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Q15834

- CC85B_HUMAN

UniProt

Q15834 - CC85B_HUMAN

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Protein

Coiled-coil domain-containing protein 85B

Gene

CCDC85B

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

Functioni

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.2 Publications

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. negative regulation of cell growth Source: UniProtKB
  3. negative regulation of fat cell differentiation Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Differentiation, Growth regulation, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Coiled-coil domain-containing protein 85B
Alternative name(s):
Hepatitis delta antigen-interacting protein A
Short name:
Delta-interacting protein A
Gene namesi
Name:CCDC85B
Synonyms:DIPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:24926. CCDC85B.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311L → A: Loss of interaction with TCF7L2 and loss of suppression of CTNNB1 activity. Loss of cell growth inhibition. 1 Publication

Organism-specific databases

PharmGKBiPA144596453.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202Coiled-coil domain-containing protein 85BPRO_0000079908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15834.
PaxDbiQ15834.
PRIDEiQ15834.

Expressioni

Tissue specificityi

Widely expressed including liver.

Inductioni

Up-regulated by doxorubicin.1 Publication

Gene expression databases

BgeeiQ15834.
CleanExiHS_CCDC85B.
GenevestigatoriQ15834.

Organism-specific databases

HPAiHPA054415.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C19orf25Q9UFG52EBI-739674,EBI-741214
CHCHD3Q9NX632EBI-739674,EBI-743375
KANSL1Q7Z3B32EBI-739674,EBI-740244
KRT17Q046952EBI-739674,EBI-297873
KRT6AP025382EBI-739674,EBI-702198
PKN1Q165122EBI-739674,EBI-602382

Protein-protein interaction databases

BioGridi116198. 135 interactions.
IntActiQ15834. 129 interactions.
MINTiMINT-1433910.
STRINGi9606.ENSP00000311695.

Structurei

3D structure databases

ProteinModelPortaliQ15834.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili43 – 9048Sequence AnalysisAdd
BLAST
Coiled coili118 – 14730Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the CCDC85 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG283239.
GeneTreeiENSGT00390000003531.
HOGENOMiHOG000234335.
HOVERGENiHBG107255.
InParanoidiQ15834.
KOiK16758.
OMAiAREWQLF.
OrthoDBiEOG7V49ZJ.
PhylomeDBiQ15834.
TreeFamiTF320243.

Family and domain databases

InterProiIPR019359. DUF2216_coiled-coil.
[Graphical view]
PfamiPF10226. DUF2216. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15834-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAEAGGLEE LTDEEMAALG KEELVRRLRR EEAARLAALV QRGRLMQEVN
60 70 80 90 100
RQLQGHLGEI RELKQLNRRL QAENRELRDL CCFLDSERQR GRRAARQWQL
110 120 130 140 150
FGTQASRAVR EDLGGCWQKL AELEGRQEEL LRENLALKEL CLALGEEWGP
160 170 180 190 200
RGGPSGAGGS GAGPAPELAL PPCGPRDLGD GSSSTGSVGS PDQLPLACSP

DD
Length:202
Mass (Da):22,091
Last modified:March 7, 2006 - v2
Checksum:iEA92D1B712A54047
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341A → T in AAB05928. (PubMed:8810253)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63825 mRNA. Translation: AAB05928.1.
AK312109 mRNA. Translation: BAG35045.1.
CH471076 Genomic DNA. Translation: EAW74468.1.
BC008796 mRNA. Translation: AAH08796.1.
CCDSiCCDS8120.1.
RefSeqiNP_006839.2. NM_006848.2.
UniGeneiHs.66713.

Genome annotation databases

EnsembliENST00000312579; ENSP00000311695; ENSG00000175602.
GeneIDi11007.
KEGGihsa:11007.
UCSCiuc001ogf.3. human.

Polymorphism databases

DMDMi92090801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63825 mRNA. Translation: AAB05928.1 .
AK312109 mRNA. Translation: BAG35045.1 .
CH471076 Genomic DNA. Translation: EAW74468.1 .
BC008796 mRNA. Translation: AAH08796.1 .
CCDSi CCDS8120.1.
RefSeqi NP_006839.2. NM_006848.2.
UniGenei Hs.66713.

3D structure databases

ProteinModelPortali Q15834.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116198. 135 interactions.
IntActi Q15834. 129 interactions.
MINTi MINT-1433910.
STRINGi 9606.ENSP00000311695.

Polymorphism databases

DMDMi 92090801.

Proteomic databases

MaxQBi Q15834.
PaxDbi Q15834.
PRIDEi Q15834.

Protocols and materials databases

DNASUi 11007.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312579 ; ENSP00000311695 ; ENSG00000175602 .
GeneIDi 11007.
KEGGi hsa:11007.
UCSCi uc001ogf.3. human.

Organism-specific databases

CTDi 11007.
GeneCardsi GC11P065657.
HGNCi HGNC:24926. CCDC85B.
HPAi HPA054415.
MIMi 605360. gene.
neXtProti NX_Q15834.
PharmGKBi PA144596453.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG283239.
GeneTreei ENSGT00390000003531.
HOGENOMi HOG000234335.
HOVERGENi HBG107255.
InParanoidi Q15834.
KOi K16758.
OMAi AREWQLF.
OrthoDBi EOG7V49ZJ.
PhylomeDBi Q15834.
TreeFami TF320243.

Miscellaneous databases

GeneWikii CCDC85B.
GenomeRNAii 11007.
NextBioi 41813.
PROi Q15834.
SOURCEi Search...

Gene expression databases

Bgeei Q15834.
CleanExi HS_CCDC85B.
Genevestigatori Q15834.

Family and domain databases

InterProi IPR019359. DUF2216_coiled-coil.
[Graphical view ]
Pfami PF10226. DUF2216. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCC85B_HUMAN
AccessioniPrimary (citable) accession number: Q15834
Secondary accession number(s): B2R598, Q96HA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: March 7, 2006
Last modified: October 29, 2014
This is version 103 of the entry and version 2 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

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3