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Q9D6Y9

- GLGB_MOUSE

UniProt

Q9D6Y9 - GLGB_MOUSE

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Protein

1,4-alpha-glucan-branching enzyme

Gene

Gbe1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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.By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei357 – 3571NucleophileBy similarity
Active sitei412 – 4121Proton donorBy similarity

GO - Molecular functioni

  1. 1,4-alpha-glucan branching enzyme activity Source: UniProtKB-EC
  2. cation binding Source: InterPro
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

ReactomeiREACT_188939. Glycogen synthesis.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-alpha-glucan-branching enzyme (EC:2.4.1.18)
Alternative name(s):
Brancher enzyme
Glycogen-branching enzyme
Gene namesi
Name:Gbe1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1921435. Gbe1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Glycogen storage disease

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 7027011,4-alpha-glucan-branching enzymePRO_0000188776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei173 – 1731PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9D6Y9.
PaxDbiQ9D6Y9.
PRIDEiQ9D6Y9.

PTM databases

PhosphoSiteiQ9D6Y9.

Expressioni

Gene expression databases

BgeeiQ9D6Y9.
CleanExiMM_GBE1.
ExpressionAtlasiQ9D6Y9. baseline and differential.
GenevestigatoriQ9D6Y9.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ9D6Y9. 1 interaction.
MINTiMINT-4127309.

Structurei

3D structure databases

ProteinModelPortaliQ9D6Y9.
SMRiQ9D6Y9. Positions 44-699.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0296.
GeneTreeiENSGT00390000017040.
HOGENOMiHOG000175159.
HOVERGENiHBG051734.
InParanoidiQ9D6Y9.
KOiK00700.
OMAiGPRGTHD.
OrthoDBiEOG7Q5HCP.
PhylomeDBiQ9D6Y9.
TreeFamiTF300783.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9D6Y9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPAAPAAG ETGPDARLEA ALADVPELAR LLEIDPYLKP FAADFQRRYK
60 70 80 90 100
KFSQVLHDIG ENEGGIDKFS RGYESFGIHR CSDGGIYCKE WAPGAEGVFL
110 120 130 140 150
TGEFSGWNPF SHPYKKLEYG KWELYIPPKQ NKSPLIPHGS KLKVVITSKS
160 170 180 190 200
GEILYRISPW AKYVVRENNN VNYDWIHWAP EDPYKFKHSR PKKPRSLRIY
210 220 230 240 250
ESHVGISSHE GKIASYKHFT SNVLPRIKDL GYNCIQLMAI MEHAYYASFG
260 270 280 290 300
YQITSFFAAS SRYGTPEELK ELVDTAHSMG IVVLLDVVHS HASKNSEDGL
310 320 330 340 350
NMFDGTDSCY FHSGPRGTHD LWDSRLFIYS SWEVLRFLLS NIRWWLEEYC
360 370 380 390 400
FDGFRFDGVT SMLYHHHGMG QGFSGDYNEY FGLQVDEDAL IYLMLANHLA
410 420 430 440 450
HTLYPDSITI AEDVSGMPAL CSPTSQGGGG FDYRLAMAIP DKWIQLLKEF
460 470 480 490 500
KDEDWNMGNI VYTLTNRRYL EKCVAYAESH DQALVGDKTL AFWLMDAEMY
510 520 530 540 550
TNMSVLAPFT PVIDRGIQLH KMIRLITHGL GGEGYLNFMG NEFGHPEWLD
560 570 580 590 600
FPRKGNNESY HYARRQFNLT DDDLLRYKFL NNFDRDMNRL EERCGWLSAP
610 620 630 640 650
QAYVSEKHEA NKTITFERAG LLFIFNFHPS KSYTDYRVGT ATPGKFKIVL
660 670 680 690 700
DSDAAEYGGH QRLDHNTNYF AEAFEHNGRP YSLLVYIPSR VALILQNVDL

QN
Length:702
Mass (Da):80,364
Last modified:June 1, 2001 - v1
Checksum:iBE2284A5CED7C060
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK009815 mRNA. Translation: BAB26519.1.
AK050365 mRNA. Translation: BAC34210.1.
BC017541 mRNA. Translation: AAH17541.1.
RefSeqiNP_083079.1. NM_028803.4.
UniGeneiMm.396102.

Genome annotation databases

EnsembliENSMUST00000163832; ENSMUSP00000132603; ENSMUSG00000022707.
GeneIDi74185.
KEGGimmu:74185.
UCSCiuc007zqu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK009815 mRNA. Translation: BAB26519.1 .
AK050365 mRNA. Translation: BAC34210.1 .
BC017541 mRNA. Translation: AAH17541.1 .
RefSeqi NP_083079.1. NM_028803.4.
UniGenei Mm.396102.

3D structure databases

ProteinModelPortali Q9D6Y9.
SMRi Q9D6Y9. Positions 44-699.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D6Y9. 1 interaction.
MINTi MINT-4127309.

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSitei Q9D6Y9.

Proteomic databases

MaxQBi Q9D6Y9.
PaxDbi Q9D6Y9.
PRIDEi Q9D6Y9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000163832 ; ENSMUSP00000132603 ; ENSMUSG00000022707 .
GeneIDi 74185.
KEGGi mmu:74185.
UCSCi uc007zqu.1. mouse.

Organism-specific databases

CTDi 2632.
MGIi MGI:1921435. Gbe1.

Phylogenomic databases

eggNOGi COG0296.
GeneTreei ENSGT00390000017040.
HOGENOMi HOG000175159.
HOVERGENi HBG051734.
InParanoidi Q9D6Y9.
KOi K00700.
OMAi GPRGTHD.
OrthoDBi EOG7Q5HCP.
PhylomeDBi Q9D6Y9.
TreeFami TF300783.

Enzyme and pathway databases

UniPathwayi UPA00164 .
Reactomei REACT_188939. Glycogen synthesis.

Miscellaneous databases

NextBioi 340028.
PROi Q9D6Y9.
SOURCEi Search...

Gene expression databases

Bgeei Q9D6Y9.
CleanExi MM_GBE1.
ExpressionAtlasi Q9D6Y9. baseline and differential.
Genevestigatori Q9D6Y9.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view ]
PIRSFi PIRSF000463. GlgB. 1 hit.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiGLGB_MOUSE
AccessioniPrimary (citable) accession number: Q9D6Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3