RCCD1_HUMAN
ID RCCD1_HUMAN Reviewed; 376 AA.
AC A6NED2; B2RTP9; Q29RX6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=RCC1 domain-containing protein 1;
GN Name=RCCD1 {ECO:0000303|PubMed:29563586, ECO:0000312|HGNC:HGNC:30457};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH KDM8, INTERACTION WITH KDM8,
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND CAUTION.
RX PubMed=24981860; DOI=10.1016/j.celrep.2014.05.050;
RA Marcon E., Ni Z., Pu S., Turinsky A.L., Trimble S.S., Olsen J.B.,
RA Silverman-Gavrila R., Silverman-Gavrila L., Phanse S., Guo H., Zhong G.,
RA Guo X., Young P., Bailey S., Roudeva D., Zhao D., Hewel J., Li J.,
RA Graeslund S., Paduch M., Kossiakoff A.A., Lupien M., Emili A., Wodak S.J.,
RA Greenblatt J.;
RT "Human-chromatin-related protein interactions identify a demethylase
RT complex required for chromosome segregation.";
RL Cell Rep. 8:297-310(2014).
RN [6]
RP FUNCTION, AND INTERACTION WITH KDM8.
RX PubMed=28455245; DOI=10.1016/j.canlet.2017.04.021;
RA Wu J., He Z., Yang X.M., Li K.L., Wang D.L., Sun F.L.;
RT "RCCD1 depletion attenuates TGF-beta-induced EMT and cell migration by
RT stabilizing cytoskeletal microtubules in NSCLC cells.";
RL Cancer Lett. 400:18-29(2017).
RN [7]
RP CAUTION.
RX PubMed=28982940; DOI=10.15252/embr.201743892;
RA Shen J., Xiang X., Chen L., Wang H., Wu L., Sun Y., Ma L., Gu X., Liu H.,
RA Wang L., Yu Y.N., Shao J., Huang C., Chin Y.E.;
RT "JMJD5 cleaves monomethylated histone H3 N-tail under DNA damaging
RT stress.";
RL EMBO Rep. 18:E201743892-E201743892(2017).
RN [8]
RP HYDROXYLATION AT ARG-141, AND MUTAGENESIS OF ARG-141.
RX PubMed=29563586; DOI=10.1038/s41467-018-03410-w;
RA Wilkins S.E., Islam S., Gannon J.M., Markolovic S., Hopkinson R.J., Ge W.,
RA Schofield C.J., Chowdhury R.;
RT "JMJD5 is a human L-arginyl C-3 hydroxylase.";
RL Nat. Commun. 9:1180-1180(2018).
CC -!- FUNCTION: Plays a role in transcriptional repression of satellite
CC repeats, possibly by regulating H3K36 methylation levels in centromeric
CC regions together with KDM8 (PubMed:24981860). Possibly together with
CC KDM8, is involved in proper mitotic spindle organization and chromosome
CC segregation (PubMed:24981860). Plays a role in regulating alpha-tubulin
CC deacetylation and cytoskeletal microtubule stability, thereby promoting
CC cell migration and TGF-beta-induced epithelial to mesenchymal
CC transition (EMT), potentially through the inhibition of KDM8
CC (PubMed:28455245). {ECO:0000269|PubMed:24981860,
CC ECO:0000269|PubMed:28455245}.
CC -!- SUBUNIT: Found in a complex with KDM8 (PubMed:24981860). Interacts (via
CC N-terminus) with KDM8 (via N-terminus)(PubMed:24981860,
CC PubMed:28455245). {ECO:0000269|PubMed:24981860,
CC ECO:0000269|PubMed:28455245}.
CC -!- INTERACTION:
CC A6NED2; Q8N371: KDM8; NbExp=2; IntAct=EBI-21552314, EBI-750326;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24981860}.
CC Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3).
CC {ECO:0000269|PubMed:24981860}.
CC -!- PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of ARG-
CC 141 by KDM8. {ECO:0000269|PubMed:29563586}.
CC -!- CAUTION: Postulated to regulate KDM8 histone demethylase activity on
CC di- and trimethylated 'Lys-36' (H3K36me2/me3) of histone H3
CC (PubMed:24981860). However the demethylase activity of JMJD5 is
CC controversial, as it was later shown to rather act as an endopeptidase
CC that cleaves monomethylated and dimethylated arginine residues of
CC histones H2, H3 and H4. In several studies, JMJD5 was shown not to
CC display any demethylase activity toward methylated H3K36 nor toward
CC other methyllysines in the N-terminal tails of H3 and H4 in vitro
CC (PubMed:28982940). {ECO:0000269|PubMed:24981860,
CC ECO:0000269|PubMed:28982940}.
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DR EMBL; AC068831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471101; EAX02130.1; -; Genomic_DNA.
DR EMBL; BC113826; AAI13827.1; -; mRNA.
DR EMBL; BC140708; AAI40709.1; -; mRNA.
DR EMBL; BC140709; AAI40710.1; -; mRNA.
DR CCDS; CCDS32333.1; -.
DR RefSeq; NP_001017919.1; NM_001017919.1.
DR RefSeq; NP_291022.2; NM_033544.2.
DR PDB; 6F4R; X-ray; 1.30 A; B=139-143.
DR PDB; 6F4S; X-ray; 1.46 A; B=139-143.
DR PDB; 6F4T; X-ray; 1.22 A; B=139-143.
DR PDBsum; 6F4R; -.
DR PDBsum; 6F4S; -.
DR PDBsum; 6F4T; -.
DR AlphaFoldDB; A6NED2; -.
DR SMR; A6NED2; -.
DR BioGRID; 124832; 89.
DR CORUM; A6NED2; -.
DR IntAct; A6NED2; 29.
DR MINT; A6NED2; -.
DR STRING; 9606.ENSP00000377801; -.
DR iPTMnet; A6NED2; -.
DR PhosphoSitePlus; A6NED2; -.
DR BioMuta; RCCD1; -.
DR EPD; A6NED2; -.
DR jPOST; A6NED2; -.
DR MassIVE; A6NED2; -.
DR MaxQB; A6NED2; -.
DR PaxDb; A6NED2; -.
DR PeptideAtlas; A6NED2; -.
DR PRIDE; A6NED2; -.
DR ProteomicsDB; 977; -.
DR Antibodypedia; 50047; 23 antibodies from 9 providers.
DR DNASU; 91433; -.
DR Ensembl; ENST00000394258.7; ENSP00000377801.2; ENSG00000166965.13.
DR Ensembl; ENST00000556618.1; ENSP00000451963.1; ENSG00000166965.13.
DR GeneID; 91433; -.
DR KEGG; hsa:91433; -.
DR MANE-Select; ENST00000394258.7; ENSP00000377801.2; NM_001017919.2; NP_001017919.1.
DR UCSC; uc002bqk.4; human.
DR CTD; 91433; -.
DR DisGeNET; 91433; -.
DR GeneCards; RCCD1; -.
DR HGNC; HGNC:30457; RCCD1.
DR HPA; ENSG00000166965; Low tissue specificity.
DR MIM; 617997; gene.
DR neXtProt; NX_A6NED2; -.
DR OpenTargets; ENSG00000166965; -.
DR PharmGKB; PA142671092; -.
DR VEuPathDB; HostDB:ENSG00000166965; -.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000162149; -.
DR InParanoid; A6NED2; -.
DR OMA; KTVTCGP; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; A6NED2; -.
DR TreeFam; TF329484; -.
DR PathwayCommons; A6NED2; -.
DR SignaLink; A6NED2; -.
DR BioGRID-ORCS; 91433; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; RCCD1; human.
DR GenomeRNAi; 91433; -.
DR Pharos; A6NED2; Tbio.
DR PRO; PR:A6NED2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; A6NED2; protein.
DR Bgee; ENSG00000166965; Expressed in secondary oocyte and 152 other tissues.
DR ExpressionAtlas; A6NED2; baseline and differential.
DR Genevisible; A6NED2; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR Pfam; PF00415; RCC1; 3.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Hydroxylation;
KW Reference proteome; Repeat.
FT CHAIN 1..376
FT /note="RCC1 domain-containing protein 1"
FT /id="PRO_0000337973"
FT REPEAT 6..56
FT /note="RCC1 1"
FT REPEAT 176..227
FT /note="RCC1 2"
FT REPEAT 229..317
FT /note="RCC1 3"
FT REPEAT 318..371
FT /note="RCC1 4"
FT REGION 1..169
FT /note="Interaction with KDM8"
FT /evidence="ECO:0000269|PubMed:24981860"
FT MOD_RES 141
FT /note="(3R)-3-hydroxyarginine"
FT /evidence="ECO:0000269|PubMed:29563586"
FT VARIANT 8
FT /note="A -> S (in dbSNP:rs4932380)"
FT /id="VAR_043727"
FT MUTAGEN 141
FT /note="R->A: Abolishes hydroxylation by KDM8."
FT /evidence="ECO:0000269|PubMed:29563586"
FT CONFLICT 133..186
FT /note="RLPLLPCARAYVSPRAPFYRPLAPELRARQLELGAEHALLLDAAGQVFSWGG
FT GR -> GGAAGGLVRLRFLRLRAGAGLRTRAPGAQPQSAAGGRRHLPRERELELHRFRD
FT P (in Ref. 3; AAI13827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 40079 MW; F72566D12352BBAE CRC64;
MAEERPGAWF GFGFCGFGQE LGSGRGRQVH SPSPLRAGVD ICRVSASWSY TAFVTRGGRL
ELSGSASGAA GRCKDAWASE GLLAVLRAGP GPEALLQVWA AESALRGEPL WAQNVVPEAE
GEDDPAGEAQ AGRLPLLPCA RAYVSPRAPF YRPLAPELRA RQLELGAEHA LLLDAAGQVF
SWGGGRHGQL GHGTLEAELE PRLLEALQGL VMAEVAAGGW HSVCVSETGD IYIWGWNESG
QLALPTRNLA EDGETVAREA TELNEDGSQV KRTGGAEDGA PAPFIAVQPF PALLDLPMGS
DAVKASCGSR HTAVVTRTGE LYTWGWGKYG QLGHEDTTSL DRPRRVEYFV DKQLQVKAVT
CGPWNTYVYA VEKGKS
