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AMY2A (human)

Overview AMY2A 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. [provided by RefSeq, Jul 2008] Protein type: Carbohydrate Metabolism - starch and sucrose; Secreted, signal peptide; EC 3.2.1.1; Hydrolase; Secreted Cellular Component: extracellular space; extracellular region Molecular Function: alpha-amylase activity; calcium ion binding; chloride ion binding Biological Process: polysaccharide digestion; carbohydrate catabolic process; carbohydrate metabolic process Reference #:  P04746 (UniProtKB) Alt. Names/Synonyms: 1,4-alpha-D-glucan glucanohydrolase; alpha-amylase; AMY2; AMY2A; AMY2B; amylase, alpha 2A (pancreatic); amylase, pancreatic, alpha-2A; AMYP; found in the pancreas; glycogenase; PA; Pancreatic alpha-amylase; pancreatic amylase 2A; pancreatic amylase alpha 2A Gene Symbols: AMY2A Molecular weight: 57,707 Da Basal Isoelectric point: 6.6  Predict pI for various phosphorylation states

Select Structure to View Below AMY2A 1B2Y - A=16-511 (human) 1BSI - A=16-511 (human) 1CPU - A=16-511 (human) 1HNY - A=16-511 (human) 1KB3 - A=16-511 (human) 1KBB - A=16-511 (human) 1KBK - A=16-511 (human) 1KGU - A=16-511 (human) 1KGW - A=16-511 (human) 1KGX - A=16-511 (human) 1U2Y - A=16-511 (human) 1U30 - A=16-511 (human) 1U33 - A=16-511 (human) 1XCW - A=16-511 (human) 1XCX - A=16-511 (human) 1XD0 - A=16-511 (human) 1XD1 - A=16-511 (human) 1XGZ - A=16-511 (human) 1XH0 - A=16-511 (human) 1XH1 - A=16-511 (human) 1XH2 - A=16-511 (human) 2CPU - A=16-511 (human) 2QMK - A=16-511 (human) 2QV4 - A=16-511 (human) 3BAI - A=16-511 (human) 3BAJ - A=16-511 (human) 3BAK - A=16-511 (human) 3BAW - A=16-511 (human) 3BAX - A=16-511 (human) 3BAY - A=16-511 (human) 3CPU - A=16-511 (human) 3IJ7 - A=16-511 (human) 3IJ8 - A=16-511 (human) 3IJ9 - A=16-511 (human) 3OLD - A=16-511 (human) 3OLE - A=16-511 (human) 3OLG - A=16-511 (human) 3OLI - A=16-511 (human) 4GQQ - A=16-511 (human) 4GQR - A=16-511 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1B2Y 1BSI 1CPU 1HNY 1KB3 1KBB 1KBK 1KGU 1KGW 1KGX 1U2Y 1U30 1U33 1XCW 1XCX 1XD0 1XD1 1XGZ 1XH0 1XH1 1XH2 2CPU 2QMK 2QV4 3BAI 3BAJ 3BAK 3BAW 3BAX 3BAY 3CPU 3IJ7 3IJ8 3IJ9 3OLD 3OLE 3OLG 3OLI 4GQQ 4GQR  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		T26	PNTQQGRTSIVHLFE
0	1		Y67-p	PNENVAIyNPFRPWW
0	1		S88	SYKLCTRSGNEDEFR
0	1		T178	QVRDCRLTGLLDLAL
1	2		Y189-p	DLALEKDyVRSkIAE
0	1		K193-u	EKDyVRSkIAEyMNH
0	2		Y197-p	VRSkIAEyMNHLIDI
0	1		K223	HMWPGDIKAILDKLH
0	1		Y357	FTRVMSSYRWPRQFQ

	mouse
T26-p	PHTSDGRtAIVHLFE
H67	PNENVVVHNPSRPWW
S88-p	SYKICTRsGNEDEFR
T175-p	QVRNCRLtGLLDLAL
Y186	DLALEKDYVRTkVAD
K190-u	EKDYVRTkVADYMNH
Y194	VRTkVADYMNHLIDI
K220-u	HMWPGDIkAVLDKLH
Y354	FTRVMSSYRWNRNFQ

	rat
T26	PHTADGRTAIVHLFE
N67	PNENIIINNPSRPWW
S88	SYKICSRSGNENEFK
S175	QVRNCRLSGLLDLAL
Y186	DLALDKDYVRTKVAD
K190	DKDYVRTKVADYMNN
Y194	VRTKVADYMNNLIDI
K220	HMWPGDIKAVLDKLH
Y354-p	FTRVMSSyRRTRNFQ

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