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Protein

Coiled-coil domain-containing protein 9

Gene

CCDC9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Coiled-coil domain-containing protein 9
Gene namesi
Name:CCDC9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:24560. CCDC9.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134946561.

Polymorphism and mutation databases

BioMutaiCCDC9.
DMDMi50400700.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 531531Coiled-coil domain-containing protein 9PRO_0000089403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei95 – 951PhosphothreonineCombined sources
Modified residuei202 – 2021PhosphoserineCombined sources
Modified residuei521 – 5211PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y3X0.
MaxQBiQ9Y3X0.
PaxDbiQ9Y3X0.
PeptideAtlasiQ9Y3X0.
PRIDEiQ9Y3X0.

PTM databases

iPTMnetiQ9Y3X0.
PhosphoSiteiQ9Y3X0.

Miscellaneous databases

PMAP-CutDBQ9Y3X0.

Expressioni

Gene expression databases

BgeeiQ9Y3X0.
CleanExiHS_CCDC9.
ExpressionAtlasiQ9Y3X0. baseline and differential.
GenevisibleiQ9Y3X0. HS.

Organism-specific databases

HPAiHPA045624.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TINF2Q9BSI42EBI-2557532,EBI-717399

Protein-protein interaction databases

BioGridi117544. 25 interactions.
IntActiQ9Y3X0. 14 interactions.
MINTiMINT-4715960.
STRINGi9606.ENSP00000221922.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3X0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili149 – 18537Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 14457Gly-richAdd
BLAST
Compositional biasi344 – 3474Poly-Arg
Compositional biasi377 – 40933Pro-richAdd
BLAST
Compositional biasi410 – 44536Glu-richAdd
BLAST
Compositional biasi429 – 44012Poly-GluAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG0Q. Eukaryota.
ENOG4111HS1. LUCA.
GeneTreeiENSGT00530000063950.
HOGENOMiHOG000273887.
HOVERGENiHBG050826.
InParanoidiQ9Y3X0.
OMAiKGGRTPP.
OrthoDBiEOG7F7W99.
PhylomeDBiQ9Y3X0.
TreeFamiTF336272.

Family and domain databases

InterProiIPR029336. DUF4594.
[Graphical view]
PANTHERiPTHR15635. PTHR15635. 1 hit.
PfamiPF15266. DUF4594. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y3X0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATLDLKSK EEKDAELDKR IEALRRKNEA LIRRYQEIEE DRKKAELEGV
60 70 80 90 100
AVTAPRKGRS VEKENVAVES EKNLGPSRRS PGTPRPPGAS KGGRTPPQQG
110 120 130 140 150
GRAGMGRASR SWEGSPGEQP RGGGAGGRGR RGRGRGSPHL SGAGDTSISD
160 170 180 190 200
RKSKEWEERR RQNIEKMNEE MEKIAEYERN QREGVLEPNP VRNFLDDPRR
210 220 230 240 250
RSGPLEESER DRREESRRHG RNWGGPDFER VRCGLEHERQ GRRAGLGSAG
260 270 280 290 300
DMTLSMTGRE RSEYLRWKQE REKIDQERLQ RHRKPTGQWR REWDAEKTDG
310 320 330 340 350
MFKDGPVPAH EPSHRYDDQA WARPPKPPTF GEFLSQHKAE ASSRRRRKSS
360 370 380 390 400
RPQAKAAPRA YSDHDDRWET KEGAASPAPE TPQPTSPETS PKETPMQPPE
410 420 430 440 450
IPAPAHRPPE DEGEENEGEE DEEWEDISED EEEEEIEVEE GDEEEPAQDH
460 470 480 490 500
QAPEAAPTGI PCSEQAHGVP FSPEEPLLEP QAPGTPSSPF SPPSGHQPVS
510 520 530
DWGEEVELNS PRTTHLAGAL SPGEAWPFES V
Length:531
Mass (Da):59,703
Last modified:November 1, 1999 - v1
Checksum:iDE6C474F3253C30C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti215 – 2151E → D.
Corresponds to variant rs2032811 [ dbSNP | Ensembl ].
VAR_033670
Natural varianti456 – 4561A → V.
Corresponds to variant rs35119724 [ dbSNP | Ensembl ].
VAR_033671
Natural varianti478 – 4781L → P.
Corresponds to variant rs888836 [ dbSNP | Ensembl ].
VAR_050767

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL050284 mRNA. Translation: CAB43385.1.
BC002787 mRNA. Translation: AAH02787.1.
BC009743 mRNA. Translation: AAH09743.1.
CCDSiCCDS12698.1.
PIRiT08760.
RefSeqiNP_056418.1. NM_015603.2.
UniGeneiHs.227782.

Genome annotation databases

EnsembliENST00000221922; ENSP00000221922; ENSG00000105321.
GeneIDi26093.
KEGGihsa:26093.
UCSCiuc010xym.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL050284 mRNA. Translation: CAB43385.1.
BC002787 mRNA. Translation: AAH02787.1.
BC009743 mRNA. Translation: AAH09743.1.
CCDSiCCDS12698.1.
PIRiT08760.
RefSeqiNP_056418.1. NM_015603.2.
UniGeneiHs.227782.

3D structure databases

ProteinModelPortaliQ9Y3X0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117544. 25 interactions.
IntActiQ9Y3X0. 14 interactions.
MINTiMINT-4715960.
STRINGi9606.ENSP00000221922.

PTM databases

iPTMnetiQ9Y3X0.
PhosphoSiteiQ9Y3X0.

Polymorphism and mutation databases

BioMutaiCCDC9.
DMDMi50400700.

Proteomic databases

EPDiQ9Y3X0.
MaxQBiQ9Y3X0.
PaxDbiQ9Y3X0.
PeptideAtlasiQ9Y3X0.
PRIDEiQ9Y3X0.

Protocols and materials databases

DNASUi26093.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221922; ENSP00000221922; ENSG00000105321.
GeneIDi26093.
KEGGihsa:26093.
UCSCiuc010xym.3. human.

Organism-specific databases

CTDi26093.
GeneCardsiCCDC9.
HGNCiHGNC:24560. CCDC9.
HPAiHPA045624.
neXtProtiNX_Q9Y3X0.
PharmGKBiPA134946561.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG0Q. Eukaryota.
ENOG4111HS1. LUCA.
GeneTreeiENSGT00530000063950.
HOGENOMiHOG000273887.
HOVERGENiHBG050826.
InParanoidiQ9Y3X0.
OMAiKGGRTPP.
OrthoDBiEOG7F7W99.
PhylomeDBiQ9Y3X0.
TreeFamiTF336272.

Miscellaneous databases

GenomeRNAii26093.
PMAP-CutDBQ9Y3X0.
PROiQ9Y3X0.

Gene expression databases

BgeeiQ9Y3X0.
CleanExiHS_CCDC9.
ExpressionAtlasiQ9Y3X0. baseline and differential.
GenevisibleiQ9Y3X0. HS.

Family and domain databases

InterProiIPR029336. DUF4594.
[Graphical view]
PANTHERiPTHR15635. PTHR15635. 1 hit.
PfamiPF15266. DUF4594. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  2. "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].
    Tissue: Skin.
  3. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95; SER-202 AND SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCCDC9_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 113 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations

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.