MASCOT Search Results

Protein View: NP_004029.2

alpha-amylase 1 precursor [Homo sapiens]

Database: NCBIprot
Score: 262
Expect: 2e-21
Monoisotopic mass (Mr): 57731
Calculated pI: 6.47
Taxonomy: Homo sapiens

This protein sequence matches the following other entries:

Sequence similarity is available as an NCBI BLAST search of NP_004029.2 against nr.

Search parameters

Enzyme:

Trypsin: cuts C-term side of KR unless next residue is P.

Variable modifications: Oxidation (M)
Mass values searched: 54
Mass values matched: 29

Protein sequence coverage: 53%

Matched peptides shown in bold red.

1 MKLFWLLFTI GFCWAQYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK
51 GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR
101 CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD
151 FNDGKCKTGS GDIENYNDAT QVRDCRLSGL LDLALGKDYV RSKIAEYMNH
201 LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG SKPFIYQEVI
251 DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG
301 FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF
351 TRVMSSYRWP RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE
401 HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT
451 FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED
501 PFIAIHAESK L

Unformatted sequence string: 511 residues (for pasting into other applications).

Sort by
Show
Start End Observed Mr(expt) Mr(calc) Delta M Peptide
26 35 1287.7952 1286.7879 1286.6772 0.1107 0 R.TSIVHLFEWR.W
36 45 1233.6978 1232.6905 1232.5859 0.1046 0 R.WVDIALECER.Y
51 76 2990.5515 2989.5442 2989.4736 0.0706 0 K.GFGGVQVSPPNENVAIHNPFRPWWER.Y
77 83 884.5222 883.5149 883.4440 0.0710 0 R.YQPVSYK.L
88 95 953.4817 952.4744 952.3886 0.0858 0 R.SGNEDEFR.N
88 100 1554.7504 1553.7431 1553.6892 0.0538 1 R.SGNEDEFRNMVTR.C
88 100 1570.7977 1569.7905 1569.6842 0.1063 1 R.SGNEDEFRNMVTR.C + Oxidation (M)
140 155 1814.9195 1813.9122 1813.7948 0.1174 0 R.DFPAVPYSGWDFNDGK.C
158 173 1739.8656 1738.8583 1738.7758 0.0825 0 K.TGSGDIENYNDATQVR.D
177 187 1099.7759 1098.7686 1098.6648 0.1038 0 R.LSGLLDLALGK.D
177 191 1633.0404 1632.0331 1631.9246 0.1085 1 R.LSGLLDLALGKDYVR.S
192 210 2150.1350 2149.1278 2149.0990 0.0288 1 R.SKIAEYMNHLIDIGVAGFR.I + Oxidation (M)
194 210 1919.0573 1918.0500 1917.9771 0.0729 0 K.IAEYMNHLIDIGVAGFR.I
194 210 1935.0726 1934.0654 1933.9720 0.0934 0 K.IAEYMNHLIDIGVAGFR.I + Oxidation (M)
216 223 999.5622 998.5549 998.4644 0.0905 0 K.HMWPGDIK.A + Oxidation (M)
259 267 1002.5170 1001.5098 1001.4203 0.0895 0 K.SSDYFGNGR.V
283 288 761.4232 760.4159 760.3868 0.0292 1 R.KWNGEK.M
294 306 1538.7499 1537.7426 1537.6409 0.1018 0 K.NWGEGWGFMPSDR.A
307 318 1427.8125 1426.8052 1426.6953 0.1099 0 R.ALVFVDNHDNQR.G
319 334 1615.9053 1614.8980 1614.7903 0.1077 0 R.GHGAGGASILTFWDAR.L
335 352 2134.0784 2133.0711 2133.0540 0.0171 1 R.LYKMAVGFMLAHPYGFTR.V + 2 Oxidation (M)
338 352 1697.8826 1696.8754 1696.8218 0.0536 0 K.MAVGFMLAHPYGFTR.V
338 352 1713.9208 1712.9136 1712.8167 0.0969 0 K.MAVGFMLAHPYGFTR.V + Oxidation (M)
338 352 1729.9345 1728.9273 1728.8116 0.1156 0 K.MAVGFMLAHPYGFTR.V + 2 Oxidation (M)
403 407 758.3979 757.3906 757.4347 -0.0441 1 R.WRQIR.N
414 436 2585.1932 2584.1859 2584.1731 0.0127 0 R.NVVDGQPFTNWYDNGSNQVAFGR.G
482 489 896.5298 895.5226 895.4287 0.0938 0 K.IYVSDDGK.A
490 510 2271.1407 2270.1334 2270.0967 0.0367 0 K.AHFSISNSAEDPFIAIHAESK.L
490 511 2384.2321 2383.2248 2383.1808 0.0440 1 K.AHFSISNSAEDPFIAIHAESKL.-

No match to: 804.3376, 826.3243, 832.3786, 841.1366, 842.2950, 857.1104, 864.2786, 909.5347, 1151.6165, 1213.6894, 1241.7763, 1243.7990, 1303.7876, 1309.7023, 1319.7822, 1647.8796, 1681.9190, 1745.9049, 1877.1879, 1951.0297, 2186.9468, 2211.1040, 2601.1933, 3006.5143, 3292.4856

Error distributionError distribution (ppm)


LOCUS       NP_004029                511 aa            linear   PRI 06-OCT-2016
DEFINITION  alpha-amylase 1 precursor [Homo sapiens].
ACCESSION   NP_004029 XP_001127960
VERSION     NP_004029.2
DBSOURCE    REFSEQ: accession NM_004038.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Nater UM, La Marca R, Erni K and Ehlert U.
  TITLE     Alpha-Amylase Activity in Blood Increases after Pharmacological,
            But Not Psychological, Activation of the Adrenergic System
  JOURNAL   PLoS ONE 10 (6), E0130449 (2015)
   PUBMED   26110636
  REMARK    GeneRIF: Alpha-amylase in blood increases after pharmacological
            activation of the adrenergic pathways suggesting that sympathetic
            receptors are responsible for these changes. Psychological stress,
            however, does not seem to have an impact on alpha-amylase in blood
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Edmonds R, Burkett B, Leicht A and McKean M.
  TITLE     Effect of chronic training on heart rate variability, salivary IgA
            and salivary alpha-amylase in elite swimmers with a disability
  JOURNAL   PLoS ONE 10 (6), E0127749 (2015)
   PUBMED   26043224
  REMARK    GeneRIF: The purpose of this study was to a) determine the heart
            rate variability (HRV) and saliva markers of immunity (salivary
            immunoglobulin A; sIgA) and stress (salivary alpha-amylase; sAA)
            responses to chronic training in elite swimmers with a disability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Yang,Z., Lin,J., Chen,L., Zhang,M., Yang,X. and Chen,W.
  TITLE     Influences of AMY1 gene copy number and protein expression on
            salivary alpha-amylase activity before and after citric acid
            stimulation in splenic asthenia children
  JOURNAL   J Tradit Chin Med 35 (3), 266-272 (2015)
   PUBMED   26237829
  REMARK    GeneRIF: Splenic asthenia children had positive correlations
            between AMY1 copy number and sAA activity before or after citric
            acid stimulation.
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Chen LH, Yang ZM, Chen WW, Lin J, Zhang M, Yang XR and Zhao LB.
  TITLE     Attenuated acute salivary alpha-amylase responses to gustatory
            stimulation with citric acid in thin children
  JOURNAL   Br. J. Nutr. 113 (7), 1078-1085 (2015)
   PUBMED   25784372
  REMARK    GeneRIF: genetic association study in population in China: Data
            suggest that copy number variation of AMY1A gene is not associated
            with down-regulation of salivary response in thin children as
            compared to salivary response in normal weight children.
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Zheng,R., Zhang,J., Ying,Z. and Zheng,N.
  TITLE     Low Serum Amylase is Associated with Gestational Diabetes Mellitus
            in Chinese Pregnant Women
  JOURNAL   Clin. Lab. 61 (10), 1423-1428 (2015)
   PUBMED   26642703
  REMARK    GeneRIF: low serum amylase level is significantly associated with
            increased risk of gestational diabetes mellitus
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Bank RA, Hettema EH, Arwert F, Amerongen AV and Pronk JC.
  TITLE     Electrophoretic characterization of posttranslational modifications
            of human parotid salivary alpha-amylase
  JOURNAL   Electrophoresis 12 (1), 74-79 (1991)
   PUBMED   1710976
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Groot PC, Mager WH, Henriquez NV, Pronk JC, Arwert F, Planta RJ,
            Eriksson AW and Frants RR.
  TITLE     Evolution of the human alpha-amylase multigene family through
            unequal, homologous, and inter- and intrachromosomal crossovers
  JOURNAL   Genomics 8 (1), 97-105 (1990)
   PUBMED   2081604
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Handy,D.E., Larsen,S.H., Karn,R.C. and Hodes,M.E.
  TITLE     Identification of a human salivary amylase gene. Partial sequence
            of genomic DNA suggests a mode of regulation different from that of
            mouse, Amy1
  JOURNAL   Mol. Biol. Med. 4 (3), 145-155 (1987)
   PUBMED   2442579
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Davis,M.M., Hodes,M.E., Munsick,R.A., Ulbright,T.M. and
            Goldstein,D.J.
  TITLE     Pancreatic amylase expression in human pancreatic development
  JOURNAL   Hybridoma 5 (2), 137-145 (1986)
   PUBMED   2424823
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Nishide,T., Nakamura,Y., Emi,M., Yamamoto,T., Ogawa,M., Mori,T. and
            Matsubara,K.
  TITLE     Primary structure of human salivary alpha-amylase gene
  JOURNAL   Gene 41 (2-3), 299-304 (1986)
   PUBMED   2423416
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB956272.1, BC063129.1 and
            BC070302.1.
            On or before Sep 20, 2006 this sequence version replaced
            gi:113412273, gi:4757750.
            
            Summary: Amylases are secreted proteins that hydrolyze
            1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides,
            and thus catalyze the first step in digestion of dietary starch and
            glycogen. The human genome has a cluster of several amylase genes
            that are expressed at high levels in either salivary gland or
            pancreas. This gene encodes an amylase isoenzyme produced by the
            salivary gland. Alternative splicing results in multiple transcript
            variants encoding the same protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.1"
     Protein         1..511
                     /product="alpha-amylase 1 precursor"
                     /EC_number="3.2.1.1"
                     /note="glycogenase; amylase, salivary, alpha-1A; salivary
                     amylase alpha 1A; alpha-amylase 1; salivary alpha-amylase;
                     1,4-alpha-D-glucan glucanohydrolase 1"
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:4.0"
                     /calculated_mol_wt=1876
     mat_peptide     16..511
                     /product="alpha-amylase 1"
                     /calculated_mol_wt=55910
     Site            16
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note=". {ECO:0000250|UniProtKB:P00687}; propagated from
                     UniProtKB/Swiss-Prot (P04745.2)"
     Region          25..416
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Region          46..>315
                     /region_name="AmyA"
                     /note="Glycosidase [Carbohydrate transport and
                     metabolism]; COG0366"
                     /db_xref="CDD:223443"
     Site            order(73..74,77..78,113,116,177..180,210,212..213,
                     215..216,248,250,255,314..315,320)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(115,182)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(212,248,315)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Site            315
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Transition state stabilizer.
                     {ECO:0000250|UniProtKB:P04746}; propagated from
                     UniProtKB/Swiss-Prot (P04745.2)"
     Site            365
                     /site_type="amidation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Deamidated asparagine, partial.
                     {ECO:0000269|PubMed:1710976}; propagated from
                     UniProtKB/Swiss-Prot (P04745.2)"
     Region          422..510
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
     Site            427
                     /site_type="amidation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Deamidated asparagine, partial, alternate.
                     {ECO:0000269|PubMed:1710976}; propagated from
                     UniProtKB/Swiss-Prot (P04745.2)"
     Site            474
                     /site_type="amidation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Deamidated asparagine, partial.
                     {ECO:0000269|PubMed:1710976}; propagated from
                     UniProtKB/Swiss-Prot (P04745.2)"
     CDS             1..511
                     /gene="AMY1A"
                     /gene_synonym="AMY1"
                     /coded_by="NM_004038.3:296..1831"
                     /db_xref="CCDS:CCDS30782.1"
                     /db_xref="GeneID:276"
                     /db_xref="HGNC:HGNC:474"
                     /db_xref="MIM:104700"
Mascot: http://www.matrixscience.com/