Q9P1Z2 (CACO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	691 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Wnt signaling pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor 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: Compara positive regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 16344550. Source: UniProtKB transcription, DNA-dependent Inferred from sequence or structural similarity. Source: HGNC
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nuclear chromatin Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: LIFEdb
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara ligand-dependent nuclear receptor transcription coactivator activity Inferred from direct assay PubMed 16344550. Source: AgBase sequence-specific DNA binding Inferred from direct assay PubMed 16344550. Source: AgBase 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 691	691	Calcium-binding and coiled-coil domain-containing protein 1		PRO_0000308899
Regions
	Region	1 – 190	190	N-terminal AD (CTNNB1 binding site) By similarity
	Region	1 – 30	30	p300 KIX-binding By similarity
	Region	501 – 691	191	C-terminal AD (CTNNB1 binding site) By similarity
	Coiled coil	145 – 205	61	Potential
	Coiled coil	232 – 339	108	Potential
	Coiled coil	417 – 514	98	Potential
	Compositional bias	367 – 372	6	Poly-Ala
Amino acid modifications
	Modified residue	563	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	87 – 119	33	Missing in isoform 4.		VSP_041471
	Alternative sequence	287 – 338	52	Missing in isoform 4.		VSP_041472
	Alternative sequence	598	1	Missing in isoform 3.		VSP_029052
	Alternative sequence	633 – 691	59	SGFTV…PFTFE → R in isoform 2.		VSP_029053
	Natural variant	393	1	R → K. Ref.5 Corresponds to variant rs3741659 [ dbSNP | Ensembl ].		VAR_036881
Experimental info
	Sequence conflict	381	1	H → R in BAG53720. Ref.5
	Sequence conflict	486	1	K → R in CAG38598. Ref.7
	Sequence conflict	660	1	K → E in CAG38598. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: 06A4C6BAB896759F	FASTA	691	77,336
	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
	Isoform 2 [UniParc]. Checksum: 44493B60B4E3BBF1	FASTA	633	70,978
	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 DEKSVLMAAV QSGGEEANLL LPELGSAFYD MAR
	Isoform 3 [UniParc]. Checksum: B9369254792722D2	FASTA	690	77,207
	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 EDSSSDSAED 610 620 630 640 650 660 EKSVLMAAVQ SGGEEANLLL PELGSAFYDM ASGFTVGTLS ETSTGGPATP TWKECPICKE 670 680 690 RFPAESDKDA LEDHMDGHFF FSTQDPFTFE
	Isoform 4 [UniParc]. Checksum: 1166472275D9A569	FASTA	606	67,542
	10 20 30 40 50 60 MEESPLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD 70 80 90 100 110 120 YHTFVWSSVP ESTTDGSPIH TSVQFQEPRP MDELVTLEEA DGGSDILLVV PKATVLQNQL 130 140 150 160 170 180 DESQQERNDL MQLKLQLEGQ VTELRSRVQE LERALATARQ EHTELMEQYK GISRSHGEIT 190 200 210 220 230 240 EERDILSRQQ GDHVARILEL EDDIQTISEK VLTKEVELDR LRDTVKALTR EQEKLLGQLK 250 260 270 280 290 300 EVQADKEQSE AELEPLKEQL RGAQELAASS QQKATLLGEE LASAAAARDR TIAELHRSRL 310 320 330 340 350 360 EVAEVNGRLA ELGLHLKEEK CQWSKERAGL LQSVEAEKDK ILKLSAEILR LEKAVQEERT 370 380 390 400 410 420 QNQVFKTELA REKDSSLVQL SESKRELTEL RSALRVLQKE KEQLQEEKQE LLEYMRKLEA 430 440 450 460 470 480 RLEKVADEKW NEDATTEDEE AAVGLSCPAA LTDSEDESPE DMRLPPYGLC ERGDPGSSPA 490 500 510 520 530 540 GPREASPLVV ISQPAPISPH LSGPAEDSSS DSEAEDEKSV LMAAVQSGGE EANLLLPELG 550 560 570 580 590 600 SAFYDMASGF TVGTLSETST GGPATPTWKE CPICKERFPA ESDKDALEDH MDGHFFFSTQ DPFTFE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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. , 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.
IPI	IPI00011232. IPI00788619. IPI00794512. IPI00902761.
RefSeq	NP_001137154.1. NM_001143682.1. NP_065949.1. NM_020898.2.
UniGene	Hs.156667.
3D structure databases
ProteinModelPortal	Q9P1Z2.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47322N.
IntAct	Q9P1Z2. 18 interactions.
MINT	MINT-1399261.
STRING	9606.ENSP00000262059.
Polymorphism databases
DMDM	160017736.
Proteomic databases
PaxDb	Q9P1Z2.
PRIDE	Q9P1Z2.
Protocols and materials databases
DNASU	57658.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262059; ENSP00000262059; ENSG00000012822. ENST00000430117; ENSP00000397189; ENSG00000012822. ENST00000548263; ENSP00000447647; ENSG00000012822. ENST00000550804; ENSP00000449960; ENSG00000012822.
GeneID	57658.
KEGG	hsa:57658.
UCSC	uc001sef.3. human. uc001seh.2. human. uc009znd.3. human.
Organism-specific databases
CTD	57658.
GeneCards	GC12M054105.
H-InvDB	HIX0129676.
HGNC	HGNC:29306. CALCOCO1.
HPA	HPA038313. HPA038314.
neXtProt	NX_Q9P1Z2.
PharmGKB	PA128394699.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG114876.
HOVERGEN	HBG107573.
InParanoid	Q9P1Z2.
OMA	YDMASGF.
OrthoDB	EOG4NZTTD.
PhylomeDB	Q9P1Z2.
Gene expression databases
ArrayExpress	Q9P1Z2.
Bgee	Q9P1Z2.
CleanEx	HS_CALCOCO1.
Genevestigator	Q9P1Z2.
Family and domain databases
InterPro	IPR012852. CoCoA. [Graphical view]
Pfam	PF07888. CALCOCO1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57658.
NextBio	64417.
PMAP-CutDB	Q9P1Z2.

Entry information

Entry name

CACO1_HUMAN

Accession

Primary (citable) accession number: Q9P1Z2
Secondary accession number(s): B3KVA8 , Q6FI59, Q71RC3, Q86WF8, Q96JU3, Q9H090

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	October 23, 2007
Last modified:	April 3, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.