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Protein

Cell differentiation protein RCD1 homolog

Gene

Rqcd1

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

Functioni

Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down-regulation of MYB- and JUN-dependent transcription. May play a role in cell differentiation. Required for retinoic acid-induced differentiation of F9 teratocarcinoma cells. Does not bind DNA by itself. Enhances ligand-dependent transcriptional activity of nuclear hormone receptors. May play a role in cell differentiation.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

RNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation

Enzyme and pathway databases

ReactomeiR-MMU-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell differentiation protein RCD1 homolog
Short name:
Rcd-1
Alternative name(s):
CCR4-NOT transcription complex subunit 9
EPO-induced protein FL10
Gene namesi
Name:Rqcd1
Synonyms:Cnot9, Rcd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1928902. Rqcd1.

Subcellular locationi

GO - Cellular componenti

  • CCR4-NOT complex Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • membrane Source: MGI
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Cell differentiation protein RCD1 homologPRO_0000327227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9JKY0.
MaxQBiQ9JKY0.
PaxDbiQ9JKY0.
PRIDEiQ9JKY0.

PTM databases

PhosphoSiteiQ9JKY0.

Expressioni

Tissue specificityi

Detected at low levels in bone marrow and thymus.1 Publication

Inductioni

Up-regulated by EPO and EGF. Transiently up-regulated by retinoic acid in F9 teratocarcinoma cells.3 Publications

Gene expression databases

BgeeiQ9JKY0.
GenevisibleiQ9JKY0. MM.

Interactioni

Subunit structurei

Homodimer. Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. Interacts with MYB, ATF2, RARA, RARB, RARG, RXRA, RXRB and RXRG. Identified in a complex with ATF2 bound to target DNA. Interacts with NANOS2. Directly interacts with ZNF335 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208377. 1 interaction.
DIPiDIP-34266N.
IntActiQ9JKY0. 7 interactions.
MINTiMINT-4618615.
STRINGi10090.ENSMUSP00000084466.

Structurei

3D structure databases

ProteinModelPortaliQ9JKY0.
SMRiQ9JKY0. Positions 16-284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RCD1 family.Curated

Phylogenomic databases

eggNOGiKOG3036. Eukaryota.
COG5209. LUCA.
GeneTreeiENSGT00390000001225.
HOGENOMiHOG000192069.
HOVERGENiHBG056785.
InParanoidiQ9JKY0.
KOiK12606.
OMAiMLWHSCG.
OrthoDBiEOG7M98GN.
PhylomeDBiQ9JKY0.
TreeFamiTF105734.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR007216. Rcd1/Caf40.
[Graphical view]
PANTHERiPTHR12262. PTHR12262. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9JKY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSLATAAPV PTALAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP
60 70 80 90 100
DLAPMLWHSF GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV
110 120 130 140 150
ASHPETRSAF LAAHIPLFLY PFLHTVSKTR PFEYLRLTSL GVIGALVKTD
160 170 180 190 200
EQEVINFLLT TEIIPLCLRI MESGSELSKT VATFILQKIL LDDTGLAYIC
210 220 230 240 250
QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS DNPRAREALR
260 270 280 290
QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ
Length:299
Mass (Da):33,601
Last modified:October 1, 2000 - v1
Checksum:iA4CA5DBE2E88DDA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221849 mRNA. Translation: AAF61701.1.
AK005025 mRNA. Translation: BAB23752.1.
BC050898 mRNA. Translation: AAH50898.1.
BC051948 mRNA. Translation: AAH51948.1.
CCDSiCCDS35615.1.
RefSeqiNP_067358.1. NM_021383.5.
UniGeneiMm.291708.

Genome annotation databases

EnsembliENSMUST00000087215; ENSMUSP00000084466; ENSMUSG00000026174.
GeneIDi58184.
KEGGimmu:58184.
UCSCiuc007bmf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221849 mRNA. Translation: AAF61701.1.
AK005025 mRNA. Translation: BAB23752.1.
BC050898 mRNA. Translation: AAH50898.1.
BC051948 mRNA. Translation: AAH51948.1.
CCDSiCCDS35615.1.
RefSeqiNP_067358.1. NM_021383.5.
UniGeneiMm.291708.

3D structure databases

ProteinModelPortaliQ9JKY0.
SMRiQ9JKY0. Positions 16-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208377. 1 interaction.
DIPiDIP-34266N.
IntActiQ9JKY0. 7 interactions.
MINTiMINT-4618615.
STRINGi10090.ENSMUSP00000084466.

PTM databases

PhosphoSiteiQ9JKY0.

Proteomic databases

EPDiQ9JKY0.
MaxQBiQ9JKY0.
PaxDbiQ9JKY0.
PRIDEiQ9JKY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087215; ENSMUSP00000084466; ENSMUSG00000026174.
GeneIDi58184.
KEGGimmu:58184.
UCSCiuc007bmf.2. mouse.

Organism-specific databases

CTDi9125.
MGIiMGI:1928902. Rqcd1.

Phylogenomic databases

eggNOGiKOG3036. Eukaryota.
COG5209. LUCA.
GeneTreeiENSGT00390000001225.
HOGENOMiHOG000192069.
HOVERGENiHBG056785.
InParanoidiQ9JKY0.
KOiK12606.
OMAiMLWHSCG.
OrthoDBiEOG7M98GN.
PhylomeDBiQ9JKY0.
TreeFamiTF105734.

Enzyme and pathway databases

ReactomeiR-MMU-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.

Miscellaneous databases

PROiQ9JKY0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JKY0.
GenevisibleiQ9JKY0. MM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR007216. Rcd1/Caf40.
[Graphical view]
PANTHERiPTHR12262. PTHR12262. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Subtraction cloning and initial characterization of novel EPO-immediate response genes."
    Gregory R.C. Jr., Lord K.A., Panek L.B., Gaines P., Dillon S.B., Wojchowski D.M.
    Cytokine 12:845-857(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Tissue: Erythroleukemia.
  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].
    Strain: C57BL/6J.
    Tissue: Liver.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Mammalian Rcd1 is a novel transcriptional cofactor that mediates retinoic acid-induced cell differentiation."
    Hiroi N., Ito T., Yamamoto H., Ochiya T., Jinno S., Okayama H.
    EMBO J. 21:5235-5244(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, IDENTIFICATION IN A COMPLEX WITH ATF2 BOUND TO TARGET DNA, INTERACTION WITH ATF2; RARA; RARB; RARG; RXRA; RXRB AND RXRG.
  5. "c-Myb protein interacts with Rcd-1, a component of the CCR4 transcription mediator complex."
    Haas M., Siegert M., Schuermann A., Sodeik B., Wolfes H.
    Biochemistry 43:8152-8159(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYB, INDUCTION, SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to suppression of specific RNAs."
    Suzuki A., Igarashi K., Aisaki K., Kanno J., Saga Y.
    Proc. Natl. Acad. Sci. U.S.A. 107:3594-3599(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NANOS2.

Entry informationi

Entry nameiRCD1_MOUSE
AccessioniPrimary (citable) accession number: Q9JKY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 126 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.