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Protein

Phosphoglucomutase-like protein 5

Gene

Pgm5

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

Functioni

Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity (By similarity).By similarity

Cofactori

Mg2+CuratedNote: Binds 1 Mg2+ ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281SubstrateBy similarity
Active sitei122 – 1221Phosphoserine intermediateBy similarity
Metal bindingi122 – 1221Magnesium; via phosphate groupBy similarity
Binding sitei135 – 1351SubstrateBy similarity
Metal bindingi293 – 2931MagnesiumBy similarity
Metal bindingi295 – 2951MagnesiumBy similarity
Metal bindingi297 – 2971MagnesiumBy similarity
Binding sitei394 – 3941SubstrateBy similarity
Binding sitei520 – 5201SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Cell adhesion, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase-like protein 5
Gene namesi
Name:Pgm5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1925668. Pgm5.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: MGI
  • cell-substrate junction Source: MGI
  • costamere Source: MGI
  • cytoplasmic side of plasma membrane Source: MGI
  • dystrophin-associated glycoprotein complex Source: MGI
  • focal adhesion Source: MGI
  • intercalated disc Source: MGI
  • sarcolemma Source: MGI
  • spot adherens junction Source: MGI
  • stress fiber Source: MGI
  • Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567Phosphoglucomutase-like protein 5PRO_0000294064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201PhosphothreonineCombined sources
Modified residuei122 – 1221PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BZF8.
PaxDbiQ8BZF8.
PRIDEiQ8BZF8.

PTM databases

iPTMnetiQ8BZF8.
PhosphoSiteiQ8BZF8.

Expressioni

Gene expression databases

BgeeiQ8BZF8.
CleanExiMM_PGM5.
GenevisibleiQ8BZF8. MM.

Interactioni

Subunit structurei

Interacts with cytoskeletal proteins dystrophin and utrophin.By similarity

Protein-protein interaction databases

BioGridi230463. 2 interactions.
STRINGi10090.ENSMUSP00000036025.

Structurei

3D structure databases

ProteinModelPortaliQ8BZF8.
SMRiQ8BZF8. Positions 6-567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1232Substrate bindingBy similarity
Regioni297 – 2982Substrate bindingBy similarity
Regioni381 – 3833Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi510 – 5134Poly-Ser

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiKOG0625. Eukaryota.
COG0033. LUCA.
GeneTreeiENSGT00390000011831.
HOGENOMiHOG000009550.
HOVERGENiHBG001599.
InParanoidiQ8BZF8.
KOiK15636.
OMAiPTAPYED.
OrthoDBiEOG76472B.
PhylomeDBiQ8BZF8.
TreeFamiTF300350.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BZF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGSPIPVLT VPTAPYEDQR PTGGGGLRRP TGLFEGQRNY LPNFIQSVLS
60 70 80 90 100
SIDLRDRQGC TMVVGSDGRY FSRTATEIVV QMAAANGIGR LIIGQNGILS
110 120 130 140 150
TPAVSCIIRK IKAAGGIILT ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD
160 170 180 190 200
KIYQISKTIE EYAICPDLRI DLSRLGRQEF DLENKFKPFR VEIVDPVDIY
210 220 230 240 250
LNLLRNIFDF NAIKSLLTGP SQLKIRVDAM HGVMGPYVRK VLCDELGAPA
260 270 280 290 300
NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM
310 320 330 340 350
ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSTALDRVA
360 370 380 390 400
KSMKVPVYET PAGWRFFSNL MDSGRCSLCG EESFGTGSDH LREKDGLWAV
410 420 430 440 450
LVWLSIIAAR KQSVEEIVRD HWAKYGRHYY CRFDYEGLEP KATYYIMRDL
460 470 480 490 500
EALVTDKSFI GQQFAVGSHI YSIAKTDSFE YVDPVDGTVT KKQGLRIIFS
510 520 530 540 550
DASRLIFRLS SSSGVRATIR LYAESYERDP SGHDQEPQAV LSPLIAIALK
560
ISQIHERTGR RGPTVIT
Length:567
Mass (Da):62,220
Last modified:July 10, 2007 - v2
Checksum:i46CD383095054BEB
GO

Sequence cautioni

The sequence BAC29083.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035507 mRNA. Translation: BAC29083.1. Different initiation.
CCDSiCCDS29714.1.
RefSeqiNP_778178.3. NM_175013.2.
UniGeneiMm.105222.
Mm.391170.

Genome annotation databases

EnsembliENSMUST00000047666; ENSMUSP00000036025; ENSMUSG00000041731.
GeneIDi226041.
KEGGimmu:226041.
UCSCiuc008has.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035507 mRNA. Translation: BAC29083.1. Different initiation.
CCDSiCCDS29714.1.
RefSeqiNP_778178.3. NM_175013.2.
UniGeneiMm.105222.
Mm.391170.

3D structure databases

ProteinModelPortaliQ8BZF8.
SMRiQ8BZF8. Positions 6-567.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230463. 2 interactions.
STRINGi10090.ENSMUSP00000036025.

PTM databases

iPTMnetiQ8BZF8.
PhosphoSiteiQ8BZF8.

Proteomic databases

MaxQBiQ8BZF8.
PaxDbiQ8BZF8.
PRIDEiQ8BZF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047666; ENSMUSP00000036025; ENSMUSG00000041731.
GeneIDi226041.
KEGGimmu:226041.
UCSCiuc008has.1. mouse.

Organism-specific databases

CTDi5239.
MGIiMGI:1925668. Pgm5.

Phylogenomic databases

eggNOGiKOG0625. Eukaryota.
COG0033. LUCA.
GeneTreeiENSGT00390000011831.
HOGENOMiHOG000009550.
HOVERGENiHBG001599.
InParanoidiQ8BZF8.
KOiK15636.
OMAiPTAPYED.
OrthoDBiEOG76472B.
PhylomeDBiQ8BZF8.
TreeFamiTF300350.

Miscellaneous databases

ChiTaRSiPgm5. mouse.
PROiQ8BZF8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BZF8.
CleanExiMM_PGM5.
GenevisibleiQ8BZF8. MM.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: Urinary bladder.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120 AND SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiPGM5_MOUSE
AccessioniPrimary (citable) accession number: Q8BZF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: June 8, 2016
This is version 102 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.