CC85B_HUMAN
ID CC85B_HUMAN Reviewed; 202 AA.
AC Q15834; B2R598; Q96HA0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Coiled-coil domain-containing protein 85B;
DE AltName: Full=Hepatitis delta antigen-interacting protein A;
DE Short=Delta-interacting protein A;
GN Name=CCDC85B; Synonyms=DIPA;
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 [MRNA], FUNCTION (MICROBIAL INFECTION), AND INTERACTION
RP WITH HEPATITIS DELTA ANTIGEN HDAG (MICROBIAL INFECTION).
RC TISSUE=Promyelocytic leukemia;
RX PubMed=8810253; DOI=10.1126/science.274.5284.90;
RA Brazas R., Ganem D.;
RT "A cellular homolog of hepatitis delta antigen: implications for viral
RT replication and evolution.";
RL Science 274:90-94(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, INTERACTION WITH MCRS1, AND SUBCELLULAR LOCATION.
RX PubMed=17014843; DOI=10.1016/j.yexmp.2006.07.008;
RA Du X., Wang Q., Hirohashi Y., Greene M.I.;
RT "DIPA, which can localize to the centrosome, associates with
RT p78/MCRS1/MSP58 and acts as a repressor of gene transcription.";
RL Exp. Mol. Pathol. 81:184-190(2006).
RN [6]
RP FUNCTION, INTERACTION WITH TCF7L2, INDUCTION BY DOXORUBICIN, MUTAGENESIS OF
RP LEU-131, AND SUBCELLULAR LOCATION.
RX PubMed=17873903; DOI=10.1038/sj.onc.1210801;
RA Iwai A., Hijikata M., Hishiki T., Isono O., Chiba T., Shimotohno K.;
RT "Coiled-coil domain containing 85B suppresses the beta-catenin activity in
RT a p53-dependent manner.";
RL Oncogene 27:1520-1526(2008).
RN [7]
RP INTERACTION WITH ANKRD26.
RX PubMed=22666460; DOI=10.1371/journal.pone.0038130;
RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.;
RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate
RT adipogenesis in 3T3-L1 cells.";
RL PLoS ONE 7:E38130-E38130(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, INTERACTION WITH ARVCF; CTNND1; CTNND2 AND PKP4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492;
RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J.,
RA McCrea P.D., Gamse J.T., Reynolds A.B.;
RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of
RT p120-catenin family: potential roles in hydrocephalus and heterotopia.";
RL Mol. Biol. Cell 25:2592-2603(2014).
CC -!- FUNCTION: Functions as a transcriptional repressor (PubMed:17014843).
CC May inhibit the activity of CTNNB1 in a TP53-dependent manner and thus
CC regulate cell growth (PubMed:17873903). May function in adipocyte
CC differentiation, negatively regulating mitotic clonal expansion (By
CC similarity). Plays a role in cell-cell adhesion and epithelium
CC development through its interaction with proteins of the beta-catenin
CC family (By similarity). {ECO:0000250|UniProtKB:A2CEM9,
CC ECO:0000250|UniProtKB:Q6PDY0, ECO:0000269|PubMed:17014843,
CC ECO:0000269|PubMed:17873903}.
CC -!- FUNCTION: (Microbial infection) Plays a role in hepatitis delta virus
CC (HDV) genomic replication. {ECO:0000269|PubMed:8810253}.
CC -!- SUBUNIT: Interacts with CEBPB (By similarity). Interacts with EURL (By
CC similarity). May interact with CEBPD (By similarity). Interacts with
CC MCRS1 (PubMed:17014843). Interacts with TCF7L2; competes with CTNNB1
CC (PubMed:17873903). Interacts with ANKRD26 (PubMed:22666460). Interacts
CC with the beta-catenin family proteins ARVCF, CTNND1, CTNND2 AND PKP4
CC (PubMed:25009281). {ECO:0000250|UniProtKB:Q6PDY0,
CC ECO:0000269|PubMed:17014843, ECO:0000269|PubMed:17873903,
CC ECO:0000269|PubMed:22666460, ECO:0000269|PubMed:25009281}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the viral phosphoprotein
CC hepatitis delta antigen (HDAG); this interaction affects hepatitis
CC delta virus (HDV) genomic replication in intact cells.
CC {ECO:0000269|PubMed:8810253}.
CC -!- INTERACTION:
CC Q15834; O15392: BIRC5; NbExp=3; IntAct=EBI-739674, EBI-518823;
CC Q15834; Q9UFG5: C19orf25; NbExp=2; IntAct=EBI-739674, EBI-741214;
CC Q15834; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-739674, EBI-10250303;
CC Q15834; Q9NX63: CHCHD3; NbExp=2; IntAct=EBI-739674, EBI-743375;
CC Q15834; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-739674, EBI-10247271;
CC Q15834; Q9C086: INO80B; NbExp=3; IntAct=EBI-739674, EBI-715611;
CC Q15834; Q7Z3B3: KANSL1; NbExp=2; IntAct=EBI-739674, EBI-740244;
CC Q15834; Q04695: KRT17; NbExp=2; IntAct=EBI-739674, EBI-297873;
CC Q15834; P02538: KRT6A; NbExp=2; IntAct=EBI-739674, EBI-702198;
CC Q15834; Q96NG3: ODAD4; NbExp=3; IntAct=EBI-739674, EBI-1046387;
CC Q15834; Q16512: PKN1; NbExp=2; IntAct=EBI-739674, EBI-602382;
CC Q15834; P57771-2: RGS8; NbExp=3; IntAct=EBI-739674, EBI-12058229;
CC Q15834; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-739674, EBI-10273713;
CC Q15834; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-739674, EBI-6427977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17014843,
CC ECO:0000269|PubMed:17873903}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:17014843}. Cell
CC junction, adherens junction {ECO:0000269|PubMed:25009281}.
CC -!- TISSUE SPECIFICITY: Widely expressed including liver.
CC -!- INDUCTION: Up-regulated by doxorubicin. {ECO:0000269|PubMed:17873903}.
CC -!- MISCELLANEOUS: May be the cellular homolog of HDAG. Overexpression
CC inhibited HDV replication, whereas overexpression of HDAG reversed the
CC inhibition, suggesting that HDAG may assist HDV replication by forming
CC a complex with DIPA.
CC -!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
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DR EMBL; U63825; AAB05928.1; -; mRNA.
DR EMBL; AK312109; BAG35045.1; -; mRNA.
DR EMBL; CH471076; EAW74468.1; -; Genomic_DNA.
DR EMBL; BC008796; AAH08796.1; -; mRNA.
DR CCDS; CCDS8120.1; -.
DR RefSeq; NP_006839.2; NM_006848.2.
DR AlphaFoldDB; Q15834; -.
DR SMR; Q15834; -.
DR BioGRID; 116198; 166.
DR CORUM; Q15834; -.
DR IntAct; Q15834; 149.
DR MINT; Q15834; -.
DR STRING; 9606.ENSP00000311695; -.
DR iPTMnet; Q15834; -.
DR PhosphoSitePlus; Q15834; -.
DR BioMuta; CCDC85B; -.
DR DMDM; 92090801; -.
DR EPD; Q15834; -.
DR jPOST; Q15834; -.
DR MassIVE; Q15834; -.
DR MaxQB; Q15834; -.
DR PaxDb; Q15834; -.
DR PeptideAtlas; Q15834; -.
DR PRIDE; Q15834; -.
DR ProteomicsDB; 60784; -.
DR Antibodypedia; 55944; 56 antibodies from 21 providers.
DR DNASU; 11007; -.
DR Ensembl; ENST00000312579.4; ENSP00000311695.2; ENSG00000175602.4.
DR GeneID; 11007; -.
DR KEGG; hsa:11007; -.
DR MANE-Select; ENST00000312579.4; ENSP00000311695.2; NM_006848.3; NP_006839.2.
DR UCSC; uc001ogf.4; human.
DR CTD; 11007; -.
DR DisGeNET; 11007; -.
DR GeneCards; CCDC85B; -.
DR HGNC; HGNC:24926; CCDC85B.
DR HPA; ENSG00000175602; Low tissue specificity.
DR MIM; 605360; gene.
DR neXtProt; NX_Q15834; -.
DR OpenTargets; ENSG00000175602; -.
DR PharmGKB; PA144596453; -.
DR VEuPathDB; HostDB:ENSG00000175602; -.
DR eggNOG; KOG3819; Eukaryota.
DR GeneTree; ENSGT00940000162317; -.
DR HOGENOM; CLU_117450_0_0_1; -.
DR InParanoid; Q15834; -.
DR OMA; IQGVNRQ; -.
DR OrthoDB; 1393196at2759; -.
DR PhylomeDB; Q15834; -.
DR TreeFam; TF320243; -.
DR PathwayCommons; Q15834; -.
DR SignaLink; Q15834; -.
DR BioGRID-ORCS; 11007; 27 hits in 1081 CRISPR screens.
DR GeneWiki; CCDC85B; -.
DR GenomeRNAi; 11007; -.
DR Pharos; Q15834; Tdark.
DR PRO; PR:Q15834; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q15834; protein.
DR Bgee; ENSG00000175602; Expressed in amygdala and 198 other tissues.
DR Genevisible; Q15834; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070097; F:delta-catenin binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR019359; CCDC85.
DR PANTHER; PTHR13546; PTHR13546; 1.
DR Pfam; PF10226; CCDC85; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Growth regulation; Host-virus interaction; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..202
FT /note="Coiled-coil domain-containing protein 85B"
FT /id="PRO_0000079908"
FT REGION 148..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..90
FT /evidence="ECO:0000255"
FT COILED 118..147
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 131
FT /note="L->A: Loss of interaction with TCF7L2 and loss of
FT suppression of CTNNB1 activity. Loss of cell growth
FT inhibition."
FT /evidence="ECO:0000269|PubMed:17873903"
FT CONFLICT 34
FT /note="A -> T (in Ref. 1; AAB05928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22091 MW; EA92D1B712A54047 CRC64;
MEAEAGGLEE LTDEEMAALG KEELVRRLRR EEAARLAALV QRGRLMQEVN RQLQGHLGEI
RELKQLNRRL QAENRELRDL CCFLDSERQR GRRAARQWQL FGTQASRAVR EDLGGCWQKL
AELEGRQEEL LRENLALKEL CLALGEEWGP RGGPSGAGGS GAGPAPELAL PPCGPRDLGD
GSSSTGSVGS PDQLPLACSP DD
