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Q53GG5

- PDLI3_HUMAN

UniProt

Q53GG5 - PDLI3_HUMAN

Protein

PDZ and LIM domain protein 3

Gene

PDLIM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    May play a role in the organization of actin filament arrays within muscle cells.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural constituent of muscle Source: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament organization Source: Ensembl
    2. heart development Source: Ensembl

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PDZ and LIM domain protein 3
    Alternative name(s):
    Actinin-associated LIM protein
    Alpha-actinin-2-associated LIM protein
    Gene namesi
    Name:PDLIM3
    Synonyms:ALP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:20767. PDLIM3.

    Subcellular locationi

    CytoplasmmyofibrilsarcomereZ line 1 Publication
    Note: Localizes to myofiber Z-lines.

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cytoplasm Source: HPA
    3. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134970631.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 364364PDZ and LIM domain protein 3PRO_0000075867Add
    BLAST

    Proteomic databases

    MaxQBiQ53GG5.
    PaxDbiQ53GG5.
    PRIDEiQ53GG5.

    PTM databases

    PhosphoSiteiQ53GG5.

    Expressioni

    Tissue specificityi

    Isoform 1 is highly expressed in differentiated skeletal muscle. Isoform 2 is heart-specific.1 Publication

    Gene expression databases

    ArrayExpressiQ53GG5.
    BgeeiQ53GG5.
    CleanExiHS_PDLIM3.
    GenevestigatoriQ53GG5.

    Organism-specific databases

    HPAiHPA004749.

    Interactioni

    Subunit structurei

    Interacts with ACTN2.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RANBP2P497923EBI-5658852,EBI-973138

    Protein-protein interaction databases

    BioGridi118119. 2 interactions.
    IntActiQ53GG5. 9 interactions.
    STRINGi9606.ENSP00000284770.

    Structurei

    3D structure databases

    ProteinModelPortaliQ53GG5.
    SMRiQ53GG5. Positions 5-93, 269-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8484PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini292 – 35160LIM zinc-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain

    Phylogenomic databases

    eggNOGiNOG258467.
    HOVERGENiHBG061371.
    InParanoidiQ53GG5.
    OMAiSMSEPTA.
    OrthoDBiEOG77DJ69.
    PhylomeDBiQ53GG5.
    TreeFamiTF106408.

    Family and domain databases

    Gene3Di2.10.110.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR001478. PDZ.
    IPR006643. ZASP.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    SMARTiSM00132. LIM. 1 hit.
    SM00228. PDZ. 1 hit.
    SM00735. ZM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q53GG5-1) [UniParc]FASTAAdd to Basket

    Also known as: ALP-SK

    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

    MPQTVILPGP APWGFRLSGG IDFNQPLVIT RITPGSKAAA ANLCPGDVIL    50
    AIDGFGTESM THADAQDRIK AAAHQLCLKI DRGETHLWSP QVSEDGKAHP 100
    FKINLESEPQ DGNYFEHKHN IRPKPFVIPG RSSGCSTPSG IDCGSGRSTP 150
    SSVSTVSTIC PGDLKVAAKL APNIPLEMEL PGVKIVHAQF NTPMQLYSDD 200
    NIMETLQGQV STALGETPLM SEPTASVPPE SDVYRMLHDN RNEPTQPRQS 250
    GSFRVLQGMV DDGSDDRPAG TRSVRAPVTK VHGGSGGAQR MPLCDKCGSG 300
    IVGAVVKARD KYRHPECFVC ADCNLNLKQK GYFFIEGELY CETHARARTK 350
    PPEGYDTVTL YPKA 364
    Length:364
    Mass (Da):39,232
    Last modified:May 24, 2005 - v1
    Checksum:i083802DF22D7A237
    GO
    Isoform 2 (identifier: Q53GG5-2) [UniParc]FASTAAdd to Basket

    Also known as: ALP-H

    The sequence of this isoform differs from the canonical sequence as follows:
         111-224: DGNYFEHKHN...GETPLMSEPT → EFKPIGTAHN...IPSSPQNEPT

    Show »
    Length:316
    Mass (Da):34,280
    Checksum:i99FB41E90188ED8A
    GO
    Isoform 3 (identifier: Q53GG5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-233: DGNYFEHKHN...TASVPPESDV → EFKPIGTAHN...TSIIFGPNLS
         234-364: Missing.

    Show »
    Length:189
    Mass (Da):20,214
    Checksum:i4DB3477EA08C336E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121P → A in AAC16670. (PubMed:9334352)Curated
    Sequence conflicti12 – 121P → A in AAC16672. (PubMed:9334352)Curated
    Sequence conflicti40 – 401A → G in AAC16670. (PubMed:9334352)Curated
    Sequence conflicti40 – 401A → G in AAC16672. (PubMed:9334352)Curated
    Sequence conflicti217 – 2171T → I in AAC16670. (PubMed:9334352)Curated
    Sequence conflicti221 – 2211S → N in AAB96665. (PubMed:10063829)Curated
    Sequence conflicti353 – 3531E → R in AAC16670. (PubMed:9334352)Curated
    Sequence conflicti353 – 3531E → R in AAC16672. (PubMed:9334352)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti127 – 1271V → M.
    Corresponds to variant rs11944325 [ dbSNP | Ensembl ].
    VAR_050166

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei111 – 233123DGNYF…PESDV → EFKPIGTAHNRRAQPFVAAA NIDDKRQVVSASYNSPIGLY STSNIQDALHGQLRGLIPSS PQKTGTTLNTSIIFGPNLS in isoform 3. 2 PublicationsVSP_016500Add
    BLAST
    Alternative sequencei111 – 224114DGNYF…MSEPT → EFKPIGTAHNRRAQPFVAAA NIDDKRQVVSASYNSPIGLY STSNIQDALHGQLRGLIPSS PQNEPT in isoform 2. 2 PublicationsVSP_016501Add
    BLAST
    Alternative sequencei234 – 364131Missing in isoform 3. 2 PublicationsVSP_016502Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF002280 mRNA. Translation: AAC16670.1.
    AF002282 mRNA. Translation: AAC16672.1.
    AF039018 mRNA. Translation: AAB96665.1.
    AK313253 mRNA. Translation: BAG36063.1.
    BT007341 mRNA. Translation: AAP36005.1.
    AK222966 mRNA. Translation: BAD96686.1.
    CH471056 Genomic DNA. Translation: EAX04641.1.
    BC001017 mRNA. No translation available.
    BC027870 mRNA. Translation: AAH27870.1.
    CCDSiCCDS3844.1. [Q53GG5-1]
    CCDS47172.1. [Q53GG5-2]
    RefSeqiNP_001107579.1. NM_001114107.4. [Q53GG5-2]
    NP_055291.2. NM_014476.5. [Q53GG5-1]
    UniGeneiHs.701364.

    Genome annotation databases

    EnsembliENST00000284767; ENSP00000284767; ENSG00000154553. [Q53GG5-3]
    ENST00000284770; ENSP00000284770; ENSG00000154553. [Q53GG5-1]
    ENST00000284771; ENSP00000284771; ENSG00000154553. [Q53GG5-2]
    GeneIDi27295.
    KEGGihsa:27295.
    UCSCiuc003ixw.4. human. [Q53GG5-1]
    uc003ixx.4. human. [Q53GG5-2]
    uc003ixy.3. human. [Q53GG5-3]

    Polymorphism databases

    DMDMi74740479.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF002280 mRNA. Translation: AAC16670.1 .
    AF002282 mRNA. Translation: AAC16672.1 .
    AF039018 mRNA. Translation: AAB96665.1 .
    AK313253 mRNA. Translation: BAG36063.1 .
    BT007341 mRNA. Translation: AAP36005.1 .
    AK222966 mRNA. Translation: BAD96686.1 .
    CH471056 Genomic DNA. Translation: EAX04641.1 .
    BC001017 mRNA. No translation available.
    BC027870 mRNA. Translation: AAH27870.1 .
    CCDSi CCDS3844.1. [Q53GG5-1 ]
    CCDS47172.1. [Q53GG5-2 ]
    RefSeqi NP_001107579.1. NM_001114107.4. [Q53GG5-2 ]
    NP_055291.2. NM_014476.5. [Q53GG5-1 ]
    UniGenei Hs.701364.

    3D structure databases

    ProteinModelPortali Q53GG5.
    SMRi Q53GG5. Positions 5-93, 269-352.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118119. 2 interactions.
    IntActi Q53GG5. 9 interactions.
    STRINGi 9606.ENSP00000284770.

    PTM databases

    PhosphoSitei Q53GG5.

    Polymorphism databases

    DMDMi 74740479.

    Proteomic databases

    MaxQBi Q53GG5.
    PaxDbi Q53GG5.
    PRIDEi Q53GG5.

    Protocols and materials databases

    DNASUi 27295.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284767 ; ENSP00000284767 ; ENSG00000154553 . [Q53GG5-3 ]
    ENST00000284770 ; ENSP00000284770 ; ENSG00000154553 . [Q53GG5-1 ]
    ENST00000284771 ; ENSP00000284771 ; ENSG00000154553 . [Q53GG5-2 ]
    GeneIDi 27295.
    KEGGi hsa:27295.
    UCSCi uc003ixw.4. human. [Q53GG5-1 ]
    uc003ixx.4. human. [Q53GG5-2 ]
    uc003ixy.3. human. [Q53GG5-3 ]

    Organism-specific databases

    CTDi 27295.
    GeneCardsi GC04M186422.
    HGNCi HGNC:20767. PDLIM3.
    HPAi HPA004749.
    MIMi 605889. gene.
    neXtProti NX_Q53GG5.
    PharmGKBi PA134970631.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258467.
    HOVERGENi HBG061371.
    InParanoidi Q53GG5.
    OMAi SMSEPTA.
    OrthoDBi EOG77DJ69.
    PhylomeDBi Q53GG5.
    TreeFami TF106408.

    Miscellaneous databases

    ChiTaRSi PDLIM3. human.
    GeneWikii PDLIM3.
    GenomeRNAii 27295.
    NextBioi 50262.
    PROi Q53GG5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53GG5.
    Bgeei Q53GG5.
    CleanExi HS_PDLIM3.
    Genevestigatori Q53GG5.

    Family and domain databases

    Gene3Di 2.10.110.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR001478. PDZ.
    IPR006643. ZASP.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM00132. LIM. 1 hit.
    SM00228. PDZ. 1 hit.
    SM00735. ZM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs."
      Xia H., Winokur S.T., Kuo W.-L., Altherr M.R., Bredt D.S.
      J. Cell Biol. 139:507-515(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Skeletal muscle.
    2. "Exclusion of muscle specific actinin-associated LIM protein (ALP) gene from 4q35 facioscapulohumeral muscular dystrophy (FSHD) candidate genes."
      Bouju S., Pietu G., Le Cunff M., Cros N., Malzac P., Pellissier J.-F., Pons F., Leger J.-J., Auffray C., Dechesne C.A.
      Neuromuscul. Disord. 9:3-10(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    3. "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].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 2 AND 3).
      Tissue: Lung and Skin.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPDLI3_HUMAN
    AccessioniPrimary (citable) accession number: Q53GG5
    Secondary accession number(s): B2R866
    , O43590, O60439, O60440, Q8N6Y6, Q9BVP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3