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Q99697 (PITX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pituitary homeobox 2
Alternative name(s):
ALL1-responsive protein ARP1
Homeobox protein PITX2
Paired-like homeodomain transcription factor 2
RIEG bicoid-related homeobox transcription factor
Solurshin
Gene names
Name:PITX2
Synonyms:ARP1, RGS, RIEG, RIEG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Controls cell proliferation in a tissue-specific manner and is involved in morphogenesis. During embryonic development, exerts a role in the expansion of muscle progenitors. May play a role in the proper localization of asymmetric organs such as the heart and stomach. Isoform PTX2C is involved in left-right asymmetry the developing embryo By similarity.

Subcellular location

Nucleus.

Post-translational modification

Phosphorylation at Thr-90 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1 By similarity.

Involvement in disease

Axenfeld-Rieger syndrome 1 (RIEG1) [MIM:180500]: An autosomal dominant disorder of morphogenesis that results in abnormal development of the anterior segment of the eye, and results in blindness from glaucoma in approximately 50% of affected individuals. Additional features include aniridia, maxillary hypoplasia, hypodontia, anal stenosis, redundant periumbilical skin.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.11 Ref.12 Ref.13 Ref.15

Iridogoniodysgenesis 2 (IRID2) [MIM:137600]: Autosomal dominant inherited disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9

Peters anomaly (PETAN) [MIM:604229]: Consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Ring dermoid of cornea (RDC) [MIM:180550]: An ocular disorder characterized by bilateral annular limbal dermoids (growths with a skin-like structure) with corneal and conjunctival extension.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.14

Sequence similarities

Belongs to the paired homeobox family. Bicoid subfamily.

Contains 1 homeobox DNA-binding domain.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Peters anomaly
   DomainHomeobox
   LigandDNA-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

atrial cardiac muscle tissue morphogenesis

Inferred from electronic annotation. Source: Ensembl

atrioventricular valve development

Inferred from electronic annotation. Source: Ensembl

camera-type eye development

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

cardiac neural crest cell migration involved in outflow tract morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cell proliferation involved in outflow tract morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

deltoid tuberosity development

Inferred from mutant phenotype PubMed 18312615. Source: BHF-UCL

determination of left/right symmetry

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic camera-type eye development

Inferred from electronic annotation. Source: Ensembl

embryonic digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

endodermal digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

extraocular skeletal muscle development

Inferred from electronic annotation. Source: Ensembl

female gonad development

Inferred from electronic annotation. Source: Ensembl

hair cell differentiation

Inferred by curator PubMed 19251162. Source: BHF-UCL

hypothalamus cell migration

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

iris morphogenesis

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

left lung morphogenesis

Inferred from electronic annotation. Source: Ensembl

left/right axis specification

Inferred from sequence or structural similarity. Source: BHF-UCL

male gonad development

Inferred from electronic annotation. Source: Ensembl

myoblast fusion

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19174163. Source: BHF-UCL

neuron migration

Inferred from electronic annotation. Source: Ensembl

odontogenesis

Inferred from mutant phenotype PubMed 14630904. Source: BHF-UCL

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of myoblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19251162PubMed 9685346PubMed 19174163PubMed 15466416. Source: BHF-UCL

prolactin secreting cell differentiation

Traceable author statement PubMed 10372733. Source: BHF-UCL

pulmonary myocardium development

Inferred from electronic annotation. Source: Ensembl

pulmonary vein morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 23975681. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15385555. Source: MGI

response to hormone

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

somatotropin secreting cell differentiation

Traceable author statement PubMed 10372733. Source: BHF-UCL

spleen development

Inferred from sequence or structural similarity. Source: BHF-UCL

subthalamic nucleus development

Inferred from electronic annotation. Source: Ensembl

superior vena cava morphogenesis

Inferred from electronic annotation. Source: Ensembl

vascular smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

ventricular septum morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 19251162PubMed 16449236. Source: BHF-UCL

transcription factor complex

Inferred from direct assay PubMed 15385555. Source: MGI

   Molecular_functionRNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 9685346PubMed 12612071. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 16449236. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription coactivator activity

Inferred from direct assay PubMed 9685346. Source: BHF-UCL

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 15466416. Source: BHF-UCL

RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 16449236. Source: BHF-UCL

chromatin DNA binding

Inferred from electronic annotation. Source: Ensembl

phosphoprotein binding

Inferred from physical interaction PubMed 19174163. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 19174163. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction PubMed 19174163PubMed 12612071. Source: BHF-UCL

ribonucleoprotein complex binding

Inferred by curator PubMed 19174163. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15385555. Source: MGI

transcription factor binding

Inferred from physical interaction PubMed 15385555. Source: MGI

transcription regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 9685346PubMed 12612071. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FOXC1Q129486EBI-1175243,EBI-1175253
Hoxa1P090223EBI-1175211,EBI-3957603From a different organism.
YBX1P678093EBI-1175211,EBI-354065

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform PTX2B (identifier: Q99697-1)

Also known as: ARP1B;

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.
Isoform PTX2C (identifier: Q99697-2)

Also known as: ARP1C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: METNCRKLVS...FFPRQHPGAN → MNCMKGPLHL...ISDTSSPEAA
Isoform PTX2A (identifier: Q99697-3)

Also known as: ARP1A;

The sequence of this isoform differs from the canonical sequence as follows:
     16-61: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Pituitary homeobox 2
PRO_0000049223

Regions

DNA binding85 – 14460Homeobox
Motif279 – 29214OAR
Motif285 – 2895Nuclear localization signal Potential

Amino acid modifications

Modified residue901Phosphothreonine; by PKB/AKT2 By similarity

Natural variations

Alternative sequence1 – 6161METNC…HPGAN → MNCMKGPLHLEHRAAGTKLS AVSSSSCHHPQPLAMASVLA PGQPRSLDSSKHRLEVHTIS DTSSPEAA in isoform PTX2C.
VSP_002260
Alternative sequence16 – 6146Missing in isoform PTX2A.
VSP_002261
Natural variant1001L → Q in RIEG1. Ref.1
VAR_003763
Natural variant1081R → H in RDC; results in 25% loss of transactivation activity. Ref.7 Ref.14
VAR_035027
Natural variant1101P → L in RIEG1. Ref.13 Ref.15
VAR_058735
Natural variant1101P → R in RIEG1. Ref.15
VAR_058736
Natural variant1141T → P in RIEG1. Ref.1
VAR_003764
Natural variant1151R → H in IRID2. Ref.9
VAR_003765
Natural variant128 – 1347Missing in RIEG1; more than 100-fold reduction in DNA binding activity as well as no detectable transactivation activity.
VAR_035028
Natural variant1291V → L in RIEG1; more than 200% increase in transactivation activity. Ref.12
VAR_035029
Natural variant1301R → W in IRID2. Ref.8
VAR_003762
Natural variant1341K → E in RIEG1. Ref.11
VAR_058737
Natural variant1361R → C in RIEG1. Ref.11 Ref.13
VAR_058738
Natural variant1371R → P in RIEG1. Ref.1
VAR_003766
Natural variant1511L → V in RIEG1. Ref.13
VAR_058739
Natural variant1541N → T in RIEG1. Ref.13
VAR_058740

Experimental info

Sequence conflict131V → L Ref.1
Sequence conflict131V → L Ref.3
Sequence conflict991E → Q in AAC16257. Ref.1
Sequence conflict1271A → T in BAF84280. Ref.4
Sequence conflict3011N → K Ref.1
Sequence conflict3011N → K Ref.3

Secondary structure

........... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PTX2B (ARP1B) [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 00853AFDBA4433CB

FASTA31735,370
        10         20         30         40         50         60 
METNCRKLVS ACVQLGVQPA AVECLFSKDS EIKKVEFTDS PESRKEAASS KFFPRQHPGA 

        70         80         90        100        110        120 
NEKDKSQQGK NEDVGAEDPS KKKRQRRQRT HFTSQQLQEL EATFQRNRYP DMSTREEIAV 

       130        140        150        160        170        180 
WTNLTEARVR VWFKNRRAKW RKRERNQQAE LCKNGFGPQF NGLMQPYDDM YPGYSYNNWA 

       190        200        210        220        230        240 
AKGLTSASLS TKSFPFFNSM NVNPLSSQSM FSPPNSISSM SMSSSMVPSA VTGVPGSSLN 

       250        260        270        280        290        300 
SLNNLNNLSS PSLNSAVPTP ACPYAPPTPP YVYRDTCNSS LASLRLKAKQ HSSFGYASVQ 

       310 
NPASNLSACQ YAVDRPV 

« Hide

Isoform PTX2C (ARP1C) [UniParc].

Checksum: 7379DD12E1B0013C
Show »

FASTA32435,796
Isoform PTX2A (ARP1A) [UniParc].

Checksum: 45D2ADA6DF03FF65
Show »

FASTA27130,336

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel bicoid-related homeobox transcription factor gene, RIEG, involved in Rieger syndrome."
Semina E.V., Reiter R., Leysens N.J., Alward W.L.M., Small K.W., Datson N.A., Siegle-Bartelt J., Bierke-Nelson D., Bitoun P., Zabel B.U., Carey J.C., Murray J.C.
Nat. Genet. 14:392-399(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PTX2B), VARIANTS RIEG1 GLN-100; PRO-114 AND PRO-137.
Tissue: Craniofacial and Fetal brain.
[2]"Identification and characterization of the ARP1 gene, a target for the human acute leukemia ALL1 gene."
Arakawa H., Nakamura T., Zhadanov A.B., Fidanza Y., Yano T., Bullrich F., Shimizu M., Blechman J., Mazo A., Canaani E., Croce C.M.
Proc. Natl. Acad. Sci. U.S.A. 95:4573-4578(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PTX2A; PTX2B AND PTX2C), ALTERNATIVE SPLICING.
[3]"Spectrum and frequency of PITX2 mutations in patients with Rieger syndrome and related ocular anomalies."
Semina E.V., Funkhauser C., Bitoun P., Daack-Hirsch S., Alward W.L.M., Amendt B., Murray J.C.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PTX2A).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PTX2A; PTX2B AND PTX2C).
Tissue: Placenta and Tongue.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS PTX2C AND PTX2A).
Tissue: Lung and Uterus.
[7]"Structural and biophysical insights into the ligand-free Pitx2 homeodomain and a ring dermoid of the cornea inducing homeodomain mutant."
Doerdelmann T., Kojetin D.J., Baird-Titus J.M., Solt L.A., Burris T.P., Rance M.
Biochemistry 51:665-676(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 85-144 OF WILD-TYPE AND MUTANT HIS-108 IN COMPLEX WITH DNA, VARIANT RDC HIS-108.
[8]"Autosomal dominant iris hypoplasia is caused by a mutation in the Rieger syndrome (RIEG/PITX2) gene."
Alward W.L.M., Semina E.V., Kalenak J.W., Heon E., Sheth B.P., Stone E.M., Murray J.C.
Am. J. Ophthalmol. 125:98-100(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IRID2 TRP-130.
[9]"Mutation in the RIEG1 gene in patients with iridogoniodysgenesis syndrome."
Kulak S.C., Kozlowski K., Semina E.V., Pearce W.G., Walter M.A.
Hum. Mol. Genet. 7:1113-1117(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IRID2 HIS-115.
[10]"A mutation in the RIEG1 gene associated with Peters' anomaly."
Doward W., Perveen R., Lloyd I.C., Ridgway A.E.A., Wilson L., Black G.C.M.
J. Med. Genet. 36:152-155(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PETAN.
[11]"Phenotypic variability and asymmetry of Rieger syndrome associated with PITX2 mutations."
Perveen R., Lloyd I.C., Clayton-Smith J., Churchill A., van Heyningen V., Hanson I., Taylor D., McKeown C., Super M., Kerr B., Winter R., Black G.C.M.
Invest. Ophthalmol. Vis. Sci. 41:2456-2460(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RIEG1 GLU-134 AND CYS-136.
[12]"Functional analyses of two newly identified PITX2 mutants reveal a novel molecular mechanism for Axenfeld-Rieger syndrome."
Priston M., Kozlowski K., Gill D., Letwin K., Buys Y., Levin A.V., Walter M.A., Heon E.
Hum. Mol. Genet. 10:1631-1638(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RIEG1 ARG-128--134-LYS DEL AND LEU-129, CHARACTERIZATION OF VARIANTS RIEG1 ARG-128--134-LYS DEL AND LEU-129.
[13]"Four novel mutations in the PITX2 gene in patients with Axenfeld-Rieger syndrome."
Phillips J.C.
Ophthalmic Res. 34:324-326(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RIEG1 LEU-110; CYS-136; VAL-151 AND THR-154.
[14]"Mutation in PITX2 is associated with ring dermoid of the cornea."
Xia K., Wu L., Liu X., Xi X., Liang D., Zheng D., Cai F., Pan Q., Long Z., Dai H., Hu Z., Tang B., Zhang Z., Xia J.
J. Med. Genet. 41:E129-E129(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RDC HIS-108.
[15]"Novel mutations of FOXC1 and PITX2 in patients with Axenfeld-Rieger malformations."
Weisschuh N., Dressler P., Schuettauf F., Wolf C., Wissinger B., Gramer E.
Invest. Ophthalmol. Vis. Sci. 47:3846-3852(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RIEG1 LEU-110 AND ARG-110.
[16]Erratum
Weisschuh N., Dressler P., Schuettauf F., Wolf C., Wissinger B., Gramer E.
Invest. Ophthalmol. Vis. Sci. 47:5162-5162(2006)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U69961 mRNA. Translation: AAC16257.1.
AF048720 mRNA. Translation: AAC39716.1.
AF048721 mRNA. Translation: AAC39717.1.
AF048722 mRNA. Translation: AAC39718.1.
AF238048 Genomic DNA. Translation: AAK15048.1.
AK127829 mRNA. Translation: BAG54582.1.
AK291591 mRNA. Translation: BAF84280.1.
AK313987 mRNA. Translation: BAG36699.1.
CH471057 Genomic DNA. Translation: EAX06262.1.
CH471057 Genomic DNA. Translation: EAX06263.1.
CH471057 Genomic DNA. Translation: EAX06264.1.
BC013998 mRNA. Translation: AAH13998.1.
BC106010 mRNA. Translation: AAI06011.1.
CCDSCCDS3692.1. [Q99697-1]
CCDS3693.1. [Q99697-3]
CCDS3694.1. [Q99697-2]
RefSeqNP_000316.2. NM_000325.5. [Q99697-2]
NP_001191326.1. NM_001204397.1. [Q99697-1]
NP_001191327.1. NM_001204398.1. [Q99697-1]
NP_001191328.1. NM_001204399.1. [Q99697-3]
NP_700475.1. NM_153426.2. [Q99697-1]
NP_700476.1. NM_153427.2. [Q99697-3]
XP_006714298.1. XM_006714235.1. [Q99697-1]
UniGeneHs.643588.
Hs.738484.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L7FNMR-P85-144[»]
2L7MNMR-P85-144[»]
2LKXNMR-A85-144[»]
ProteinModelPortalQ99697.
SMRQ99697. Positions 85-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111325. 14 interactions.
IntActQ99697. 12 interactions.
STRING9606.ENSP00000304169.

Polymorphism databases

DMDM6174907.

Proteomic databases

MaxQBQ99697.
PaxDbQ99697.
PRIDEQ99697.

Protocols and materials databases

DNASU5308.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306732; ENSP00000304169; ENSG00000164093. [Q99697-2]
ENST00000354925; ENSP00000347004; ENSG00000164093. [Q99697-1]
ENST00000355080; ENSP00000347192; ENSG00000164093. [Q99697-3]
ENST00000394598; ENSP00000378097; ENSG00000164093. [Q99697-1]
GeneID5308.
KEGGhsa:5308.
UCSCuc003iac.3. human. [Q99697-2]
uc003iad.3. human. [Q99697-1]
uc003iae.3. human. [Q99697-3]

Organism-specific databases

CTD5308.
GeneCardsGC04M111538.
GeneReviewsPITX2.
HGNCHGNC:9005. PITX2.
HPAHPA050074.
MIM137600. phenotype.
180500. phenotype.
180550. phenotype.
601542. gene.
604229. phenotype.
neXtProtNX_Q99697.
Orphanet98978. Axenfeld anomaly.
782. Axenfeld-Rieger syndrome.
334. Familial atrial fibrillation.
708. Peters anomaly.
91483. Rieger anomaly.
91481. Ring dermoid of cornea.
PharmGKBPA33339.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249113.
HOVERGENHBG068770.
KOK04686.
OMADMYPSYT.
OrthoDBEOG7VTDNW.
PhylomeDBQ99697.
TreeFamTF351940.

Enzyme and pathway databases

SignaLinkQ99697.

Gene expression databases

ArrayExpressQ99697.
BgeeQ99697.
CleanExHS_PITX2.
GenevestigatorQ99697.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR016233. Homeobox_Pitx/unc30.
IPR009057. Homeodomain-like.
IPR003654. OAR_dom.
[Graphical view]
PfamPF00046. Homeobox. 1 hit.
PF03826. OAR. 1 hit.
[Graphical view]
PIRSFPIRSF000563. Homeobox_protein_Pitx/Unc30. 1 hit.
SMARTSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
PS50803. OAR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPITX2. human.
EvolutionaryTraceQ99697.
GeneWikiPITX2.
GenomeRNAi5308.
NextBio20518.
PROQ99697.
SOURCESearch...

Entry information

Entry namePITX2_HUMAN
AccessionPrimary (citable) accession number: Q99697
Secondary accession number(s): A8K6C6 expand/collapse secondary AC list , B2RA02, B3KXS0, O60578, O60579, O60580, Q3KQX9, Q9BY17
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM