Full text data of CER1
CER1
(DAND4)
[Confidence: low (only semi-automatic identification from reviews)]
Cerberus (Cerberus-related protein; DAN domain family member 4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cerberus (Cerberus-related protein; DAN domain family member 4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95813
ID CER1_HUMAN Reviewed; 267 AA.
AC O95813; Q6ISJ1; Q6ISJ6; Q6ISQ2; Q6ISS1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Cerberus;
DE AltName: Full=Cerberus-related protein;
DE AltName: Full=DAN domain family member 4;
DE Flags: Precursor;
GN Name=CER1; Synonyms=DAND4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=10049596; DOI=10.1006/geno.1998.5671;
RA Lah M., Brodnicki T., Maccarone P., Nash A., Stanley E., Harvey R.P.;
RT "Human cerberus related gene CER1 maps to chromosome 9.";
RL Genomics 55:364-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Feng Z., Zhang B., Peng X., Yuan J., Qiang B.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TRP-19; GLY-65
RP AND ILE-179.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 18-32.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
CC -!- FUNCTION: Cytokine that may play a role in anterior neural
CC induction and somite formation during embryogenesis in part
CC through a BMP-inhibitory mechanism. Can regulate Nodal signaling
CC during gastrulation as well as the formation and patterning of the
CC primitive streak (By similarity).
CC -!- SUBUNIT: Forms monomers and predominantly dimers (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (Probable).
CC -!- PTM: N-glycosylated (By similarity).
CC -!- SIMILARITY: Belongs to the DAN family.
CC -!- SIMILARITY: Contains 1 CTCK (C-terminal cystine knot-like) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69503.1; Type=Erroneous termination; Positions=266; Note=Translated as Ser;
CC -----------------------------------------------------------------------
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DR EMBL; AF090189; AAD19879.1; -; Genomic_DNA.
DR EMBL; AF400435; AAK92484.1; -; mRNA.
DR EMBL; AL390732; CAH73850.1; -; Genomic_DNA.
DR EMBL; BC069371; AAH69371.1; -; mRNA.
DR EMBL; BC069405; AAH69405.1; -; mRNA.
DR EMBL; BC069491; AAH69491.1; -; mRNA.
DR EMBL; BC069503; AAH69503.1; ALT_SEQ; mRNA.
DR RefSeq; NP_005445.1; NM_005454.2.
DR UniGene; Hs.248204; -.
DR ProteinModelPortal; O95813; -.
DR SMR; O95813; 144-245.
DR STRING; 9606.ENSP00000370297; -.
DR PhosphoSite; O95813; -.
DR PaxDb; O95813; -.
DR PRIDE; O95813; -.
DR DNASU; 9350; -.
DR Ensembl; ENST00000380911; ENSP00000370297; ENSG00000147869.
DR GeneID; 9350; -.
DR KEGG; hsa:9350; -.
DR UCSC; uc003zlj.3; human.
DR CTD; 9350; -.
DR GeneCards; GC09M014710; -.
DR H-InvDB; HIX0034784; -.
DR HGNC; HGNC:1862; CER1.
DR HPA; HPA019917; -.
DR MIM; 603777; gene.
DR neXtProt; NX_O95813; -.
DR PharmGKB; PA26417; -.
DR eggNOG; NOG40714; -.
DR HOGENOM; HOG000231309; -.
DR HOVERGEN; HBG050902; -.
DR InParanoid; O95813; -.
DR KO; K01645; -.
DR OMA; CFGKCGS; -.
DR OrthoDB; EOG7VX8X6; -.
DR PhylomeDB; O95813; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR GeneWiki; Cerberus_(protein); -.
DR GenomeRNAi; 9350; -.
DR NextBio; 35013; -.
DR PRO; PR:O95813; -.
DR Bgee; O95813; -.
DR CleanEx; HS_CER1; -.
DR Genevestigator; O95813; -.
DR GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
DR GO; GO:0036122; F:BMP binding; IDA:BHF-UCL.
DR GO; GO:0016015; F:morphogen activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
DR GO; GO:0030282; P:bone mineralization; IMP:BHF-UCL.
DR GO; GO:0042074; P:cell migration involved in gastrulation; ISS:BHF-UCL.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISS:BHF-UCL.
DR GO; GO:0048263; P:determination of dorsal identity; IMP:BHF-UCL.
DR GO; GO:0003419; P:growth plate cartilage chondrocyte proliferation; ISS:BHF-UCL.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:BHF-UCL.
DR GO; GO:2000381; P:negative regulation of mesoderm development; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IMP:BHF-UCL.
DR GO; GO:0035582; P:sequestering of BMP in extracellular matrix; IDA:BHF-UCL.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR InterPro; IPR016860; Cerberus.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR004133; DAN.
DR Pfam; PF03045; DAN; 1.
DR PIRSF; PIRSF027807; Cerberus; 1.
DR SMART; SM00041; CT; 1.
DR PROSITE; PS01185; CTCK_1; FALSE_NEG.
DR PROSITE; PS01225; CTCK_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Polymorphism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 17
FT CHAIN 18 267 Cerberus.
FT /FTId=PRO_0000006711.
FT DOMAIN 162 246 CTCK.
FT CARBOHYD 26 26 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 222 222 N-linked (GlcNAc...) (Potential).
FT DISULFID 162 209 By similarity.
FT DISULFID 176 223 By similarity.
FT DISULFID 186 239 By similarity.
FT DISULFID 190 241 By similarity.
FT VARIANT 19 19 R -> W (in dbSNP:rs10115703).
FT /FTId=VAR_021591.
FT VARIANT 65 65 A -> G (in dbSNP:rs3747532).
FT /FTId=VAR_021592.
FT VARIANT 179 179 V -> I (in dbSNP:rs7036635).
FT /FTId=VAR_021593.
FT CONFLICT 57 57 F -> L (in Ref. 4; AAH69503).
FT CONFLICT 221 221 L -> V (in Ref. 4; AAH69405).
SQ SEQUENCE 267 AA; 30084 MW; C9FB048CD8558ED7 CRC64;
MHLLLFQLLV LLPLGKTTRH QDGRQNQSSL SPVLLPRNQR ELPTGNHEEA EEKPDLFVAV
PHLVATSPAG EGQRQREKML SRFGRFWKKP EREMHPSRDS DSEPFPPGTQ SLIQPIDGMK
MEKSPLREEA KKFWHHFMFR KTPASQGVIL PIKSHEVHWE TCRTVPFSQT ITHEGCEKVV
VQNNLCFGKC GSVHFPGAAQ HSHTSCSHCL PAKFTTMHLP LNCTELSSVI KVVMLVEECQ
CKVKTEHEDG HILHAGSQDS FIPGVSA
//
ID CER1_HUMAN Reviewed; 267 AA.
AC O95813; Q6ISJ1; Q6ISJ6; Q6ISQ2; Q6ISS1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Cerberus;
DE AltName: Full=Cerberus-related protein;
DE AltName: Full=DAN domain family member 4;
DE Flags: Precursor;
GN Name=CER1; Synonyms=DAND4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=10049596; DOI=10.1006/geno.1998.5671;
RA Lah M., Brodnicki T., Maccarone P., Nash A., Stanley E., Harvey R.P.;
RT "Human cerberus related gene CER1 maps to chromosome 9.";
RL Genomics 55:364-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Feng Z., Zhang B., Peng X., Yuan J., Qiang B.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TRP-19; GLY-65
RP AND ILE-179.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 18-32.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
CC -!- FUNCTION: Cytokine that may play a role in anterior neural
CC induction and somite formation during embryogenesis in part
CC through a BMP-inhibitory mechanism. Can regulate Nodal signaling
CC during gastrulation as well as the formation and patterning of the
CC primitive streak (By similarity).
CC -!- SUBUNIT: Forms monomers and predominantly dimers (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (Probable).
CC -!- PTM: N-glycosylated (By similarity).
CC -!- SIMILARITY: Belongs to the DAN family.
CC -!- SIMILARITY: Contains 1 CTCK (C-terminal cystine knot-like) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69503.1; Type=Erroneous termination; Positions=266; Note=Translated as Ser;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF090189; AAD19879.1; -; Genomic_DNA.
DR EMBL; AF400435; AAK92484.1; -; mRNA.
DR EMBL; AL390732; CAH73850.1; -; Genomic_DNA.
DR EMBL; BC069371; AAH69371.1; -; mRNA.
DR EMBL; BC069405; AAH69405.1; -; mRNA.
DR EMBL; BC069491; AAH69491.1; -; mRNA.
DR EMBL; BC069503; AAH69503.1; ALT_SEQ; mRNA.
DR RefSeq; NP_005445.1; NM_005454.2.
DR UniGene; Hs.248204; -.
DR ProteinModelPortal; O95813; -.
DR SMR; O95813; 144-245.
DR STRING; 9606.ENSP00000370297; -.
DR PhosphoSite; O95813; -.
DR PaxDb; O95813; -.
DR PRIDE; O95813; -.
DR DNASU; 9350; -.
DR Ensembl; ENST00000380911; ENSP00000370297; ENSG00000147869.
DR GeneID; 9350; -.
DR KEGG; hsa:9350; -.
DR UCSC; uc003zlj.3; human.
DR CTD; 9350; -.
DR GeneCards; GC09M014710; -.
DR H-InvDB; HIX0034784; -.
DR HGNC; HGNC:1862; CER1.
DR HPA; HPA019917; -.
DR MIM; 603777; gene.
DR neXtProt; NX_O95813; -.
DR PharmGKB; PA26417; -.
DR eggNOG; NOG40714; -.
DR HOGENOM; HOG000231309; -.
DR HOVERGEN; HBG050902; -.
DR InParanoid; O95813; -.
DR KO; K01645; -.
DR OMA; CFGKCGS; -.
DR OrthoDB; EOG7VX8X6; -.
DR PhylomeDB; O95813; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR GeneWiki; Cerberus_(protein); -.
DR GenomeRNAi; 9350; -.
DR NextBio; 35013; -.
DR PRO; PR:O95813; -.
DR Bgee; O95813; -.
DR CleanEx; HS_CER1; -.
DR Genevestigator; O95813; -.
DR GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
DR GO; GO:0036122; F:BMP binding; IDA:BHF-UCL.
DR GO; GO:0016015; F:morphogen activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
DR GO; GO:0030282; P:bone mineralization; IMP:BHF-UCL.
DR GO; GO:0042074; P:cell migration involved in gastrulation; ISS:BHF-UCL.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISS:BHF-UCL.
DR GO; GO:0048263; P:determination of dorsal identity; IMP:BHF-UCL.
DR GO; GO:0003419; P:growth plate cartilage chondrocyte proliferation; ISS:BHF-UCL.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:BHF-UCL.
DR GO; GO:2000381; P:negative regulation of mesoderm development; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IMP:BHF-UCL.
DR GO; GO:0035582; P:sequestering of BMP in extracellular matrix; IDA:BHF-UCL.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR InterPro; IPR016860; Cerberus.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR004133; DAN.
DR Pfam; PF03045; DAN; 1.
DR PIRSF; PIRSF027807; Cerberus; 1.
DR SMART; SM00041; CT; 1.
DR PROSITE; PS01185; CTCK_1; FALSE_NEG.
DR PROSITE; PS01225; CTCK_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Polymorphism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 17
FT CHAIN 18 267 Cerberus.
FT /FTId=PRO_0000006711.
FT DOMAIN 162 246 CTCK.
FT CARBOHYD 26 26 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 222 222 N-linked (GlcNAc...) (Potential).
FT DISULFID 162 209 By similarity.
FT DISULFID 176 223 By similarity.
FT DISULFID 186 239 By similarity.
FT DISULFID 190 241 By similarity.
FT VARIANT 19 19 R -> W (in dbSNP:rs10115703).
FT /FTId=VAR_021591.
FT VARIANT 65 65 A -> G (in dbSNP:rs3747532).
FT /FTId=VAR_021592.
FT VARIANT 179 179 V -> I (in dbSNP:rs7036635).
FT /FTId=VAR_021593.
FT CONFLICT 57 57 F -> L (in Ref. 4; AAH69503).
FT CONFLICT 221 221 L -> V (in Ref. 4; AAH69405).
SQ SEQUENCE 267 AA; 30084 MW; C9FB048CD8558ED7 CRC64;
MHLLLFQLLV LLPLGKTTRH QDGRQNQSSL SPVLLPRNQR ELPTGNHEEA EEKPDLFVAV
PHLVATSPAG EGQRQREKML SRFGRFWKKP EREMHPSRDS DSEPFPPGTQ SLIQPIDGMK
MEKSPLREEA KKFWHHFMFR KTPASQGVIL PIKSHEVHWE TCRTVPFSQT ITHEGCEKVV
VQNNLCFGKC GSVHFPGAAQ HSHTSCSHCL PAKFTTMHLP LNCTELSSVI KVVMLVEECQ
CKVKTEHEDG HILHAGSQDS FIPGVSA
//
MIM
603777
*RECORD*
*FIELD* NO
603777
*FIELD* TI
*603777 CERBERUS 1 HOMOLOG, CYSTINE KNOT SUPERFAMILY; CER1
;;CERBERUS, XENOPUS, HOMOLOG OF, 1
read more*FIELD* TX
The Xenopus 'cerberus' (Xcer) gene product is a cytokine expressed in
anterior mesendoderm of gastrula-stage embryos. When misexpressed in
blastomeres, Xcer can induce the formation of ectopic heads. Biben et
al. (1998) stated that Xcer, which has the characteristics of both a BMP
(bone morphogenetic protein; see 112265) and a Wnt (see 164820)
inhibitor, may act by freeing the prospective head region of the
influence of these ventralizing factors. Both Biben et al. (1998) and
Shawlot et al. (1998) identified the mouse cerberus gene, designating it
Cer1 and Cerr1, respectively. Biben et al. (1998) found that the mouse
and frog proteins share only 26% identity, with the greatest similarity
seen in a C-terminal cysteine-rich region containing a cystine knot
motif. Cystine knots are the structural backbone of a number of
cytokines, including members of the transforming growth factor-beta
superfamily (see 190180) and BMPs. These authors found that mouse Cer1
is a secreted glycoprotein that forms dimers when expressed in mammalian
cells. Cer1 mimicked the anti-BMP activity of Xcer in Xenopus animal
caps, although with reduced potency. In situ hybridization to early
gastrula mouse embryos revealed that Cer1 expression was restricted to
the anterior primitive endoderm, the tissue thought to initiate head
induction. Expression was also detected in anterior embryonic
mesendoderm, required for regionalization of the cranial central nervous
system, and in the rostral domain of nascent somites. Biben et al.
(1998) concluded that mouse Cer1 shares structural, functional, and
expression characteristics with Xcer and may participate in patterning
the anterior of the embryo and nascent somite region, in part through a
BMP-inhibitory mechanism.
By screening a human genomic library with a mouse Cer1 cDNA, Lah et al.
(1999) cloned the human CER1 gene. The predicted 267-amino acid human
protein is approximately 70% identical to mouse Cer1.
By analysis of an interspecific backcross, Shawlot et al. (1998) mapped
Cerr1 to the central portion of mouse chromosome 4, in a region that
shares homology of synteny with human chromosome 9p22. Lah et al. (1999)
confirmed that the human CER1 gene maps to 9p22 using analysis of a
radiation hybrid panel.
*FIELD* RF
1. Biben, C.; Stanley, E.; Fabri, L.; Kotecha, S.; Rhinn, M.; Drinkwater,
C.; Lah, M.; Wang, C.-C.; Nash, A.; Hilton, D.; Ang, S.-L.; Mohun,
T.; Harvey, R. P.: Murine cerberus homologue mCer-1: a candidate
anterior patterning molecule. Dev. Biol. 194: 135-151, 1998.
2. Lah, M.; Brodnicki, T.; Maccarone, P.; Nash, A.; Stanley, E.; Harvey,
R. P.: Human cerberus related gene CER1 maps to chromosome 9. Genomics 55:
364-366, 1999.
3. Shawlot, W.; Deng, J. M.; Behringer, R. R.: Expression of the
mouse cerberus-related gene, Cerr1, suggests a role in anterior neural
induction and somitogenesis. Proc. Nat. Acad. Sci. 95: 6198-6203,
1998.
*FIELD* CD
Rebekah S. Rasooly: 4/27/1999
*FIELD* ED
terry: 07/27/2007
carol: 4/17/2006
mgross: 12/8/2004
alopez: 4/27/1999
*RECORD*
*FIELD* NO
603777
*FIELD* TI
*603777 CERBERUS 1 HOMOLOG, CYSTINE KNOT SUPERFAMILY; CER1
;;CERBERUS, XENOPUS, HOMOLOG OF, 1
read more*FIELD* TX
The Xenopus 'cerberus' (Xcer) gene product is a cytokine expressed in
anterior mesendoderm of gastrula-stage embryos. When misexpressed in
blastomeres, Xcer can induce the formation of ectopic heads. Biben et
al. (1998) stated that Xcer, which has the characteristics of both a BMP
(bone morphogenetic protein; see 112265) and a Wnt (see 164820)
inhibitor, may act by freeing the prospective head region of the
influence of these ventralizing factors. Both Biben et al. (1998) and
Shawlot et al. (1998) identified the mouse cerberus gene, designating it
Cer1 and Cerr1, respectively. Biben et al. (1998) found that the mouse
and frog proteins share only 26% identity, with the greatest similarity
seen in a C-terminal cysteine-rich region containing a cystine knot
motif. Cystine knots are the structural backbone of a number of
cytokines, including members of the transforming growth factor-beta
superfamily (see 190180) and BMPs. These authors found that mouse Cer1
is a secreted glycoprotein that forms dimers when expressed in mammalian
cells. Cer1 mimicked the anti-BMP activity of Xcer in Xenopus animal
caps, although with reduced potency. In situ hybridization to early
gastrula mouse embryos revealed that Cer1 expression was restricted to
the anterior primitive endoderm, the tissue thought to initiate head
induction. Expression was also detected in anterior embryonic
mesendoderm, required for regionalization of the cranial central nervous
system, and in the rostral domain of nascent somites. Biben et al.
(1998) concluded that mouse Cer1 shares structural, functional, and
expression characteristics with Xcer and may participate in patterning
the anterior of the embryo and nascent somite region, in part through a
BMP-inhibitory mechanism.
By screening a human genomic library with a mouse Cer1 cDNA, Lah et al.
(1999) cloned the human CER1 gene. The predicted 267-amino acid human
protein is approximately 70% identical to mouse Cer1.
By analysis of an interspecific backcross, Shawlot et al. (1998) mapped
Cerr1 to the central portion of mouse chromosome 4, in a region that
shares homology of synteny with human chromosome 9p22. Lah et al. (1999)
confirmed that the human CER1 gene maps to 9p22 using analysis of a
radiation hybrid panel.
*FIELD* RF
1. Biben, C.; Stanley, E.; Fabri, L.; Kotecha, S.; Rhinn, M.; Drinkwater,
C.; Lah, M.; Wang, C.-C.; Nash, A.; Hilton, D.; Ang, S.-L.; Mohun,
T.; Harvey, R. P.: Murine cerberus homologue mCer-1: a candidate
anterior patterning molecule. Dev. Biol. 194: 135-151, 1998.
2. Lah, M.; Brodnicki, T.; Maccarone, P.; Nash, A.; Stanley, E.; Harvey,
R. P.: Human cerberus related gene CER1 maps to chromosome 9. Genomics 55:
364-366, 1999.
3. Shawlot, W.; Deng, J. M.; Behringer, R. R.: Expression of the
mouse cerberus-related gene, Cerr1, suggests a role in anterior neural
induction and somitogenesis. Proc. Nat. Acad. Sci. 95: 6198-6203,
1998.
*FIELD* CD
Rebekah S. Rasooly: 4/27/1999
*FIELD* ED
terry: 07/27/2007
carol: 4/17/2006
mgross: 12/8/2004
alopez: 4/27/1999