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Q9P0U4 (CXXC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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:
CXXC-type zinc finger protein 1
Alternative name(s):
CpG-binding protein
PHD finger and CXXC domain-containing protein 1
Gene names
Name:CXXC1
Synonyms:CFP1, CGBP, PCCX1, PHF18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length656 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG. Ref.17

Subunit structure

Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1 HCFC1 and DPY30. Interacts with SETD1A. Interacts with ZNF335. Ref.9 Ref.10 Ref.11 Ref.12 Ref.16

Subcellular location

Nucleus speckle. Note: Associated with euchromatin. During mitosis, excluded from condensed chromosomes. Ref.8 Ref.10

Tissue specificity

Ubiquitous.

Domain

The acidic domain carries the potential to activate transcription. Ref.7

Post-translational modification

May be regulated by proteolysis.

Sequence similarities

Contains 1 CXXC-type zinc finger.

Contains 1 PHD-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

histone H3-K4 methylation

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSet1C/COMPASS complex

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

histone methyltransferase complex

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear matrix

Inferred from electronic annotation. Source: Ensembl

nuclear speck

Inferred from direct assay. Source: LIFEdb

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionunmethylated CpG binding

Inferred from direct assay Ref.1. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P0U4-1)

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: Q9P0U4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     340-340: K → KVMER

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 656656CXXC-type zinc finger protein 1
PRO_0000079743

Regions

Zinc finger28 – 7649PHD-type
Zinc finger160 – 20950CXXC-type
Coiled coil422 – 47453 Potential
Compositional bias256 – 31762Asp/Glu-rich (acidic)
Compositional bias321 – 35939Arg/Lys-rich (basic)

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue61Phosphoserine Ref.15
Modified residue191Phosphoserine Ref.15
Modified residue2271Phosphothreonine Ref.13

Natural variations

Alternative sequence3401K → KVMER in isoform 2.
VSP_040132

Experimental info

Mutagenesis1691C → A: Complete loss of DNA binding activity. No effect on localization in nuclear speckles. Ref.7
Mutagenesis2081C → A: Complete loss of DNA binding activity. No effect on localization in nuclear speckles. Ref.7
Sequence conflict1171D → N in AAF37799. Ref.1
Sequence conflict1751C → R in BAG37400. Ref.4
Sequence conflict2351P → S in BAG37400. Ref.4
Sequence conflict3021H → N in AAF37799. Ref.1

Secondary structure

............... 656
Helix Strand Turn

Details...

Sequences

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

Last modified March 27, 2002. Version 2.
Checksum: 6D2376E449905A18

FASTA65675,712
        10         20         30         40         50         60 
MEGDGSDPEP PDAGEDSKSE NGENAPIYCI CRKPDINCFM IGCDNCNEWF HGDCIRITEK 

        70         80         90        100        110        120 
MAKAIREWYC RECREKDPKL EIRYRHKKSR ERDGNERDSS EPRDEGGGRK RPVPDPDLQR 

       130        140        150        160        170        180 
RAGSGTGVGA MLARGSASPH KSSPQPLVAT PSQHHQQQQQ QIKRSARMCG ECEACRRTED 

       190        200        210        220        230        240 
CGHCDFCRDM KKFGGPNKIR QKCRLRQCQL RARESYKYFP SSLSPVTPSE SLPRPRRPLP 

       250        260        270        280        290        300 
TQQQPQPSQK LGRIREDEGA VASSTVKEPP EATATPEPLS DEDLPLDPDL YQDFCAGAFD 

       310        320        330        340        350        360 
DHGLPWMSDT EESPFLDPAL RKRAVKVKHV KRREKKSEKK KEERYKRHRQ KQKHKDKWKH 

       370        380        390        400        410        420 
PERADAKDPA SLPQCLGPGC VRPAQPSSKY CSDDCGMKLA ANRIYEILPQ RIQQWQQSPC 

       430        440        450        460        470        480 
IAEEHGKKLL ERIRREQQSA RTRLQEMERR FHELEAIILR AKQQAVREDE ESNEGDSDDT 

       490        500        510        520        530        540 
DLQIFCVSCG HPINPRVALR HMERCYAKYE SQTSFGSMYP TRIEGATRLF CDVYNPQSKT 

       550        560        570        580        590        600 
YCKRLQVLCP EHSRDPKVPA DEVCGCPLVR DVFELTGDFC RLPKRQCNRH YCWEKLRRAE 

       610        620        630        640        650 
VDLERVRVWY KLDELFEQER NVRTAMTNRA GLLALMLHQT IQHDPLTTDL RSSADR 

« Hide

Isoform 2 [UniParc].

Checksum: 502AD163711D50E7
Show »

FASTA66076,227

References

« Hide 'large scale' references
[1]"Cloning of a mammalian transcriptional activator that binds unmethylated CpG motifs and shares a CXXC domain with DNA methyltransferase, human trithorax, and methyl-CpG binding domain protein 1."
Voo K.S., Carlone D.L., Jacobsen B.M., Flodin A., Skalnik D.G.
Mol. Cell. Biol. 20:2108-2121(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"PCCX1, a novel DNA-binding protein with PHD finger and CXXC domain, is regulated by proteolysis."
Fujino T., Hasegawa M., Shibata S., Kishimoto T., Imai S., Takano T.
Biochem. Biophys. Res. Commun. 271:305-310(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING.
[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]"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] (ISOFORM 1).
[5]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Cervix, Colon and Skin.
[7]"Identification and characterization of the DNA binding domain of CpG-binding protein."
Lee J.-H., Voo K.S., Skalnik D.G.
J. Biol. Chem. 276:44669-44676(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING DOMAIN, MUTAGENESIS OF CYS-169 AND CYS-208.
[8]"CpG-binding protein is a nuclear matrix- and euchromatin-associated protein localized to nuclear speckles containing human trithorax. Identification of nuclear matrix targeting signals."
Lee J.-H., Skalnik D.G.
J. Biol. Chem. 277:42259-42267(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex."
Lee J.-H., Skalnik D.G.
J. Biol. Chem. 280:41725-41731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET1 COMPLEX.
[10]"Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex."
Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.
J. Biol. Chem. 282:13419-13428(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET1 COMPLEX, SUBCELLULAR LOCATION.
[11]"Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes."
Lee J.H., Skalnik D.G.
Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A.
[12]"Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SET1 COMPLEX.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Microcephaly gene links trithorax and REST/NRSF to control neural stem cell proliferation and differentiation."
Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D., Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J., Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M., Shenhav R., Walsh C.A.
Cell 151:1097-1112(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF335.
[17]"The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain."
Xu C., Bian C., Lam R., Dong A., Min J.
Nat. Commun. 2:227-227(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 161-222 IN COMPLEX WITH DNA, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF149758 mRNA. Translation: AAF37799.1.
AB031069 mRNA. Translation: BAA96307.1.
AL136862 mRNA. Translation: CAB66796.1.
AK314886 mRNA. Translation: BAG37400.1.
AC090246 Genomic DNA. No translation available.
BC014940 mRNA. Translation: AAH14940.1.
BC015733 mRNA. Translation: AAH15733.1.
BC029922 mRNA. Translation: AAH29922.1.
RefSeqNP_001095124.1. NM_001101654.1.
NP_055408.2. NM_014593.3.
UniGeneHs.180933.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QMBX-ray2.06A161-222[»]
3QMCX-ray2.10A161-222[»]
3QMDX-ray1.90A161-222[»]
3QMGX-ray2.30A161-222[»]
3QMHX-ray2.50A161-222[»]
3QMIX-ray2.10A161-222[»]
ProteinModelPortalQ9P0U4.
SMRQ9P0U4. Positions 27-106, 165-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119045. 24 interactions.
DIPDIP-50001N.
IntActQ9P0U4. 12 interactions.
MINTMINT-3078078.
STRING9606.ENSP00000390475.

PTM databases

PhosphoSiteQ9P0U4.

Polymorphism databases

DMDM20138037.

Proteomic databases

PaxDbQ9P0U4.
PRIDEQ9P0U4.

Protocols and materials databases

DNASU30827.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285106; ENSP00000285106; ENSG00000154832. [Q9P0U4-1]
ENST00000412036; ENSP00000390475; ENSG00000154832. [Q9P0U4-2]
GeneID30827.
KEGGhsa:30827.
UCSCuc002leq.4. human. [Q9P0U4-1]
uc002ler.4. human. [Q9P0U4-2]

Organism-specific databases

CTD30827.
GeneCardsGC18M047808.
HGNCHGNC:24343. CXXC1.
HPAHPA044511.
MIM609150. gene.
neXtProtNX_Q9P0U4.
PharmGKBPA134908762.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246725.
HOGENOMHOG000116258.
HOVERGENHBG051274.
InParanoidQ9P0U4.
KOK14960.
OMACINITEK.
OrthoDBEOG7FXZZ0.
PhylomeDBQ9P0U4.
TreeFamTF320326.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9P0U4.
BgeeQ9P0U4.
CleanExHS_CXXC1.
GenevestigatorQ9P0U4.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR022056. CpG-bd_C.
IPR019786. Zinc_finger_PHD-type_CS.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00628. PHD. 1 hit.
PF12269. zf-CpG_bind_C. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCXXC1. human.
EvolutionaryTraceQ9P0U4.
GeneWikiCXXC1.
GenomeRNAi30827.
NextBio52928.
PROQ9P0U4.
SOURCESearch...

Entry information

Entry nameCXXC1_HUMAN
AccessionPrimary (citable) accession number: Q9P0U4
Secondary accession number(s): B2RC03 expand/collapse secondary AC list , Q8N2W4, Q96BC8, Q9P2V7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: April 16, 2014
This is version 122 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM