AMY2B - Misplaced Pages

Protein-coding gene in the species Homo sapiens

AMY2B

Identifiers

AMY2B, AMY2, AMY3, HXA, amylase, alpha 2B (pancreatic), amylase alpha 2B (pancreatic), amylase alpha 2B

External IDs

OMIM: 104660; MGI: 3714985; HomoloGene: 134663; GeneCards: AMY2B; OMA:AMY2B - orthologs

Gene location (Human)

Chr.	Chromosome 1 (human)

Band	1p21.1	Start	103,553,815 bp
Band	1p21.1	End	103,579,534 bp

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)

Band	3 F3\|3	Start	113,219,771 bp
Band	3 F3\|3	End	113,231,368 bp

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

body of pancreas

right uterine tube

cerebellar hemisphere

right hemisphere of cerebellum

gastric mucosa

left lobe of thyroid gland

tibial nerve

right lobe of thyroid gland

apex of heart

Achilles tendon

Top expressed in

pancreas

islet of Langerhans

stomach

colon

esophagus

duodenum

jejunum

quadriceps femoris muscle

spermatid

ileum

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	catalytic activity alpha-amylase activity hydrolase activity metal ion binding hydrolase activity, acting on glycosyl bonds cation binding
Cellular component	extracellular region extracellular exosome
Biological process	digestion metabolism carbohydrate metabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


280


100043686

Ensembl


ENSG00000240038


ENSMUSG00000093931

UniProt


P19961


P00688

RefSeq (mRNA)


NM_020978 NM_001386109 NM_001387437


NM_001160151

RefSeq (protein)


NP_066188


NP_001036176 NP_001153622 NP_001153623 NP_001153624

Location (UCSC)

Chr 1: 103.55 – 103.58 Mb

Chr 3: 113.22 – 113.23 Mb

PubMed search

Wikidata

View/Edit Human

View/Edit Mouse

Alpha-amylase 2B is an enzyme that in humans is encoded by the AMY2B gene.

Function

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 pancreas.

References

^ GRCh38: Ensembl release 89: ENSG00000240038 – Ensembl, May 2017
^ GRCm38: Ensembl release 89: ENSMUSG00000093931 – Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Omichi K, Hase S (December 1993). "Identification of the characteristic amino-acid sequence for human alpha-amylase encoded by the AMY2B gene". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1203 (2): 224–9. doi:10.1016/0167-4838(93)90087-8. PMID 8268204.
^ "Entrez Gene: AMY2B amylase, alpha 2B (pancreatic)".

External links

Human AMY2B genome location and AMY2B gene details page in the UCSC Genome Browser.

Kaczmarek MJ, Rosenmund H (August 1977). "The action of human pancreatic and salivary isoamylases on starch and glycogen". Clinica Chimica Acta; International Journal of Clinical Chemistry. 79 (1): 69–73. doi:10.1016/0009-8981(77)90462-4. PMID 890964.
Groot PC, Mager WH, Henriquez NV, Pronk JC, Arwert F, Planta RJ, Eriksson AW, Frants RR (September 1990). "Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers". Genomics. 8 (1): 97–105. doi:10.1016/0888-7543(90)90230-R. PMID 2081604.
Yokouchi H, Horii A, Emi M, Tomita N, Doi S, Ogawa M, Mori T, Matsubara K (June 1990). "Cloning and characterization of a third type of human alpha-amylase gene, AMY2B". Gene. 90 (2): 281–6. doi:10.1016/0378-1119(90)90191-S. PMID 2401405.
Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH (March 1988). "Concerted evolution of human amylase genes". Molecular and Cellular Biology. 8 (3): 1197–205. doi:10.1128/mcb.8.3.1197. PMC 363264. PMID 2452973.
Samuelson LC, Wiebauer K, Gumucio DL, Meisler MH (September 1988). "Expression of the human amylase genes: recent origin of a salivary amylase promoter from an actin pseudogene". Nucleic Acids Research. 16 (17): 8261–76. doi:10.1093/nar/16.17.8261. PMC 338557. PMID 2458567.
Tomita N, Horii A, Doi S, Yokouchi H, Shiosaki K, Higashiyama M, Matsuura N, Ogawa M, Mori T, Matsubara K (March 1989). "A novel type of human alpha-amylase produced in lung carcinoid tumor". Gene. 76 (1): 11–8. doi:10.1016/0378-1119(89)90003-6. PMID 2701942.
Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR (July 1989). "The human alpha-amylase multigene family consists of haplotypes with variable numbers of genes". Genomics. 5 (1): 29–42. doi:10.1016/0888-7543(89)90083-9. PMID 2788608.
Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR (May 1988). "Human pancreatic amylase is encoded by two different genes". Nucleic Acids Research. 16 (10): 4724. doi:10.1093/nar/16.10.4724. PMC 336663. PMID 3260028.
Tricoli JV, Shows TB (March 1984). "Regional assignment of human amylase (AMY) to p22----p21 of chromosome 1". Somatic Cell and Molecular Genetics. 10 (2): 205–10. doi:10.1007/BF01534909. PMID 6608795. S2CID 21230969.
Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O (April 2001). "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 8 (2): 85–95. doi:10.1093/dnares/8.2.85. PMID 11347906.
Aughsteen AA (May 2001). "A comparative immunohistochemical study on amylase localization in the rat and human exocrine pancreas". Saudi Medical Journal. 22 (5): 410–5. PMID 11376382.
Koyama I, Komine S, Iino N, Hokari S, Igarashi S, Alpers DH, Komoda T (July 2001). "alpha-Amylase expressed in human liver is encoded by the AMY-2B gene identified in tumorous tissues". Clinica Chimica Acta; International Journal of Clinical Chemistry. 309 (1): 73–83. doi:10.1016/S0009-8981(01)00501-0. PMID 11408008.
Iafrate AJ, Feuk L, Rivera MN, Listewnik ML, Donahoe PK, Qi Y, Scherer SW, Lee C (September 2004). "Detection of large-scale variation in the human genome". Nature Genetics. 36 (9): 949–51. doi:10.1038/ng1416. PMID 15286789.

v t e PDB gallery
1b2y: STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE 1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN 1c8q: STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE 1cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT 1hny: The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes 1jxj: Role of mobile loop in the mechanism of human salivary amylase 1jxk: Role of the mobile loop in the mechanism of human salivary amylase 1kb3: Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase 1kbb: Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids 1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids 1kgu: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE 1kgw: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE 1kgx: Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase 1mfu: Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant 1mfv: Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme 1nm9: Crystal structure of recombinant human salivary amylase mutant W58A 1q4n: Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity 1smd: HUMAN SALIVARY AMYLASE 1u2y: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam 1u30: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam 1u33: In situ extension as an approach for identifying novel alpha-amylase inhibitors 1xcw: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xcx: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xd0: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xd1: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts 1xgz: Structure of the N298S variant of human pancreatic alpha-amylase 1xh0: Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose 1xh1: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride 1xh2: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose 1xv8: Crystal Structure of Human Salivary Alpha-Amylase Dimer 1z32: Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues 2cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT 3cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT

PDB gallery

1b2y: STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE
1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN
1c8q: STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE
1cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
1hny: The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes
1jxj: Role of mobile loop in the mechanism of human salivary amylase
1jxk: Role of the mobile loop in the mechanism of human salivary amylase
1kb3: Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase
1kbb: Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
1kgu: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE
1kgw: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE
1kgx: Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase
1mfu: Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant
1mfv: Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme
1nm9: Crystal structure of recombinant human salivary amylase mutant W58A
1q4n: Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
1smd: HUMAN SALIVARY AMYLASE
1u2y: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam
1u30: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam
1u33: In situ extension as an approach for identifying novel alpha-amylase inhibitors
1xcw: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
1xcx: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
1xd0: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
1xd1: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
1xgz: Structure of the N298S variant of human pancreatic alpha-amylase
1xh0: Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose
1xh1: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride
1xh2: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose
1xv8: Crystal Structure of Human Salivary Alpha-Amylase Dimer
1z32: Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues
2cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
3cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT

This article on a gene on human chromosome 1 is a stub. You can help Misplaced Pages by expanding it.

Categories:

Function

References

External links

Further reading