RIPP1_HUMAN
ID RIPP1_HUMAN Reviewed; 151 AA.
AC Q0D2K3; A0JP63; Q0VGB3; Q5JRB8; Q5JRB9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein ripply1;
GN Name=RIPPLY1 {ECO:0000312|HGNC:HGNC:25117};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000312|EMBL:CAI40160.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2] {ECO:0000312|EMBL:EAX02733.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI05692.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP IDENTIFICATION AS RIPPLY1.
RX PubMed=16326386; DOI=10.1016/j.devcel.2005.09.021;
RA Kawamura A., Koshida S., Hijikata H., Ohbayashi A., Kondoh H., Takada S.;
RT "Groucho-associated transcriptional repressor ripply1 is required for
RT proper transition from the presomitic mesoderm to somites.";
RL Dev. Cell 9:735-744(2005).
CC -!- FUNCTION: Plays a role in somitogenesis. Essential for transcriptional
CC repression of the segmental patterning genes, thus terminating the
CC segmentation program in the presomitic mesoderm, and also required for
CC the maintenance of rostrocaudal polarity in somites (By similarity).
CC {ECO:0000250|UniProtKB:Q2WG80}.
CC -!- INTERACTION:
CC Q0D2K3; Q5T686: AVPI1; NbExp=3; IntAct=EBI-10226430, EBI-8640233;
CC Q0D2K3; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-10226430, EBI-10181188;
CC Q0D2K3; Q5T655: CFAP58; NbExp=3; IntAct=EBI-10226430, EBI-10245749;
CC Q0D2K3; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-10226430, EBI-11962928;
CC Q0D2K3; Q66K64: DCAF15; NbExp=3; IntAct=EBI-10226430, EBI-2559052;
CC Q0D2K3; Q96HU8: DIRAS2; NbExp=3; IntAct=EBI-10226430, EBI-911391;
CC Q0D2K3; Q14192: FHL2; NbExp=3; IntAct=EBI-10226430, EBI-701903;
CC Q0D2K3; Q8TC17: GRAPL; NbExp=3; IntAct=EBI-10226430, EBI-18300553;
CC Q0D2K3; Q8TE85-2: GRHL3; NbExp=3; IntAct=EBI-10226430, EBI-12827521;
CC Q0D2K3; Q16695: H3-4; NbExp=3; IntAct=EBI-10226430, EBI-358900;
CC Q0D2K3; P61296-2: HAND2; NbExp=3; IntAct=EBI-10226430, EBI-13086076;
CC Q0D2K3; Q8WUI4-5: HDAC7; NbExp=3; IntAct=EBI-10226430, EBI-10276431;
CC Q0D2K3; Q8WUI4-6: HDAC7; NbExp=6; IntAct=EBI-10226430, EBI-12094670;
CC Q0D2K3; Q5VVH5: IRAK1BP1; NbExp=3; IntAct=EBI-10226430, EBI-9658404;
CC Q0D2K3; O76011: KRT34; NbExp=3; IntAct=EBI-10226430, EBI-1047093;
CC Q0D2K3; P59942: MCCD1; NbExp=3; IntAct=EBI-10226430, EBI-11987923;
CC Q0D2K3; Q99750: MDFI; NbExp=6; IntAct=EBI-10226430, EBI-724076;
CC Q0D2K3; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-10226430, EBI-13288755;
CC Q0D2K3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10226430, EBI-16439278;
CC Q0D2K3; P17568: NDUFB7; NbExp=3; IntAct=EBI-10226430, EBI-1246238;
CC Q0D2K3; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-10226430, EBI-11022007;
CC Q0D2K3; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-10226430, EBI-10302990;
CC Q0D2K3; Q99471: PFDN5; NbExp=3; IntAct=EBI-10226430, EBI-357275;
CC Q0D2K3; Q9UPG8: PLAGL2; NbExp=5; IntAct=EBI-10226430, EBI-2876622;
CC Q0D2K3; P86480: PRR20D; NbExp=3; IntAct=EBI-10226430, EBI-12754095;
CC Q0D2K3; Q9NZH5-2: PTTG2; NbExp=3; IntAct=EBI-10226430, EBI-17630019;
CC Q0D2K3; Q93062: RBPMS; NbExp=3; IntAct=EBI-10226430, EBI-740322;
CC Q0D2K3; Q04864: REL; NbExp=3; IntAct=EBI-10226430, EBI-307352;
CC Q0D2K3; Q15669: RHOH; NbExp=3; IntAct=EBI-10226430, EBI-1244971;
CC Q0D2K3; Q5SSQ6-2: SAPCD1; NbExp=3; IntAct=EBI-10226430, EBI-13072754;
CC Q0D2K3; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-10226430, EBI-741515;
CC Q0D2K3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10226430, EBI-11741437;
CC Q0D2K3; Q13077: TRAF1; NbExp=3; IntAct=EBI-10226430, EBI-359224;
CC Q0D2K3; Q12933: TRAF2; NbExp=6; IntAct=EBI-10226430, EBI-355744;
CC Q0D2K3; Q13114: TRAF3; NbExp=3; IntAct=EBI-10226430, EBI-357631;
CC Q0D2K3; Q08AM6: VAC14; NbExp=3; IntAct=EBI-10226430, EBI-2107455;
CC Q0D2K3; Q99990: VGLL1; NbExp=3; IntAct=EBI-10226430, EBI-11983165;
CC Q0D2K3; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-10226430, EBI-12030590;
CC Q0D2K3; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10226430, EBI-4395669;
CC Q0D2K3; Q8NCA9: ZNF784; NbExp=3; IntAct=EBI-10226430, EBI-7138303;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2WG80}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15772651};
CC IsoId=Q0D2K3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15772651};
CC IsoId=Q0D2K3-2; Sequence=VSP_052555;
CC -!- DOMAIN: The ripply homology domain is required for transcriptional
CC repression. {ECO:0000250}.
CC -!- DOMAIN: The WRPW motif is required for binding to TLE/GROUCHO proteins.
CC {ECO:0000250|UniProtKB:Q2WG80}.
CC -!- SIMILARITY: Belongs to the ripply family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10437.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAI40159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI40160.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL591849; CAI40159.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL591849; CAI40160.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471120; EAX02733.1; -; Genomic_DNA.
DR EMBL; BC105691; AAI05692.1; -; mRNA.
DR EMBL; BC105692; AAI05693.1; -; mRNA.
DR EMBL; BC110436; AAI10437.1; ALT_SEQ; mRNA.
DR EMBL; BC127250; AAI27251.1; -; mRNA.
DR CCDS; CCDS48145.1; -. [Q0D2K3-1]
DR CCDS; CCDS55471.1; -. [Q0D2K3-2]
DR RefSeq; NP_001165177.1; NM_001171706.1. [Q0D2K3-2]
DR RefSeq; NP_612391.1; NM_138382.2. [Q0D2K3-1]
DR AlphaFoldDB; Q0D2K3; -.
DR BioGRID; 124912; 56.
DR IntAct; Q0D2K3; 44.
DR STRING; 9606.ENSP00000276173; -.
DR PhosphoSitePlus; Q0D2K3; -.
DR BioMuta; RIPPLY1; -.
DR MassIVE; Q0D2K3; -.
DR PaxDb; Q0D2K3; -.
DR PeptideAtlas; Q0D2K3; -.
DR PRIDE; Q0D2K3; -.
DR Antibodypedia; 63924; 12 antibodies from 8 providers.
DR DNASU; 92129; -.
DR Ensembl; ENST00000276173.5; ENSP00000276173.4; ENSG00000147223.6. [Q0D2K3-1]
DR Ensembl; ENST00000411805.1; ENSP00000400539.1; ENSG00000147223.6. [Q0D2K3-2]
DR GeneID; 92129; -.
DR KEGG; hsa:92129; -.
DR MANE-Select; ENST00000276173.5; ENSP00000276173.4; NM_138382.3; NP_612391.1.
DR UCSC; uc004emr.3; human. [Q0D2K3-1]
DR CTD; 92129; -.
DR DisGeNET; 92129; -.
DR GeneCards; RIPPLY1; -.
DR HGNC; HGNC:25117; RIPPLY1.
DR HPA; ENSG00000147223; Group enriched (kidney, liver).
DR MIM; 300575; gene.
DR neXtProt; NX_Q0D2K3; -.
DR OpenTargets; ENSG00000147223; -.
DR PharmGKB; PA162401348; -.
DR VEuPathDB; HostDB:ENSG00000147223; -.
DR eggNOG; ENOG502S6U6; Eukaryota.
DR GeneTree; ENSGT00940000161952; -.
DR HOGENOM; CLU_117697_0_0_1; -.
DR InParanoid; Q0D2K3; -.
DR OMA; ADSEFHH; -.
DR PhylomeDB; Q0D2K3; -.
DR TreeFam; TF336045; -.
DR PathwayCommons; Q0D2K3; -.
DR SignaLink; Q0D2K3; -.
DR BioGRID-ORCS; 92129; 15 hits in 697 CRISPR screens.
DR GenomeRNAi; 92129; -.
DR Pharos; Q0D2K3; Tdark.
DR PRO; PR:Q0D2K3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q0D2K3; protein.
DR Bgee; ENSG00000147223; Expressed in right lobe of liver and 63 other tissues.
DR Genevisible; Q0D2K3; HS.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0032525; P:somite rostral/caudal axis specification; ISS:UniProtKB.
DR GO; GO:0001757; P:somite specification; ISS:UniProtKB.
DR InterPro; IPR028127; Ripply_fam.
DR PANTHER; PTHR16770; PTHR16770; 1.
DR Pfam; PF14998; Ripply; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..151
FT /note="Protein ripply1"
FT /id="PRO_0000307756"
FT REGION 96..131
FT /note="Ripply homology domain"
FT /evidence="ECO:0000255"
FT REGION 130..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..60
FT /note="WRPW motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 132..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 53..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15772651"
FT /id="VSP_052555"
SQ SEQUENCE 151 AA; 16379 MW; 201C7BA5C5C8025F CRC64;
MDSAACAAAA TPVPALALAL APDLAQAPLA LPGLLSPSCL LSSGQEVNGS ERGTCLWRPW
LSSTNDSPRQ MRKLVDLAAG GATAAEVTKA ESKFHHPVRL FWPKSRSFDY LYSAGEILLQ
NFPVQATINL YEDSDSEEEE EDEEQEDEEE K
