Full text data of CALCOCO1
CALCOCO1
(KIAA1536)
[Confidence: low (only semi-automatic identification from reviews)]
Calcium-binding and coiled-coil domain-containing protein 1 (Calphoglin; Coiled-coil coactivator protein; Sarcoma antigen NY-SAR-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Calcium-binding and coiled-coil domain-containing protein 1 (Calphoglin; Coiled-coil coactivator protein; Sarcoma antigen NY-SAR-3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9P1Z2
ID CACO1_HUMAN Reviewed; 691 AA.
AC Q9P1Z2; B3KVA8; Q6FI59; Q71RC3; Q86WF8; Q96JU3; Q9H090;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-OCT-2007, sequence version 2.
DT 22-JAN-2014, entry version 83.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 1;
DE AltName: Full=Calphoglin;
DE AltName: Full=Coiled-coil coactivator protein;
DE AltName: Full=Sarcoma antigen NY-SAR-3;
GN Name=CALCOCO1; Synonyms=KIAA1536; ORFNames=PP13275, UNQ2436/PRO4996;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP PHOSPHOGLUCOMUTASE AND PPA1.
RX DOI=10.1016/J.BBRC.2004.10.021;
RA Takahashi K., Inuzuka M., Ingi T.;
RT "Cellular signaling mediated by calphoglin-induced activation of IPP
RT and PGM.";
RL Biochem. Biophys. Res. Commun. 325:203-214(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP LYS-393.
RC TISSUE=Spleen, and Thyroid;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-455.
RX PubMed=12601173; DOI=10.1073/pnas.0437972100;
RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
RT "Immunomic analysis of human sarcoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
CC -!- FUNCTION: Functions as a coactivator for aryl hydrocarbon and
CC nuclear receptors (NR). Recruited to promoters through its contact
CC with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS)
CC domain of transcription factors or coactivators, such as NCOA2.
CC During ER-activation acts synergistically in combination with
CC other NCOA2-binding proteins, such as EP300, CREBBP and CARM1.
CC Involved in the transcriptional activation of target genes in the
CC Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-
CC mediated transcriptional activation via its interaction with
CC CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1
CC involves differential utilization of two different activation
CC regions (By similarity).
CC -!- FUNCTION: Seems to enhance inorganic pyrphosphatase thus
CC activating phosphogluomutase (PMG). Probably functions as
CC component of the calphoglin complex, which is involved in linking
CC cellular metabolism (phosphate and glucose metabolism) with other
CC core functions including protein synthesis and degradation,
CC calcium signaling and cell growth.
CC -!- SUBUNIT: Part of a calphoglin complex consisting of CALCOCO1, PPA1
CC and PGM. Interacts with the bHLH-PAS domains of GRIP1, AHR and
CC ARNT. Interacts with CTNNB1 via both its N- and C-terminal
CC regions. Interacts with EP300 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC nucleus and cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P1Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P1Z2-2; Sequence=VSP_029053;
CC Name=3;
CC IsoId=Q9P1Z2-3; Sequence=VSP_029052;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9P1Z2-4; Sequence=VSP_041471, VSP_041472;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The C-terminal activation region (AD) is used for
CC downstream signaling. Seems to be essential for coactivator
CC function with nuclear receptors and with the aryl hydrocarbon
CC receptor (By similarity).
CC -!- DOMAIN: The N-terminal activation region (AD) is necessary and
CC sufficient for synergistic activation of LEF1-mediated
CC transcription by CTNNB1. Contains a EP3000 binding region which is
CC important for synergistic cooperation (By similarity).
CC -!- DOMAIN: Recruitment by nuclear receptors is accomplished by the
CC interaction of the coiled-coiled domain with p160 coactivators (By
CC similarity).
CC -!- SIMILARITY: Belongs to the CALCOCO family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96060.1; Type=Erroneous initiation;
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DR EMBL; AY563137; AAT68474.1; -; mRNA.
DR EMBL; AB040969; BAA96060.1; ALT_INIT; mRNA.
DR EMBL; AL136895; CAB66829.1; -; mRNA.
DR EMBL; AY358397; AAQ88763.1; -; mRNA.
DR EMBL; AK122773; BAG53720.1; -; mRNA.
DR EMBL; AK027881; BAB55428.1; -; mRNA.
DR EMBL; AF370415; AAQ15251.1; -; mRNA.
DR EMBL; CR533567; CAG38598.1; -; mRNA.
DR EMBL; CH471054; EAW96728.1; -; Genomic_DNA.
DR EMBL; BC003177; AAH03177.1; -; mRNA.
DR EMBL; AY211909; AAO65163.1; -; mRNA.
DR RefSeq; NP_001137154.1; NM_001143682.1.
DR RefSeq; NP_065949.1; NM_020898.2.
DR RefSeq; XP_005269106.1; XM_005269049.1.
DR UniGene; Hs.156667; -.
DR ProteinModelPortal; Q9P1Z2; -.
DR SMR; Q9P1Z2; 15-128.
DR DIP; DIP-47322N; -.
DR IntAct; Q9P1Z2; 18.
DR MINT; MINT-1399261; -.
DR STRING; 9606.ENSP00000262059; -.
DR DMDM; 160017736; -.
DR PaxDb; Q9P1Z2; -.
DR PRIDE; Q9P1Z2; -.
DR DNASU; 57658; -.
DR Ensembl; ENST00000262059; ENSP00000262059; ENSG00000012822.
DR Ensembl; ENST00000430117; ENSP00000397189; ENSG00000012822.
DR Ensembl; ENST00000548263; ENSP00000447647; ENSG00000012822.
DR Ensembl; ENST00000550804; ENSP00000449960; ENSG00000012822.
DR GeneID; 57658; -.
DR KEGG; hsa:57658; -.
DR UCSC; uc001sef.3; human.
DR CTD; 57658; -.
DR GeneCards; GC12M054105; -.
DR H-InvDB; HIX0129676; -.
DR HGNC; HGNC:29306; CALCOCO1.
DR HPA; HPA038313; -.
DR HPA; HPA038314; -.
DR neXtProt; NX_Q9P1Z2; -.
DR PharmGKB; PA128394699; -.
DR eggNOG; NOG114876; -.
DR HOVERGEN; HBG107573; -.
DR InParanoid; Q9P1Z2; -.
DR OMA; YDMASGF; -.
DR OrthoDB; EOG7RRF8H; -.
DR PhylomeDB; Q9P1Z2; -.
DR GeneWiki; CALCOCO1; -.
DR GenomeRNAi; 57658; -.
DR NextBio; 64417; -.
DR PMAP-CutDB; Q9P1Z2; -.
DR PRO; PR:Q9P1Z2; -.
DR ArrayExpress; Q9P1Z2; -.
DR Bgee; Q9P1Z2; -.
DR CleanEx; HS_CALCOCO1; -.
DR Genevestigator; Q9P1Z2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:AgBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:HGNC.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; ISS:HGNC.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR012852; CoCoA.
DR Pfam; PF07888; CALCOCO1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Nucleus; Polymorphism; Reference proteome; Wnt signaling pathway.
FT CHAIN 1 691 Calcium-binding and coiled-coil domain-
FT containing protein 1.
FT /FTId=PRO_0000308899.
FT REGION 1 190 N-terminal AD (CTNNB1 binding site) (By
FT similarity).
FT REGION 1 30 p300 KIX-binding (By similarity).
FT REGION 501 691 C-terminal AD (CTNNB1 binding site) (By
FT similarity).
FT COILED 145 205 Potential.
FT COILED 232 339 Potential.
FT COILED 417 514 Potential.
FT COMPBIAS 367 372 Poly-Ala.
FT VAR_SEQ 87 119 Missing (in isoform 4).
FT /FTId=VSP_041471.
FT VAR_SEQ 287 338 Missing (in isoform 4).
FT /FTId=VSP_041472.
FT VAR_SEQ 598 598 Missing (in isoform 3).
FT /FTId=VSP_029052.
FT VAR_SEQ 633 691 SGFTVGTLSETSTGGPATPTWKECPICKERFPAESDKDALE
FT DHMDGHFFFSTQDPFTFE -> R (in isoform 2).
FT /FTId=VSP_029053.
FT VARIANT 393 393 R -> K (in dbSNP:rs3741659).
FT /FTId=VAR_036881.
FT CONFLICT 381 381 H -> R (in Ref. 5; BAG53720).
FT CONFLICT 486 486 K -> R (in Ref. 7; CAG38598).
FT CONFLICT 660 660 K -> E (in Ref. 7; CAG38598).
SQ SEQUENCE 691 AA; 77336 MW; 06A4C6BAB896759F CRC64;
MEESPLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD
YHTFVWSSVP ESTTDGSPIH TSVQFQASYL PKPGAQLYQF RYVNRQGQVC GQSPPFQFRE
PRPMDELVTL EEADGGSDIL LVVPKATVLQ NQLDESQQER NDLMQLKLQL EGQVTELRSR
VQELERALAT ARQEHTELME QYKGISRSHG EITEERDILS RQQGDHVARI LELEDDIQTI
SEKVLTKEVE LDRLRDTVKA LTREQEKLLG QLKEVQADKE QSEAELQVAQ QENHHLNLDL
KEAKSWQEEQ SAQAQRLKDK VAQMKDTLGQ AQQRVAELEP LKEQLRGAQE LAASSQQKAT
LLGEELASAA AARDRTIAEL HRSRLEVAEV NGRLAELGLH LKEEKCQWSK ERAGLLQSVE
AEKDKILKLS AEILRLEKAV QEERTQNQVF KTELAREKDS SLVQLSESKR ELTELRSALR
VLQKEKEQLQ EEKQELLEYM RKLEARLEKV ADEKWNEDAT TEDEEAAVGL SCPAALTDSE
DESPEDMRLP PYGLCERGDP GSSPAGPREA SPLVVISQPA PISPHLSGPA EDSSSDSEAE
DEKSVLMAAV QSGGEEANLL LPELGSAFYD MASGFTVGTL SETSTGGPAT PTWKECPICK
ERFPAESDKD ALEDHMDGHF FFSTQDPFTF E
//
ID CACO1_HUMAN Reviewed; 691 AA.
AC Q9P1Z2; B3KVA8; Q6FI59; Q71RC3; Q86WF8; Q96JU3; Q9H090;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-OCT-2007, sequence version 2.
DT 22-JAN-2014, entry version 83.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 1;
DE AltName: Full=Calphoglin;
DE AltName: Full=Coiled-coil coactivator protein;
DE AltName: Full=Sarcoma antigen NY-SAR-3;
GN Name=CALCOCO1; Synonyms=KIAA1536; ORFNames=PP13275, UNQ2436/PRO4996;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP PHOSPHOGLUCOMUTASE AND PPA1.
RX DOI=10.1016/J.BBRC.2004.10.021;
RA Takahashi K., Inuzuka M., Ingi T.;
RT "Cellular signaling mediated by calphoglin-induced activation of IPP
RT and PGM.";
RL Biochem. Biophys. Res. Commun. 325:203-214(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP LYS-393.
RC TISSUE=Spleen, and Thyroid;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-455.
RX PubMed=12601173; DOI=10.1073/pnas.0437972100;
RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
RT "Immunomic analysis of human sarcoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
CC -!- FUNCTION: Functions as a coactivator for aryl hydrocarbon and
CC nuclear receptors (NR). Recruited to promoters through its contact
CC with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS)
CC domain of transcription factors or coactivators, such as NCOA2.
CC During ER-activation acts synergistically in combination with
CC other NCOA2-binding proteins, such as EP300, CREBBP and CARM1.
CC Involved in the transcriptional activation of target genes in the
CC Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-
CC mediated transcriptional activation via its interaction with
CC CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1
CC involves differential utilization of two different activation
CC regions (By similarity).
CC -!- FUNCTION: Seems to enhance inorganic pyrphosphatase thus
CC activating phosphogluomutase (PMG). Probably functions as
CC component of the calphoglin complex, which is involved in linking
CC cellular metabolism (phosphate and glucose metabolism) with other
CC core functions including protein synthesis and degradation,
CC calcium signaling and cell growth.
CC -!- SUBUNIT: Part of a calphoglin complex consisting of CALCOCO1, PPA1
CC and PGM. Interacts with the bHLH-PAS domains of GRIP1, AHR and
CC ARNT. Interacts with CTNNB1 via both its N- and C-terminal
CC regions. Interacts with EP300 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC nucleus and cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P1Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P1Z2-2; Sequence=VSP_029053;
CC Name=3;
CC IsoId=Q9P1Z2-3; Sequence=VSP_029052;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9P1Z2-4; Sequence=VSP_041471, VSP_041472;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The C-terminal activation region (AD) is used for
CC downstream signaling. Seems to be essential for coactivator
CC function with nuclear receptors and with the aryl hydrocarbon
CC receptor (By similarity).
CC -!- DOMAIN: The N-terminal activation region (AD) is necessary and
CC sufficient for synergistic activation of LEF1-mediated
CC transcription by CTNNB1. Contains a EP3000 binding region which is
CC important for synergistic cooperation (By similarity).
CC -!- DOMAIN: Recruitment by nuclear receptors is accomplished by the
CC interaction of the coiled-coiled domain with p160 coactivators (By
CC similarity).
CC -!- SIMILARITY: Belongs to the CALCOCO family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96060.1; Type=Erroneous initiation;
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DR EMBL; AY563137; AAT68474.1; -; mRNA.
DR EMBL; AB040969; BAA96060.1; ALT_INIT; mRNA.
DR EMBL; AL136895; CAB66829.1; -; mRNA.
DR EMBL; AY358397; AAQ88763.1; -; mRNA.
DR EMBL; AK122773; BAG53720.1; -; mRNA.
DR EMBL; AK027881; BAB55428.1; -; mRNA.
DR EMBL; AF370415; AAQ15251.1; -; mRNA.
DR EMBL; CR533567; CAG38598.1; -; mRNA.
DR EMBL; CH471054; EAW96728.1; -; Genomic_DNA.
DR EMBL; BC003177; AAH03177.1; -; mRNA.
DR EMBL; AY211909; AAO65163.1; -; mRNA.
DR RefSeq; NP_001137154.1; NM_001143682.1.
DR RefSeq; NP_065949.1; NM_020898.2.
DR RefSeq; XP_005269106.1; XM_005269049.1.
DR UniGene; Hs.156667; -.
DR ProteinModelPortal; Q9P1Z2; -.
DR SMR; Q9P1Z2; 15-128.
DR DIP; DIP-47322N; -.
DR IntAct; Q9P1Z2; 18.
DR MINT; MINT-1399261; -.
DR STRING; 9606.ENSP00000262059; -.
DR DMDM; 160017736; -.
DR PaxDb; Q9P1Z2; -.
DR PRIDE; Q9P1Z2; -.
DR DNASU; 57658; -.
DR Ensembl; ENST00000262059; ENSP00000262059; ENSG00000012822.
DR Ensembl; ENST00000430117; ENSP00000397189; ENSG00000012822.
DR Ensembl; ENST00000548263; ENSP00000447647; ENSG00000012822.
DR Ensembl; ENST00000550804; ENSP00000449960; ENSG00000012822.
DR GeneID; 57658; -.
DR KEGG; hsa:57658; -.
DR UCSC; uc001sef.3; human.
DR CTD; 57658; -.
DR GeneCards; GC12M054105; -.
DR H-InvDB; HIX0129676; -.
DR HGNC; HGNC:29306; CALCOCO1.
DR HPA; HPA038313; -.
DR HPA; HPA038314; -.
DR neXtProt; NX_Q9P1Z2; -.
DR PharmGKB; PA128394699; -.
DR eggNOG; NOG114876; -.
DR HOVERGEN; HBG107573; -.
DR InParanoid; Q9P1Z2; -.
DR OMA; YDMASGF; -.
DR OrthoDB; EOG7RRF8H; -.
DR PhylomeDB; Q9P1Z2; -.
DR GeneWiki; CALCOCO1; -.
DR GenomeRNAi; 57658; -.
DR NextBio; 64417; -.
DR PMAP-CutDB; Q9P1Z2; -.
DR PRO; PR:Q9P1Z2; -.
DR ArrayExpress; Q9P1Z2; -.
DR Bgee; Q9P1Z2; -.
DR CleanEx; HS_CALCOCO1; -.
DR Genevestigator; Q9P1Z2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:AgBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:HGNC.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; ISS:HGNC.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR012852; CoCoA.
DR Pfam; PF07888; CALCOCO1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Nucleus; Polymorphism; Reference proteome; Wnt signaling pathway.
FT CHAIN 1 691 Calcium-binding and coiled-coil domain-
FT containing protein 1.
FT /FTId=PRO_0000308899.
FT REGION 1 190 N-terminal AD (CTNNB1 binding site) (By
FT similarity).
FT REGION 1 30 p300 KIX-binding (By similarity).
FT REGION 501 691 C-terminal AD (CTNNB1 binding site) (By
FT similarity).
FT COILED 145 205 Potential.
FT COILED 232 339 Potential.
FT COILED 417 514 Potential.
FT COMPBIAS 367 372 Poly-Ala.
FT VAR_SEQ 87 119 Missing (in isoform 4).
FT /FTId=VSP_041471.
FT VAR_SEQ 287 338 Missing (in isoform 4).
FT /FTId=VSP_041472.
FT VAR_SEQ 598 598 Missing (in isoform 3).
FT /FTId=VSP_029052.
FT VAR_SEQ 633 691 SGFTVGTLSETSTGGPATPTWKECPICKERFPAESDKDALE
FT DHMDGHFFFSTQDPFTFE -> R (in isoform 2).
FT /FTId=VSP_029053.
FT VARIANT 393 393 R -> K (in dbSNP:rs3741659).
FT /FTId=VAR_036881.
FT CONFLICT 381 381 H -> R (in Ref. 5; BAG53720).
FT CONFLICT 486 486 K -> R (in Ref. 7; CAG38598).
FT CONFLICT 660 660 K -> E (in Ref. 7; CAG38598).
SQ SEQUENCE 691 AA; 77336 MW; 06A4C6BAB896759F CRC64;
MEESPLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD
YHTFVWSSVP ESTTDGSPIH TSVQFQASYL PKPGAQLYQF RYVNRQGQVC GQSPPFQFRE
PRPMDELVTL EEADGGSDIL LVVPKATVLQ NQLDESQQER NDLMQLKLQL EGQVTELRSR
VQELERALAT ARQEHTELME QYKGISRSHG EITEERDILS RQQGDHVARI LELEDDIQTI
SEKVLTKEVE LDRLRDTVKA LTREQEKLLG QLKEVQADKE QSEAELQVAQ QENHHLNLDL
KEAKSWQEEQ SAQAQRLKDK VAQMKDTLGQ AQQRVAELEP LKEQLRGAQE LAASSQQKAT
LLGEELASAA AARDRTIAEL HRSRLEVAEV NGRLAELGLH LKEEKCQWSK ERAGLLQSVE
AEKDKILKLS AEILRLEKAV QEERTQNQVF KTELAREKDS SLVQLSESKR ELTELRSALR
VLQKEKEQLQ EEKQELLEYM RKLEARLEKV ADEKWNEDAT TEDEEAAVGL SCPAALTDSE
DESPEDMRLP PYGLCERGDP GSSPAGPREA SPLVVISQPA PISPHLSGPA EDSSSDSEAE
DEKSVLMAAV QSGGEEANLL LPELGSAFYD MASGFTVGTL SETSTGGPAT PTWKECPICK
ERFPAESDKD ALEDHMDGHF FFSTQDPFTF E
//