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Q9ERU3 (ZNF22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein 22
Alternative name(s):
Zinc finger protein 422
Zinc finger protein Krox-25
Zinc finger protein Krox-26
Gene names
Name:Znf22
Synonyms:Krox25, Krox26, Zfp422
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds DNA through the consensus sequence 5'-CAATG-3'. May be involved in transcriptional regulation and may play a role in tooth formation. Ref.2 Ref.5

Subcellular location

Nucleus By similarity UniProtKB Q9ERU2.

Tissue specificity

Expressed predominantly in developing craniofacial bones and dental organs, and in molar tooth germs of postnatal animals. Also detected in embryonic heart, liver, thymus, kidney, brain, lung, muscle and calvaria. In the adult, highly expressed in lung, kidney, bone and incisors. Ref.1 Ref.2 Ref.5

Developmental stage

In the embryo, expression is detected from day 7 with highest levels between days 11 and 15. Ref.2 Ref.5

Sequence similarities

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

Contains 5 C2H2-type zinc fingers.

Sequence caution

The sequence AAG12466.1 differs from that shown. Reason: Frameshift at position 224.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237Zinc finger protein 22
PRO_0000047349

Regions

Zinc finger55 – 7723C2H2-type 1
Zinc finger83 – 10523C2H2-type 2
Zinc finger111 – 13323C2H2-type 3
Zinc finger139 – 16123C2H2-type 4
Zinc finger167 – 18923C2H2-type 5

Amino acid modifications

Modified residue181N6-acetyllysine Ref.6
Modified residue231N6-acetyllysine Ref.6

Experimental info

Sequence conflict1921K → N in AAG12466. Ref.1
Sequence conflict2161R → K Ref.1
Sequence conflict2161R → K Ref.2
Sequence conflict2241Q → R Ref.1
Sequence conflict2241Q → R Ref.2
Sequence conflict225 – 23713Missing Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9ERU3 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 1653220411F3C7DD

FASTA23727,294
        10         20         30         40         50         60 
MRLGKPKGGI SRSASQGKAY ESKRKTARQR QKWGVAIRFD SGLSRRRRNV DEKPYKCAKC 

        70         80         90        100        110        120 
SKSFSQSSTL FQHKKIHTGK KSHKCADCGK SFFQSSNLIQ HRRIHTGEKP YKCDECGERF 

       130        140        150        160        170        180 
KQSSNLIQHQ RIHTGEKPYC CDECGRCFSQ SSHLIQHQRT HTGEKPYQCE ECDKCFSQSS 

       190        200        210        220        230 
HLRQHMKVHK EKKPHKRGKN ARVKTHPVSW KRGKGRKAVA GIRQVKGATS GLFKKKK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, chromosomal mapping, and characteristic expression in tooth organ of rat and mouse Krox-25."
Lee S.K., Kim Y.S., Lee S.S., Lee Y.J., Song I.S., Park S.C., Kozak C., Yamada Y.
Genomics 83:243-253(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Craniofacial.
[2]"Krox-26 is a novel C2H2 zinc finger transcription factor expressed in developing dental and osteogenic tissues."
Ganss B., Teo W., Chen H., Poon T.
Connect. Tissue Res. 43:161-166(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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].
Strain: C57BL/6J.
Tissue: Kidney and Spinal cord.
[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: Mammary gland.
[5]"Developmental expression pattern and DNA-binding properties of the zinc finger transcription factor Krox-26."
Teo W., Chen H., Poon T., Ganss B.
Connect. Tissue Res. 44:161-166(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18 AND LYS-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF281634 mRNA. Translation: AAG12466.1. Frameshift.
AK082970 mRNA. Translation: BAC38716.1.
AK169251 mRNA. Translation: BAE41015.1.
BC018339 mRNA. Translation: AAH18339.1.
CCDSCCDS20459.1.
RefSeqNP_080333.1. NM_026057.2.
XP_006506566.1. XM_006506503.1.
XP_006506567.1. XM_006506504.1.
UniGeneMm.18810.

3D structure databases

ProteinModelPortalQ9ERU3.
SMRQ9ERU3. Positions 24-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9ERU3. 1 interaction.
MINTMINT-4140652.

PTM databases

PhosphoSiteQ9ERU3.

Proteomic databases

PaxDbQ9ERU3.
PRIDEQ9ERU3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057540; ENSMUSP00000084926; ENSMUSG00000059878.
ENSMUST00000079749; ENSMUSP00000078685; ENSMUSG00000059878.
ENSMUST00000112880; ENSMUSP00000108501; ENSMUSG00000059878.
GeneID67255.
KEGGmmu:67255.
UCSCuc009dkj.1. mouse.

Organism-specific databases

CTD67255.
MGIMGI:1914505. Zfp422.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00740000115574.
HOGENOMHOG000234617.
HOVERGENHBG018163.
InParanoidQ9ERU3.
OMATHLVSSW.
OrthoDBEOG7QG44V.
PhylomeDBQ9ERU3.
TreeFamTF350836.

Gene expression databases

BgeeQ9ERU3.
CleanExMM_ZFP422.
GenevestigatorQ9ERU3.

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. 1 hit.
[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

NextBio324022.
PROQ9ERU3.
SOURCESearch...

Entry information

Entry nameZNF22_MOUSE
AccessionPrimary (citable) accession number: Q9ERU3
Secondary accession number(s): Q3TF83, Q8VEK7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: July 9, 2014
This is version 103 of the entry and version 2 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

MGD cross-references

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