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Q9P1Z2 (CACO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-binding and coiled-coil domain-containing protein 1
Alternative name(s):
Calphoglin
Coiled-coil coactivator protein
Sarcoma antigen NY-SAR-3
Gene names
Name:CALCOCO1
Synonyms:KIAA1536
ORF Names:PP13275, UNQ2436/PRO4996
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length691 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions By similarity. Ref.1

Seems to enhance inorganic pyrphosphatase thus activating phosphogluomutase (PMG). Probably functions as component of the calphoglin complex, which is involved in linking cellular metabolism (phosphate and glucose metabolism) with other core functions including protein synthesis and degradation, calcium signaling and cell growth. Ref.1

Subunit structure

Part of a calphoglin complex consisting of CALCOCO1, PPA1 and PGM. Interacts with the bHLH-PAS domains of GRIP1, AHR and ARNT. Interacts with CTNNB1 via both its N- and C-terminal regions. Interacts with EP300 By similarity. Ref.1

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles between nucleus and cytoplasm By similarity.

Domain

The C-terminal activation region (AD) is used for downstream signaling. Seems to be essential for coactivator function with nuclear receptors and with the aryl hydrocarbon receptor By similarity.

The N-terminal activation region (AD) is necessary and sufficient for synergistic activation of LEF1-mediated transcription by CTNNB1. Contains a EP3000 binding region which is important for synergistic cooperation By similarity.

Recruitment by nuclear receptors is accomplished by the interaction of the coiled-coiled domain with p160 coactivators By similarity.

Sequence similarities

Belongs to the CALCOCO family.

Sequence caution

The sequence BAA96060.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular steroid hormone receptor signaling pathway

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16344550. Source: UniProtKB

signal transduction

Inferred from sequence or structural similarity. Source: HGNC

transcription, DNA-templated

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: LIFEdb

   Molecular_functionarmadillo repeat domain binding

Inferred from physical interaction PubMed 16344550. Source: UniProtKB

beta-catenin binding

Inferred from physical interaction PubMed 16344550. Source: AgBase

chromatin binding

Inferred from electronic annotation. Source: Ensembl

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 16344550. Source: AgBase

protein C-terminus binding

Inferred from physical interaction PubMed 16344550. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 16344550. Source: AgBase

transcription coactivator activity

Inferred from mutant phenotype PubMed 16344550. Source: UniProtKB

transcription cofactor activity

Inferred from direct assay PubMed 16344550. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 16344550. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P1Z2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9P1Z2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     633-691: SGFTVGTLSETSTGGPATPTWKECPICKERFPAESDKDALEDHMDGHFFFSTQDPFTFE → R
Isoform 3 (identifier: Q9P1Z2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     598-598: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9P1Z2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     87-119: Missing.
     287-338: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 691691Calcium-binding and coiled-coil domain-containing protein 1
PRO_0000308899

Regions

Region1 – 190190N-terminal AD (CTNNB1 binding site) By similarity
Region1 – 3030p300 KIX-binding By similarity
Region501 – 691191C-terminal AD (CTNNB1 binding site) By similarity
Coiled coil145 – 20561 Potential
Coiled coil232 – 339108 Potential
Coiled coil417 – 51498 Potential
Compositional bias367 – 3726Poly-Ala

Natural variations

Alternative sequence87 – 11933Missing in isoform 4.
VSP_041471
Alternative sequence287 – 33852Missing in isoform 4.
VSP_041472
Alternative sequence5981Missing in isoform 3.
VSP_029052
Alternative sequence633 – 69159SGFTV…PFTFE → R in isoform 2.
VSP_029053
Natural variant3931R → K. Ref.5
Corresponds to variant rs3741659 [ dbSNP | Ensembl ].
VAR_036881

Experimental info

Sequence conflict3811H → R in BAG53720. Ref.5
Sequence conflict4861K → R in CAG38598. Ref.7
Sequence conflict6601K → E in CAG38598. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 06A4C6BAB896759F

FASTA69177,336
        10         20         30         40         50         60 
MEESPLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD 

        70         80         90        100        110        120 
YHTFVWSSVP ESTTDGSPIH TSVQFQASYL PKPGAQLYQF RYVNRQGQVC GQSPPFQFRE 

       130        140        150        160        170        180 
PRPMDELVTL EEADGGSDIL LVVPKATVLQ NQLDESQQER NDLMQLKLQL EGQVTELRSR 

       190        200        210        220        230        240 
VQELERALAT ARQEHTELME QYKGISRSHG EITEERDILS RQQGDHVARI LELEDDIQTI 

       250        260        270        280        290        300 
SEKVLTKEVE LDRLRDTVKA LTREQEKLLG QLKEVQADKE QSEAELQVAQ QENHHLNLDL 

       310        320        330        340        350        360 
KEAKSWQEEQ SAQAQRLKDK VAQMKDTLGQ AQQRVAELEP LKEQLRGAQE LAASSQQKAT 

       370        380        390        400        410        420 
LLGEELASAA AARDRTIAEL HRSRLEVAEV NGRLAELGLH LKEEKCQWSK ERAGLLQSVE 

       430        440        450        460        470        480 
AEKDKILKLS AEILRLEKAV QEERTQNQVF KTELAREKDS SLVQLSESKR ELTELRSALR 

       490        500        510        520        530        540 
VLQKEKEQLQ EEKQELLEYM RKLEARLEKV ADEKWNEDAT TEDEEAAVGL SCPAALTDSE 

       550        560        570        580        590        600 
DESPEDMRLP PYGLCERGDP GSSPAGPREA SPLVVISQPA PISPHLSGPA EDSSSDSEAE 

       610        620        630        640        650        660 
DEKSVLMAAV QSGGEEANLL LPELGSAFYD MASGFTVGTL SETSTGGPAT PTWKECPICK 

       670        680        690 
ERFPAESDKD ALEDHMDGHF FFSTQDPFTF E 

« Hide

Isoform 2 [UniParc].

Checksum: 44493B60B4E3BBF1
Show »

FASTA63370,978
Isoform 3 [UniParc].

Checksum: B9369254792722D2
Show »

FASTA69077,207
Isoform 4 [UniParc].

Checksum: 1166472275D9A569
Show »

FASTA60667,542

References

« Hide 'large scale' references
[1]"Cellular signaling mediated by calphoglin-induced activation of IPP and PGM."
Takahashi K., Inuzuka M., Ingi T.
Biochem. Biophys. Res. Commun. 325:203-214(2004)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PHOSPHOGLUCOMUTASE AND PPA1.
[2]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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] (ISOFORMS 3 AND 4), VARIANT LYS-393.
Tissue: Spleen and Thyroid.
[6]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]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].
[9]"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] (ISOFORM 1).
Tissue: Kidney.
[10]"Immunomic analysis of human sarcoma."
Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.
Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-455.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY563137 mRNA. Translation: AAT68474.1.
AB040969 mRNA. Translation: BAA96060.1. Different initiation.
AL136895 mRNA. Translation: CAB66829.1.
AY358397 mRNA. Translation: AAQ88763.1.
AK122773 mRNA. Translation: BAG53720.1.
AK027881 mRNA. Translation: BAB55428.1.
AF370415 mRNA. Translation: AAQ15251.1.
CR533567 mRNA. Translation: CAG38598.1.
CH471054 Genomic DNA. Translation: EAW96728.1.
BC003177 mRNA. Translation: AAH03177.1.
AY211909 mRNA. Translation: AAO65163.1.
RefSeqNP_001137154.1. NM_001143682.1.
NP_065949.1. NM_020898.2.
UniGeneHs.156667.

3D structure databases

ProteinModelPortalQ9P1Z2.
SMRQ9P1Z2. Positions 15-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121692. 17 interactions.
DIPDIP-47322N.
IntActQ9P1Z2. 18 interactions.
MINTMINT-1399261.
STRING9606.ENSP00000262059.

Polymorphism databases

DMDM160017736.

Proteomic databases

PaxDbQ9P1Z2.
PRIDEQ9P1Z2.

Protocols and materials databases

DNASU57658.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262059; ENSP00000262059; ENSG00000012822. [Q9P1Z2-3]
ENST00000430117; ENSP00000397189; ENSG00000012822. [Q9P1Z2-4]
ENST00000548263; ENSP00000447647; ENSG00000012822. [Q9P1Z2-2]
ENST00000550804; ENSP00000449960; ENSG00000012822. [Q9P1Z2-1]
GeneID57658.
KEGGhsa:57658.
UCSCuc001sef.3. human. [Q9P1Z2-1]
uc001seg.3. human. [Q9P1Z2-4]
uc001seh.2. human. [Q9P1Z2-2]
uc009znd.3. human. [Q9P1Z2-3]

Organism-specific databases

CTD57658.
GeneCardsGC12M054105.
H-InvDBHIX0129676.
HGNCHGNC:29306. CALCOCO1.
HPAHPA038313.
HPA038314.
neXtProtNX_Q9P1Z2.
PharmGKBPA128394699.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG114876.
HOVERGENHBG107573.
InParanoidQ9P1Z2.
OMAYDMASGF.
OrthoDBEOG7RRF8H.
PhylomeDBQ9P1Z2.
TreeFamTF329501.

Gene expression databases

ArrayExpressQ9P1Z2.
BgeeQ9P1Z2.
CleanExHS_CALCOCO1.
GenevestigatorQ9P1Z2.

Family and domain databases

InterProIPR012852. CoCoA.
[Graphical view]
PfamPF07888. CALCOCO1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCALCOCO1.
GenomeRNAi57658.
NextBio64417.
PMAP-CutDBQ9P1Z2.
PROQ9P1Z2.

Entry information

Entry nameCACO1_HUMAN
AccessionPrimary (citable) accession number: Q9P1Z2
Secondary accession number(s): B3KVA8 expand/collapse secondary AC list , Q6FI59, Q71RC3, Q86WF8, Q96JU3, Q9H090
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 86 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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM