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Q15124 (PGM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucomutase-like protein 5
Alternative name(s):
Aciculin
Phosphoglucomutase-related protein
Short name=PGM-RP
Gene names
Name:PGM5
Synonyms:PGMRP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity.

Cofactor

Binds 1 magnesium ion per subunit Potential.

Subunit structure

Interacts with cytoskeletal proteins dystrophin and utrophin.

Subcellular location

Cell junctionadherens junction. Cytoplasmcytoskeleton. Note: Adherens-type cellular junctions. Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments. Ref.7

Tissue specificity

Detected in smooth and cardiac muscle at high levels and in skeletal muscle at low level. Present in other tissues due to vascular or other smooth muscle component. Low levels are present in liver, kidney, skin and brain (at protein level). Ref.6 Ref.7

Developmental stage

In the developing aorta, expressed at low levels in 10-12 week old fetuses. Levels increase progressively in 24 week fetus, 6 month old child and 1.5 year old child aortic smooth muscle, reaching a maximum at maturity. Ref.7

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence caution

The sequence AAC41948.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH33073.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA73882.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell adhesion
Glucose metabolism
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Metal-binding
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentZ disc

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell-cell adherens junction

Inferred from direct assay Ref.7. Source: MGI

costamere

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 10867799. Source: UniProtKB

dystrophin-associated glycoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

focal adhesion

Inferred from direct assay Ref.7. Source: UniProtKB

intercalated disc

Inferred from direct assay Ref.7. Source: UniProtKB

sarcolemma

Inferred from direct assay PubMed 10867799. Source: UniProtKB

spot adherens junction

Inferred from direct assay Ref.7. Source: UniProtKB

stress fiber

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionintramolecular transferase activity, phosphotransferases

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Non-traceable author statement Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15124-1)

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.
Isoform 2 (identifier: Q15124-2)

The sequence of this isoform differs from the canonical sequence as follows:
     387-387: G → V
     388-567: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Phosphoglucomutase-like protein 5
PRO_0000147787

Regions

Compositional bias510 – 5134Poly-Ser

Sites

Metal binding2931Magnesium Potential
Metal binding2951Magnesium Potential
Metal binding2971Magnesium Potential

Natural variations

Alternative sequence3871G → V in isoform 2.
VSP_030014
Alternative sequence388 – 567180Missing in isoform 2.
VSP_030015

Experimental info

Sequence conflict221A → S in CAA73882. Ref.4
Sequence conflict2441D → E AA sequence Ref.7
Sequence conflict260 – 2612ED → DE AA sequence Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 00583A442977A025

FASTA56762,225
        10         20         30         40         50         60 
MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC 

        70         80         90        100        110        120 
TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT 

       130        140        150        160        170        180 
ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYAICPDLRI DLSRLGRQEF 

       190        200        210        220        230        240 
DLENKFKPFR VEIVDPVDIY LNLLRTIFDF HAIKGLLTGP SQLKIRIDAM HGVMGPYVRK 

       250        260        270        280        290        300 
VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM 

       310        320        330        340        350        360 
ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA KSMKVPVYET 

       370        380        390        400        410        420 
PAGWRFFSNL MDSGRCNLCG EESFGTGSDH LREKDGLWAV LVWLSIIAAR KQSVEEIVRD 

       430        440        450        460        470        480 
HWAKFGRHYY CRFDYEGLDP KTTYYIMRDL EALVTDKSFI GQQFAVGSHV YSVAKTDSFE 

       490        500        510        520        530        540 
YVDPVDGTVT KKQGLRIIFS DASRLIFRLS SSSGVRATLR LYAESYERDP SGHDQEPQAV 

       550        560 
LSPLIAIALK ISQIHERTGR RGPTVIT 

« Hide

Isoform 2 [UniParc].

Checksum: 31FF5EACAFB47DC4
Show »

FASTA38741,790

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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] (ISOFORM 1).
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2).
Tissue: Muscle.
[4]"Characterisation of the promoter which regulates expression of a phosphoglucomutase-related protein, a component of the dystrophin/utrophin cytoskeleton predominantly expressed in smooth muscle."
Moiseeva E.P., Critchley D.R.
Eur. J. Biochem. 248:634-643(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-87.
[5]Parker K.
Submitted (JUN-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 29-55; 158-169; 191-224; 227-239; 355-375; 433-492 AND 497-504, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"A novel dystrophin/utrophin-associated protein is an enzymatically inactive member of the phosphoglucomutase superfamily."
Moiseeva E.P., Belkin A.M., Spurr N.K., Koteliansky V.E., Critchley D.R.
Eur. J. Biochem. 235:103-113(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-567, TISSUE SPECIFICITY.
Tissue: Uterus.
[7]"A novel phosphoglucomutase-related protein is concentrated in adherens junctions of muscle and nonmuscle cells."
Belkin A.M., Klimanskaya I.V., Lukashev M.E., Lilley K., Critchley D.R., Koteliansky V.E.
J. Cell Sci. 107:159-173(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 82-104; 234-262 AND 447-467, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK297108 mRNA. Translation: BAG59618.1.
AL161457, AL353608, AL353616 Genomic DNA. Translation: CAI16959.2.
AL353608, AL161457, AL353616 Genomic DNA. Translation: CAI41169.2.
AL353616, AL161457, AL353608 Genomic DNA. Translation: CAH71906.2.
AL353608, AL161457 Genomic DNA. Translation: CAO03528.1.
AL161457, AL353608 Genomic DNA. Translation: CAO03529.1.
BC033073 mRNA. Translation: AAH33073.1. Different initiation.
Y13478 Genomic DNA. Translation: CAA73882.1. Different initiation.
L40933 Genomic DNA. Translation: AAC41948.1. Different initiation.
PIRS62629.
RefSeqNP_068800.2. NM_021965.3.
UniGeneHs.307835.

3D structure databases

ProteinModelPortalQ15124.
SMRQ15124. Positions 6-567.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111258. 2 interactions.
STRING9606.ENSP00000379678.

PTM databases

PhosphoSiteQ15124.

Polymorphism databases

DMDM152031655.

Proteomic databases

PaxDbQ15124.
PRIDEQ15124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396392; ENSP00000379674; ENSG00000154330. [Q15124-2]
ENST00000396396; ENSP00000379678; ENSG00000154330. [Q15124-1]
ENST00000579791; ENSP00000464667; ENSG00000266607. [Q15124-2]
GeneID5239.
KEGGhsa:5239.
UCSCuc004agr.3. human. [Q15124-1]

Organism-specific databases

CTD5239.
GeneCardsGC09P070971.
H-InvDBHIX0020782.
HGNCHGNC:8908. PGM5.
HPACAB034397.
MIM600981. gene.
neXtProtNX_Q15124.
PharmGKBPA33245.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0033.
HOGENOMHOG000009550.
HOVERGENHBG001599.
InParanoidQ15124.
KOK15636.
OMAPTAPYED.
PhylomeDBQ15124.
TreeFamTF300350.

Gene expression databases

ArrayExpressQ15124.
BgeeQ15124.
CleanExHS_PGM5.
GenevestigatorQ15124.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProIPR005844. 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]
PfamPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPGM5. human.
GeneWikiPGM5.
GenomeRNAi5239.
NextBio20240.
PROQ15124.
SOURCESearch...

Entry information

Entry namePGM5_HUMAN
AccessionPrimary (citable) accession number: Q15124
Secondary accession number(s): B1AM46 expand/collapse secondary AC list , B4DLQ6, Q5VYV3, Q8N527, Q9UDH4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM