Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein ripply1

Gene

RIPPLY1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in somitogenesis. Essential for transcriptional repression of the segmental patterning genes, thus terminating the segmentation program in the presomitic mesoderm, and also required for the maintenance of rostrocaudal polarity in somites (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ripply1
Gene namesi
Name:RIPPLY1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:25117. RIPPLY1.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401348.

Polymorphism and mutation databases

BioMutaiRIPPLY1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151Protein ripply1PRO_0000307756Add
BLAST

Proteomic databases

PaxDbiQ0D2K3.
PRIDEiQ0D2K3.

PTM databases

PhosphoSiteiQ0D2K3.

Expressioni

Gene expression databases

BgeeiQ0D2K3.
CleanExiHS_RIPPLY1.
GenevisibleiQ0D2K3. HS.

Organism-specific databases

HPAiHPA052284.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC7Q8WUI4-53EBI-10226430,EBI-10276431
MDFIQ997503EBI-10226430,EBI-724076
RBPMSQ930623EBI-10226430,EBI-740322
RELQ048643EBI-10226430,EBI-307352
THAP1Q9NVV93EBI-10226430,EBI-741515
TRAF2Q129333EBI-10226430,EBI-355744

Protein-protein interaction databases

BioGridi124912. 12 interactions.
IntActiQ0D2K3. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ0D2K3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 13136Ripply homology domainSequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 604WRPW motifSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 107Poly-AlaSequence analysis
Compositional biasi137 – 15014Poly-GluSequence analysisAdd
BLAST

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

eggNOGiENOG410J6ZC. Eukaryota.
ENOG4112884. LUCA.
GeneTreeiENSGT00390000008909.
HOGENOMiHOG000154131.
HOVERGENiHBG098215.
InParanoidiQ0D2K3.
OMAiERGTCLW.
OrthoDBiEOG7JT70D.
PhylomeDBiQ0D2K3.
TreeFamiTF336045.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 12 Publications (identifier: Q0D2K3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDSAACAAAA TPVPALALAL APDLAQAPLA LPGLLSPSCL LSSGQEVNGS
60 70 80 90 100
ERGTCLWRPW LSSTNDSPRQ MRKLVDLAAG GATAAEVTKA ESKFHHPVRL
110 120 130 140 150
FWPKSRSFDY LYSAGEILLQ NFPVQATINL YEDSDSEEEE EDEEQEDEEE

K
Note: No experimental confirmation available.Curated
Length:151
Mass (Da):16,379
Last modified:October 17, 2006 - v1
Checksum:i201C7BA5C5C8025F
GO
Isoform 22 Publications (identifier: Q0D2K3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-99: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:104
Mass (Da):11,219
Checksum:iCFDC92C64319535F
GO

Sequence cautioni

The sequence AAI10437.1 differs from that shown.Intron retention.Curated
The sequence CAI40159.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI40160.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 9947Missing in isoform 2. 2 PublicationsVSP_052555Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591849 Genomic DNA. Translation: CAI40159.1. Different initiation.
AL591849 Genomic DNA. Translation: CAI40160.1. Different initiation.
CH471120 Genomic DNA. Translation: EAX02733.1.
BC105691 mRNA. Translation: AAI05692.1.
BC105692 mRNA. Translation: AAI05693.1.
BC110436 mRNA. Translation: AAI10437.1. Sequence problems.
BC127250 mRNA. Translation: AAI27251.1.
CCDSiCCDS48145.1. [Q0D2K3-1]
CCDS55471.1. [Q0D2K3-2]
RefSeqiNP_001165177.1. NM_001171706.1. [Q0D2K3-2]
NP_612391.1. NM_138382.2. [Q0D2K3-1]
UniGeneiHs.334726.

Genome annotation databases

EnsembliENST00000276173; ENSP00000276173; ENSG00000147223. [Q0D2K3-1]
ENST00000411805; ENSP00000400539; ENSG00000147223. [Q0D2K3-2]
GeneIDi92129.
KEGGihsa:92129.
UCSCiuc004emr.3. human. [Q0D2K3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591849 Genomic DNA. Translation: CAI40159.1. Different initiation.
AL591849 Genomic DNA. Translation: CAI40160.1. Different initiation.
CH471120 Genomic DNA. Translation: EAX02733.1.
BC105691 mRNA. Translation: AAI05692.1.
BC105692 mRNA. Translation: AAI05693.1.
BC110436 mRNA. Translation: AAI10437.1. Sequence problems.
BC127250 mRNA. Translation: AAI27251.1.
CCDSiCCDS48145.1. [Q0D2K3-1]
CCDS55471.1. [Q0D2K3-2]
RefSeqiNP_001165177.1. NM_001171706.1. [Q0D2K3-2]
NP_612391.1. NM_138382.2. [Q0D2K3-1]
UniGeneiHs.334726.

3D structure databases

ProteinModelPortaliQ0D2K3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124912. 12 interactions.
IntActiQ0D2K3. 6 interactions.

PTM databases

PhosphoSiteiQ0D2K3.

Polymorphism and mutation databases

BioMutaiRIPPLY1.

Proteomic databases

PaxDbiQ0D2K3.
PRIDEiQ0D2K3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276173; ENSP00000276173; ENSG00000147223. [Q0D2K3-1]
ENST00000411805; ENSP00000400539; ENSG00000147223. [Q0D2K3-2]
GeneIDi92129.
KEGGihsa:92129.
UCSCiuc004emr.3. human. [Q0D2K3-1]

Organism-specific databases

CTDi92129.
GeneCardsiRIPPLY1.
H-InvDBHIX0056217.
HGNCiHGNC:25117. RIPPLY1.
HPAiHPA052284.
MIMi300575. gene.
neXtProtiNX_Q0D2K3.
PharmGKBiPA162401348.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J6ZC. Eukaryota.
ENOG4112884. LUCA.
GeneTreeiENSGT00390000008909.
HOGENOMiHOG000154131.
HOVERGENiHBG098215.
InParanoidiQ0D2K3.
OMAiERGTCLW.
OrthoDBiEOG7JT70D.
PhylomeDBiQ0D2K3.
TreeFamiTF336045.

Miscellaneous databases

GenomeRNAii92129.
PROiQ0D2K3.
SOURCEiSearch...

Gene expression databases

BgeeiQ0D2K3.
CleanExiHS_RIPPLY1.
GenevisibleiQ0D2K3. HS.

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. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 1 AND 2).
  4. "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: IDENTIFICATION AS RIPPLY1.

Entry informationi

Entry nameiRIPP1_HUMAN
AccessioniPrimary (citable) accession number: Q0D2K3
Secondary accession number(s): A0JP63
, Q0VGB3, Q5JRB8, Q5JRB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 17, 2006
Last modified: June 8, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.