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Protein

Odontogenic ameloblast-associated protein

Gene

ODAM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process.

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. odontogenesis of dentin-containing tooth Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Biomineralization

Enzyme and pathway databases

ReactomeiREACT_75925. Amyloids.

Names & Taxonomyi

Protein namesi
Recommended name:
Odontogenic ameloblast-associated protein
Alternative name(s):
Apin
Gene namesi
Name:ODAM
Synonyms:APIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:26043. ODAM.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. extracellular region Source: Reactome
  3. fibril Source: UniProtKB
  4. nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148342.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 279264Odontogenic ameloblast-associated proteinPRO_5000183879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi115 – 1151O-linked (GalNAc...)Sequence Analysis
Glycosylationi119 – 1191O-linked (GalNAc...)Sequence Analysis
Glycosylationi244 – 2441O-linked (GalNAc...)Sequence Analysis
Glycosylationi249 – 2491O-linked (GalNAc...)Sequence Analysis
Glycosylationi250 – 2501O-linked (GalNAc...)Sequence Analysis
Glycosylationi251 – 2511O-linked (GalNAc...)Sequence Analysis
Glycosylationi255 – 2551O-linked (GalNAc...)Sequence Analysis
Glycosylationi256 – 2561O-linked (GalNAc...)Sequence Analysis
Glycosylationi261 – 2611O-linked (GalNAc...)Sequence Analysis
Glycosylationi263 – 2631O-linked (GalNAc...)Sequence Analysis
Glycosylationi273 – 2731O-linked (GalNAc...)Sequence Analysis
Glycosylationi275 – 2751O-linked (GalNAc...)Sequence Analysis

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiA1E959.

Expressioni

Gene expression databases

BgeeiA1E959.
CleanExiHS_ODAM.
ExpressionAtlasiA1E959. baseline and differential.
GenevestigatoriA1E959.

Interactioni

Protein-protein interaction databases

BioGridi120297. 2 interactions.
IntActiA1E959. 2 interactions.
STRINGi9606.ENSP00000379401.

Structurei

3D structure databases

ProteinModelPortaliA1E959.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 206145Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the ODAM family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG74202.
GeneTreeiENSGT00390000011100.
HOGENOMiHOG000115257.
HOVERGENiHBG096669.
InParanoidiA1E959.
OMAiNSWIPPF.
OrthoDBiEOG7673CG.
PhylomeDBiA1E959.
TreeFamiTF338424.

Family and domain databases

InterProiIPR026802. Odam.
[Graphical view]
PANTHERiPTHR16237. PTHR16237. 1 hit.
PfamiPF15424. ODAM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A1E959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIIILLGFL GATLSAPLIP QRLMSASNSN ELLLNLNNGQ LLPLQLQGPL
60 70 80 90 100
NSWIPPFSGI LQQQQQAQIP GLSQFSLSAL DQFAGLLPNQ IPLTGEASFA
110 120 130 140 150
QGAQAGQVDP LQLQTPPQTQ PGPSHVMPYV FSFKMPQEQG QMFQYYPVYM
160 170 180 190 200
VLPWEQPQQT VPRSPQQTRQ QQYEEQIPFY AQFGYIPQLA EPAISGGQQQ
210 220 230 240 250
LAFDPQLGTA PEIAVMSTGE EIPYLQKEAI NFRHDSAGVF MPSTSPKPST
260 270
TNVFTSAVDQ TITPELPEEK DKTDSLREP
Length:279
Mass (Da):30,777
Last modified:January 22, 2007 - v1
Checksum:iDE0E42076B572318
GO

Sequence cautioni

The sequence BAA91226.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti222 – 2221I → T.1 Publication
Corresponds to variant rs3196714 [ dbSNP | Ensembl ].
VAR_039812
Natural varianti269 – 2691E → D in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_039813

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF113908 mRNA. Translation: ABL11577.1.
CH471057 Genomic DNA. Translation: EAX05612.1.
AK000520 mRNA. Translation: BAA91226.1. Different initiation.
BC017796 mRNA. Translation: AAH17796.1.
CCDSiCCDS3536.2.
RefSeqiNP_060325.3. NM_017855.3.
UniGeneiHs.143811.

Genome annotation databases

EnsembliENST00000396094; ENSP00000379401; ENSG00000109205.
GeneIDi54959.
KEGGihsa:54959.
UCSCiuc003hfc.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF113908 mRNA. Translation: ABL11577.1.
CH471057 Genomic DNA. Translation: EAX05612.1.
AK000520 mRNA. Translation: BAA91226.1. Different initiation.
BC017796 mRNA. Translation: AAH17796.1.
CCDSiCCDS3536.2.
RefSeqiNP_060325.3. NM_017855.3.
UniGeneiHs.143811.

3D structure databases

ProteinModelPortaliA1E959.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120297. 2 interactions.
IntActiA1E959. 2 interactions.
STRINGi9606.ENSP00000379401.

Proteomic databases

PRIDEiA1E959.

Protocols and materials databases

DNASUi54959.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396094; ENSP00000379401; ENSG00000109205.
GeneIDi54959.
KEGGihsa:54959.
UCSCiuc003hfc.3. human.

Organism-specific databases

CTDi54959.
GeneCardsiGC04P071062.
HGNCiHGNC:26043. ODAM.
MIMi614843. gene.
neXtProtiNX_A1E959.
PharmGKBiPA145148342.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG74202.
GeneTreeiENSGT00390000011100.
HOGENOMiHOG000115257.
HOVERGENiHBG096669.
InParanoidiA1E959.
OMAiNSWIPPF.
OrthoDBiEOG7673CG.
PhylomeDBiA1E959.
TreeFamiTF338424.

Enzyme and pathway databases

ReactomeiREACT_75925. Amyloids.

Miscellaneous databases

GeneWikiiODAM_(gene).
GenomeRNAii54959.
NextBioi58156.
PROiA1E959.
SOURCEiSearch...

Gene expression databases

BgeeiA1E959.
CleanExiHS_ODAM.
ExpressionAtlasiA1E959. baseline and differential.
GenevestigatoriA1E959.

Family and domain databases

InterProiIPR026802. Odam.
[Graphical view]
PANTHERiPTHR16237. PTHR16237. 1 hit.
PfamiPF15424. ODAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Moffatt P., Smith C.E., Nanci A.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-279, VARIANT THR-222.
    Tissue: Carcinoma.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-279.
    Tissue: Lung.
  5. "Calcifying epithelial odontogenic (Pindborg) tumor-associated amyloid consists of a novel human protein."
    Solomon A., Murphy C.L., Weaver K., Weiss D.T., Hrncic R., Eulitz M., Donnell R.L., Sletten K., Westermark G., Westermark P.
    J. Lab. Clin. Med. 142:348-355(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INVOLVEMENT IN CEOT.
  6. "Characterization of Apin, a secreted protein highly expressed in tooth-associated epithelia."
    Moffatt P., Smith C.E., St Arnaud R., Nanci A.
    J. Cell. Biochem. 103:941-956(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-269.

Entry informationi

Entry nameiODAM_HUMAN
AccessioniPrimary (citable) accession number: A1E959
Secondary accession number(s): Q8WWE5, Q9NWZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 17, 2008
Last sequence update: January 22, 2007
Last modified: February 3, 2015
This is version 67 of the entry and version 1 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

Miscellaneous

ODAM protein is the unique constituent of calcifying epithelial odontogenic tumors (CEOTs), also known as Pindborg tumors. CEOTs are benign but locally aggressive pathologic entities arising mainly in the mandible and commonly associated with an unerupted or embedded tooth. They are characterized by the presence of squamous-cell proliferation, calcification, and, notably, amyloid deposits.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.