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Q15124

- PGM5_HUMAN

UniProt

Q15124 - PGM5_HUMAN

Protein

Phosphoglucomutase-like protein 5

Gene

PGM5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      Previous versions | rss
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    Functioni

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

    Cofactori

    Binds 1 magnesium ion per subunit.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi293 – 2931MagnesiumSequence Analysis
    Metal bindingi295 – 2951MagnesiumSequence Analysis
    Metal bindingi297 – 2971MagnesiumSequence Analysis

    GO - Molecular functioni

    1. intramolecular transferase activity, phosphotransferases Source: InterPro
    2. magnesium ion binding Source: InterPro
    3. structural molecule activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW

    Keywords - Biological processi

    Carbohydrate metabolism, Cell adhesion, Glucose metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglucomutase-like protein 5
    Alternative name(s):
    Aciculin
    Phosphoglucomutase-related protein
    Short name:
    PGM-RP
    Gene namesi
    Name:PGM5
    Synonyms:PGMRP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8908. PGM5.

    Subcellular locationi

    Cell junctionadherens junction 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Adherens-type cellular junctions. Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments.

    GO - Cellular componenti

    1. cell-cell adherens junction Source: MGI
    2. costamere Source: UniProtKB
    3. cytoplasmic side of plasma membrane Source: UniProtKB
    4. dystrophin-associated glycoprotein complex Source: UniProtKB
    5. focal adhesion Source: UniProtKB
    6. intercalated disc Source: UniProtKB
    7. sarcolemma Source: UniProtKB
    8. spot adherens junction Source: UniProtKB
    9. stress fiber Source: UniProtKB
    10. Z disc Source: RefGenome

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33245.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 567567Phosphoglucomutase-like protein 5PRO_0000147787Add
    BLAST

    Proteomic databases

    MaxQBiQ15124.
    PaxDbiQ15124.
    PRIDEiQ15124.

    PTM databases

    PhosphoSiteiQ15124.

    Expressioni

    Tissue specificityi

    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).2 Publications

    Developmental stagei

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ15124.
    BgeeiQ15124.
    CleanExiHS_PGM5.
    GenevestigatoriQ15124.

    Organism-specific databases

    HPAiCAB034397.

    Interactioni

    Subunit structurei

    Interacts with cytoskeletal proteins dystrophin and utrophin.

    Protein-protein interaction databases

    BioGridi111258. 2 interactions.
    STRINGi9606.ENSP00000379678.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15124.
    SMRiQ15124. Positions 6-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG0033.
    HOGENOMiHOG000009550.
    HOVERGENiHBG001599.
    InParanoidiQ15124.
    KOiK15636.
    OMAiDQRPTGG.
    PhylomeDBiQ15124.
    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.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15124-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS    50
    SIDLRDRQGC TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS 100
    TPAVSCIIRK IKAAGGIILT ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD 150
    KIYQISKTIE EYAICPDLRI DLSRLGRQEF DLENKFKPFR VEIVDPVDIY 200
    LNLLRTIFDF HAIKGLLTGP SQLKIRIDAM HGVMGPYVRK VLCDELGAPA 250
    NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM 300
    ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA 350
    KSMKVPVYET PAGWRFFSNL MDSGRCNLCG EESFGTGSDH LREKDGLWAV 400
    LVWLSIIAAR KQSVEEIVRD HWAKFGRHYY CRFDYEGLDP KTTYYIMRDL 450
    EALVTDKSFI GQQFAVGSHV YSVAKTDSFE YVDPVDGTVT KKQGLRIIFS 500
    DASRLIFRLS SSSGVRATLR LYAESYERDP SGHDQEPQAV LSPLIAIALK 550
    ISQIHERTGR RGPTVIT 567
    Length:567
    Mass (Da):62,225
    Last modified:July 10, 2007 - v2
    Checksum:i00583A442977A025
    GO
    Isoform 2 (identifier: Q15124-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         387-387: G → V
         388-567: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:387
    Mass (Da):41,790
    Checksum:i31FF5EACAFB47DC4
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221A → S in CAA73882. (PubMed:9342213)Curated
    Sequence conflicti244 – 2441D → E AA sequence (PubMed:8175905)Curated
    Sequence conflicti260 – 2612ED → DE AA sequence (PubMed:8175905)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei387 – 3871G → V in isoform 2. 1 PublicationVSP_030014
    Alternative sequencei388 – 567180Missing in isoform 2. 1 PublicationVSP_030015Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS6622.2. [Q15124-1]
    PIRiS62629.
    RefSeqiNP_068800.2. NM_021965.3. [Q15124-1]
    UniGeneiHs.307835.

    Genome annotation databases

    EnsembliENST00000396392; ENSP00000379674; ENSG00000154330. [Q15124-2]
    ENST00000396396; ENSP00000379678; ENSG00000154330. [Q15124-1]
    GeneIDi5239.
    KEGGihsa:5239.
    UCSCiuc004agr.3. human. [Q15124-1]

    Polymorphism databases

    DMDMi152031655.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS6622.2. [Q15124-1 ]
    PIRi S62629.
    RefSeqi NP_068800.2. NM_021965.3. [Q15124-1 ]
    UniGenei Hs.307835.

    3D structure databases

    ProteinModelPortali Q15124.
    SMRi Q15124. Positions 6-567.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111258. 2 interactions.
    STRINGi 9606.ENSP00000379678.

    PTM databases

    PhosphoSitei Q15124.

    Polymorphism databases

    DMDMi 152031655.

    Proteomic databases

    MaxQBi Q15124.
    PaxDbi Q15124.
    PRIDEi Q15124.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396392 ; ENSP00000379674 ; ENSG00000154330 . [Q15124-2 ]
    ENST00000396396 ; ENSP00000379678 ; ENSG00000154330 . [Q15124-1 ]
    GeneIDi 5239.
    KEGGi hsa:5239.
    UCSCi uc004agr.3. human. [Q15124-1 ]

    Organism-specific databases

    CTDi 5239.
    GeneCardsi GC09P070971.
    H-InvDB HIX0020782.
    HGNCi HGNC:8908. PGM5.
    HPAi CAB034397.
    MIMi 600981. gene.
    neXtProti NX_Q15124.
    PharmGKBi PA33245.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0033.
    HOGENOMi HOG000009550.
    HOVERGENi HBG001599.
    InParanoidi Q15124.
    KOi K15636.
    OMAi DQRPTGG.
    PhylomeDBi Q15124.
    TreeFami TF300350.

    Miscellaneous databases

    ChiTaRSi PGM5. human.
    GeneWikii PGM5.
    GenomeRNAii 5239.
    NextBioi 20240.
    PROi Q15124.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15124.
    Bgeei Q15124.
    CleanExi HS_PGM5.
    Genevestigatori Q15124.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    InterProi IPR005844. 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 ]
    Pfami PF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    [Graphical view ]
    PRINTSi PR00509. PGMPMM.
    SUPFAMi SSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEi PS00710. PGM_PMM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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.

    Entry informationi

    Entry nameiPGM5_HUMAN
    AccessioniPrimary (citable) accession number: Q15124
    Secondary accession number(s): B1AM46
    , B4DLQ6, Q5VYV3, Q8N527, Q9UDH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3