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Protein

Pirin

Gene

PIR

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

Functioni

Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro).4 Publications

Catalytic activityi

Quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+.1 Publication

Cofactori

Fe cation2 PublicationsNote: Binds 1 Fe cation per subunit.2 Publications

Enzyme regulationi

Inhibited by kojic acid, sodium diethyldithiocarbamate and 1,10-phenanthroline monohydrochloride.1 Publication

Pathwayi: quercetin degradation

This protein is involved in the pathway quercetin degradation, which is part of Flavonoid metabolism.
View all proteins of this organism that are known to be involved in the pathway quercetin degradation and in Flavonoid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Iron; via tele nitrogenCombined sources2 Publications1
Metal bindingi58Iron; via tele nitrogenCombined sources2 Publications1
Metal bindingi101Iron; via tele nitrogenCombined sources2 Publications1
Metal bindingi103IronCombined sources2 Publications1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB
  • quercetin 2,3-dioxygenase activity Source: UniProtKB
  • transcription cofactor activity Source: UniProtKB

GO - Biological processi

  • monocyte differentiation Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087842-MONOMER.
UniPathwayiUPA00724.

Names & Taxonomyi

Protein namesi
Recommended name:
Pirin (EC:1.13.11.24)
Alternative name(s):
Probable quercetin 2,3-dioxygenase PIR
Short name:
Probable quercetinase
Gene namesi
Name:PIR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:30048. PIR.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi8544.
OpenTargetsiENSG00000087842.
PharmGKBiPA134870022.

Chemistry databases

ChEMBLiCHEMBL2010627.

Polymorphism and mutation databases

BioMutaiPIR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002140511 – 290PirinAdd BLAST290

Proteomic databases

EPDiO00625.
MaxQBiO00625.
PaxDbiO00625.
PeptideAtlasiO00625.
PRIDEiO00625.
TopDownProteomicsiO00625.

2D gel databases

UCD-2DPAGEO00625.

PTM databases

iPTMnetiO00625.
PhosphoSitePlusiO00625.

Expressioni

Tissue specificityi

Highly expressed in a subset of melanomas. Detected at very low levels in most tissues (at protein level). Expressed in all tissues, with highest level of expression in heart and liver.2 Publications

Inductioni

Up-regulated in CD34+ cells upon myelomonocytic differentiation. Down-regulated in many acute myeloid leukemias. Up-regulated in primary bronchial epithelial cells exposed to cigarette smoke extract.2 Publications

Gene expression databases

BgeeiENSG00000087842.
CleanExiHS_PIR.
ExpressionAtlasiO00625. baseline and differential.
GenevisibleiO00625. HS.

Organism-specific databases

HPAiHPA000697.

Interactioni

Subunit structurei

May interact with NF1/CTF1. Interacts with BCL3. Identified in a complex comprised of PIR, BLC3, NFKB1 and target DNA.4 Publications

Protein-protein interaction databases

BioGridi114114. 53 interactors.
IntActiO00625. 2 interactors.
MINTiMINT-1189585.
STRINGi9606.ENSP00000369785.

Chemistry databases

BindingDBiO00625.

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Beta strandi14 – 18Combined sources5
Beta strandi22 – 26Combined sources5
Helixi31 – 33Combined sources3
Beta strandi39 – 47Combined sources9
Beta strandi52 – 67Combined sources16
Beta strandi69 – 71Combined sources3
Beta strandi73 – 77Combined sources5
Beta strandi82 – 85Combined sources4
Beta strandi90 – 94Combined sources5
Beta strandi99 – 105Combined sources7
Beta strandi107 – 109Combined sources3
Beta strandi111 – 119Combined sources9
Helixi122 – 124Combined sources3
Beta strandi130 – 134Combined sources5
Helixi136 – 138Combined sources3
Beta strandi147 – 156Combined sources10
Beta strandi169 – 176Combined sources8
Beta strandi181 – 185Combined sources5
Beta strandi191 – 199Combined sources9
Beta strandi201 – 204Combined sources4
Beta strandi210 – 212Combined sources3
Beta strandi216 – 220Combined sources5
Beta strandi224 – 229Combined sources6
Beta strandi232 – 234Combined sources3
Beta strandi236 – 243Combined sources8
Beta strandi251 – 253Combined sources3
Beta strandi256 – 260Combined sources5
Helixi261 – 272Combined sources12
Helixi279 – 281Combined sources3
Turni287 – 289Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J1LX-ray2.10A1-290[»]
3ACLX-ray2.35A2-290[»]
4EROX-ray2.65A1-290[»]
4EWAX-ray2.47A1-290[»]
4EWDX-ray2.15A1-290[»]
4EWEX-ray1.56A1-290[»]
4GULX-ray1.80A3-290[»]
4HLTX-ray1.70A3-290[»]
ProteinModelPortaliO00625.
SMRiO00625.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00625.

Family & Domainsi

Sequence similaritiesi

Belongs to the pirin family.Curated

Phylogenomic databases

eggNOGiENOG410IF52. Eukaryota.
COG1741. LUCA.
GeneTreeiENSGT00390000008044.
HOGENOMiHOG000248360.
HOVERGENiHBG019151.
InParanoidiO00625.
KOiK06911.
OMAiDLDPFVH.
OrthoDBiEOG091G0PKY.
PhylomeDBiO00625.
TreeFamiTF300002.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR012093. Pirin.
IPR008778. Pirin_C_dom.
IPR003829. Pirin_N_dom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR13903. PTHR13903. 1 hit.
PfamiPF02678. Pirin. 1 hit.
PF05726. Pirin_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006232. Pirin. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

O00625-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSSKKVTLS VLSREQSEGV GARVRRSIGR PELKNLDPFL LFDEFKGGRP
60 70 80 90 100
GGFPDHPHRG FETVSYLLEG GSMAHEDFCG HTGKMNPGDL QWMTAGRGIL
110 120 130 140 150
HAEMPCSEEP AHGLQLWVNL RSSEKMVEPQ YQELKSEEIP KPSKDGVTVA
160 170 180 190 200
VISGEALGIK SKVYTRTPTL YLDFKLDPGA KHSQPIPKGW TSFIYTISGD
210 220 230 240 250
VYIGPDDAQQ KIEPHHTAVL GEGDSVQVEN KDPKRSHFVL IAGEPLREPV
260 270 280 290
IQHGPFVMNT NEEISQAILD FRNAKNGFER AKTWKSKIGN
Length:290
Mass (Da):32,113
Last modified:July 1, 1997 - v1
Checksum:iD06AC100F356496D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24V → D in CAG46621 (Ref. 2) Curated1
Sequence conflicti162K → R in CAG46621 (Ref. 2) Curated1

Polymorphismi

Genetic variations in PIR might have a sex-specific influence on bone mineral density differences in some populations, as reported by PubMed:19766747. In a cohort of 4000 Chinese, a significant statistical association has been identified, in women but not in men, between the intronic SNP rs5935970 and lumbar spine bone mineral density, and between a haplotype composed of three SNPs with bone mineral density at other sites.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050543228V → A.Corresponds to variant rs34104000dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07868 mRNA. Translation: CAA69195.1.
Y07867 mRNA. Translation: CAA69194.1.
CR541822 mRNA. Translation: CAG46621.1.
BT019583 mRNA. Translation: AAV38390.1.
BT019584 mRNA. Translation: AAV38391.1.
BC002517 mRNA. Translation: AAH02517.1.
CCDSiCCDS14167.1.
RefSeqiNP_001018119.1. NM_001018109.2.
NP_003653.1. NM_003662.3.
UniGeneiHs.495728.
Hs.732521.

Genome annotation databases

EnsembliENST00000380420; ENSP00000369785; ENSG00000087842.
ENST00000380421; ENSP00000369786; ENSG00000087842.
GeneIDi8544.
KEGGihsa:8544.
UCSCiuc004cwu.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07868 mRNA. Translation: CAA69195.1.
Y07867 mRNA. Translation: CAA69194.1.
CR541822 mRNA. Translation: CAG46621.1.
BT019583 mRNA. Translation: AAV38390.1.
BT019584 mRNA. Translation: AAV38391.1.
BC002517 mRNA. Translation: AAH02517.1.
CCDSiCCDS14167.1.
RefSeqiNP_001018119.1. NM_001018109.2.
NP_003653.1. NM_003662.3.
UniGeneiHs.495728.
Hs.732521.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J1LX-ray2.10A1-290[»]
3ACLX-ray2.35A2-290[»]
4EROX-ray2.65A1-290[»]
4EWAX-ray2.47A1-290[»]
4EWDX-ray2.15A1-290[»]
4EWEX-ray1.56A1-290[»]
4GULX-ray1.80A3-290[»]
4HLTX-ray1.70A3-290[»]
ProteinModelPortaliO00625.
SMRiO00625.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114114. 53 interactors.
IntActiO00625. 2 interactors.
MINTiMINT-1189585.
STRINGi9606.ENSP00000369785.

Chemistry databases

BindingDBiO00625.
ChEMBLiCHEMBL2010627.

PTM databases

iPTMnetiO00625.
PhosphoSitePlusiO00625.

Polymorphism and mutation databases

BioMutaiPIR.

2D gel databases

UCD-2DPAGEO00625.

Proteomic databases

EPDiO00625.
MaxQBiO00625.
PaxDbiO00625.
PeptideAtlasiO00625.
PRIDEiO00625.
TopDownProteomicsiO00625.

Protocols and materials databases

DNASUi8544.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380420; ENSP00000369785; ENSG00000087842.
ENST00000380421; ENSP00000369786; ENSG00000087842.
GeneIDi8544.
KEGGihsa:8544.
UCSCiuc004cwu.5. human.

Organism-specific databases

CTDi8544.
DisGeNETi8544.
GeneCardsiPIR.
HGNCiHGNC:30048. PIR.
HPAiHPA000697.
MIMi300931. gene.
neXtProtiNX_O00625.
OpenTargetsiENSG00000087842.
PharmGKBiPA134870022.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF52. Eukaryota.
COG1741. LUCA.
GeneTreeiENSGT00390000008044.
HOGENOMiHOG000248360.
HOVERGENiHBG019151.
InParanoidiO00625.
KOiK06911.
OMAiDLDPFVH.
OrthoDBiEOG091G0PKY.
PhylomeDBiO00625.
TreeFamiTF300002.

Enzyme and pathway databases

UniPathwayiUPA00724.
BioCyciZFISH:ENSG00000087842-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO00625.
GeneWikiiPIR_(gene).
GenomeRNAii8544.
PROiO00625.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087842.
CleanExiHS_PIR.
ExpressionAtlasiO00625. baseline and differential.
GenevisibleiO00625. HS.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR012093. Pirin.
IPR008778. Pirin_C_dom.
IPR003829. Pirin_N_dom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR13903. PTHR13903. 1 hit.
PfamiPF02678. Pirin. 1 hit.
PF05726. Pirin_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006232. Pirin. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPIR_HUMAN
AccessioniPrimary (citable) accession number: O00625
Secondary accession number(s): Q5U0G0, Q6FHD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 141 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, 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.