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Q15834 (CC85B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coiled-coil domain-containing protein 85B
Alternative name(s):
Hepatitis delta antigen-interacting protein A
Short name=Delta-interacting protein A
Gene names
Name:CCDC85B
Synonyms:DIPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a transcriptional repressor. May inhibit the activity of CTNNB1 in a TP53-dependent manner and thus regulate cell growth. May function in adipocyte differentiation, negatively regulating mitotic clonal expansion. Ref.5 Ref.6

Subunit structure

Interacts with CEBPB By similarity. May interact with CEBPD By similarity. Interacts with MCRS1. Interacts with TCF7L2; competes with CTNNB1. Interacts with the viral phosphoprotein hepatitis delta antigen (HDAG). This interaction affects viral genomic replication in intact cells. Ref.5 Ref.6

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.5 Ref.6.

Tissue specificity

Widely expressed including liver.

Induction

Up-regulated by doxorubicin. Ref.6

Miscellaneous

May be the cellular homolog of HDAG. Overexpression inhibited HDV replication, whereas overexpression of HDAG reversed the inhibition, suggesting that HDAG may assist HDV replication by forming a complex with DIPA.

Sequence similarities

Belongs to the CCDC85 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202Coiled-coil domain-containing protein 85B
PRO_0000079908

Regions

Coiled coil43 – 9048 Potential
Coiled coil118 – 14730 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7

Experimental info

Mutagenesis1311L → A: Loss of interaction with TCF7L2 and loss of suppression of CTNNB1 activity. Loss of cell growth inhibition. Ref.6
Sequence conflict341A → T in AAB05928. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q15834 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: EA92D1B712A54047

FASTA20222,091
        10         20         30         40         50         60 
MEAEAGGLEE LTDEEMAALG KEELVRRLRR EEAARLAALV QRGRLMQEVN RQLQGHLGEI 

        70         80         90        100        110        120 
RELKQLNRRL QAENRELRDL CCFLDSERQR GRRAARQWQL FGTQASRAVR EDLGGCWQKL 

       130        140        150        160        170        180 
AELEGRQEEL LRENLALKEL CLALGEEWGP RGGPSGAGGS GAGPAPELAL PPCGPRDLGD 

       190        200 
GSSSTGSVGS PDQLPLACSP DD 

« Hide

References

« Hide 'large scale' references
[1]"A cellular homolog of hepatitis delta antigen: implications for viral replication and evolution."
Brazas R., Ganem D.
Science 274:90-94(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Promyelocytic leukemia.
[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. expand/collapse author list , 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].
Tissue: Skeletal muscle.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Skin.
[5]"DIPA, which can localize to the centrosome, associates with p78/MCRS1/MSP58 and acts as a repressor of gene transcription."
Du X., Wang Q., Hirohashi Y., Greene M.I.
Exp. Mol. Pathol. 81:184-190(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MCRS1, SUBCELLULAR LOCATION.
[6]"Coiled-coil domain containing 85B suppresses the beta-catenin activity in a p53-dependent manner."
Iwai A., Hijikata M., Hishiki T., Isono O., Chiba T., Shimotohno K.
Oncogene 27:1520-1526(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TCF7L2, INDUCTION BY DOXORUBICIN, MUTAGENESIS OF LEU-131, SUBCELLULAR LOCATION.
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U63825 mRNA. Translation: AAB05928.1.
AK312109 mRNA. Translation: BAG35045.1.
CH471076 Genomic DNA. Translation: EAW74468.1.
BC008796 mRNA. Translation: AAH08796.1.
RefSeqNP_006839.2. NM_006848.2.
UniGeneHs.66713.

3D structure databases

ProteinModelPortalQ15834.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116198. 130 interactions.
IntActQ15834. 129 interactions.
MINTMINT-1433910.
STRING9606.ENSP00000311695.

Polymorphism databases

DMDM92090801.

Proteomic databases

PaxDbQ15834.
PRIDEQ15834.

Protocols and materials databases

DNASU11007.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312579; ENSP00000311695; ENSG00000175602.
GeneID11007.
KEGGhsa:11007.
UCSCuc001ogf.3. human.

Organism-specific databases

CTD11007.
GeneCardsGC11P065657.
HGNCHGNC:24926. CCDC85B.
HPAHPA054415.
MIM605360. gene.
neXtProtNX_Q15834.
PharmGKBPA144596453.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283239.
HOGENOMHOG000234335.
HOVERGENHBG107255.
InParanoidQ15834.
KOK16758.
OMAAREWQLF.
OrthoDBEOG7V49ZJ.
PhylomeDBQ15834.
TreeFamTF320243.

Gene expression databases

BgeeQ15834.
CleanExHS_CCDC85B.
GenevestigatorQ15834.

Family and domain databases

InterProIPR019359. DUF2216_coiled-coil.
[Graphical view]
PfamPF10226. DUF2216. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCCDC85B.
GenomeRNAi11007.
NextBio41813.
PROQ15834.
SOURCESearch...

Entry information

Entry nameCC85B_HUMAN
AccessionPrimary (citable) accession number: Q15834
Secondary accession number(s): B2R598, Q96HA0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: March 7, 2006
Last modified: March 19, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM