CCDC9_HUMAN
ID CCDC9_HUMAN Reviewed; 531 AA.
AC Q9Y3X0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Coiled-coil domain-containing protein 9 {ECO:0000305};
GN Name=CCDC9 {ECO:0000312|HGNC:HGNC:24560};
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 MRNA].
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95; SER-202 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-111; SER-137;
RP SER-202; SER-248; SER-255; SER-376; SER-386; SER-390 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-131; ARG-133 AND ARG-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP IDENTIFICATION AS PART OF THE EXON JUNCTION COMPLEX, AND FUNCTION.
RX PubMed=33973408; DOI=10.15252/msb.202010016;
RA Drew K., Wallingford J.B., Marcotte E.M.;
RT "hu.MAP 2.0: integration of over 15,000 proteomic experiments builds a
RT global compendium of human multiprotein assemblies.";
RL Mol. Syst. Biol. 17:e10016-e10016(2021).
CC -!- FUNCTION: Probable component of the exon junction complex (EJC), a
CC multiprotein complex that associates immediately upstream of the exon-
CC exon junction on mRNAs and serves as a positional landmark for the
CC intron exon structure of genes and directs post-transcriptional
CC processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA
CC decay (NMD) or translation. {ECO:0000305|PubMed:33973408}.
CC -!- SUBUNIT: Probable component of the exon junction complex (EJC); the
CC association is RNA-dependent. {ECO:0000269|PubMed:33973408}.
CC -!- INTERACTION:
CC Q9Y3X0; P42858: HTT; NbExp=3; IntAct=EBI-2557532, EBI-466029;
CC Q9Y3X0; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2557532, EBI-10975473;
CC Q9Y3X0; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-2557532, EBI-717399;
CC Q9Y3X0; O76024: WFS1; NbExp=3; IntAct=EBI-2557532, EBI-720609;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL050284; CAB43385.1; -; mRNA.
DR EMBL; BC002787; AAH02787.1; -; mRNA.
DR EMBL; BC009743; AAH09743.1; -; mRNA.
DR CCDS; CCDS12698.1; -.
DR PIR; T08760; T08760.
DR RefSeq; NP_056418.1; NM_015603.2.
DR RefSeq; XP_016882067.1; XM_017026578.1.
DR AlphaFoldDB; Q9Y3X0; -.
DR SMR; Q9Y3X0; -.
DR BioGRID; 117544; 223.
DR IntAct; Q9Y3X0; 35.
DR MINT; Q9Y3X0; -.
DR STRING; 9606.ENSP00000221922; -.
DR GlyGen; Q9Y3X0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3X0; -.
DR PhosphoSitePlus; Q9Y3X0; -.
DR BioMuta; CCDC9; -.
DR DMDM; 50400700; -.
DR EPD; Q9Y3X0; -.
DR jPOST; Q9Y3X0; -.
DR MassIVE; Q9Y3X0; -.
DR MaxQB; Q9Y3X0; -.
DR PaxDb; Q9Y3X0; -.
DR PeptideAtlas; Q9Y3X0; -.
DR PRIDE; Q9Y3X0; -.
DR ProteomicsDB; 86083; -.
DR Antibodypedia; 31544; 110 antibodies from 21 providers.
DR DNASU; 26093; -.
DR Ensembl; ENST00000221922.11; ENSP00000221922.5; ENSG00000105321.14.
DR GeneID; 26093; -.
DR KEGG; hsa:26093; -.
DR MANE-Select; ENST00000221922.11; ENSP00000221922.5; NM_015603.3; NP_056418.1.
DR UCSC; uc010xym.3; human.
DR CTD; 26093; -.
DR DisGeNET; 26093; -.
DR GeneCards; CCDC9; -.
DR HGNC; HGNC:24560; CCDC9.
DR HPA; ENSG00000105321; Low tissue specificity.
DR neXtProt; NX_Q9Y3X0; -.
DR PharmGKB; PA134946561; -.
DR VEuPathDB; HostDB:ENSG00000105321; -.
DR eggNOG; ENOG502QUM9; Eukaryota.
DR GeneTree; ENSGT00530000063950; -.
DR HOGENOM; CLU_037213_1_0_1; -.
DR InParanoid; Q9Y3X0; -.
DR OrthoDB; 602532at2759; -.
DR PhylomeDB; Q9Y3X0; -.
DR TreeFam; TF336272; -.
DR PathwayCommons; Q9Y3X0; -.
DR SignaLink; Q9Y3X0; -.
DR BioGRID-ORCS; 26093; 129 hits in 1094 CRISPR screens.
DR ChiTaRS; CCDC9; human.
DR GenomeRNAi; 26093; -.
DR Pharos; Q9Y3X0; Tdark.
DR PRO; PR:Q9Y3X0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y3X0; protein.
DR Bgee; ENSG00000105321; Expressed in sural nerve and 125 other tissues.
DR ExpressionAtlas; Q9Y3X0; baseline and differential.
DR Genevisible; Q9Y3X0; HS.
DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR InterPro; IPR029336; DUF4594.
DR PANTHER; PTHR15635; PTHR15635; 1.
DR Pfam; PF15266; DUF4594; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..531
FT /note="Coiled-coil domain-containing protein 9"
FT /id="PRO_0000089403"
FT REGION 40..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..185
FT /evidence="ECO:0000255"
FT COMPBIAS 148..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 107
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VC31"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VC31"
FT MOD_RES 128
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VC31"
FT MOD_RES 130
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VC31"
FT MOD_RES 131
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 133
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 135
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 215
FT /note="E -> D (in dbSNP:rs2032811)"
FT /id="VAR_033670"
FT VARIANT 456
FT /note="A -> V (in dbSNP:rs35119724)"
FT /id="VAR_033671"
FT VARIANT 478
FT /note="L -> P (in dbSNP:rs888836)"
FT /id="VAR_050767"
SQ SEQUENCE 531 AA; 59703 MW; DE6C474F3253C30C CRC64;
MAATLDLKSK EEKDAELDKR IEALRRKNEA LIRRYQEIEE DRKKAELEGV AVTAPRKGRS
VEKENVAVES EKNLGPSRRS PGTPRPPGAS KGGRTPPQQG GRAGMGRASR SWEGSPGEQP
RGGGAGGRGR RGRGRGSPHL SGAGDTSISD RKSKEWEERR RQNIEKMNEE MEKIAEYERN
QREGVLEPNP VRNFLDDPRR RSGPLEESER DRREESRRHG RNWGGPDFER VRCGLEHERQ
GRRAGLGSAG DMTLSMTGRE RSEYLRWKQE REKIDQERLQ RHRKPTGQWR REWDAEKTDG
MFKDGPVPAH EPSHRYDDQA WARPPKPPTF GEFLSQHKAE ASSRRRRKSS RPQAKAAPRA
YSDHDDRWET KEGAASPAPE TPQPTSPETS PKETPMQPPE IPAPAHRPPE DEGEENEGEE
DEEWEDISED EEEEEIEVEE GDEEEPAQDH QAPEAAPTGI PCSEQAHGVP FSPEEPLLEP
QAPGTPSSPF SPPSGHQPVS DWGEEVELNS PRTTHLAGAL SPGEAWPFES V
