P04745 (AMY1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Traceable author statement. Source: ProtInc digestion Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-amylase activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MUC7	Q8TAX7	2	EBI-738586,EBI-738582

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Potential

Chain

16 – 511

496

Alpha-amylase 1

PRO_0000001401

Sites

Active site

212

1

Nucleophile

Active site

248

1

Proton donor

Metal binding

115

1

Calcium

Metal binding

173

1

Calcium; via carbonyl oxygen

Metal binding

182

1

Calcium

Metal binding

216

1

Calcium; via carbonyl oxygen

Binding site

210

1

Chloride

Binding site

313

1

Chloride

Binding site

352

1

Chloride

Site

315

1

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

16

1

Pyrrolidone carboxylic acid

Modified residue

365

1

Deamidated asparagine; partial

Modified residue

427

1

Deamidated asparagine; partial

Modified residue

474

1

Deamidated asparagine; partial

Glycosylation

427

1

N-linked (GlcNAc...) Ref.10

Glycosylation

476

1

N-linked (GlcNAc...) Potential

Disulfide bond

43 ↔ 101

Disulfide bond

85 ↔ 130

Disulfide bond

156 ↔ 175

Disulfide bond

393 ↔ 399

Disulfide bond

465 ↔ 477

Experimental info

Sequence conflict

285

1

N → T in AAA57345. Ref.8

Secondary structure

1

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511

Helix Strand Turn

Details...

Beta strand

27 – 31

5

Helix

36 – 45

10

Turn

46 – 51

6

Beta strand

54 – 58

5

Turn

67 – 70

4

Helix

73 – 77

5

Beta strand

78 – 80

3

Helix

91 – 103

13

Beta strand

107 – 112

6

Beta strand

115 – 119

5

Beta strand

124 – 126

3

Turn

136 – 139

4

Turn

142 – 145

4

Helix

148 – 150

3

Turn

153 – 155

3

Beta strand

158 – 162

5

Helix

169 – 174

6

Beta strand

175 – 177

3

Beta strand

180 – 183

4

Helix

188 – 204

17

Beta strand

208 – 211

4

Helix

214 – 216

3

Helix

219 – 226

8

Turn

234 – 236

3

Beta strand

244 – 247

4

Beta strand

253 – 257

5

Helix

259 – 262

4

Turn

263 – 265

3

Beta strand

266 – 269

4

Helix

271 – 281

11

Helix

289 – 294

6

Helix

297 – 299

3

Turn

304 – 306

3

Beta strand

307 – 309

3

Helix

316 – 318

3

Helix

330 – 332

3

Helix

333 – 345

13

Beta strand

348 – 355

8

Beta strand

363 – 366

4

Turn

369 – 372

4

Beta strand

375 – 378

4

Helix

400 – 402

3

Helix

404 – 416

13

Beta strand

421 – 426

6

Beta strand

428 – 436

9

Turn

437 – 439

3

Beta strand

440 – 445

6

Beta strand

447 – 449

3

Beta strand

451 – 456

6

Beta strand

461 – 465

5

Turn

467 – 469

3

Beta strand

474 – 479

6

Beta strand

481 – 484

4

Beta strand

488 – 494

7

Beta strand

502 – 506

5

Sequences

	Sequence		Length	Mass (Da)
	P04745 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 7710BCAC83EBE8B2	FASTA	511	57,768
	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

References

	« Hide 'large scale' referencesShow '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: 2423416] [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: 6610603] [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. , 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: 14702039] [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. , 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: 16710414] [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: 15489334] [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: 2452973] [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: 2442579] [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: 1710976] [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: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427, MASS SPECTROMETRY. 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: 15299664] [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: 12527308] [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 , 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.

IPI

IPI00300786.

PIR

ALHUS. A91543.

RefSeq

NP_001008219.1. NM_001008218.1.
NP_001008220.1. NM_001008219.1.
NP_001008222.1. NM_001008221.1.
NP_004029.2. NM_004038.3.

UniGene

Hs.599274.
Hs.654437.
Hs.655232.
Hs.662103.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C8Q	X-ray	2.30	A	17-511	[»]
1JXJ	X-ray	1.99	A	17-511	[»]
1JXK	X-ray	1.90	A	17-511	[»]
1MFU	X-ray	2.00	A	17-511	[»]
1MFV	X-ray	2.00	A	17-511	[»]
1NM9	X-ray	2.10	A	17-511	[»]
1Q4N	X-ray	2.07	X	17-511	[»]
1SMD	X-ray	1.60	A	17-511	[»]
1XV8	X-ray	3.00	A/B	17-511	[»]
1Z32	X-ray	1.60	X	17-511	[»]
3BLK	X-ray	2.00	A	17-511	[»]
3BLP	X-ray	1.60	X	17-511	[»]
3DHP	X-ray	1.50	A	17-511	[»]

ProteinModelPortal

P04745.

SMR

P04745. Positions 16-511.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04745. 1 interaction.

STRING

P04745.

Protein family/group databases

CAZy

GH13. Glycoside Hydrolase Family 13.

PTM databases

GlycoSuiteDB

P04745.

PhosphoSite

P04745.

Proteomic databases

PeptideAtlas

P04745.

PRIDE

P04745.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330330; ENSP00000330484; ENSG00000174876.
ENST00000370079; ENSP00000359096; ENSG00000187733.
ENST00000370080; ENSP00000359097; ENSG00000174876.
ENST00000370083; ENSP00000359100; ENSG00000237763.
ENST00000416771; ENSP00000393463; ENSG00000174876.
ENST00000456929; ENSP00000416142; ENSG00000237763.

GeneID

276.
277.
278.

KEGG

hsa:276.
hsa:277.
hsa:278.

UCSC

uc001duu.1. human.

Organism-specific databases

CTD

276.
277.
278.

GeneCards

GC01M104230.
GC01P104197.
GC01P104292.

HGNC

HGNC:474. AMY1A.
HGNC:475. AMY1B.
HGNC:476. AMY1C.

HPA

CAB004310.

MIM

104700. gene.
104701. gene.
104702. gene.

neXtProt

NX_P04745.

PharmGKB

PA24783.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12837.

HOGENOM

HBG404170.

HOVERGEN

HBG000061.

InParanoid

P04745.

OMA

MSSYRWS.

OrthoDB

EOG4RV2R1.

PhylomeDB

P04745.

Enzyme and pathway databases

BRENDA

3.2.1.1. 2681.

Reactome

REACT_474. Metabolism of carbohydrates.

Gene expression databases

Bgee

P04745.

CleanEx

HS_AMY1A.

Genevestigator

P04745.

GermOnline

ENSG00000051415. Homo sapiens.
ENSG00000174876. Homo sapiens.
ENSG00000187733. Homo sapiens.

Family and domain databases

InterPro

IPR006048. A-amylase_b_C.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

KO

K01176.

PANTHER

PTHR10357. Alpha_amylase. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]

PRINTS

PR00110. ALPHAAMYLASE.

SMART

SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Other

BindingDB

P04745.

NextBio

1113.

SOURCE

Search...

Entry information

Entry name

AMY1_HUMAN

Accession

Primary (citable) accession number: P04745
Secondary accession number(s): A6NJS5 , A8K8H6, Q13763, Q5T083

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 145 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.