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Protein

Protein ripply2

Gene

Ripply2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a role in somitogenesis. Required for somite segregation and establishment of rostrocaudal polarity in somites.2 Publications

GO - Biological processi

  • axis specification Source: MGI
  • bone morphogenesis Source: MGI
  • determination of left/right symmetry Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • Notch signaling pathway Source: MGI
  • ossification Source: MGI
  • post-anal tail morphogenesis Source: MGI
  • regulation of gene expression Source: MGI
  • somite rostral/caudal axis specification Source: UniProtKB
  • somitogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ripply2
Gene namesi
Name:Ripply2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2685968. Ripply2.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128128Protein ripply2PRO_0000307760Add
BLAST

Proteomic databases

PaxDbiQ2WG76.
PRIDEiQ2WG76.

Expressioni

Tissue specificityi

Expressed in the embryonic anterior presomitic mesoderm. First expressed in S-I at E8.5, where expression is maintained until E13.5, with an additional stripe of expression sometimes seen in the rostral part of S0 and S-I.2 Publications

Inductioni

By MESP2, and acts in a negative feedback loop with MESP2, functioning negatively toward MESP2 to regulate NOTCH signaling in the anterior presomitic mesoderm.1 Publication

Gene expression databases

BgeeiQ2WG76.
CleanExiMM_RIPPLY2.
ExpressionAtlasiQ2WG76. baseline and differential.
GenevisibleiQ2WG76. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055369.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 10936Ripply homology domainSequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 374WRPW motifSequence analysis

Domaini

The ripply homology domain is required for transcriptional repression.By similarity
The WRPW motif is required for binding to tle/groucho proteins.By similarity

Sequence similaritiesi

Belongs to the ripply family.Curated

Phylogenomic databases

eggNOGiENOG410J290. Eukaryota.
ENOG4112884. LUCA.
GeneTreeiENSGT00390000008909.
HOGENOMiHOG000063681.
HOVERGENiHBG095612.
InParanoidiQ2WG76.
OMAiMPDGPGM.
OrthoDBiEOG7JT70D.
PhylomeDBiQ2WG76.
TreeFamiTF336045.

Family and domain databases

InterProiIPR028127. Ripply_fam.
[Graphical view]
PANTHERiPTHR16770. PTHR16770. 1 hit.
PfamiPF14998. Ripply. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2WG76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTTESAESA HNPARPPSRS RCPPSAQPGS EGFWRPWVRT PGEKEKRTGP
60 70 80 90 100
RAAEALPSGP GMAEASGKLL QYQHPVRLFW PKSKCYDYLY QEAETLLKNF
110 120
PIQATISFYE DSDSEDEIEG LACENQSN
Length:128
Mass (Da):14,305
Last modified:January 10, 2006 - v1
Checksum:i4B9FFB58B5499506
GO

Sequence cautioni

The sequence BAC38162.1 differs from that shown.Intron retention.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB212223 mRNA. Translation: BAE53720.1.
AK081203 mRNA. Translation: BAC38162.1. Sequence problems.
CCDSiCCDS40715.1.
RefSeqiNP_001032996.1. NM_001037907.1.
UniGeneiMm.92244.

Genome annotation databases

EnsembliENSMUST00000058846; ENSMUSP00000055369; ENSMUSG00000047897.
GeneIDi382089.
KEGGimmu:382089.
UCSCiuc009qya.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB212223 mRNA. Translation: BAE53720.1.
AK081203 mRNA. Translation: BAC38162.1. Sequence problems.
CCDSiCCDS40715.1.
RefSeqiNP_001032996.1. NM_001037907.1.
UniGeneiMm.92244.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055369.

Proteomic databases

PaxDbiQ2WG76.
PRIDEiQ2WG76.

Protocols and materials databases

DNASUi382089.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058846; ENSMUSP00000055369; ENSMUSG00000047897.
GeneIDi382089.
KEGGimmu:382089.
UCSCiuc009qya.1. mouse.

Organism-specific databases

CTDi134701.
MGIiMGI:2685968. Ripply2.

Phylogenomic databases

eggNOGiENOG410J290. Eukaryota.
ENOG4112884. LUCA.
GeneTreeiENSGT00390000008909.
HOGENOMiHOG000063681.
HOVERGENiHBG095612.
InParanoidiQ2WG76.
OMAiMPDGPGM.
OrthoDBiEOG7JT70D.
PhylomeDBiQ2WG76.
TreeFamiTF336045.

Miscellaneous databases

PROiQ2WG76.
SOURCEiSearch...

Gene expression databases

BgeeiQ2WG76.
CleanExiMM_RIPPLY2.
ExpressionAtlasiQ2WG76. baseline and differential.
GenevisibleiQ2WG76. MM.

Family and domain databases

InterProiIPR028127. Ripply_fam.
[Graphical view]
PANTHERiPTHR16770. PTHR16770. 1 hit.
PfamiPF14998. Ripply. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Groucho-associated transcriptional repressor ripply1 is required for proper transition from the presomitic mesoderm to somites."
    Kawamura A., Koshida S., Hijikata H., Ohbayashi A., Kondoh H., Takada S.
    Dev. Cell 9:735-744(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Embryo1 Publication.
  2. "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] OF 30-128.
    Strain: C57BL/6JImported.
    Tissue: Corpus striatumImported.
  3. "Ripply2 is essential for precise somite formation during mouse early development."
    Chan T., Kondow A., Hosoya A., Hitachi K., Yukita A., Okabayashi K., Nakamura H., Ozawa H., Kiyonari H., Michiue T., Ito Y., Asashima M.
    FEBS Lett. 581:2691-2696(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  4. "The negative regulation of Mesp2 by mouse Ripply2 is required to establish the rostro-caudal patterning within a somite."
    Morimoto M., Sasaki N., Oginuma M., Kiso M., Igarashi K., Aizaki K., Kanno J., Saga Y.
    Development 134:1561-1569(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiRIPP2_MOUSE
AccessioniPrimary (citable) accession number: Q2WG76
Secondary accession number(s): Q8BNN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: January 10, 2006
Last modified: July 6, 2016
This is version 60 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. 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.