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Protein

Alpha-amylase 2B

Gene

AMY2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl(-) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151CalciumBy similarity
Metal bindingi173 – 1731Calcium; via carbonyl oxygenBy similarity
Metal bindingi182 – 1821CalciumBy similarity
Binding sitei210 – 2101ChlorideBy similarity
Active sitei212 – 2121NucleophileBy similarity
Metal bindingi216 – 2161Calcium; via carbonyl oxygenBy similarity
Active sitei248 – 2481Proton donorBy similarity
Binding sitei313 – 3131ChlorideBy similarity
Sitei315 – 3151Transition state stabilizerBy similarity
Binding sitei352 – 3521ChlorideBy similarity

GO - Molecular functioni

  • alpha-amylase activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • carbohydrate metabolic process Source: ProtInc
  • digestion Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_9472. Digestion of dietary carbohydrate.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase 2B (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 2B
Carcinoid alpha-amylase
Gene namesi
Name:AMY2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:478. AMY2B.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24785.

Polymorphism and mutation databases

DMDMi113789.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Add
BLAST
Chaini16 – 511496Alpha-amylase 2BPRO_0000001402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Pyrrolidone carboxylic acidBy similarity
Disulfide bondi43 ↔ 101By similarity
Disulfide bondi85 ↔ 130By similarity
Disulfide bondi156 ↔ 175By similarity
Disulfide bondi393 ↔ 399By similarity
Disulfide bondi465 ↔ 477By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP19961.
PaxDbiP19961.
PRIDEiP19961.

PTM databases

PhosphoSiteiP19961.

Expressioni

Gene expression databases

BgeeiP19961.
CleanExiHS_AMY2B.
ExpressionAtlasiP19961. baseline.
GenevisibleiP19961. HS.

Organism-specific databases

HPAiHPA045394.
HPA045399.
HPA046980.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi106777. 1 interaction.
IntActiP19961. 2 interactions.
STRINGi9606.ENSP00000354610.

Structurei

3D structure databases

ProteinModelPortaliP19961.
SMRiP19961. Positions 17-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP19961.
KOiK01176.
OMAiGKCRTGS.
OrthoDBiEOG7RJPR2.
PhylomeDBiP19961.
TreeFamiTF312850.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19961-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK
60 70 80 90 100
GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR
110 120 130 140 150
CNNVGVRIYV DAVINHMSGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD
160 170 180 190 200
FNDGKCKTGS GDIENYNDAT QVRDCRLVGL LDLALEKDYV RSKIAEYMNH
210 220 230 240 250
LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG SKPFIYQEVI
260 270 280 290 300
DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG
310 320 330 340 350
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF
360 370 380 390 400
TRVMSSYRWP RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE
410 420 430 440 450
HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT
460 470 480 490 500
FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED
510
PFIAIHAESK L
Length:511
Mass (Da):57,710
Last modified:February 1, 1991 - v1
Checksum:i05FC3B1EC1143857
GO
Isoform 2 (identifier: P19961-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     368-370: DVN → EHG
     371-511: Missing.

Note: No experimental confirmation available.
Show »
Length:370
Mass (Da):42,021
Checksum:i2E294536A637C8CB
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei368 – 3703DVN → EHG in isoform 2. 1 PublicationVSP_056932
Alternative sequencei371 – 511141Missing in isoform 2. 1 PublicationVSP_056933Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24895 mRNA. Translation: AAA35525.1.
D90097 Genomic DNA. Translation: BAA14130.1.
AK095605 mRNA. Translation: BAG53093.1.
AK127047 mRNA. Translation: BAG54429.1.
AC105272 Genomic DNA. No translation available.
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.
CCDSiCCDS782.1. [P19961-1]
PIRiJS0165. ALHU2B.
RefSeqiNP_066188.1. NM_020978.4. [P19961-1]
UniGeneiHs.484588.

Genome annotation databases

EnsembliENST00000361355; ENSP00000354610; ENSG00000240038.
ENST00000477657; ENSP00000433347; ENSG00000240038. [P19961-2]
ENST00000610648; ENSP00000481588; ENSG00000240038.
GeneIDi280.
KEGGihsa:280.
UCSCiuc001duq.3. human. [P19961-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24895 mRNA. Translation: AAA35525.1.
D90097 Genomic DNA. Translation: BAA14130.1.
AK095605 mRNA. Translation: BAG53093.1.
AK127047 mRNA. Translation: BAG54429.1.
AC105272 Genomic DNA. No translation available.
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.
CCDSiCCDS782.1. [P19961-1]
PIRiJS0165. ALHU2B.
RefSeqiNP_066188.1. NM_020978.4. [P19961-1]
UniGeneiHs.484588.

3D structure databases

ProteinModelPortaliP19961.
SMRiP19961. Positions 17-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106777. 1 interaction.
IntActiP19961. 2 interactions.
STRINGi9606.ENSP00000354610.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteiP19961.

Polymorphism and mutation databases

DMDMi113789.

Proteomic databases

MaxQBiP19961.
PaxDbiP19961.
PRIDEiP19961.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361355; ENSP00000354610; ENSG00000240038.
ENST00000477657; ENSP00000433347; ENSG00000240038. [P19961-2]
ENST00000610648; ENSP00000481588; ENSG00000240038.
GeneIDi280.
KEGGihsa:280.
UCSCiuc001duq.3. human. [P19961-1]

Organism-specific databases

CTDi280.
GeneCardsiGC01P104096.
HGNCiHGNC:478. AMY2B.
HPAiHPA045394.
HPA045399.
HPA046980.
MIMi104660. gene.
neXtProtiNX_P19961.
PharmGKBiPA24785.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP19961.
KOiK01176.
OMAiGKCRTGS.
OrthoDBiEOG7RJPR2.
PhylomeDBiP19961.
TreeFamiTF312850.

Enzyme and pathway databases

ReactomeiREACT_9472. Digestion of dietary carbohydrate.

Miscellaneous databases

ChiTaRSiAMY2B. human.
GeneWikiiAMY2B.
GenomeRNAii280.
NextBioi1133.
PROiP19961.
SOURCEiSearch...

Gene expression databases

BgeeiP19961.
CleanExiHS_AMY2B.
ExpressionAtlasiP19961. baseline.
GenevisibleiP19961. HS.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  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.
    , 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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain and Kidney.
  7. "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.
  8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
    Tissue: Pancreas.
  9. "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.

Entry informationi

Entry nameiAMY2B_HUMAN
AccessioniPrimary (citable) accession number: P19961
Secondary accession number(s): B3KTI1
, B3KXB7, D3DT76, Q9UBH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 22, 2015
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.