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Q99217 (AMELX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amelogenin, X isoform
Gene names
Name:AMELX
Synonyms:AMG, AMGX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Developmental stage

Transiently but abundantly expressed by ameloblasts during tooth development. Amelogenin is the predominant protein in developing dental enamel.

Involvement in disease

Amelogenesis imperfecta 1E (AI1E) [MIM:301200]: A X-linked defect of dental enamel formation. Teeth have only a thin layer of enamel with normal hardness. The thinness of the enamel makes the teeth appear small.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the amelogenin family.

Ontologies

Keywords
   Biological processBiomineralization
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DiseaseAmelogenesis imperfecta
Disease mutation
   DomainRepeat
Signal
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbiomineral tissue development

Traceable author statement Ref.5. Source: BHF-UCL

cell adhesion

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

cell proliferation

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

chondrocyte differentiation

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

enamel mineralization

Inferred from mutant phenotype PubMed 1916828. Source: BHF-UCL

epithelial to mesenchymal transition

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

ion homeostasis

Traceable author statement Ref.5. Source: BHF-UCL

odontogenesis of dentin-containing tooth

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

osteoblast differentiation

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

positive regulation of collagen biosynthetic process

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

positive regulation of tooth mineralization

Traceable author statement Ref.5. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 16674683. Source: BHF-UCL

tooth mineralization

Inferred from mutant phenotype PubMed 1483698. Source: BHF-UCL

   Cellular_componentcell surface

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

proteinaceous extracellular matrix

Inferred from direct assay Ref.5. Source: BHF-UCL

   Molecular_functiongrowth factor activity

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

hydroxyapatite binding

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

identical protein binding

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

protein binding

Inferred from physical interaction PubMed 18434575. Source: BHF-UCL

structural constituent of tooth enamel

Inferred from direct assay Ref.1Ref.5. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q99217-1)

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.
Isoform 2 (identifier: Q99217-2)

The sequence of this isoform differs from the canonical sequence as follows:
     19-34: Missing.
Isoform 3 (identifier: Q99217-3)

Also known as: Rare;

The sequence of this isoform differs from the canonical sequence as follows:
     34-34: E → ENSHSQAINVDRTAL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.5
Chain17 – 191175Amelogenin, X isoform
PRO_0000001199

Amino acid modifications

Modified residue321Phosphoserine By similarity

Natural variations

Alternative sequence19 – 3416Missing in isoform 2.
VSP_000228
Alternative sequence341E → ENSHSQAINVDRTAL in isoform 3.
VSP_000229
Natural variant41W → S in AI1E. Ref.13
VAR_037581
Natural variant5 – 84ILFA → T in AI1E.
VAR_000559
Natural variant371T → I in AI1E. Ref.10
VAR_037582
Natural variant561P → T in AI1E. Ref.11 Ref.12
VAR_037583

Experimental info

Sequence conflict50 – 512PS → SP AA sequence Ref.5
Sequence conflict1731D → H AA sequence Ref.8
Sequence conflict1911D → VSIF in AAA62826. Ref.7
Sequence conflict1911D → VSIF in CAA32613. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 322C88DA3F7155DC

FASTA19121,603
        10         20         30         40         50         60 
MGTWILFACL LGAAFAMPLP PHPGHPGYIN FSYEVLTPLK WYQSIRPPYP SYGYEPMGGW 

        70         80         90        100        110        120 
LHHQIIPVLS QQHPPTHTLQ PHHHIPVVPA QQPVIPQQPM MPVPGQHSMT PIQHHQPNLP 

       130        140        150        160        170        180 
PPAQQPYQPQ PVQPQPHQPM QPQPPVHPMQ PLPPQPPLPP MFPMQPLPPM LPDLTLEAWP 

       190 
STDKTKREEV D 

« Hide

Isoform 2 [UniParc].

Checksum: 214D3018D9B50F1B
Show »

FASTA17519,796
Isoform 3 (Rare) [UniParc].

Checksum: 535F5454018E3D6E
Show »

FASTA20523,111

References

« Hide 'large scale' references
[1]"The human enamel protein gene amelogenin is expressed from both the X and the Y chromosomes."
Salido E.C., Yen P.H., Koprivnikar K., Yu L.-C., Shapiro L.J.
Am. J. Hum. Genet. 50:303-316(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Tooth bud.
[2]"A nomenclature for X-linked amelogenesis imperfecta."
Hart P.S., Hart T.C., Simmer J.P., Wright J.T.
Arch. Oral Biol. 47:255-260(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [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] (ISOFORM 1).
[5]"Human amelogenins: sequences of 'TRAP' molecules."
Fincham A.G., Hu Y., Pavlova Z., Slavkin H.C., Snead M.L.
Calcif. Tissue Int. 45:243-250(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-60.
[6]"Production of a monoclonal antibody against human amelogenin."
Catalano-Sherman J., Laskov R., Palmon A., David S., Deutsch D.
Calcif. Tissue Int. 54:76-80(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-37.
[7]"A human X-Y homologous region encodes 'amelogenin'."
Nakahori Y., Takenaka O., Nakagome Y.
Genomics 9:264-269(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-191 (ISOFORM 1).
[8]"Amino acid sequence of a major human amelogenin protein employing Edman degradation and cDNA sequencing."
Catalano-Sherman J., Palmon A., Burstein Y., Deutsch D.
J. Dent. Res. 72:1566-1572(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-190, PARTIAL PROTEIN SEQUENCE.
Tissue: Tooth bud.
[9]"Amelogenin signal peptide mutation: correlation between mutations in the amelogenin gene (AMGX) and manifestations of X-linked amelogenesis imperfecta."
Lagerstroem-Fermer M., Nilddon M., Baeckman B., Salido E., Shapiro L., Pettersson U., Landergren U.
Genomics 26:159-162(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AI1E 5-ILE--ALA-8 DELINS THR.
[10]"Characterisation of molecular defects in X-linked amelogenesis imperfecta (AIH1)."
Lench N.J., Winter G.B.
Hum. Mutat. 5:251-259(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AI1E ILE-37.
[11]"Mutational analysis of X-linked amelogenesis imperfecta in multiple families."
Hart S., Hart T., Gibson C., Wright J.T.
Arch. Oral Biol. 45:79-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AI1E THR-56.
[12]"An amelogenin gene defect associated with human X-linked amelogenesis imperfecta."
Collier P.M., Sauk J.J., Rosenbloom S.J., Yuan Z.A., Gibson C.W.
Arch. Oral Biol. 42:235-242(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AI1E THR-56.
[13]"Amelogenin p.M1T and p.W4S mutations underlying hypoplastic X-linked amelogenesis imperfecta."
Kim J.-W., Simmer J.P., Hu Y.Y., Lin B.P.-L., Boyd C., Wright J.T., Yamada C.J.M., Rayes S.K., Feigal R.J., Hu J.C.-C.
J. Dent. Res. 83:378-383(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AI1E SER-4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86932 mRNA. Translation: AAA51717.1.
AF436849 mRNA. Translation: AAL30432.1.
AY040206 Genomic DNA. Translation: AAK77213.1.
AC002366 Genomic DNA. Translation: AAC21581.1.
BC074951 mRNA. Translation: AAH74951.1.
M55418 Genomic DNA. Translation: AAA62826.1.
X14440 Genomic DNA. Translation: CAA32613.1.
S67147 mRNA. Translation: AAB29184.1.
CCDSCCDS14144.1. [Q99217-1]
CCDS14145.1. [Q99217-3]
CCDS14146.1. [Q99217-2]
PIRA41816. B41816.
RefSeqNP_001133.1. NM_001142.2. [Q99217-1]
NP_872621.1. NM_182680.1. [Q99217-3]
NP_872622.1. NM_182681.1. [Q99217-2]
UniGeneHs.654436.

3D structure databases

ProteinModelPortalQ99217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000370088.

Polymorphism databases

DMDM1168430.

Proteomic databases

PRIDEQ99217.

Protocols and materials databases

DNASU265.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348912; ENSP00000335312; ENSG00000125363. [Q99217-2]
ENST00000380712; ENSP00000370088; ENSG00000125363. [Q99217-3]
ENST00000380714; ENSP00000370090; ENSG00000125363. [Q99217-1]
GeneID265.
KEGGhsa:265.
UCSCuc004cus.3. human. [Q99217-3]
uc004cut.3. human. [Q99217-1]
uc004cuu.3. human. [Q99217-2]

Organism-specific databases

CTD265.
GeneCardsGC0XP011221.
H-InvDBHIX0176766.
HGNCHGNC:461. AMELX.
HPAHPA005988.
MIM300391. gene.
301200. phenotype.
neXtProtNX_Q99217.
Orphanet100033. Hypomaturation amelogenesis imperfecta.
PharmGKBPA24766.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69988.
HOGENOMHOG000231643.
HOVERGENHBG016835.
OMAHSMTPTQ.
OrthoDBEOG7JQBQ8.
PhylomeDBQ99217.
TreeFamTF337092.

Gene expression databases

ArrayExpressQ99217.
BgeeQ99217.
CleanExHS_AMELX.
GenevestigatorQ99217.

Family and domain databases

InterProIPR004116. Amelogenin.
[Graphical view]
PfamPF02948. Amelogenin. 1 hit.
[Graphical view]
PRINTSPR01757. AMELOGENIN.
SMARTSM00818. Amelogenin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAMELX.
GenomeRNAi265.
NextBio1037.
PMAP-CutDBQ99217.
PROQ99217.
SOURCESearch...

Entry information

Entry nameAMELX_HUMAN
AccessionPrimary (citable) accession number: Q99217
Secondary accession number(s): Q96NW6, Q9UCA7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 138 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 X

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