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O95813 (CER1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cerberus
Alternative name(s):
Cerberus-related protein
DAN domain family member 4
Gene names
Name:CER1
Synonyms:DAND4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak By similarity.

Subunit structure

Forms monomers and predominantly dimers By similarity.

Subcellular location

Secreted Probable.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the DAN family.

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Sequence caution

The sequence AAH69503.1 differs from that shown. Reason: Erroneous termination at position 266. Translated as Ser.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionCytokine
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Traceable author statement. Source: Reactome

anterior/posterior axis specification

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

anterior/posterior pattern specification

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

bone mineralization

Inferred from mutant phenotype PubMed 19113921. Source: BHF-UCL

cell migration involved in gastrulation

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

cellular response to BMP stimulus

Inferred from sequence or structural similarity PubMed 16798745. Source: BHF-UCL

determination of dorsal identity

Inferred from mutant phenotype PubMed 9660951. Source: BHF-UCL

gastrulation

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

growth plate cartilage chondrocyte proliferation

Inferred from sequence or structural similarity PubMed 19113921. Source: BHF-UCL

negative regulation of BMP signaling pathway

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

negative regulation of activin receptor signaling pathway

Inferred from direct assay PubMed 9660951. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

negative regulation of mesoderm development

Inferred from mutant phenotype PubMed 9660951. Source: BHF-UCL

nervous system development

Inferred from mutant phenotype PubMed 9660951. Source: BHF-UCL

sequestering of BMP in extracellular matrix

Inferred from direct assay PubMed 9660951. Source: BHF-UCL

signal transduction involved in regulation of gene expression

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

ureteric bud development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

extracellular space

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionBMP binding

Inferred from direct assay PubMed 9660951. Source: BHF-UCL

morphogen activity

Inferred from direct assay PubMed 9660951. Source: BHF-UCL

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.5
Chain18 – 267250Cerberus
PRO_0000006711

Regions

Domain162 – 24685CTCK

Amino acid modifications

Glycosylation261N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Disulfide bond162 ↔ 209 By similarity
Disulfide bond176 ↔ 223 By similarity
Disulfide bond186 ↔ 239 By similarity
Disulfide bond190 ↔ 241 By similarity

Natural variations

Natural variant191R → W. Ref.4
Corresponds to variant rs10115703 [ dbSNP | Ensembl ].
VAR_021591
Natural variant651A → G. Ref.4
Corresponds to variant rs3747532 [ dbSNP | Ensembl ].
VAR_021592
Natural variant1791V → I. Ref.4
Corresponds to variant rs7036635 [ dbSNP | Ensembl ].
VAR_021593

Experimental info

Sequence conflict571F → L in AAH69503. Ref.4
Sequence conflict2211L → V in AAH69405. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O95813 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C9FB048CD8558ED7

FASTA26730,084
        10         20         30         40         50         60 
MHLLLFQLLV LLPLGKTTRH QDGRQNQSSL SPVLLPRNQR ELPTGNHEEA EEKPDLFVAV 

        70         80         90        100        110        120 
PHLVATSPAG EGQRQREKML SRFGRFWKKP EREMHPSRDS DSEPFPPGTQ SLIQPIDGMK 

       130        140        150        160        170        180 
MEKSPLREEA KKFWHHFMFR KTPASQGVIL PIKSHEVHWE TCRTVPFSQT ITHEGCEKVV 

       190        200        210        220        230        240 
VQNNLCFGKC GSVHFPGAAQ HSHTSCSHCL PAKFTTMHLP LNCTELSSVI KVVMLVEECQ 

       250        260 
CKVKTEHEDG HILHAGSQDS FIPGVSA 

« Hide

References

« Hide 'large scale' references
[1]"Human cerberus related gene CER1 maps to chromosome 9."
Lah M., Brodnicki T., Maccarone P., Nash A., Stanley E., Harvey R.P.
Genomics 55:364-366(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[2]Feng Z., Zhang B., Peng X., Yuan J., Qiang B.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANTS TRP-19; GLY-65 AND ILE-179.
[5]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-32.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090189 Genomic DNA. Translation: AAD19879.1.
AF400435 mRNA. Translation: AAK92484.1.
AL390732 Genomic DNA. Translation: CAH73850.1.
BC069371 mRNA. Translation: AAH69371.1.
BC069405 mRNA. Translation: AAH69405.1.
BC069491 mRNA. Translation: AAH69491.1.
BC069503 mRNA. Translation: AAH69503.1. Sequence problems.
CCDSCCDS6476.1.
RefSeqNP_005445.1. NM_005454.2.
UniGeneHs.248204.

3D structure databases

ProteinModelPortalO95813.
SMRO95813. Positions 155-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000370297.

PTM databases

PhosphoSiteO95813.

Proteomic databases

PaxDbO95813.
PRIDEO95813.

Protocols and materials databases

DNASU9350.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380911; ENSP00000370297; ENSG00000147869.
GeneID9350.
KEGGhsa:9350.
UCSCuc003zlj.3. human.

Organism-specific databases

CTD9350.
GeneCardsGC09M014710.
H-InvDBHIX0034784.
HGNCHGNC:1862. CER1.
HPAHPA019917.
MIM603777. gene.
neXtProtNX_O95813.
PharmGKBPA26417.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40714.
HOGENOMHOG000231309.
HOVERGENHBG050902.
InParanoidO95813.
KOK01645.
OMACFGKCGS.
OrthoDBEOG7VX8X6.
PhylomeDBO95813.
TreeFamTF106445.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

BgeeO95813.
CleanExHS_CER1.
GenevestigatorO95813.

Family and domain databases

InterProIPR016860. Cerberus.
IPR006207. Cys_knot_C.
IPR004133. DAN.
[Graphical view]
PfamPF03045. DAN. 1 hit.
[Graphical view]
PIRSFPIRSF027807. Cerberus. 1 hit.
SMARTSM00041. CT. 1 hit.
[Graphical view]
PROSITEPS01225. CTCK_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCerberus_(protein).
GenomeRNAi9350.
NextBio35013.
PROO95813.
SOURCESearch...

Entry information

Entry nameCER1_HUMAN
AccessionPrimary (citable) accession number: O95813
Secondary accession number(s): Q6ISJ1 expand/collapse secondary AC list , Q6ISJ6, Q6ISQ2, Q6ISS1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 98 of the entry and version 1 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM