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Protein

CXXC-type zinc finger protein 1

Gene

CXXC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • unmethylated CpG binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:24343. CXXC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • histone methyltransferase complex Source: UniProtKB
  • nuclear matrix Source: Ensembl
  • nuclear speck Source: LIFEdb
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiCXXC1.
DMDMi20138037.

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

BgeeiQ9P0U4.
CleanExiHS_CXXC1.
ExpressionAtlasiQ9P0U4. baseline and differential.
GenevisibleiQ9P0U4. HS.

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
MEOX2A4D1273EBI-949911,EBI-10172134
RBBP5Q152915EBI-949911,EBI-592823
TAX1BP1Q86VP13EBI-949911,EBI-529518
TP53P046377EBI-949911,EBI-366083

Protein-protein interaction databases

BioGridi119045. 40 interactions.
DIPiDIP-50001N.
IntActiQ9P0U4. 15 interactions.
MINTiMINT-3078078.
STRINGi9606.ENSP00000390475.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000111044.
HOGENOMiHOG000116258.
HOVERGENiHBG051274.
InParanoidiQ9P0U4.
KOiK14960.
OMAiNEWFHGH.
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. AlignAdd to basket

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

        10         20         30         40         50
MEGDGSDPEP PDAGEDSKSE NGENAPIYCI CRKPDINCFM IGCDNCNEWF
60 70 80 90 100
HGDCIRITEK MAKAIREWYC RECREKDPKL EIRYRHKKSR ERDGNERDSS
110 120 130 140 150
EPRDEGGGRK RPVPDPDLQR RAGSGTGVGA MLARGSASPH KSSPQPLVAT
160 170 180 190 200
PSQHHQQQQQ QIKRSARMCG ECEACRRTED CGHCDFCRDM KKFGGPNKIR
210 220 230 240 250
QKCRLRQCQL RARESYKYFP SSLSPVTPSE SLPRPRRPLP TQQQPQPSQK
260 270 280 290 300
LGRIREDEGA VASSTVKEPP EATATPEPLS DEDLPLDPDL YQDFCAGAFD
310 320 330 340 350
DHGLPWMSDT EESPFLDPAL RKRAVKVKHV KRREKKSEKK KEERYKRHRQ
360 370 380 390 400
KQKHKDKWKH PERADAKDPA SLPQCLGPGC VRPAQPSSKY CSDDCGMKLA
410 420 430 440 450
ANRIYEILPQ RIQQWQQSPC IAEEHGKKLL ERIRREQQSA RTRLQEMERR
460 470 480 490 500
FHELEAIILR AKQQAVREDE ESNEGDSDDT DLQIFCVSCG HPINPRVALR
510 520 530 540 550
HMERCYAKYE SQTSFGSMYP TRIEGATRLF CDVYNPQSKT YCKRLQVLCP
560 570 580 590 600
EHSRDPKVPA DEVCGCPLVR DVFELTGDFC RLPKRQCNRH YCWEKLRRAE
610 620 630 640 650
VDLERVRVWY KLDELFEQER NVRTAMTNRA GLLALMLHQT IQHDPLTTDL

RSSADR
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:
EMBLi
GenBanki
DDBJi
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]
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.180933.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi119045. 40 interactions.
DIPiDIP-50001N.
IntActiQ9P0U4. 15 interactions.
MINTiMINT-3078078.
STRINGi9606.ENSP00000390475.

PTM databases

PhosphoSiteiQ9P0U4.

Polymorphism and mutation databases

BioMutaiCXXC1.
DMDMi20138037.

Proteomic databases

MaxQBiQ9P0U4.
PaxDbiQ9P0U4.
PRIDEiQ9P0U4.

Protocols and materials databases

DNASUi30827.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi30827.
GeneCardsiGC18M047808.
HGNCiHGNC:24343. CXXC1.
HPAiHPA044511.
MIMi609150. gene.
neXtProtiNX_Q9P0U4.
PharmGKBiPA134908762.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG246725.
GeneTreeiENSGT00730000111044.
HOGENOMiHOG000116258.
HOVERGENiHBG051274.
InParanoidiQ9P0U4.
KOiK14960.
OMAiNEWFHGH.
OrthoDBiEOG7FXZZ0.
PhylomeDBiQ9P0U4.
TreeFamiTF320326.

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSiCXXC1. human.
EvolutionaryTraceiQ9P0U4.
GeneWikiiCXXC1.
GenomeRNAii30827.
NextBioi52928.
PROiQ9P0U4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0U4.
CleanExiHS_CXXC1.
ExpressionAtlasiQ9P0U4. baseline and differential.
GenevisibleiQ9P0U4. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 134 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.