Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P04745

- AMY1_HUMAN

UniProt

P04745 - AMY1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alpha-amylase 1

Gene

AMY1A

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

Functioni

Catalytic activityi

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

Cofactori

Binds 1 calcium ion per subunit.
Binds 1 chloride ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151Calcium
Metal bindingi173 – 1731Calcium; via carbonyl oxygen
Metal bindingi182 – 1821Calcium
Binding sitei210 – 2101Chloride
Active sitei212 – 2121Nucleophile
Metal bindingi216 – 2161Calcium; via carbonyl oxygen
Active sitei248 – 2481Proton donor
Binding sitei313 – 3131Chloride
Sitei315 – 3151Transition state stabilizerBy similarity
Binding sitei352 – 3521Chloride

GO - Molecular functioni

  1. alpha-amylase activity Source: ProtInc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: ProtInc
  2. digestion Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.1. 2681.
ReactomeiREACT_9472. Digestion of dietary carbohydrate.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase 1 (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 1
Salivary alpha-amylase
Gene namesi
Name:AMY1A
Synonyms:AMY1
AND
Name:AMY1B
Synonyms:AMY1
AND
Name:AMY1C
Synonyms:AMY1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24783.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 511496Alpha-amylase 1PRO_0000001401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Pyrrolidone carboxylic acidBy similarity
Disulfide bondi43 ↔ 101
Disulfide bondi85 ↔ 130
Disulfide bondi156 ↔ 175
Modified residuei365 – 3651Deamidated asparagine; partial
Disulfide bondi393 ↔ 399
Modified residuei427 – 4271Deamidated asparagine; partial
Glycosylationi427 – 4271N-linked (GlcNAc...); alternate1 Publication
Disulfide bondi465 ↔ 477
Modified residuei474 – 4741Deamidated asparagine; partial
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP04745.
PaxDbiP04745.
PeptideAtlasiP04745.
PRIDEiP04745.

PTM databases

PhosphoSiteiP04745.
UniCarbKBiP04745.

Expressioni

Gene expression databases

BgeeiP04745.
CleanExiHS_AMY1A.
ExpressionAtlasiP04745. baseline.
GenevestigatoriP04745.

Organism-specific databases

HPAiCAB004310.
HPA045394.
HPA045399.
HPA046980.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
MUC7Q8TAX72EBI-738586,EBI-738582

Protein-protein interaction databases

BioGridi106773. 4 interactions.
106774. 1 interaction.
106775. 15 interactions.
IntActiP04745. 2 interactions.
STRINGi9606.ENSP00000330484.

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315
Helixi36 – 4510
Turni46 – 516
Beta strandi54 – 574
Turni67 – 704
Helixi73 – 775
Beta strandi78 – 803
Helixi91 – 10313
Beta strandi107 – 1126
Beta strandi115 – 1195
Beta strandi124 – 1263
Turni136 – 1394
Turni142 – 1454
Helixi148 – 1503
Turni153 – 1553
Beta strandi158 – 1625
Helixi169 – 1746
Helixi177 – 1793
Beta strandi180 – 1834
Helixi188 – 20417
Beta strandi208 – 2114
Helixi214 – 2163
Helixi219 – 2268
Turni234 – 2363
Beta strandi244 – 2474
Beta strandi253 – 2564
Helixi259 – 2624
Turni263 – 2653
Beta strandi266 – 2694
Helixi272 – 28211
Helixi289 – 2946
Helixi297 – 2993
Turni304 – 3063
Beta strandi307 – 3093
Helixi316 – 3183
Beta strandi321 – 3233
Helixi324 – 3263
Helixi330 – 3323
Helixi333 – 34513
Beta strandi348 – 3558
Beta strandi363 – 3686
Turni369 – 3724
Beta strandi375 – 3784
Helixi400 – 4023
Helixi404 – 41512
Turni416 – 4183
Beta strandi421 – 4266
Beta strandi428 – 4369
Turni437 – 4393
Beta strandi440 – 4456
Beta strandi447 – 4493
Beta strandi451 – 4566
Beta strandi461 – 4655
Turni467 – 4693
Beta strandi476 – 4794
Beta strandi481 – 4844
Beta strandi488 – 4947
Beta strandi498 – 5003
Beta strandi502 – 5065
Helixi507 – 5093

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP04745.
SMRiP04745. Positions 16-511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04745.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP04745.
KOiK01176.
OMAiVAINHES.
OrthoDBiEOG7RJPR2.
PhylomeDBiP04745.
TreeFamiTF312850.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P04745 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLFWLLFTI GFCWAQYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK
60 70 80 90 100
GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR
110 120 130 140 150
CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD
160 170 180 190 200
FNDGKCKTGS GDIENYNDAT QVRDCRLSGL LDLALGKDYV RSKIAEYMNH
210 220 230 240 250
LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG SKPFIYQEVI
260 270 280 290 300
DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG
310 320 330 340 350
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF
360 370 380 390 400
TRVMSSYRWP RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE
410 420 430 440 450
HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT
460 470 480 490 500
FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED
510
PFIAIHAESK L
Length:511
Mass (Da):57,768
Last modified:February 1, 1996 - v2
Checksum:i7710BCAC83EBE8B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851N → T in AAA57345. (PubMed:2442579)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30782.1.
CCDS30783.1.
CCDS30784.1.
PIRiA91543. ALHUS.
RefSeqiNP_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.
UniGeneiHs.599274.
Hs.654437.
Hs.655232.
Hs.662103.

Genome annotation databases

EnsembliENST00000330330; ENSP00000330484; ENSG00000174876.
ENST00000370079; ENSP00000359096; ENSG00000187733.
ENST00000370080; ENSP00000359097; ENSG00000174876.
ENST00000370083; ENSP00000359100; ENSG00000237763.
GeneIDi276.
277.
278.
KEGGihsa:276.
hsa:277.
hsa:278.
UCSCiuc001duu.3. human.

Polymorphism databases

DMDMi1351933.

Cross-referencesi

Web resourcesi

Wikipedia

Amylase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS30782.1.
CCDS30783.1.
CCDS30784.1.
PIRi A91543. ALHUS.
RefSeqi NP_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.
UniGenei Hs.599274.
Hs.654437.
Hs.655232.
Hs.662103.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C8Q X-ray 2.30 A 16-511 [» ]
1JXJ X-ray 1.99 A 16-511 [» ]
1JXK X-ray 1.90 A 16-511 [» ]
1MFU X-ray 2.00 A 17-511 [» ]
1MFV X-ray 2.00 A 17-511 [» ]
1NM9 X-ray 2.10 A 16-511 [» ]
1Q4N X-ray 2.07 X 16-511 [» ]
1SMD X-ray 1.60 A 17-511 [» ]
1XV8 X-ray 3.00 A/B 16-511 [» ]
1Z32 X-ray 1.60 X 16-511 [» ]
3BLK X-ray 2.00 A 16-511 [» ]
3BLP X-ray 1.60 X 16-511 [» ]
3DHP X-ray 1.50 A 16-511 [» ]
ProteinModelPortali P04745.
SMRi P04745. Positions 16-511.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106773. 4 interactions.
106774. 1 interaction.
106775. 15 interactions.
IntActi P04745. 2 interactions.
STRINGi 9606.ENSP00000330484.

Chemistry

BindingDBi P04745.
ChEMBLi CHEMBL2478.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSitei P04745.
UniCarbKBi P04745.

Polymorphism databases

DMDMi 1351933.

Proteomic databases

MaxQBi P04745.
PaxDbi P04745.
PeptideAtlasi P04745.
PRIDEi P04745.

Protocols and materials databases

DNASUi 277.
278.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330330 ; ENSP00000330484 ; ENSG00000174876 .
ENST00000370079 ; ENSP00000359096 ; ENSG00000187733 .
ENST00000370080 ; ENSP00000359097 ; ENSG00000174876 .
ENST00000370083 ; ENSP00000359100 ; ENSG00000237763 .
GeneIDi 276.
277.
278.
KEGGi hsa:276.
hsa:277.
hsa:278.
UCSCi uc001duu.3. human.

Organism-specific databases

CTDi 276.
277.
278.
GeneCardsi GC01M104230.
GC01P104197.
GC01P104292.
HGNCi HGNC:474. AMY1A.
HGNC:475. AMY1B.
HGNC:476. AMY1C.
HPAi CAB004310.
HPA045394.
HPA045399.
HPA046980.
MIMi 104700. gene.
104701. gene.
104702. gene.
neXtProti NX_P04745.
PharmGKBi PA24783.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0366.
GeneTreei ENSGT00390000002882.
HOGENOMi HOG000253313.
HOVERGENi HBG000061.
InParanoidi P04745.
KOi K01176.
OMAi VAINHES.
OrthoDBi EOG7RJPR2.
PhylomeDBi P04745.
TreeFami TF312850.

Enzyme and pathway databases

BRENDAi 3.2.1.1. 2681.
Reactomei REACT_9472. Digestion of dietary carbohydrate.

Miscellaneous databases

EvolutionaryTracei P04745.
GeneWikii AMY1A.
NextBioi 1113.
PROi P04745.
SOURCEi Search...

Gene expression databases

Bgeei P04745.
CleanExi HS_AMY1A.
ExpressionAtlasi P04745. baseline.
Genevestigatori P04745.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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] [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.
    , 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.

Entry informationi

Entry nameiAMY1_HUMAN
AccessioniPrimary (citable) accession number: P04745
Secondary accession number(s): A6NJS5
, A8K8H6, Q13763, Q5T083
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 172 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3