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Q9D6Y9 (GLGB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 106. 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:
1,4-alpha-glucan-branching enzyme

EC=2.4.1.18
Alternative name(s):
Brancher enzyme
Glycogen-branching enzyme
Gene names
Name:Gbe1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Required for sufficient glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule and, consequently, in reducing the osmotic pressure within cells By similarity.

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.

Pathway

Glycan biosynthesis; glycogen biosynthesis.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7027011,4-alpha-glucan-branching enzyme
PRO_0000188776

Sites

Active site3571Nucleophile By similarity
Active site4121Proton donor By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1731Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D6Y9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: BE2284A5CED7C060

FASTA70280,364
        10         20         30         40         50         60 
MAAPAAPAAG ETGPDARLEA ALADVPELAR LLEIDPYLKP FAADFQRRYK KFSQVLHDIG 

        70         80         90        100        110        120 
ENEGGIDKFS RGYESFGIHR CSDGGIYCKE WAPGAEGVFL TGEFSGWNPF SHPYKKLEYG 

       130        140        150        160        170        180 
KWELYIPPKQ NKSPLIPHGS KLKVVITSKS GEILYRISPW AKYVVRENNN VNYDWIHWAP 

       190        200        210        220        230        240 
EDPYKFKHSR PKKPRSLRIY ESHVGISSHE GKIASYKHFT SNVLPRIKDL GYNCIQLMAI 

       250        260        270        280        290        300 
MEHAYYASFG YQITSFFAAS SRYGTPEELK ELVDTAHSMG IVVLLDVVHS HASKNSEDGL 

       310        320        330        340        350        360 
NMFDGTDSCY FHSGPRGTHD LWDSRLFIYS SWEVLRFLLS NIRWWLEEYC FDGFRFDGVT 

       370        380        390        400        410        420 
SMLYHHHGMG QGFSGDYNEY FGLQVDEDAL IYLMLANHLA HTLYPDSITI AEDVSGMPAL 

       430        440        450        460        470        480 
CSPTSQGGGG FDYRLAMAIP DKWIQLLKEF KDEDWNMGNI VYTLTNRRYL EKCVAYAESH 

       490        500        510        520        530        540 
DQALVGDKTL AFWLMDAEMY TNMSVLAPFT PVIDRGIQLH KMIRLITHGL GGEGYLNFMG 

       550        560        570        580        590        600 
NEFGHPEWLD FPRKGNNESY HYARRQFNLT DDDLLRYKFL NNFDRDMNRL EERCGWLSAP 

       610        620        630        640        650        660 
QAYVSEKHEA NKTITFERAG LLFIFNFHPS KSYTDYRVGT ATPGKFKIVL DSDAAEYGGH 

       670        680        690        700 
QRLDHNTNYF AEAFEHNGRP YSLLVYIPSR VALILQNVDL QN 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver and Tongue.
[2]"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: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009815 mRNA. Translation: BAB26519.1.
AK050365 mRNA. Translation: BAC34210.1.
BC017541 mRNA. Translation: AAH17541.1.
RefSeqNP_083079.1. NM_028803.4.
UniGeneMm.396102.

3D structure databases

ProteinModelPortalQ9D6Y9.
SMRQ9D6Y9. Positions 44-699.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D6Y9. 1 interaction.
MINTMINT-4127309.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteQ9D6Y9.

Proteomic databases

MaxQBQ9D6Y9.
PaxDbQ9D6Y9.
PRIDEQ9D6Y9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000163832; ENSMUSP00000132603; ENSMUSG00000022707.
GeneID74185.
KEGGmmu:74185.
UCSCuc007zqu.1. mouse.

Organism-specific databases

CTD2632.
MGIMGI:1921435. Gbe1.

Phylogenomic databases

eggNOGCOG0296.
GeneTreeENSGT00390000017040.
HOGENOMHOG000175159.
HOVERGENHBG051734.
InParanoidQ9D6Y9.
KOK00700.
OMAGPRGTHD.
OrthoDBEOG7Q5HCP.
PhylomeDBQ9D6Y9.
TreeFamTF300783.

Enzyme and pathway databases

UniPathwayUPA00164.

Gene expression databases

BgeeQ9D6Y9.
CleanExMM_GBE1.
GenevestigatorQ9D6Y9.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006407. GlgB.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

NextBio340028.
PROQ9D6Y9.
SOURCESearch...

Entry information

Entry nameGLGB_MOUSE
AccessionPrimary (citable) accession number: Q9D6Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries