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Protein

Coiled-coil domain-containing protein 86

Gene

CCDC86

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
Coiled-coil domain-containing protein 86
Alternative name(s):
Cytokine-induced protein with coiled-coil domain
Gene namesi
Name:CCDC86
Synonyms:CYCLON
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28359. CCDC86.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA144596454.

Polymorphism and mutation databases

BioMutaiCCDC86.
DMDMi74733605.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Coiled-coil domain-containing protein 86PRO_0000286092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei65 – 651PhosphothreonineCombined sources
Modified residuei66 – 661PhosphoserineCombined sources
Modified residuei69 – 691PhosphoserineCombined sources
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei91 – 911PhosphoserineCombined sources
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei128 – 1281PhosphoserineCombined sources
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei217 – 2171PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineBy similarity
Modified residuei342 – 3421CitrullineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

EPDiQ9H6F5.
MaxQBiQ9H6F5.
PaxDbiQ9H6F5.
PeptideAtlasiQ9H6F5.
PRIDEiQ9H6F5.

PTM databases

iPTMnetiQ9H6F5.
PhosphoSiteiQ9H6F5.

Expressioni

Gene expression databases

BgeeiQ9H6F5.
CleanExiHS_CCDC86.
ExpressionAtlasiQ9H6F5. baseline and differential.
GenevisibleiQ9H6F5. HS.

Organism-specific databases

HPAiHPA041117.
HPA041540.

Interactioni

Subunit structurei

Interacts with hepatitis C virus (HCV) protein NS5A.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
P279583EBI-721289,EBI-8753518From a different organism.

Protein-protein interaction databases

BioGridi122529. 21 interactions.
IntActiQ9H6F5. 11 interactions.
MINTiMINT-1399934.
STRINGi9606.ENSP00000227520.

Structurei

3D structure databases

ProteinModelPortaliQ9H6F5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili272 – 32352Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi45 – 200156Pro-richAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4538. Eukaryota.
ENOG41129IK. LUCA.
GeneTreeiENSGT00390000017281.
HOGENOMiHOG000111441.
HOVERGENiHBG097194.
InParanoidiQ9H6F5.
KOiK14822.
OMAiLRTSWQR.
OrthoDBiEOG779P17.
PhylomeDBiQ9H6F5.
TreeFamiTF325663.

Family and domain databases

InterProiIPR026570. CCDC86.
IPR005579. Cgr1-like.
[Graphical view]
PANTHERiPTHR13557. PTHR13557. 1 hit.
PfamiPF03879. Cgr1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H6F5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDTPLRRSRR LGGLRPESPE SLTSVSRTRR ALVEFESNPE ETREPGSPPS
60 70 80 90 100
VQRAGLGSPE RPPKTSPGSP RLQQGAGLES PQGQPEPGAA SPQRQQDLHL
110 120 130 140 150
ESPQRQPEYS PESPRCQPKP SEEAPKCSQD QGVLASELAQ NKEELTPGAP
160 170 180 190 200
QHQLPPVPGS PEPYPGQQAP GPEPSQPLLE LTPRAPGSPR GQHEPSKPPP
210 220 230 240 250
AGETVTGGFG AKKRKGSSSQ APASKKLNKE ELPVIPKGKP KSGRVWKDRS
260 270 280 290 300
KKRFSQMLQD KPLRTSWQRK MKERQERKLA KDFARHLEEE KERRRQEKKQ
310 320 330 340 350
RRAENLKRRL ENERKAEVVQ VIRNPAKLKR AKKKQLRSIE KRDTLALLQK
360
QPPQQPAAKI
Length:360
Mass (Da):40,236
Last modified:March 1, 2001 - v1
Checksum:i5599506F3E799A6C
GO
Isoform 2 (identifier: Q9H6F5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-256: Missing.

Note: No experimental confirmation available.
Show »
Length:104
Mass (Da):12,743
Checksum:i0E08850779677306
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531Q → H.
Corresponds to variant rs2074421 [ dbSNP | Ensembl ].
VAR_032069

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 256256Missing in isoform 2. 1 PublicationVSP_056905Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ501251 mRNA. Translation: ABF68612.1.
AK025974 mRNA. Translation: BAB15304.1.
AK302329 mRNA. Translation: BAG63661.1.
AP000777 Genomic DNA. No translation available.
BC001378 mRNA. Translation: AAH01378.1.
CCDSiCCDS7993.1. [Q9H6F5-1]
RefSeqiNP_077003.1. NM_024098.3. [Q9H6F5-1]
UniGeneiHs.4253.

Genome annotation databases

EnsembliENST00000227520; ENSP00000227520; ENSG00000110104. [Q9H6F5-1]
ENST00000545580; ENSP00000440906; ENSG00000110104. [Q9H6F5-2]
GeneIDi79080.
KEGGihsa:79080.
UCSCiuc001nqa.3. human. [Q9H6F5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ501251 mRNA. Translation: ABF68612.1.
AK025974 mRNA. Translation: BAB15304.1.
AK302329 mRNA. Translation: BAG63661.1.
AP000777 Genomic DNA. No translation available.
BC001378 mRNA. Translation: AAH01378.1.
CCDSiCCDS7993.1. [Q9H6F5-1]
RefSeqiNP_077003.1. NM_024098.3. [Q9H6F5-1]
UniGeneiHs.4253.

3D structure databases

ProteinModelPortaliQ9H6F5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122529. 21 interactions.
IntActiQ9H6F5. 11 interactions.
MINTiMINT-1399934.
STRINGi9606.ENSP00000227520.

PTM databases

iPTMnetiQ9H6F5.
PhosphoSiteiQ9H6F5.

Polymorphism and mutation databases

BioMutaiCCDC86.
DMDMi74733605.

Proteomic databases

EPDiQ9H6F5.
MaxQBiQ9H6F5.
PaxDbiQ9H6F5.
PeptideAtlasiQ9H6F5.
PRIDEiQ9H6F5.

Protocols and materials databases

DNASUi79080.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000227520; ENSP00000227520; ENSG00000110104. [Q9H6F5-1]
ENST00000545580; ENSP00000440906; ENSG00000110104. [Q9H6F5-2]
GeneIDi79080.
KEGGihsa:79080.
UCSCiuc001nqa.3. human. [Q9H6F5-1]

Organism-specific databases

CTDi79080.
GeneCardsiCCDC86.
HGNCiHGNC:28359. CCDC86.
HPAiHPA041117.
HPA041540.
MIMi611293. gene.
neXtProtiNX_Q9H6F5.
PharmGKBiPA144596454.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4538. Eukaryota.
ENOG41129IK. LUCA.
GeneTreeiENSGT00390000017281.
HOGENOMiHOG000111441.
HOVERGENiHBG097194.
InParanoidiQ9H6F5.
KOiK14822.
OMAiLRTSWQR.
OrthoDBiEOG779P17.
PhylomeDBiQ9H6F5.
TreeFamiTF325663.

Miscellaneous databases

ChiTaRSiCCDC86. human.
GenomeRNAii79080.
NextBioi35476165.
PROiQ9H6F5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H6F5.
CleanExiHS_CCDC86.
ExpressionAtlasiQ9H6F5. baseline and differential.
GenevisibleiQ9H6F5. HS.

Family and domain databases

InterProiIPR026570. CCDC86.
IPR005579. Cgr1-like.
[Graphical view]
PANTHERiPTHR13557. PTHR13557. 1 hit.
PfamiPF03879. Cgr1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Redundant promoter elements mediate IL-3-induced expression of a novel cytokine-inducible gene, cyclon."
    Hoshino A., Fujii H.
    FEBS Lett. 581:975-980(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Skin.
  5. "Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus."
    Ahn J., Chung K.-S., Kim D.-U., Won M., Kim L., Kim K.-S., Nam M., Choi S.-J., Kim H.-C., Yoon M., Chae S.-K., Hoe K.-L.
    J. Biochem. Mol. Biol. 37:741-748(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV NS5A.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-47; SER-58; SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-47; SER-50; SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21; SER-24; SER-47; SER-50; SER-58; THR-65; SER-66; SER-69; SER-91; SER-102 AND SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. "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-18; SER-21; SER-47; SER-50; SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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 SER-18; SER-47; SER-58; THR-65; SER-69; SER-80; SER-91; SER-102; SER-113 AND SER-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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-18; SER-47; SER-58; THR-65; SER-80; SER-91; SER-102 AND SER-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-18; SER-47; SER-58 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCCD86_HUMAN
AccessioniPrimary (citable) accession number: Q9H6F5
Secondary accession number(s): B4DY99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 120 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 11
    Human chromosome 11: 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
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.