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Q9P0U4

- CXXC1_HUMAN

UniProt

Q9P0U4 - CXXC1_HUMAN

Protein

CXXC-type zinc finger protein 1

Gene

CXXC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (27 Mar 2002)
      Previous versions | rss
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    Functioni

    Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri28 – 7649PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri160 – 20950CXXC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. unmethylated CpG binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. endoplasmic reticulum unfolded protein response Source: Reactome
    4. histone H3-K4 methylation Source: UniProtKB
    5. positive regulation of transcription, DNA-templated Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CXXC-type zinc finger protein 1
    Alternative name(s):
    CpG-binding protein
    PHD finger and CXXC domain-containing protein 1
    Gene namesi
    Name:CXXC1
    Synonyms:CFP1, CGBP, PCCX1, PHF18
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:24343. CXXC1.

    Subcellular locationi

    Nucleus speckle 2 Publications
    Note: Associated with euchromatin. During mitosis, excluded from condensed chromosomes.

    GO - Cellular componenti

    1. histone methyltransferase complex Source: UniProtKB
    2. nuclear matrix Source: Ensembl
    3. nuclear speck Source: LIFEdb
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. Set1C/COMPASS complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1691C → A: Complete loss of DNA binding activity. No effect on localization in nuclear speckles. 1 Publication
    Mutagenesisi208 – 2081C → A: Complete loss of DNA binding activity. No effect on localization in nuclear speckles. 1 Publication

    Organism-specific databases

    PharmGKBiPA134908762.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 656656CXXC-type zinc finger protein 1PRO_0000079743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei6 – 61Phosphoserine1 Publication
    Modified residuei19 – 191Phosphoserine1 Publication
    Modified residuei227 – 2271Phosphothreonine1 Publication

    Post-translational modificationi

    May be regulated by proteolysis.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9P0U4.
    PaxDbiQ9P0U4.
    PRIDEiQ9P0U4.

    PTM databases

    PhosphoSiteiQ9P0U4.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9P0U4.
    BgeeiQ9P0U4.
    CleanExiHS_CXXC1.
    GenevestigatoriQ9P0U4.

    Organism-specific databases

    HPAiHPA044511.

    Interactioni

    Subunit structurei

    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 ZNF335.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RBBP5Q152915EBI-949911,EBI-592823
    TP53P046377EBI-949911,EBI-366083

    Protein-protein interaction databases

    BioGridi119045. 26 interactions.
    DIPiDIP-50001N.
    IntActiQ9P0U4. 13 interactions.
    MINTiMINT-3078078.
    STRINGi9606.ENSP00000390475.

    Structurei

    Secondary structure

    1
    656
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi170 – 1723
    Helixi173 – 1764
    Beta strandi182 – 1843
    Helixi185 – 1895
    Helixi191 – 1933
    Helixi204 – 2063
    Turni209 – 2113
    Helixi214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ9P0U4.
    SMRiQ9P0U4. Positions 27-106, 165-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P0U4.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili422 – 47453Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi256 – 31762Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi321 – 35939Arg/Lys-rich (basic)Add
    BLAST

    Domaini

    The acidic domain carries the potential to activate transcription.

    Sequence similaritiesi

    Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri28 – 7649PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri160 – 20950CXXC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG246725.
    HOGENOMiHOG000116258.
    HOVERGENiHBG051274.
    InParanoidiQ9P0U4.
    KOiK14960.
    OMAiCINITEK.
    OrthoDBiEOG7FXZZ0.
    PhylomeDBiQ9P0U4.
    TreeFamiTF320326.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR022056. 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]
    PfamiPF00628. PHD. 1 hit.
    PF12269. zf-CpG_bind_C. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS51058. ZF_CXXC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P0U4-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEGDGSDPEP PDAGEDSKSE NGENAPIYCI CRKPDINCFM IGCDNCNEWF    50
    HGDCIRITEK MAKAIREWYC RECREKDPKL EIRYRHKKSR ERDGNERDSS 100
    EPRDEGGGRK RPVPDPDLQR RAGSGTGVGA MLARGSASPH KSSPQPLVAT 150
    PSQHHQQQQQ QIKRSARMCG ECEACRRTED CGHCDFCRDM KKFGGPNKIR 200
    QKCRLRQCQL RARESYKYFP SSLSPVTPSE SLPRPRRPLP TQQQPQPSQK 250
    LGRIREDEGA VASSTVKEPP EATATPEPLS DEDLPLDPDL YQDFCAGAFD 300
    DHGLPWMSDT EESPFLDPAL RKRAVKVKHV KRREKKSEKK KEERYKRHRQ 350
    KQKHKDKWKH PERADAKDPA SLPQCLGPGC VRPAQPSSKY CSDDCGMKLA 400
    ANRIYEILPQ RIQQWQQSPC IAEEHGKKLL ERIRREQQSA RTRLQEMERR 450
    FHELEAIILR AKQQAVREDE ESNEGDSDDT DLQIFCVSCG HPINPRVALR 500
    HMERCYAKYE SQTSFGSMYP TRIEGATRLF CDVYNPQSKT YCKRLQVLCP 550
    EHSRDPKVPA DEVCGCPLVR DVFELTGDFC RLPKRQCNRH YCWEKLRRAE 600
    VDLERVRVWY KLDELFEQER NVRTAMTNRA GLLALMLHQT IQHDPLTTDL 650
    RSSADR 656
    Length:656
    Mass (Da):75,712
    Last modified:March 27, 2002 - v2
    Checksum:i6D2376E449905A18
    GO
    Isoform 2 (identifier: Q9P0U4-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:660
    Mass (Da):76,227
    Checksum:i502AD163711D50E7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti117 – 1171D → N in AAF37799. (PubMed:10688657)Curated
    Sequence conflicti175 – 1751C → R in BAG37400. (PubMed:14702039)Curated
    Sequence conflicti235 – 2351P → S in BAG37400. (PubMed:14702039)Curated
    Sequence conflicti302 – 3021H → N in AAF37799. (PubMed:10688657)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei340 – 3401K → KVMER in isoform 2. 1 PublicationVSP_040132

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11945.1. [Q9P0U4-1]
    CCDS45866.1. [Q9P0U4-2]
    RefSeqiNP_001095124.1. NM_001101654.1. [Q9P0U4-2]
    NP_055408.2. NM_014593.3. [Q9P0U4-1]
    XP_006722509.1. XM_006722446.1. [Q9P0U4-1]
    UniGeneiHs.180933.

    Genome annotation databases

    EnsembliENST00000285106; ENSP00000285106; ENSG00000154832. [Q9P0U4-1]
    ENST00000412036; ENSP00000390475; ENSG00000154832. [Q9P0U4-2]
    GeneIDi30827.
    KEGGihsa:30827.
    UCSCiuc002leq.4. human. [Q9P0U4-1]
    uc002ler.4. human. [Q9P0U4-2]

    Polymorphism databases

    DMDMi20138037.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11945.1. [Q9P0U4-1 ]
    CCDS45866.1. [Q9P0U4-2 ]
    RefSeqi NP_001095124.1. NM_001101654.1. [Q9P0U4-2 ]
    NP_055408.2. NM_014593.3. [Q9P0U4-1 ]
    XP_006722509.1. XM_006722446.1. [Q9P0U4-1 ]
    UniGenei Hs.180933.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QMB X-ray 2.06 A 161-222 [» ]
    3QMC X-ray 2.10 A 161-222 [» ]
    3QMD X-ray 1.90 A 161-222 [» ]
    3QMG X-ray 2.30 A 161-222 [» ]
    3QMH X-ray 2.50 A 161-222 [» ]
    3QMI X-ray 2.10 A 161-222 [» ]
    ProteinModelPortali Q9P0U4.
    SMRi Q9P0U4. Positions 27-106, 165-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119045. 26 interactions.
    DIPi DIP-50001N.
    IntActi Q9P0U4. 13 interactions.
    MINTi MINT-3078078.
    STRINGi 9606.ENSP00000390475.

    PTM databases

    PhosphoSitei Q9P0U4.

    Polymorphism databases

    DMDMi 20138037.

    Proteomic databases

    MaxQBi Q9P0U4.
    PaxDbi Q9P0U4.
    PRIDEi Q9P0U4.

    Protocols and materials databases

    DNASUi 30827.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285106 ; ENSP00000285106 ; ENSG00000154832 . [Q9P0U4-1 ]
    ENST00000412036 ; ENSP00000390475 ; ENSG00000154832 . [Q9P0U4-2 ]
    GeneIDi 30827.
    KEGGi hsa:30827.
    UCSCi uc002leq.4. human. [Q9P0U4-1 ]
    uc002ler.4. human. [Q9P0U4-2 ]

    Organism-specific databases

    CTDi 30827.
    GeneCardsi GC18M047808.
    HGNCi HGNC:24343. CXXC1.
    HPAi HPA044511.
    MIMi 609150. gene.
    neXtProti NX_Q9P0U4.
    PharmGKBi PA134908762.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG246725.
    HOGENOMi HOG000116258.
    HOVERGENi HBG051274.
    InParanoidi Q9P0U4.
    KOi K14960.
    OMAi CINITEK.
    OrthoDBi EOG7FXZZ0.
    PhylomeDBi Q9P0U4.
    TreeFami TF320326.

    Enzyme and pathway databases

    Reactomei REACT_18273. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi CXXC1. human.
    EvolutionaryTracei Q9P0U4.
    GeneWikii CXXC1.
    GenomeRNAii 30827.
    NextBioi 52928.
    PROi Q9P0U4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0U4.
    Bgeei Q9P0U4.
    CleanExi HS_CXXC1.
    Genevestigatori Q9P0U4.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR022056. 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 ]
    Pfami PF00628. PHD. 1 hit.
    PF12269. zf-CpG_bind_C. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS51058. ZF_CXXC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. 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. 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.

    Entry informationi

    Entry nameiCXXC1_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0U4
    Secondary accession number(s): B2RC03
    , Q8N2W4, Q96BC8, Q9P2V7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: March 27, 2002
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3