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P04745 (AMY1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase 1

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 1
Salivary alpha-amylase
Gene names
Name:AMY1A
Synonyms:AMY1
AND
Name:AMY1B
Synonyms:AMY1
AND
Name:AMY1C
Synonyms:AMY1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 1 calcium ion per subunit.

Binds 1 chloride ion per subunit.

Subunit structure

Monomer.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MUC7Q8TAX72EBI-738586,EBI-738582

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 511496Alpha-amylase 1
PRO_0000001401

Sites

Active site2121Nucleophile
Active site2481Proton donor
Metal binding1151Calcium
Metal binding1731Calcium; via carbonyl oxygen
Metal binding1821Calcium
Metal binding2161Calcium; via carbonyl oxygen
Binding site2101Chloride
Binding site3131Chloride
Binding site3521Chloride
Site3151Transition state stabilizer By similarity

Amino acid modifications

Modified residue161Pyrrolidone carboxylic acid By similarity
Modified residue3651Deamidated asparagine; partial
Modified residue4271Deamidated asparagine; partial
Modified residue4741Deamidated asparagine; partial
Glycosylation4271N-linked (GlcNAc...); alternate Ref.10
Glycosylation4761N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 101
Disulfide bond85 ↔ 130
Disulfide bond156 ↔ 175
Disulfide bond393 ↔ 399
Disulfide bond465 ↔ 477

Experimental info

Sequence conflict2851N → T in AAA57345. Ref.8

Secondary structure

............................................................................................................ 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04745 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 7710BCAC83EBE8B2

FASTA51157,768
        10         20         30         40         50         60 
MKLFWLLFTI GFCWAQYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP 

        70         80         90        100        110        120 
NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMCGN 

       130        140        150        160        170        180 
AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLSGL 

       190        200        210        220        230        240 
LDLALGKDYV RSKIAEYMNH LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG 

       250        260        270        280        290        300 
SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG 

       310        320        330        340        350        360 
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP 

       370        380        390        400        410        420 
RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE HRWRQIRNMV NFRNVVDGQP 

       430        440        450        460        470        480 
FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT FSLTLQTGLP AGTYCDVISG DKINGNCTGI 

       490        500        510 
KIYVSDDGKA HFSISNSAED PFIAIHAESK L 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human salivary alpha-amylase gene."
Nishide T., Nakamura Y., Emi M., Yamamoto T., Ogawa M., Mori T., Matsubara K.
Gene 41:299-304(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases."
Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S., Matsubara K.
Gene 28:263-270(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Erratum
Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S., Matsubara K.
Gene 50:371-372(1986)
Cited for: SEQUENCE REVISION.
[4]"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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Thyroid.
[7]"Concerted evolution of human amylase genes."
Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C., Meisler M.H.
Mol. Cell. Biol. 8:1197-1205(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56 AND 408-448.
[8]"Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1."
Handy D.E., Larsen S.H., Karn R.C., Hodes M.E.
Mol. Biol. Med. 4:145-155(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293 AND 450-511.
[9]"Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase."
Bank R.A., Hettema E.H., Arwert F., Amerongen A.V., Pronk J.C.
Electrophoresis 12:74-79(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[10]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
Tissue: Saliva.
[11]"Structure of human salivary alpha-amylase at 1.6-A resolution: implications for its role in the oral cavity."
Ramasubbu N., Paloth V., Luo Y., Brayer G.D., Levine M.J.
Acta Crystallogr. D 52:435-446(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[12]"Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase."
Ramasubbu N., Ragunath C., Mishra P.J.
J. Mol. Biol. 325:1061-1076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF WILD-TYPE AND MUTANT 321-GLY--ALA-325 DEL.
+Additional computationally mapped references.

Web resources

Wikipedia

Amylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18786 expand/collapse EMBL AC list , M18715, M18717, M18719, M18721, M18723, M18725, M18727, M18784 Genomic DNA. Translation: AAA52279.1.
AK292341 mRNA. Translation: BAF85030.1.
AL513482 Genomic DNA. Translation: CAI14928.1.
AL513482 Genomic DNA. Translation: CAI14932.1.
BC063129 mRNA. Translation: AAH63129.1.
BC069347 mRNA. Translation: AAH69347.1.
BC069463 mRNA. Translation: AAH69463.1.
BC092444 mRNA. Translation: AAH92444.1.
BC132985 mRNA. Translation: AAI32986.1.
BC132987 mRNA. Translation: AAI32988.1.
BC132995 mRNA. Translation: AAI32996.1.
BC132997 mRNA. Translation: AAI32998.1.
M18671 Genomic DNA. Translation: AAA58368.1.
M18674 Genomic DNA. Translation: AAA16183.2.
M19233, M17883 Genomic DNA. Translation: AAA57345.1. Different termination.
M17884 Genomic DNA. No translation available.
CCDSCCDS30782.1.
CCDS30783.1.
CCDS30784.1.
PIRALHUS. A91543.
RefSeqNP_001008219.1. NM_001008218.1.
NP_001008220.1. NM_001008219.1.
NP_001008222.1. NM_001008221.1.
NP_004029.2. NM_004038.3.
XP_005270812.1. XM_005270755.1.
XP_005270815.1. XM_005270758.1.
XP_005270818.1. XM_005270761.1.
XP_006710642.1. XM_006710579.1.
XP_006710643.1. XM_006710580.1.
XP_006710644.1. XM_006710581.1.
UniGeneHs.599274.
Hs.654437.
Hs.655232.
Hs.662103.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8QX-ray2.30A16-511[»]
1JXJX-ray1.99A16-511[»]
1JXKX-ray1.90A16-511[»]
1MFUX-ray2.00A17-511[»]
1MFVX-ray2.00A17-511[»]
1NM9X-ray2.10A16-511[»]
1Q4NX-ray2.07X16-511[»]
1SMDX-ray1.60A17-511[»]
1XV8X-ray3.00A/B16-511[»]
1Z32X-ray1.60X16-511[»]
3BLKX-ray2.00A16-511[»]
3BLPX-ray1.60X16-511[»]
3DHPX-ray1.50A16-511[»]
ProteinModelPortalP04745.
SMRP04745. Positions 16-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106773. 4 interactions.
106774. 1 interaction.
106775. 1 interaction.
IntActP04745. 2 interactions.
STRING9606.ENSP00000330484.

Chemistry

BindingDBP04745.
ChEMBLCHEMBL2478.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteP04745.
UniCarbKBP04745.

Polymorphism databases

DMDM1351933.

Proteomic databases

MaxQBP04745.
PaxDbP04745.
PeptideAtlasP04745.
PRIDEP04745.

Protocols and materials databases

DNASU277.
278.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330330; ENSP00000330484; ENSG00000174876.
ENST00000370079; ENSP00000359096; ENSG00000187733.
ENST00000370080; ENSP00000359097; ENSG00000174876.
ENST00000370083; ENSP00000359100; ENSG00000237763.
GeneID276.
277.
278.
KEGGhsa:276.
hsa:277.
hsa:278.
UCSCuc001duu.3. human.

Organism-specific databases

CTD276.
277.
278.
GeneCardsGC01M104230.
GC01P104197.
GC01P104292.
HGNCHGNC:474. AMY1A.
HGNC:475. AMY1B.
HGNC:476. AMY1C.
HPACAB004310.
HPA045394.
HPA045399.
HPA046980.
MIM104700. gene.
104701. gene.
104702. gene.
neXtProtNX_P04745.
PharmGKBPA24783.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000253313.
HOVERGENHBG000061.
InParanoidP04745.
KOK01176.
OMAVAINHES.
OrthoDBEOG7RJPR2.
PhylomeDBP04745.
TreeFamTF312850.

Enzyme and pathway databases

BRENDA3.2.1.1. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeP04745.
CleanExHS_AMY1A.
GenevestigatorP04745.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04745.
GeneWikiAMY1A.
NextBio1113.
PROP04745.
SOURCESearch...

Entry information

Entry nameAMY1_HUMAN
AccessionPrimary (citable) accession number: P04745
Secondary accession number(s): A6NJS5 expand/collapse secondary AC list , A8K8H6, Q13763, Q5T083
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 169 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries