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Protein

Pirin

Gene

PIR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • digestion Source: Reactome
  • monocyte differentiation Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription by RNA polymerase II Source: ProtInc

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processTranscription, Transcription regulation
LigandIron, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-8935690 Digestion
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

Organism-specific databases

EuPathDBiHostDB:ENSG00000087842.10
HGNCiHGNC:30048 PIR
MIMi300931 gene
neXtProtiNX_O00625

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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-2DPAGEiO00625

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, 54 interactors
IntActiO00625, 2 interactors
MINTiO00625
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[»]
5JCTX-ray1.73A1-290[»]
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
OMAiFVFFDHM
OrthoDBiEOG091G0PKY
PhylomeDBiO00625
TreeFamiTF300002

Family and domain databases

Gene3Di2.60.120.10, 3 hits
InterProiView protein in InterPro
IPR012093 Pirin
IPR008778 Pirin_C_dom
IPR003829 Pirin_N_dom
IPR014710 RmlC-like_jellyroll
IPR011051 RmlC_Cupin_sf
PfamiView protein in Pfam
PF02678 Pirin, 1 hit
PF05726 Pirin_C, 1 hit
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 dbSNP:rs34104000Ensembl.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

Entry informationi

Entry nameiPIR_HUMAN
AccessioniPrimary (citable) accession number: O00625
Secondary accession number(s): Q5U0G0, Q6FHD2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: July 1, 1997
Last modified: March 28, 2018
This is version 151 of the entry and version 1 of the sequence. See 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

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