Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P19961 (AMY2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

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 processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Non-traceable author statement Ref.2. Source: ProtInc

digestion

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-amylase activity

Traceable author statement Ref.2. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Chain16 – 511496Alpha-amylase 2B
PRO_0000001402

Sites

Active site2121Nucleophile By similarity
Active site2481Proton donor By similarity
Metal binding1151Calcium By similarity
Metal binding1731Calcium; via carbonyl oxygen By similarity
Metal binding1821Calcium By similarity
Metal binding2161Calcium; via carbonyl oxygen By similarity
Binding site2101Chloride By similarity
Binding site3131Chloride By similarity
Binding site3521Chloride By similarity
Site3151Transition state stabilizer By similarity

Amino acid modifications

Modified residue161Pyrrolidone carboxylic acid By similarity
Disulfide bond43 ↔ 101 By similarity
Disulfide bond85 ↔ 130 By similarity
Disulfide bond156 ↔ 175 By similarity
Disulfide bond393 ↔ 399 By similarity
Disulfide bond465 ↔ 477 By similarity

Sequences

Sequence LengthMass (Da)Tools
P19961 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 05FC3B1EC1143857

FASTA51157,710
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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. expand/collapse author list , 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].
Tissue: Brain.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Brain and Kidney.
[6]"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.
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
Tissue: Pancreas.
[8]"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] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Urine.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24895 mRNA. Translation: AAA35525.1.
D90097 Genomic DNA. Translation: BAA14130.1.
AK127047 mRNA. Translation: BAG54429.1.
CH471097 Genomic DNA. Translation: EAW72902.1.
CH471097 Genomic DNA. Translation: EAW72903.1.
CH471097 Genomic DNA. Translation: EAW72904.1.
BC011179 mRNA. Translation: AAH11179.1.
BC020861 mRNA. Translation: AAH20861.1.
X07057 Genomic DNA. Translation: CAA30100.1.
M18670 Genomic DNA. Translation: AAA51725.1.
PIRALHU2B. JS0165.
RefSeqNP_066188.1. NM_020978.4.
UniGeneHs.484588.

3D structure databases

ProteinModelPortalP19961.
SMRP19961. Positions 17-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106777. 1 interaction.
IntActP19961. 2 interactions.
STRING9606.ENSP00000341734.

Chemistry

BindingDBP19961.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteP19961.

Polymorphism databases

DMDM113789.

Proteomic databases

PaxDbP19961.
PRIDEP19961.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361355; ENSP00000354610; ENSG00000240038.
GeneID280.
KEGGhsa:280.
UCSCuc001duq.3. human.

Organism-specific databases

CTD280.
GeneCardsGC01P104096.
HGNCHGNC:478. AMY2B.
MIM104660. gene.
neXtProtNX_P19961.
PharmGKBPA24785.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000253313.
HOVERGENHBG000061.
InParanoidP19961.
KOK01176.
OMADSTCGND.
PhylomeDBP19961.
TreeFamTF312850.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP19961.
CleanExHS_AMY2B.
GenevestigatorP19961.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAMY2B. human.
GeneWikiAMY2B.
GenomeRNAi280.
NextBio1133.
PROP19961.
SOURCESearch...

Entry information

Entry nameAMY2B_HUMAN
AccessionPrimary (citable) accession number: P19961
Secondary accession number(s): B3KXB7, D3DT76, Q9UBH3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries