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Protein

Pirin

Gene

Pir

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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) (By similarity).By similarity1 Publication

Catalytic activityi

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

Cofactori

Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi56 – 561IronBy similarity
Metal bindingi58 – 581IronBy similarity
Metal bindingi101 – 1011IronBy similarity
Metal bindingi103 – 1031IronBy similarity

GO - Molecular functioni

GO - Biological processi

  • monocyte differentiation Source: MGI
  • myeloid cell differentiation Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1916906. Pir.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Predominantly localized in dot-like subnuclear structures.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290PirinPRO_0000214052Add
BLAST

Proteomic databases

EPDiQ9D711.
MaxQBiQ9D711.
PaxDbiQ9D711.
PRIDEiQ9D711.

PTM databases

PhosphoSiteiQ9D711.

Expressioni

Tissue specificityi

Weakly expressed in bone marrow.1 Publication

Inductioni

Down-regulated in mice with acute myeloid leukemias induced by either PML-RAR or AML1-ETO fusion oncoproteins.1 Publication

Gene expression databases

BgeeiQ9D711.
CleanExiMM_PIR.
ExpressionAtlasiQ9D711. baseline and differential.
GenevisibleiQ9D711. MM.

Interactioni

Subunit structurei

May interact with NF1/CTF1. Interacts with BCL3. Identified in a complex comprised of PIR, BLC3, NFKB1 and target DNA (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9D711. 1 interaction.
MINTiMINT-4107667.
STRINGi10090.ENSMUSP00000033749.

Structurei

3D structure databases

ProteinModelPortaliQ9D711.
SMRiQ9D711. Positions 3-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pirin family.Curated

Phylogenomic databases

eggNOGiENOG410IF52. Eukaryota.
COG1741. LUCA.
GeneTreeiENSGT00390000008044.
HOGENOMiHOG000248360.
HOVERGENiHBG019151.
InParanoidiQ9D711.
KOiK06911.
OMAiDPFVHMD.
PhylomeDBiQ9D711.
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.

Q9D711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSKKVTLS VLSREQSEGV GARVRRSIGR PELKNLDPFL LFDEFKGGKP
60 70 80 90 100
GGFPDHPHRG FETVSYLLEG GSMAHEDFCG HVGKMNPGDL QWMTAGRGIL
110 120 130 140 150
HAEMPCSEEP AHGLQLWVNL RRSEKMVAPQ YQELKSEEIP KPTKDGVTVA
160 170 180 190 200
VISGEALGIK SKVYTRTPTL YLDFKLDQGA KHSQPIPKGW TSFIYTISGD
210 220 230 240 250
VYIGPDDAQQ KIEPHHTAVL GEGDAVQLEN KDPKRSHFVL IAGEPLREPV
260 270 280 290
VQHGPFVMNT NEEISQAILD FRNAKNGFEG ARTWKSKIGN
Length:290
Mass (Da):32,066
Last modified:June 1, 2001 - v1
Checksum:iB95915522F62EC5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491K → R in AAH24062 (PubMed:19468303).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009757 mRNA. Translation: BAB26481.1.
AK138314 mRNA. Translation: BAE23621.1.
AK151301 mRNA. Translation: BAE30284.1.
AL671706, AL732475 Genomic DNA. Translation: CAM21159.1.
AL732475, AL671706 Genomic DNA. Translation: CAM17376.1.
CH466571 Genomic DNA. Translation: EDL40759.1.
BC024062 mRNA. Translation: AAH24062.1.
AF345635 Genomic DNA. Translation: AAK54068.1.
CCDSiCCDS30520.1.
RefSeqiNP_081429.1. NM_027153.3.
XP_006529040.1. XM_006528977.2.
UniGeneiMm.293463.

Genome annotation databases

EnsembliENSMUST00000033749; ENSMUSP00000033749; ENSMUSG00000031379.
GeneIDi69656.
KEGGimmu:69656.
UCSCiuc009uvl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009757 mRNA. Translation: BAB26481.1.
AK138314 mRNA. Translation: BAE23621.1.
AK151301 mRNA. Translation: BAE30284.1.
AL671706, AL732475 Genomic DNA. Translation: CAM21159.1.
AL732475, AL671706 Genomic DNA. Translation: CAM17376.1.
CH466571 Genomic DNA. Translation: EDL40759.1.
BC024062 mRNA. Translation: AAH24062.1.
AF345635 Genomic DNA. Translation: AAK54068.1.
CCDSiCCDS30520.1.
RefSeqiNP_081429.1. NM_027153.3.
XP_006529040.1. XM_006528977.2.
UniGeneiMm.293463.

3D structure databases

ProteinModelPortaliQ9D711.
SMRiQ9D711. Positions 3-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D711. 1 interaction.
MINTiMINT-4107667.
STRINGi10090.ENSMUSP00000033749.

PTM databases

PhosphoSiteiQ9D711.

Proteomic databases

EPDiQ9D711.
MaxQBiQ9D711.
PaxDbiQ9D711.
PRIDEiQ9D711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033749; ENSMUSP00000033749; ENSMUSG00000031379.
GeneIDi69656.
KEGGimmu:69656.
UCSCiuc009uvl.2. mouse.

Organism-specific databases

CTDi8544.
MGIiMGI:1916906. Pir.

Phylogenomic databases

eggNOGiENOG410IF52. Eukaryota.
COG1741. LUCA.
GeneTreeiENSGT00390000008044.
HOGENOMiHOG000248360.
HOVERGENiHBG019151.
InParanoidiQ9D711.
KOiK06911.
OMAiDPFVHMD.
PhylomeDBiQ9D711.
TreeFamiTF300002.

Enzyme and pathway databases

UniPathwayiUPA00724.

Miscellaneous databases

NextBioi329994.
PROiQ9D711.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D711.
CleanExiMM_PIR.
ExpressionAtlasiQ9D711. baseline and differential.
GenevisibleiQ9D711. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Hypothalamus and Tongue.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. "Hypoxia upregulates VEGF-D promoter in pulmonary vascular smooth muscle cells."
    Teng X., Li D., Johns R.A.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 255-290.
    Strain: ICR.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver, Lung and Spleen.
  7. "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, TISSUE SPECIFICITY, INDUCTION.
    Strain: 129/SvEv.

Entry informationi

Entry nameiPIR_MOUSE
AccessioniPrimary (citable) accession number: Q9D711
Secondary accession number(s): A2AIH9, Q3UAN0, Q8CIE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.