Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Coiled-coil domain-containing protein 85B (Hepatitis delta antigen-interacting protein A) (Delta-interacting protein A)

 CC85B_HUMAN             Reviewed;         202 AA.
Q15834; B2R598; Q96HA0;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
12-SEP-2018, entry version 132.
RecName: Full=Coiled-coil domain-containing protein 85B;
AltName: Full=Hepatitis delta antigen-interacting protein A;
Short=Delta-interacting protein A;
Name=CCDC85B; Synonyms=DIPA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), AND
INTERACTION WITH HEPATITIS DELTA ANTIGEN HDAG (MICROBIAL INFECTION).
TISSUE=Promyelocytic leukemia;
PubMed=8810253; DOI=10.1126/science.274.5284.90;
Brazas R., Ganem D.;
"A cellular homolog of hepatitis delta antigen: implications for viral
replication and evolution.";
Science 274:90-94(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH MCRS1, AND SUBCELLULAR LOCATION.
PubMed=17014843; DOI=10.1016/j.yexmp.2006.07.008;
Du X., Wang Q., Hirohashi Y., Greene M.I.;
"DIPA, which can localize to the centrosome, associates with
p78/MCRS1/MSP58 and acts as a repressor of gene transcription.";
Exp. Mol. Pathol. 81:184-190(2006).
[6]
FUNCTION, INTERACTION WITH TCF7L2, INDUCTION BY DOXORUBICIN,
MUTAGENESIS OF LEU-131, AND SUBCELLULAR LOCATION.
PubMed=17873903; DOI=10.1038/sj.onc.1210801;
Iwai A., Hijikata M., Hishiki T., Isono O., Chiba T., Shimotohno K.;
"Coiled-coil domain containing 85B suppresses the beta-catenin
activity in a p53-dependent manner.";
Oncogene 27:1520-1526(2008).
[7]
INTERACTION WITH ANKRD26.
PubMed=22666460; DOI=10.1371/journal.pone.0038130;
Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A.,
Pastan I.;
"ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA
regulate adipogenesis in 3T3-L1 cells.";
PLoS ONE 7:E38130-E38130(2012).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Functions as a transcriptional repressor
(PubMed:17014843). May inhibit the activity of CTNNB1 in a TP53-
dependent manner and thus regulate cell growth (PubMed:17873903).
May function in adipocyte differentiation, negatively regulating
mitotic clonal expansion (By similarity).
{ECO:0000250|UniProtKB:Q6PDY0, ECO:0000269|PubMed:17014843,
ECO:0000269|PubMed:17873903}.
-!- FUNCTION: (Microbial infection) Plays a role in hepatitis delta
virus (HDV) genomic replication. {ECO:0000269|PubMed:8810253}.
-!- SUBUNIT: Interacts with CEBPB (By similarity). Interacts with EURL
(By similarity). May interact with CEBPD (By similarity).
Interacts with MCRS1 (PubMed:17014843). Interacts with TCF7L2;
competes with CTNNB1 (PubMed:17873903). Interacts with ANKRD26
(PubMed:22666460). {ECO:0000250|UniProtKB:Q6PDY0,
ECO:0000269|PubMed:17014843, ECO:0000269|PubMed:17873903,
ECO:0000269|PubMed:22666460}.
-!- SUBUNIT: (Microbial infection) Interacts with the viral
phosphoprotein hepatitis delta antigen (HDAG); this interaction
affects hepatitis delta virus (HDV) genomic replication in intact
cells. {ECO:0000269|PubMed:8810253}.
-!- INTERACTION:
Q9UFG5:C19orf25; NbExp=2; IntAct=EBI-739674, EBI-741214;
Q9NX63:CHCHD3; NbExp=2; IntAct=EBI-739674, EBI-743375;
Q5TZK3:FAM74A6; NbExp=3; IntAct=EBI-739674, EBI-10247271;
Q7Z3B3:KANSL1; NbExp=2; IntAct=EBI-739674, EBI-740244;
Q04695:KRT17; NbExp=2; IntAct=EBI-739674, EBI-297873;
P02538:KRT6A; NbExp=2; IntAct=EBI-739674, EBI-702198;
Q16512:PKN1; NbExp=2; IntAct=EBI-739674, EBI-602382;
Q96NG3:TTC25; NbExp=3; IntAct=EBI-739674, EBI-1046387;
Q8TBZ8:ZNF564; NbExp=3; IntAct=EBI-739674, EBI-10273713;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17014843,
ECO:0000269|PubMed:17873903}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:17014843}.
-!- TISSUE SPECIFICITY: Widely expressed including liver.
-!- INDUCTION: Up-regulated by doxorubicin.
{ECO:0000269|PubMed:17873903}.
-!- 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.
-!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U63825; AAB05928.1; -; mRNA.
EMBL; AK312109; BAG35045.1; -; mRNA.
EMBL; CH471076; EAW74468.1; -; Genomic_DNA.
EMBL; BC008796; AAH08796.1; -; mRNA.
CCDS; CCDS8120.1; -.
RefSeq; NP_006839.2; NM_006848.2.
UniGene; Hs.66713; -.
ProteinModelPortal; Q15834; -.
SMR; Q15834; -.
BioGrid; 116198; 151.
CORUM; Q15834; -.
IntAct; Q15834; 138.
STRING; 9606.ENSP00000311695; -.
iPTMnet; Q15834; -.
PhosphoSitePlus; Q15834; -.
BioMuta; CCDC85B; -.
DMDM; 92090801; -.
EPD; Q15834; -.
MaxQB; Q15834; -.
PaxDb; Q15834; -.
PeptideAtlas; Q15834; -.
PRIDE; Q15834; -.
ProteomicsDB; 60784; -.
DNASU; 11007; -.
Ensembl; ENST00000312579; ENSP00000311695; ENSG00000175602.
GeneID; 11007; -.
KEGG; hsa:11007; -.
UCSC; uc001ogf.4; human.
CTD; 11007; -.
EuPathDB; HostDB:ENSG00000175602.3; -.
GeneCards; CCDC85B; -.
HGNC; HGNC:24926; CCDC85B.
HPA; HPA054415; -.
MIM; 605360; gene.
neXtProt; NX_Q15834; -.
OpenTargets; ENSG00000175602; -.
PharmGKB; PA144596453; -.
eggNOG; KOG3819; Eukaryota.
eggNOG; ENOG410YXPD; LUCA.
GeneTree; ENSGT00390000003531; -.
HOGENOM; HOG000234335; -.
HOVERGEN; HBG107255; -.
InParanoid; Q15834; -.
KO; K16758; -.
OMA; GHHAAKV; -.
OrthoDB; EOG091G0MA4; -.
PhylomeDB; Q15834; -.
TreeFam; TF320243; -.
GeneWiki; CCDC85B; -.
GenomeRNAi; 11007; -.
PRO; PR:Q15834; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000175602; Expressed in 224 organ(s), highest expression level in substantia nigra.
CleanEx; HS_CCDC85B; -.
Genevisible; Q15834; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019359; CCDC85.
Pfam; PF10226; CCDC85; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Growth regulation; Nucleus; Reference proteome;
Repressor; Transcription; Transcription regulation.
CHAIN 1 202 Coiled-coil domain-containing protein
85B.
/FTId=PRO_0000079908.
COILED 43 90 {ECO:0000255}.
COILED 118 147 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MUTAGEN 131 131 L->A: Loss of interaction with TCF7L2 and
loss of suppression of CTNNB1 activity.
Loss of cell growth inhibition.
{ECO:0000269|PubMed:17873903}.
CONFLICT 34 34 A -> T (in Ref. 1; AAB05928).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
EIAAB05864 CCDC85B,Coiled-coil domain-containing protein 85B,Delta-interacting protein A,DIPA,Hepatitis delta antigen-interacting protein A,Homo sapiens,Human
EIAAB05863 Ccdc85b,Coiled-coil domain-containing protein 85B,Delta-interacting protein A homolog,Dipa,Hepatitis delta antigen-interacting protein A homolog,Mouse,Mus musculus
10-663-45436 Hepatitis Delta Virus - Hepatitis delta antigen-interacting protein A; Coiled-coil domain-containing protein 85B N_A 0.1 mg
10-663-45436 Hepatitis Delta Virus - Hepatitis delta antigen-interacting protein A; Coiled-coil domain-containing protein 85B N_A 0.5 mg
10-663-45436 Hepatitis Delta Virus - Hepatitis delta antigen-interacting protein A; Coiled-coil domain-containing protein 85B N_A 1 mg
EIAAB34872 ANKRD3,Ankyrin repeat domain-containing protein 3,DIK,Homo sapiens,Human,PKC-delta-interacting protein kinase,Receptor-interacting serine_threonine-protein kinase 4,RIPK4
18-003-42675 BTB_POZ domain-containing protein KCTD13 - Polymerase delta-interacting protein 1; TNFAIP1-like protein Polyclonal 0.05 mg Aff Pur
EIAAB06037 Bc8 orange-interacting protein,Boip,Ccdc89,Coiled-coil domain-containing protein 89,Mouse,Mus musculus
EIAAB06034 Bc8 orange-interacting protein,Boip,Ccdc89,Coiled-coil domain-containing protein 89,Rat,Rattus norvegicus
EIAAB06035 Bc8 orange-interacting protein,BOIP,CCDC89,Coiled-coil domain-containing protein 89,Homo sapiens,Human
EIAAB42996 C13orf11,Homo sapiens,Human,Putative LAG1-interacting protein,TMCO3,Transmembrane and coiled-coil domain-containing protein 3,UNQ2419_PRO4976
EIAAB10308 Cytip,Cytohesin-interacting protein,Pleckstrin homology Sec7 and coiled-coil domain-binding protein,Pscdbp,Rat,Rattus norvegicus
EIAAB30376 38 kDa DNA polymerase delta interaction protein,Homo sapiens,HSPC017,Human,p38,PDIP38,POLD4,POLDIP2,Polymerase delta-interacting protein 2
EIAAB30378 46 kDa DNA polymerase delta interaction protein,Homo sapiens,Human,KIAA1649,p46,PDIP46,POLDIP3,Polymerase delta-interacting protein 3,S6K1 Aly_REF-like target,SKAR
EIAAB39603 54 kDa VacA-interacting protein,90 kDa N-WASP-interacting protein,90 kDa SH3 protein interacting with Nck,Mouse,Mus musculus,NCK-interacting protein with SH3 domain,Nckipsd,N-WASP-binding protein,SH3
E1313h ELISA HBV X-interacting protein,HBX-interacting protein,HBXIP,Hepatitis B virus X-interacting protein,Homo sapiens,Human,XIP 96T
E1313h ELISA kit HBV X-interacting protein,HBX-interacting protein,HBXIP,Hepatitis B virus X-interacting protein,Homo sapiens,Human,XIP 96T
U1313h CLIA HBV X-interacting protein,HBX-interacting protein,HBXIP,Hepatitis B virus X-interacting protein,Homo sapiens,Human,XIP 96T
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
15-288-22084A Polymerase delta-interacting protein 2 - 38 kDa DNA polymerase delta interaction protein; p38 Polyclonal 0.05 mg
15-288-22084A Polymerase delta-interacting protein 2 - 38 kDa DNA polymerase delta interaction protein; p38 Polyclonal 0.1 mg
EIAAB04804 AKI1,Akt kinase-interacting protein 1,CC2D1A,Coiled-coil and C2 domain-containing protein 1A,Five repressor element under dual repression-binding protein 1,FRE under dual repression-binding protein 1,
EIAAB05058 Calcium-binding and coiled-coil domain-containing protein 1,CALCOCO1,Calphoglin,Coiled-coil coactivator protein,Homo sapiens,Human,KIAA1536,PP13275,Sarcoma antigen NY-SAR-3,UNQ2436_PRO4996
15-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur