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P19961

- AMY2B_HUMAN

UniProt

P19961 - AMY2B_HUMAN

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Protein

Alpha-amylase 2B

Gene
AMY2B
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 calcium ion per subunit By similarity.
Binds 1 chloride ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151Calcium By similarity
Metal bindingi173 – 1731Calcium; via carbonyl oxygen By similarity
Metal bindingi182 – 1821Calcium By similarity
Binding sitei210 – 2101Chloride By similarity
Active sitei212 – 2121Nucleophile By similarity
Metal bindingi216 – 2161Calcium; via carbonyl oxygen By similarity
Active sitei248 – 2481Proton donor By similarity
Binding sitei313 – 3131Chloride By similarity
Sitei315 – 3151Transition state stabilizer By similarity
Binding sitei352 – 3521Chloride By similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: ProtInc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: ProtInc
  2. 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: Chromosome 1

Organism-specific databases

HGNCiHGNC:478. AMY2B.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24785.

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 acid By similarity
Disulfide bondi43 ↔ 101 By similarity
Disulfide bondi85 ↔ 130 By similarity
Disulfide bondi156 ↔ 175 By similarity
Disulfide bondi393 ↔ 399 By similarity
Disulfide bondi465 ↔ 477 By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP19961.
PaxDbiP19961.
PRIDEiP19961.

PTM databases

PhosphoSiteiP19961.

Expressioni

Gene expression databases

BgeeiP19961.
CleanExiHS_AMY2B.
GenevestigatoriP19961.

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

BioGridi106777. 1 interaction.
IntActiP19961. 2 interactions.
STRINGi9606.ENSP00000341734.

Structurei

3D structure databases

ProteinModelPortaliP19961.
SMRiP19961. Positions 17-511.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP19961.
KOiK01176.
OMAiSQVRDCR.
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.

Sequencei

Sequence statusi: Complete.

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

P19961-1 [UniParc]FASTAAdd to Basket

« Hide

MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK    50
GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR 100
CNNVGVRIYV DAVINHMSGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD 150
FNDGKCKTGS GDIENYNDAT QVRDCRLVGL LDLALEKDYV RSKIAEYMNH 200
LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG SKPFIYQEVI 250
DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG 300
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF 350
TRVMSSYRWP RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE 400
HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT 450
FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED 500
PFIAIHAESK L 511
Length:511
Mass (Da):57,710
Last modified:February 1, 1991 - v1
Checksum:i05FC3B1EC1143857
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS782.1.
PIRiJS0165. ALHU2B.
RefSeqiNP_066188.1. NM_020978.4.
UniGeneiHs.484588.

Genome annotation databases

EnsembliENST00000361355; ENSP00000354610; ENSG00000240038.
GeneIDi280.
KEGGihsa:280.
UCSCiuc001duq.3. human.

Polymorphism databases

DMDMi113789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS782.1.
PIRi JS0165. ALHU2B.
RefSeqi NP_066188.1. NM_020978.4.
UniGenei Hs.484588.

3D structure databases

ProteinModelPortali P19961.
SMRi P19961. Positions 17-511.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106777. 1 interaction.
IntActi P19961. 2 interactions.
STRINGi 9606.ENSP00000341734.

Chemistry

BindingDBi P19961.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSitei P19961.

Polymorphism databases

DMDMi 113789.

Proteomic databases

MaxQBi P19961.
PaxDbi P19961.
PRIDEi P19961.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361355 ; ENSP00000354610 ; ENSG00000240038 .
GeneIDi 280.
KEGGi hsa:280.
UCSCi uc001duq.3. human.

Organism-specific databases

CTDi 280.
GeneCardsi GC01P104096.
HGNCi HGNC:478. AMY2B.
MIMi 104660. gene.
neXtProti NX_P19961.
PharmGKBi PA24785.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0366.
HOGENOMi HOG000253313.
HOVERGENi HBG000061.
InParanoidi P19961.
KOi K01176.
OMAi SQVRDCR.
PhylomeDBi P19961.
TreeFami TF312850.

Enzyme and pathway databases

Reactomei REACT_9472. Digestion of dietary carbohydrate.

Miscellaneous databases

ChiTaRSi AMY2B. human.
GeneWikii AMY2B.
GenomeRNAii 280.
NextBioi 1133.
PROi P19961.
SOURCEi Search...

Gene expression databases

Bgeei P19961.
CleanExi HS_AMY2B.
Genevestigatori P19961.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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].
  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].
    Tissue: Brain.
  4. 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. 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.

Entry informationi

Entry nameiAMY2B_HUMAN
AccessioniPrimary (citable) accession number: P19961
Secondary accession number(s): B3KXB7, D3DT76, Q9UBH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: September 3, 2014
This is version 148 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

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