Reviewed, UniProtKB/Swiss-Prot P19961 (AMY2B_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-amylase 2B
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase 2B
    Carcinoid alpha-amylase

Gene names

Name:

AMY2B

Organism

Homo sapiens (Human) [Complete proteome]

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 oligosaccharides and polysaccharides.
Cofactor	Binds 1 calcium ion per subunit By similarity. Binds 1 chloride ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Secreted By similarity.
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 Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Ref.2 Non-traceable author statement. Source: ProtInc digestion Ref.2 Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-amylase activity Ref.2 Traceable author statement. Source: ProtInc calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15
	Chain	16 – 511	496	Alpha-amylase 2B		PRO_0000001402
Sites
	Active site	212	1	Nucleophile By similarity
	Active site	248	1	Proton donor By similarity
	Active site	315	1	By similarity
	Metal binding	115	1	Calcium By similarity
	Metal binding	173	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	182	1	Calcium By similarity
	Metal binding	216	1	Calcium; via carbonyl oxygen By similarity
	Binding site	210	1	Chloride By similarity
	Binding site	313	1	Chloride By similarity
	Binding site	352	1	Chloride By similarity
Amino acid modifications
	Modified residue	16	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	43 ↔ 101		By similarity
	Disulfide bond	85 ↔ 130		By similarity
	Disulfide bond	156 ↔ 175		By similarity
	Disulfide bond	393 ↔ 399		By similarity
	Disulfide bond	465 ↔ 477		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19961-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 05FC3B1EC1143857	FASTA	511	57,710
	10 20 30 40 50 60 MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP 70 80 90 100 110 120 NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMSGN 130 140 150 160 170 180 AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLVGL 190 200 210 220 230 240 LDLALEKDYV RSKIAEYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG 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 RQFQNGNDVN DWVGPPNNNG VIKEVTINPD 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]	"A novel type of human alpha-amylase produced in lung carcinoid tumor." Tomita N., Horii A., Doi S., Yokouchi H., Shiosaki K., Higashiyama M., Matsuura N., Ogawa M., Mori T., Matsubara K. Gene 76:11-18(1989) [PubMed: 2701942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and characterization of a third type of human alpha-amylase gene, AMY2B." Yokouchi H., Horii A., Emi M., Tomita N., Doi S., Ogawa M., Mori T., Matsubara K. Gene 90:281-286(1990) [PubMed: 2401405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: Brain and Kidney.
[4]	"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.
[5]	"Human pancreatic amylase is encoded by two different genes." Groot P.C., Bleeker M.J., Pronk J.C., Arwert F., Mager W.H., Planta R.J., Eriksson A.W., Frants R.R. Nucleic Acids Res. 16:4724-4724(1988) [PubMed: 3260028] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. Tissue: Pancreas.
[6]	"Identification of the characteristic amino-acid sequence for human alpha-amylase encoded by the AMY2B gene." Omichi K., Hase S. Biochim. Biophys. Acta 1203:224-229(1993) [PubMed: 8268204] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Urine.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M24895 mRNA. Translation: AAA35525.1. D90097 Genomic DNA. Translation: BAA14130.1. BC011179 mRNA. Translation: AAH11179.1. BC020861 mRNA. Translation: AAH20861.1. X07057 Genomic DNA. Translation: CAA30100.1. M18670 Genomic DNA. Translation: AAA51725.1.
IPI	IPI00021447.
PIR	ALHU2B. JS0165.
RefSeq	NP_066188.1.
UniGene	Hs.484588
3D structure databases
HSSP	HSSP built from PDB template 1HNY based on UniProtKB P04746.
SMR	P19961. Positions 16-511.
ModBase	Search...
Protein-protein interaction databases
STRING	P19961.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Proteomic databases
PRIDE	P19961.
Genome annotation databases
Ensembl	ENST00000305865; ENSP00000307372; ENSG00000197839; Homo sapiens. [Genome view] ENST00000338852; ENSP00000341734; ENSG00000197839; Homo sapiens. [Genome view] ENST00000361355; ENSP00000354610; ENSG00000197839; Homo sapiens. [Genome view] ENST00000393932; ENSP00000377509; ENSG00000197839; Homo sapiens. [Genome view] ENST00000414303; ENSP00000397582; ENSG00000197839; Homo sapiens. [Genome view] ENST00000423678; ENSP00000390832; ENSG00000197839; Homo sapiens. [Genome view] ENST00000435302; ENSP00000391423; ENSG00000197839; Homo sapiens. [Genome view] ENST00000453959; ENSP00000401627; ENSG00000197839; Homo sapiens. [Genome view] ENST00000456136; ENSP00000398158; ENSG00000197839; Homo sapiens. [Genome view]
GeneID	280.
KEGG	hsa:280.
UCSC	uc001duo.1. human.
Organism-specific databases
CTD	280.
GeneCards	GC01P103897.
H-InvDB	HIX0080309.
HGNC	HGNC:478. AMY2B.
MIM	104660. gene.
PharmGKB	PA24785.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P19961.
HOVERGEN	P19961.
OMA	HDTERNG.
Enzyme and pathway databases
BRENDA	3.2.1.1. 247.
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P19961.
Bgee	P19961.
CleanEx	HS_AMY2B.
Genevestigator	P19961.
GermOnline	ENSG00000197839. Homo sapiens.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 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]
ProtoNet	Search...
Other Resources
NextBio	1133.
SOURCE	Search...

Entry information

Entry name

AMY2B_HUMAN

Accession

Primary (citable) accession number: P19961
Secondary accession number(s): Q9UBH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	November 3, 2009
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.