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Protein

Craniofacial development protein 1

Gene

Cfdp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role during embryogenesis. May modulate tooth organogenesis since alterations of this protein function affect tooth organs size as well as individual cell fate and survival. In embryonic cells, blockage of the function results in increased number of apoptotic cells, reduced proliferation, alterations in cell shape and fibronection matrix synthesis.3 Publications

GO - Biological processi

  • cell adhesion Source: MGI
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of fibroblast apoptotic process Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of cell shape Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Craniofacial development protein 1
Alternative name(s):
27 kDa craniofacial protein
Bucentaur
Protein Cp27
Gene namesi
Name:Cfdp1
Synonyms:Bcnt, Cfdp, Cp27
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1344403. Cfdp1.

Subcellular locationi

  • Chromosomecentromerekinetochore By similarity

GO - Cellular componenti

  • basement membrane Source: MGI
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Craniofacial development protein 1PRO_0000212495Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801PhosphoserineBy similarity
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei84 – 841PhosphoserineBy similarity
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei246 – 2461PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO88271.
MaxQBiO88271.
PaxDbiO88271.
PeptideAtlasiO88271.
PRIDEiO88271.

PTM databases

iPTMnetiO88271.
PhosphoSiteiO88271.

Expressioni

Tissue specificityi

Expressed in lung, liver and heart, with higher expression in teeth.1 Publication

Developmental stagei

Detected at E8 in developing organs, including brain, heart, lung and intestines. Expressed at E14 and E16 at the periphery of developing organs such as bones and teeth.1 Publication

Gene expression databases

BgeeiO88271.
CleanExiMM_CFDP1.
GenevisibleiO88271. MM.

Interactioni

Protein-protein interaction databases

IntActiO88271. 2 interactions.
MINTiMINT-4105417.
STRINGi10090.ENSMUSP00000034432.

Structurei

3D structure databases

ProteinModelPortaliO88271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 29582BCNT-CPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 21340HydrophilicAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 108107Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 BCNT-C domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4776. Eukaryota.
ENOG4111H9K. LUCA.
GeneTreeiENSGT00390000018141.
HOGENOMiHOG000247045.
HOVERGENiHBG081120.
InParanoidiO88271.
OMAiAGFENSG.
OrthoDBiEOG7FZ01C.
PhylomeDBiO88271.
TreeFamiTF313182.

Family and domain databases

InterProiIPR011421. BCNT-C.
IPR027124. Swc5/CFDP.
[Graphical view]
PANTHERiPTHR23227. PTHR23227. 1 hit.
PfamiPF07572. BCNT. 1 hit.
[Graphical view]
PROSITEiPS51279. BCNT_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEFDSEDFS TSDEDEDYLP SGGEYSEDDV NELVKEDEVD GEEQAEKTKG
60 70 80 90 100
KRRKAQGIPA RKRKQSGLLL EEEEDGKEDS GGSSSEEDEE EQEGGLGSEN
110 120 130 140 150
ARKKKEDELW ASFLNDVGPK SKAAPGSQTK VAEETEEISS NKPLVKADEL
160 170 180 190 200
DKPRESEKVK ITKVFDFAGE EVRVTKEVDA ASKEAKSFLK QTEREKPQAL
210 220 230 240 250
VTSPATPLPA GSGIKRASGM SSLLGKIGAK KQKMSTLEKS KLDWESFKEE
260 270 280 290
EGIGEELAIH NRGKEGYIER KAFLDRVDHR QFEIERDLRL SKMKP
Length:295
Mass (Da):32,921
Last modified:November 1, 1998 - v1
Checksum:i245D161EA56F9DB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941G → A in CAA69396 (PubMed:10415329).Curated
Sequence conflicti264 – 2641K → E in CAA69396 (PubMed:10415329).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010828 mRNA. Translation: BAA31696.1.
Y08219 mRNA. Translation: CAA69396.1.
AK160532 mRNA. Translation: BAE35849.1.
AK133989 mRNA. Translation: BAE21971.1.
BC005589 mRNA. Translation: AAH05589.1.
AB033766 Genomic DNA. Translation: BAA94844.1.
CCDSiCCDS22680.1.
RefSeqiNP_035931.1. NM_011801.1.
UniGeneiMm.279437.

Genome annotation databases

EnsembliENSMUST00000034432; ENSMUSP00000034432; ENSMUSG00000031954.
GeneIDi23837.
KEGGimmu:23837.
UCSCiuc009nmx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010828 mRNA. Translation: BAA31696.1.
Y08219 mRNA. Translation: CAA69396.1.
AK160532 mRNA. Translation: BAE35849.1.
AK133989 mRNA. Translation: BAE21971.1.
BC005589 mRNA. Translation: AAH05589.1.
AB033766 Genomic DNA. Translation: BAA94844.1.
CCDSiCCDS22680.1.
RefSeqiNP_035931.1. NM_011801.1.
UniGeneiMm.279437.

3D structure databases

ProteinModelPortaliO88271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88271. 2 interactions.
MINTiMINT-4105417.
STRINGi10090.ENSMUSP00000034432.

PTM databases

iPTMnetiO88271.
PhosphoSiteiO88271.

Proteomic databases

EPDiO88271.
MaxQBiO88271.
PaxDbiO88271.
PeptideAtlasiO88271.
PRIDEiO88271.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034432; ENSMUSP00000034432; ENSMUSG00000031954.
GeneIDi23837.
KEGGimmu:23837.
UCSCiuc009nmx.1. mouse.

Organism-specific databases

CTDi10428.
MGIiMGI:1344403. Cfdp1.

Phylogenomic databases

eggNOGiKOG4776. Eukaryota.
ENOG4111H9K. LUCA.
GeneTreeiENSGT00390000018141.
HOGENOMiHOG000247045.
HOVERGENiHBG081120.
InParanoidiO88271.
OMAiAGFENSG.
OrthoDBiEOG7FZ01C.
PhylomeDBiO88271.
TreeFamiTF313182.

Miscellaneous databases

ChiTaRSiCfdp1. mouse.
PROiO88271.
SOURCEiSearch...

Gene expression databases

BgeeiO88271.
CleanExiMM_CFDP1.
GenevisibleiO88271. MM.

Family and domain databases

InterProiIPR011421. BCNT-C.
IPR027124. Swc5/CFDP.
[Graphical view]
PANTHERiPTHR23227. PTHR23227. 1 hit.
PfamiPF07572. BCNT. 1 hit.
[Graphical view]
PROSITEiPS51279. BCNT_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Existence of a bovine LINE repetitive insert that appears in the cDNA of bovine protein BCNT in ruminant, but not in human, genomes."
    Takahashi I., Nobukuni T., Ohmori H., Kobayashi M., Tanaka S., Ohshima K., Okada N., Masui T., Hashimoto K., Iwashita S.
    Gene 211:387-394(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning, gene expression, and characterization of CP27, a novel gene in mouse embryogenesis."
    Diekwisch T.G.H., Marches F., Williams A., Luan X.
    Gene 235:19-30(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Gene organization of bovine BCNT that contains a portion corresponding to an endonuclease domain derived from an RTE-1 (Bov-B LINE), non-LTR retrotransposable element: duplication of an intramolecular repeat unit downstream of the truncated RTE-1."
    Iwashita S., Itoh T., Takeda H., Sugimoto Y., Takahashi I., Nobukuni T., Sezaki M., Masui T., Hashimoto K.
    Gene 268:59-66(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266.
    Strain: 129/SvJ.
  6. "CP27 function is necessary for cell survival and differentiation during tooth morphogenesis in organ culture."
    Diekwisch T.G.H., Luan X.
    Gene 287:141-147(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "CP27 affects viability, proliferation, attachment and gene expression in embryonic fibroblasts."
    Luan X., Diekwisch T.G.H.
    Cell Prolif. 35:207-219(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCFDP1_MOUSE
AccessioniPrimary (citable) accession number: O88271
Secondary accession number(s): O70565, Q9JMA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.