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O00625

- PIR_HUMAN

UniProt

O00625 - PIR_HUMAN

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Protein

Pirin

Gene
PIR
Organism
Homo sapiens (Human)
Status
Reviewed - 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).5 Publications

Catalytic activityi

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

Cofactori

Binds 1 iron ion per subunit.2 Publications

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi56 – 561Iron
Metal bindingi58 – 581Iron
Metal bindingi101 – 1011Iron
Metal bindingi103 – 1031Iron

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. quercetin 2,3-dioxygenase activity Source: UniProtKB
  4. transcription cofactor activity Source: UniProtKB

GO - Biological processi

  1. monocyte differentiation Source: MGI
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. 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

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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:30048. PIR.

Subcellular locationi

Nucleus. Cytoplasm
Note: Predominantly localized in dot-like subnuclear structures. Cytoplasmic localization of PIR seems to positively correlate with melanoma progression.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134870022.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290PirinPRO_0000214051Add
BLAST

Proteomic databases

MaxQBiO00625.
PaxDbiO00625.
PeptideAtlasiO00625.
PRIDEiO00625.

2D gel databases

UCD-2DPAGEO00625.

PTM databases

PhosphoSiteiO00625.

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.3 Publications

Gene expression databases

BgeeiO00625.
CleanExiHS_PIR.
GenevestigatoriO00625.

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.3 Publications

Protein-protein interaction databases

BioGridi114114. 13 interactions.
IntActiO00625. 1 interaction.
MINTiMINT-1189585.
STRINGi9606.ENSP00000369785.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126
Beta strandi14 – 185
Beta strandi22 – 265
Helixi31 – 333
Beta strandi39 – 479
Beta strandi52 – 6716
Beta strandi69 – 713
Beta strandi73 – 775
Beta strandi82 – 854
Beta strandi90 – 945
Beta strandi99 – 1057
Beta strandi107 – 1093
Beta strandi111 – 1199
Helixi122 – 1243
Beta strandi130 – 1345
Helixi136 – 1383
Beta strandi147 – 15610
Beta strandi169 – 1768
Beta strandi181 – 1855
Beta strandi191 – 1999
Beta strandi201 – 2044
Beta strandi210 – 2123
Beta strandi216 – 2205
Beta strandi224 – 2296
Beta strandi232 – 2343
Beta strandi236 – 2438
Beta strandi251 – 2533
Beta strandi256 – 2605
Helixi261 – 27212
Helixi279 – 2813
Turni287 – 2893

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 3-290.

Miscellaneous databases

EvolutionaryTraceiO00625.

Family & Domainsi

Sequence similaritiesi

Belongs to the pirin family.

Phylogenomic databases

eggNOGiCOG1741.
HOGENOMiHOG000248360.
HOVERGENiHBG019151.
InParanoidiO00625.
KOiK06911.
OMAiQWMTAAR.
OrthoDBiEOG7JMGFH.
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

MGSSKKVTLS VLSREQSEGV GARVRRSIGR PELKNLDPFL LFDEFKGGRP    50
GGFPDHPHRG FETVSYLLEG GSMAHEDFCG HTGKMNPGDL QWMTAGRGIL 100
HAEMPCSEEP AHGLQLWVNL RSSEKMVEPQ YQELKSEEIP KPSKDGVTVA 150
VISGEALGIK SKVYTRTPTL YLDFKLDPGA KHSQPIPKGW TSFIYTISGD 200
VYIGPDDAQQ KIEPHHTAVL GEGDSVQVEN KDPKRSHFVL IAGEPLREPV 250
IQHGPFVMNT NEEISQAILD FRNAKNGFER AKTWKSKIGN 290
Length:290
Mass (Da):32,113
Last modified:July 1, 1997 - v1
Checksum:iD06AC100F356496D
GO

Polymorphismi

Genetic variations in PIR might have a sex-specific influence on bone mineral density differences in some populations, as reported by 1 Publication. 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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti228 – 2281V → A.
Corresponds to variant rs34104000 [ dbSNP | Ensembl ].
VAR_050543

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241V → D in CAG46621. 1 Publication
Sequence conflicti162 – 1621K → R in CAG46621. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14167.1.
RefSeqi NP_001018119.1. NM_001018109.2.
NP_003653.1. NM_003662.3.
UniGenei Hs.495728.
Hs.732521.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J1L X-ray 2.10 A 1-290 [» ]
3ACL X-ray 2.35 A 2-290 [» ]
4ERO X-ray 2.65 A 1-290 [» ]
4EWA X-ray 2.47 A 1-290 [» ]
4EWD X-ray 2.15 A 1-290 [» ]
4EWE X-ray 1.56 A 1-290 [» ]
4GUL X-ray 1.80 A 3-290 [» ]
4HLT X-ray 1.70 A 3-290 [» ]
ProteinModelPortali O00625.
SMRi O00625. Positions 3-290.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114114. 13 interactions.
IntActi O00625. 1 interaction.
MINTi MINT-1189585.
STRINGi 9606.ENSP00000369785.

Chemistry

ChEMBLi CHEMBL2010627.

PTM databases

PhosphoSitei O00625.

2D gel databases

UCD-2DPAGE O00625.

Proteomic databases

MaxQBi O00625.
PaxDbi O00625.
PeptideAtlasi O00625.
PRIDEi O00625.

Protocols and materials databases

DNASUi 8544.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380420 ; ENSP00000369785 ; ENSG00000087842 .
ENST00000380421 ; ENSP00000369786 ; ENSG00000087842 .
GeneIDi 8544.
KEGGi hsa:8544.
UCSCi uc004cwu.3. human.

Organism-specific databases

CTDi 8544.
GeneCardsi GC0XM015402.
HGNCi HGNC:30048. PIR.
HPAi HPA000697.
MIMi 603329. gene.
neXtProti NX_O00625.
PharmGKBi PA134870022.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1741.
HOGENOMi HOG000248360.
HOVERGENi HBG019151.
InParanoidi O00625.
KOi K06911.
OMAi QWMTAAR.
OrthoDBi EOG7JMGFH.
PhylomeDBi O00625.
TreeFami TF300002.

Enzyme and pathway databases

UniPathwayi UPA00724 .

Miscellaneous databases

EvolutionaryTracei O00625.
GeneWikii PIR_(gene).
GenomeRNAii 8544.
NextBioi 32006.
PROi O00625.
SOURCEi Search...

Gene expression databases

Bgeei O00625.
CleanExi HS_PIR.
Genevestigatori O00625.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
InterProi IPR012093. Pirin.
IPR008778. Pirin_C_dom.
IPR003829. Pirin_N_dom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
PANTHERi PTHR13903. PTHR13903. 1 hit.
Pfami PF02678. Pirin. 1 hit.
PF05726. Pirin_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF006232. Pirin. 1 hit.
SUPFAMi SSF51182. SSF51182. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of pirin, a novel highly conserved nuclear protein."
    Wendler W.M.F., Kremmer E., Foerster R., Winnacker E.-L.
    J. Biol. Chem. 272:8482-8489(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROPOSED FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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: Placenta.
  5. "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators."
    Dechend R., Hirano F., Lehmann K., Heissmeyer V., Ansieau S., Wulczyn F.G., Scheidereit C., Leutz A.
    Oncogene 18:3316-3323(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL3, IDENTIFICATION IN A COMPLEX WITH BLC3; NFKB1; PIR AND TARGET DNA.
  6. "Structural and biochemical analysis reveal pirins to possess quercetinase activity."
    Adams M., Jia Z.
    J. Biol. Chem. 280:28675-28682(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
  7. "Upregulation of pirin expression by chronic cigarette smoking is associated with bronchial epithelial cell apoptosis."
    Gelbman B.D., Heguy A., O'Connor T.P., Zabner J., Crystal R.G.
    Respir. Res. 8:10-10(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  8. "Pirin delocalization in melanoma progression identified by high content immuno-detection based approaches."
    Licciulli S., Luise C., Zanardi A., Giorgetti L., Viale G., Lanfrancone L., Carbone R., Alcalay M.
    BMC Cell Biol. 11:5-5(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Sex-specific effect of Pirin gene on bone mineral density in a cohort of 4000 Chinese."
    Tang N.L., Liao C.D., Ching J.K., Suen E.W., Chan I.H., Orwoll E., Ho S.C., Chan F.W., Kwok A.W., Kwok T., Woo J., Leung P.C.
    Bone 46:543-550(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INFLUENCE OF PIR POLYMORPHISMS ON BONE MINERAL DENSITY.
  10. "Pirin downregulation is a feature of AML and leads to impairment of terminal myeloid differentiation."
    Licciulli S., Cambiaghi V., Scafetta G., Gruszka A.M., Alcalay M.
    Leukemia 24:429-437(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of human pirin: an iron-binding nuclear protein and transcription cofactor."
    Pang H., Bartlam M., Zeng Q., Miyatake H., Hisano T., Miki K., Wong L.L., Gao G.F., Rao Z.
    J. Biol. Chem. 279:1491-1498(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS, COFACTOR.
  14. "A small-molecule inhibitor shows that pirin regulates migration of melanoma cells."
    Miyazaki I., Simizu S., Okumura H., Takagi S., Osada H.
    Nat. Chem. Biol. 6:667-673(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH A SYNTHETIC INHIBITOR AND IRON IONS, INTERACTION WITH BCL3, COFACTOR, FUNCTION.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS), FUNCTION.

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: July 9, 2014
This is version 123 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

External Data

Dasty 3

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