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Q91ZD1 (OSR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein odd-skipped-related 2
Gene names
Name:Osr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Nucleus Probable.

Developmental stage

First detected at E9.25, specifically in the mesonephric vesicles. By E10.0 expression is also observed in the rostro-lateral mandibular mesenchyme immediately adjacent to the maxillary processes. In the developing limb buds it is expressed in a unique mesenchymal domain and the onset of the expression follows a distinct dorsal to ventral developmental time sequence beginning in the forelimb and then in the hindlimb. It exhibits a dynamic expression pattern during craniofacial development, in the mandibular and maxillary processes as well as the developing palate. It is also expressed at sites of epithelial-mesenchymal interactions during tooth and kidney development. Ref.1

Sequence similarities

Belongs to the Odd C2H2-type zinc-finger protein family.

Contains 5 C2H2-type zinc fingers.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone morphogenesis

Inferred from mutant phenotype PubMed 17547533. Source: UniProtKB

cell differentiation

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

chondrocyte differentiation

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

embryo development

Inferred from expression pattern Ref.1. Source: UniProtKB

embryonic digit morphogenesis

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

embryonic forelimb morphogenesis

Inferred from expression pattern Ref.1. Source: UniProtKB

embryonic hindlimb morphogenesis

Inferred from expression pattern Ref.1. Source: UniProtKB

embryonic skeletal joint development

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

embryonic skeletal joint morphogenesis

Inferred from mutant phenotype PubMed 21262216. Source: BHF-UCL

embryonic skeletal limb joint morphogenesis

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

embryonic skeletal system morphogenesis

Inferred from mutant phenotype PubMed 15175245. Source: MGI

eyelid development in camera-type eye

Inferred from mutant phenotype PubMed 19389375. Source: UniProtKB

head development

Inferred from mutant phenotype PubMed 21262216. Source: BHF-UCL

mesonephros development

Inferred from expression pattern Ref.1. Source: UniProtKB

metanephros development

Inferred from expression pattern Ref.1. Source: UniProtKB

middle ear morphogenesis

Inferred from mutant phenotype PubMed 19389375. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

odontogenesis

Inferred from mutant phenotype PubMed 19389375. Source: UniProtKB

osteoblast proliferation

Inferred from mutant phenotype PubMed 17547533. Source: UniProtKB

palate development

Inferred from mutant phenotype PubMed 19389375. Source: UniProtKB

positive regulation of bone mineralization

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15175245. Source: MGI

positive regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 19389375. Source: UniProtKB

positive regulation of gastrulation

Inferred from mutant phenotype PubMed 21281489. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 19389375PubMed 17547533PubMed 17547533. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 21262216. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19389375PubMed 17547533PubMed 17547533. Source: UniProtKB

pronephros development

Inferred from mutant phenotype PubMed 21281489. Source: UniProtKB

   Cellular_componentnucleus

Inferred from direct assay PubMed 17547533. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from direct assay PubMed 17547533. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91ZD1-1)

Also known as: OSR2A;

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 2 (identifier: Q91ZD1-2)

Also known as: OSR2B;

The sequence of this isoform differs from the canonical sequence as follows:
     253-312: ESPHKCPTCG...SLTHTPRQNF → TSSPTAASSAAKCSGETAICGGTA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Protein odd-skipped-related 2
PRO_0000047008

Regions

Zinc finger172 – 19423C2H2-type 1
Zinc finger200 – 22223C2H2-type 2
Zinc finger228 – 25023C2H2-type 3
Zinc finger256 – 27823C2H2-type 4
Zinc finger284 – 30623C2H2-type 5

Natural variations

Alternative sequence253 – 31260ESPHK…PRQNF → TSSPTAASSAAKCSGETAIC GGTA in isoform 2.
VSP_017122

Experimental info

Sequence conflict1421G → W in BAC34859. Ref.3

Secondary structure

.............. 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (OSR2A) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 33B4B92B1FA11D20

FASTA31235,454
        10         20         30         40         50         60 
MGSKALPAPI PLHPSLQLTN YSFLQAVNTF PAAVDHLQGL YGLSAVQTMH MNHWTLGYPS 

        70         80         90        100        110        120 
VHEITRSTIT EMAAAQGLVD ARFPFPSLPF ATHLFHPKQG AIAHVLPALH KDRPRFDFAN 

       130        140        150        160        170        180 
LAVAATQEDP PKMGDLSKLS PGLGSPISGL SKLNPDRKPS RGRLPSKTKK EFICKFCGRH 

       190        200        210        220        230        240 
FTKSYNLLIH ERTHTDERPY TCDICHKAFR RQDHLRDHRY IHSKEKPFKC QECGKGFCQS 

       250        260        270        280        290        300 
RTLAVHKTLH MQESPHKCPT CGRTFNQRSN LKTHLLTHTD IKPYSCEQCG KVFRRNCDLR 

       310 
RHSLTHTPRQ NF 

« Hide

Isoform 2 (OSR2B) [UniParc].

Checksum: A0E28AA0979CB1ED
Show »

FASTA27630,487

References

« Hide 'large scale' references
[1]"Osr2, a new mouse gene related to Drosophila odd-skipped, exhibits dynamic expression patterns during craniofacial, limb, and kidney development."
Lan Y., Kingsley P.D., Cho E.-S., Jiang R.
Mech. Dev. 107:175-179(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DEVELOPMENTAL STAGE.
Tissue: Mammary gland.
[2]"Alternative splicing of the mouse Osr2 mRNA produces two protein isoforms differing in the zinc finger region."
Jiang R., Cho E.-S., Lan Y.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Eye.
[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] (ISOFORM 2).
Strain: FVB/N.
Tissue: Colon.
[5]"Solution structure of three ZF-C2H2 domains from mouse protein odd-skipped-related 2 splicing isoform 2."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 162-252 IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF370121 mRNA. Translation: AAL07364.1.
AY038074 mRNA. Translation: AAK74068.1.
AK052147 mRNA. Translation: BAC34859.1.
BC013504 mRNA. Translation: AAH13504.1.
CCDSCCDS27422.1. [Q91ZD1-2]
RefSeqNP_473390.1. NM_054049.2. [Q91ZD1-2]
XP_006520076.1. XM_006520013.1. [Q91ZD1-1]
UniGeneMm.46336.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EE8NMR-A162-252[»]
ProteinModelPortalQ91ZD1.
SMRQ91ZD1. Positions 163-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91ZD1. 2 interactions.

Proteomic databases

PRIDEQ91ZD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022952; ENSMUSP00000022952; ENSMUSG00000022330. [Q91ZD1-2]
GeneID107587.
KEGGmmu:107587.
UCSCuc007vma.1. mouse. [Q91ZD1-2]
uc007vmb.1. mouse. [Q91ZD1-1]

Organism-specific databases

CTD116039.
MGIMGI:1930813. Osr2.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00750000117413.
HOGENOMHOG000013107.
HOVERGENHBG054398.
InParanoidQ91ZD1.
KOK09215.
OMAKTLHMQT.
OrthoDBEOG754HQ2.
PhylomeDBQ91ZD1.
TreeFamTF350876.

Gene expression databases

BgeeQ91ZD1.
CleanExMM_OSR2.
GenevestigatorQ91ZD1.

Family and domain databases

Gene3D3.30.160.60. 5 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 2 hits.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ91ZD1.
NextBio359096.
PROQ91ZD1.
SOURCESearch...

Entry information

Entry nameOSR2_MOUSE
AccessionPrimary (citable) accession number: Q91ZD1
Secondary accession number(s): Q8BPV6, Q91V54
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot