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y3Y4-1) [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
MPAENSPAPA YKVSSHGGDS GLDGLGGPGV QLGSPDKKKR KANTQGPSFP
60 70 80 90 100
PLSEYAPPPN PNSDHLVAAN PFDDNYNTIS YKPLPSSNPY LGPGYPGFGG
110 120 130 140 150
YSTFRMPPHV PPRMSSPYCG PYSLRNQPHP FPQNPLGMGF NRPHAFNFGP
160 170 180 190 200
HDNSSFGNPS YNNALSQNVN MPNQHFRQNP AENFSQIPPQ NASQVSNPDL
210 220 230 240 250
ASNFVPGNNS NFTSPLESNH SFIPPPNTFG QAKAPPPKQD FTQGATKNTN
260 270 280 290 300
QNSSAHPPHL NMDDTVNQSN IELKNVNRNN AVNQENSRSS STEATNNNPA
310 320 330 340 350
NGTQNKPRQP RGAADACTTE KSNKSSLHPN RHGHSSSDPV YPCGICTNEV
360 370 380 390 400
NDDQDAILCE ASCQKWFHRI CTGMTETAYG LLTAEASAVW GCDTCMADKD
410
VQLMRTRETF GPSAVGSDA
Length:419
Mass (Da):45,116
Last modified:September 19, 2002 - v2
Checksum:iD5D4E4AA416FD8E4
GO
Isoform 2 (identifier: Q9Y3Y4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MPAENSPAPAYKVSSH → MSAEQEKDPISLKRVR

Show »
Length:419
Mass (Da):45,318
Checksum:iE30602D469C7E1CD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991P → H.
Corresponds to variant rs11858624 [ dbSNP | Ensembl ].
VAR_051292

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616MPAEN…KVSSH → MSAEQEKDPISLKRVR in isoform 2. 1 PublicationVSP_056648Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF457207 mRNA. Translation: AAL91370.1.
EF625686 mRNA. Translation: ABU93489.1.
AC012378 Genomic DNA. No translation available.
AC022083 Genomic DNA. No translation available.
AL049925 mRNA. Translation: CAB43209.1.
CCDSiCCDS10155.1. [Q9Y3Y4-1]
PIRiT08663.
RefSeqiNP_056432.1. NM_015617.2. [Q9Y3Y4-1]
XP_005254357.1. XM_005254300.3. [Q9Y3Y4-2]
XP_011519748.1. XM_011521446.1. [Q9Y3Y4-2]
UniGeneiHs.256587.
Hs.87194.

Genome annotation databases

EnsembliENST00000302000; ENSP00000302327; ENSG00000171016. [Q9Y3Y4-1]
ENST00000563719; ENSP00000457777; ENSG00000171016. [Q9Y3Y4-2]
GeneIDi26108.
KEGGihsa:26108.
UCSCiuc002adf.3. human. [Q9Y3Y4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF457207 mRNA. Translation: AAL91370.1.
EF625686 mRNA. Translation: ABU93489.1.
AC012378 Genomic DNA. No translation available.
AC022083 Genomic DNA. No translation available.
AL049925 mRNA. Translation: CAB43209.1.
CCDSiCCDS10155.1. [Q9Y3Y4-1]
PIRiT08663.
RefSeqiNP_056432.1. NM_015617.2. [Q9Y3Y4-1]
XP_005254357.1. XM_005254300.3. [Q9Y3Y4-2]
XP_011519748.1. XM_011521446.1. [Q9Y3Y4-2]
UniGeneiHs.256587.
Hs.87194.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VP7X-ray1.65A333-402[»]
2VPBX-ray1.59A333-397[»]
2VPDX-ray2.77A/C333-398[»]
2VPEX-ray1.70A/C340-398[»]
2VPGX-ray1.60A/C340-398[»]
ProteinModelPortaliQ9Y3Y4.
SMRiQ9Y3Y4. Positions 341-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117557. 6 interactions.
IntActiQ9Y3Y4. 7 interactions.
MINTiMINT-7969845.
STRINGi9606.ENSP00000302327.

PTM databases

iPTMnetiQ9Y3Y4.
PhosphoSiteiQ9Y3Y4.

Polymorphism and mutation databases

DMDMi23396828.

Proteomic databases

PaxDbiQ9Y3Y4.
PeptideAtlasiQ9Y3Y4.
PRIDEiQ9Y3Y4.

Protocols and materials databases

DNASUi26108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302000; ENSP00000302327; ENSG00000171016. [Q9Y3Y4-1]
ENST00000563719; ENSP00000457777; ENSG00000171016. [Q9Y3Y4-2]
GeneIDi26108.
KEGGihsa:26108.
UCSCiuc002adf.3. human. [Q9Y3Y4-1]

Organism-specific databases

CTDi26108.
GeneCardsiPYGO1.
HGNCiHGNC:30256. PYGO1.
HPAiHPA042248.
MIMi606902. gene.
neXtProtiNX_Q9Y3Y4.
PharmGKBiPA134875127.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IDYF. Eukaryota.
ENOG4111FFC. LUCA.
GeneTreeiENSGT00530000063948.
HOGENOMiHOG000001580.
HOVERGENiHBG053774.
InParanoidiQ9Y3Y4.
OMAiSAVWGCD.
OrthoDBiEOG79W952.
PhylomeDBiQ9Y3Y4.
TreeFamiTF333020.

Enzyme and pathway databases

ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
SIGNORiQ9Y3Y4.

Miscellaneous databases

EvolutionaryTraceiQ9Y3Y4.
GenomeRNAii26108.
PROiQ9Y3Y4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3Y4.
CleanExiHS_PYGO1.
GenevisibleiQ9Y3Y4. HS.

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]
ProtoNetiSearch...

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] (ISOFORM 1).
  2. "Research on human heart developmental candidate gene PYGO1."
    Wang C.D., Wu X.S., Liu M.Y.
    Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Heart.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-419 (ISOFORM 1).
    Tissue: Fetal brain.
  5. "BCL9-2 binds Arm/beta-catenin in a Tyr142-independent manner and requires Pygopus for its function in Wg/Wnt signaling."
    Hoffmans R., Basler K.
    Mech. Dev. 124:59-67(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH BCL9L; CDC73 AND CTNNB1.
  6. "Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex."
    Fiedler M., Sanchez-Barrena M.J., Nekrasov M., Mieszczanek J., Rybin V., Muller J., Evans P., Bienz M.
    Mol. Cell 30:507-518(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 333-397 IN COMPLEX WITH ZINC IONS; HISTONE H3K4ME2 AND BCL9, INTERACTION WITH BCL9 AND HISTONE H3KME1; H3K4M2; H3K4ME3, ZINC-BINDING, MUTAGENESIS OF GLU-349; VAL-350; ASN-351; GLN-354; ALA-356; ILE-357; GLU-360 AND TRP-366.

Entry informationi

Entry nameiPYGO1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3Y4
Secondary accession number(s): A7Y2D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: July 6, 2016
This is version 124 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 15
    Human chromosome 15: 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

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 one 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.