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Q9NR12

- PDLI7_HUMAN

UniProt

Q9NR12 - PDLI7_HUMAN

Protein

PDZ and LIM domain protein 7

Gene

PDLIM7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. cell differentiation Source: UniProtKB-KW
    3. multicellular organismal development Source: UniProtKB-KW
    4. ossification Source: UniProtKB-KW
    5. positive regulation of osteoblast differentiation Source: Ensembl
    6. receptor-mediated endocytosis Source: ProtInc

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Osteogenesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PDZ and LIM domain protein 7
    Alternative name(s):
    LIM mineralization protein
    Short name:
    LMP
    Protein enigma
    Gene namesi
    Name:PDLIM7
    Synonyms:ENIGMA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:22958. PDLIM7.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity
    Note: Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin filaments By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. cytoplasm Source: UniProtKB-SubCell
    3. focal adhesion Source: HPA
    4. nucleus Source: HPA
    5. ruffle Source: Ensembl
    6. stress fiber Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 162GF → AA: Loss of binding to TPM2.
    Mutagenesisi63 – 631H → A: Loss of binding to TPM2. 1 Publication

    Organism-specific databases

    PharmGKBiPA128394546.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 457457PDZ and LIM domain protein 7PRO_0000075881Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei247 – 2471Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NR12.
    PaxDbiQ9NR12.
    PRIDEiQ9NR12.

    PTM databases

    PhosphoSiteiQ9NR12.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed ubiquitously, however, isoform 2 predominates in skeletal muscle, isoform 1 is more abundant in lung, spleen, leukocytes and fetal liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9NR12.
    BgeeiQ9NR12.
    CleanExiHS_PDLIM7.
    GenevestigatoriQ9NR12.

    Organism-specific databases

    HPAiHPA018794.
    HPA048815.

    Interactioni

    Subunit structurei

    Binds via its LIM zinc-binding 3 domain (LIM 3) to endocytic codes of INSR, but not with those of IGF1R, LDLR, TFRC, or EGFR. Interacts with various PKC isoforms through the LIM zinc-binding domains. Binds to RET in a phosphorylation-independent manner via its LIM zinc-binding domain 2 (LIM 2). Probably part of a complex with SHC and the RET dimer. Interacts with TPM2. Interacts with TBX4 and TBX5 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hoxa1P090223EBI-350517,EBI-3957603From a different organism.
    UBQLN4Q9NRR52EBI-350517,EBI-711226

    Protein-protein interaction databases

    BioGridi114682. 42 interactions.
    IntActiQ9NR12. 27 interactions.
    MINTiMINT-94304.
    STRINGi9606.ENSP00000348099.

    Structurei

    Secondary structure

    457
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 1212
    Beta strandi16 – 216
    Helixi22 – 243
    Beta strandi26 – 338
    Helixi38 – 414
    Beta strandi49 – 535
    Helixi58 – 603
    Helixi63 – 719
    Beta strandi76 – 849

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q3GX-ray1.11A/B1-84[»]
    ProteinModelPortaliQ9NR12.
    SMRiQ9NR12. Positions 1-84, 278-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NR12.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8585PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini280 – 33859LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 39860LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini399 – 45759LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The LIM zinc-binding 2 (LIM 2) domain interacts with TBX4.By similarity
    The LIM zinc-binding 3 (LIM 3) domain provides the structural basis for recognition of tyrosine-containing tight turn structures. This domain is necessary and sufficient for interaction with TBX5 By similarity.By similarity
    Anchored to cell periphery via its N-terminal PDZ domain.

    Sequence similaritiesi

    Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG286537.
    HOVERGENiHBG051478.
    InParanoidiQ9NR12.
    OMAiWPGPTAP.
    OrthoDBiEOG7HXCQB.
    PhylomeDBiQ9NR12.
    TreeFamiTF106408.

    Family and domain databases

    Gene3Di2.10.110.10. 3 hits.
    2.30.42.10. 1 hit.
    InterProiIPR001478. PDZ.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 3 hits.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    SMARTiSM00132. LIM. 3 hits.
    SM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NR12-1) [UniParc]FASTAAdd to Basket

    Also known as: LMP-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.

    « Hide

    MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV    50
    LSIDGENAGS LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD 100
    PPRYTFAPSV SLNKTARPFG APPPADSAPQ QNGQPLRPLV PDASKQRLME 150
    NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ DPDEEHLKKS SQVPRTEAPA 200
    PASSTPQEPW PGPTAPSPTS RPPWAVDPAF AERYAPDKTS TVLTRHSQPA 250
    TPTPLQSRTS IVQAAAGGVP GGGSNNGKTP VCHQCHKVIR GRYLVALGHA 300
    YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP PCYDVRYAPS CAKCKKKITG 350
    EIMHALKMTW HVHCFTCAAC KTPIRNRAFY MEEGVPYCER DYEKMFGTKC 400
    HGCDFKIDAG DRFLEALGFS WHDTCFVCAI CQINLEGKTF YSKKDRPLCK 450
    SHAFSHV 457
    Length:457
    Mass (Da):49,845
    Last modified:October 1, 2000 - v1
    Checksum:iAA37F9E8E987D990
    GO
    Isoform 2 (identifier: Q9NR12-2) [UniParc]FASTAAdd to Basket

    Also known as: LMP-2

    The sequence of this isoform differs from the canonical sequence as follows:
         94-133: ASAPAADPPRYTFAPSVSLNKTARPFGAPPPADSAPQQNG → VQTPDK

    Note: Did not induce bone induction.

    Show »
    Length:423
    Mass (Da):46,510
    Checksum:i486E854CABB4D494
    GO
    Isoform 3 (identifier: Q9NR12-3) [UniParc]FASTAAdd to Basket

    Also known as: LMP-3

    The sequence of this isoform differs from the canonical sequence as follows:
         134-153: QPLRPLVPDASKQRLMENTE → CRPLTNSRSDRWSQMPASSG
         154-457: Missing.

    Note: Same activity as isoform 1 in bone nodule induction.

    Show »
    Length:153
    Mass (Da):16,034
    Checksum:i257AD5C3CD61F6F1
    GO
    Isoform 4 (identifier: Q9NR12-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-287: SQVPRTEAPA...KTPVCHQCHK → RPYRPQPYQP...PRVPPGGVCV
         288-457: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:287
    Mass (Da):30,411
    Checksum:i7B30CF3E6197899C
    GO
    Isoform 5 (identifier: Q9NR12-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         192-457: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:191
    Mass (Da):20,514
    Checksum:iB9B6B99E12B23B25
    GO
    Isoform 6 (identifier: Q9NR12-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-222: SQVPRTEAPAPASSTPQEPWPGPTAPSPTSRP → REKYVLELQSPRYTRLRDWHHQRSAHVLNVQS
         223-457: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:222
    Mass (Da):24,413
    Checksum:iADF21719E4928621
    GO

    Sequence cautioni

    The sequence AAC37565.1 differs from that shown. Reason: Frameshift at positions 103, 128, 161, 183, 195 and 245.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381P → Q in BC067806. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti326 – 3261A → T.
    Corresponds to variant rs2306764 [ dbSNP | Ensembl ].
    VAR_050168
    Natural varianti450 – 4501K → N in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036193

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei94 – 13340ASAPA…PQQNG → VQTPDK in isoform 2. 1 PublicationVSP_016509Add
    BLAST
    Alternative sequencei134 – 15320QPLRP…MENTE → CRPLTNSRSDRWSQMPASSG in isoform 3. 1 PublicationVSP_016510Add
    BLAST
    Alternative sequencei154 – 457304Missing in isoform 3. 1 PublicationVSP_016513Add
    BLAST
    Alternative sequencei191 – 28797SQVPR…HQCHK → RPYRPQPYQPPALGCGPCVC RALCPGQNEHSADPAQPAGH AHAAAEPHLHCAGSCRRGAR RGQQQRQDSRVSPVPQGHPG PLPGGAGPRVPPGGVCV in isoform 4. 1 PublicationVSP_016511Add
    BLAST
    Alternative sequencei191 – 22232SQVPR…PTSRP → REKYVLELQSPRYTRLRDWH HQRSAHVLNVQS in isoform 6. 1 PublicationVSP_016512Add
    BLAST
    Alternative sequencei192 – 457266Missing in isoform 5. 1 PublicationVSP_016514Add
    BLAST
    Alternative sequencei223 – 457235Missing in isoform 6. 1 PublicationVSP_016515Add
    BLAST
    Alternative sequencei288 – 457170Missing in isoform 4. 1 PublicationVSP_016516Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35240 Genomic DNA. Translation: AAC37565.1. Frameshift.
    AF345904 mRNA. Translation: AAK30567.1.
    AF345905 mRNA. Translation: AAK30568.1.
    AF345906 mRNA. Translation: AAK30569.1.
    AF265209 mRNA. Translation: AAF76152.1.
    BC001093 mRNA. Translation: AAH01093.1.
    BC014521 mRNA. Translation: AAH14521.1.
    BC067806 mRNA. No translation available.
    BC084575 mRNA. Translation: AAH84575.1.
    CCDSiCCDS4422.1. [Q9NR12-1]
    CCDS4423.1. [Q9NR12-2]
    CCDS4424.1. [Q9NR12-6]
    PIRiA55050.
    RefSeqiNP_005442.2. NM_005451.4. [Q9NR12-1]
    NP_976227.1. NM_203352.2. [Q9NR12-2]
    NP_998801.1. NM_213636.2. [Q9NR12-6]
    UniGeneiHs.533040.
    Hs.736984.

    Genome annotation databases

    EnsembliENST00000355572; ENSP00000347776; ENSG00000196923. [Q9NR12-6]
    ENST00000355841; ENSP00000348099; ENSG00000196923. [Q9NR12-1]
    ENST00000359895; ENSP00000352964; ENSG00000196923. [Q9NR12-2]
    ENST00000393551; ENSP00000377182; ENSG00000196923. [Q9NR12-4]
    ENST00000486828; ENSP00000439157; ENSG00000196923. [Q9NR12-5]
    ENST00000493815; ENSP00000431236; ENSG00000196923. [Q9NR12-3]
    GeneIDi9260.
    KEGGihsa:9260.
    UCSCiuc003mha.1. human. [Q9NR12-1]
    uc003mhb.1. human. [Q9NR12-2]
    uc003mhf.3. human. [Q9NR12-4]
    uc003mhg.1. human. [Q9NR12-6]

    Polymorphism databases

    DMDMi74752914.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35240 Genomic DNA. Translation: AAC37565.1 . Frameshift.
    AF345904 mRNA. Translation: AAK30567.1 .
    AF345905 mRNA. Translation: AAK30568.1 .
    AF345906 mRNA. Translation: AAK30569.1 .
    AF265209 mRNA. Translation: AAF76152.1 .
    BC001093 mRNA. Translation: AAH01093.1 .
    BC014521 mRNA. Translation: AAH14521.1 .
    BC067806 mRNA. No translation available.
    BC084575 mRNA. Translation: AAH84575.1 .
    CCDSi CCDS4422.1. [Q9NR12-1 ]
    CCDS4423.1. [Q9NR12-2 ]
    CCDS4424.1. [Q9NR12-6 ]
    PIRi A55050.
    RefSeqi NP_005442.2. NM_005451.4. [Q9NR12-1 ]
    NP_976227.1. NM_203352.2. [Q9NR12-2 ]
    NP_998801.1. NM_213636.2. [Q9NR12-6 ]
    UniGenei Hs.533040.
    Hs.736984.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q3G X-ray 1.11 A/B 1-84 [» ]
    ProteinModelPortali Q9NR12.
    SMRi Q9NR12. Positions 1-84, 278-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114682. 42 interactions.
    IntActi Q9NR12. 27 interactions.
    MINTi MINT-94304.
    STRINGi 9606.ENSP00000348099.

    PTM databases

    PhosphoSitei Q9NR12.

    Polymorphism databases

    DMDMi 74752914.

    Proteomic databases

    MaxQBi Q9NR12.
    PaxDbi Q9NR12.
    PRIDEi Q9NR12.

    Protocols and materials databases

    DNASUi 9260.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355572 ; ENSP00000347776 ; ENSG00000196923 . [Q9NR12-6 ]
    ENST00000355841 ; ENSP00000348099 ; ENSG00000196923 . [Q9NR12-1 ]
    ENST00000359895 ; ENSP00000352964 ; ENSG00000196923 . [Q9NR12-2 ]
    ENST00000393551 ; ENSP00000377182 ; ENSG00000196923 . [Q9NR12-4 ]
    ENST00000486828 ; ENSP00000439157 ; ENSG00000196923 . [Q9NR12-5 ]
    ENST00000493815 ; ENSP00000431236 ; ENSG00000196923 . [Q9NR12-3 ]
    GeneIDi 9260.
    KEGGi hsa:9260.
    UCSCi uc003mha.1. human. [Q9NR12-1 ]
    uc003mhb.1. human. [Q9NR12-2 ]
    uc003mhf.3. human. [Q9NR12-4 ]
    uc003mhg.1. human. [Q9NR12-6 ]

    Organism-specific databases

    CTDi 9260.
    GeneCardsi GC05M176912.
    HGNCi HGNC:22958. PDLIM7.
    HPAi HPA018794.
    HPA048815.
    MIMi 605903. gene.
    neXtProti NX_Q9NR12.
    PharmGKBi PA128394546.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG286537.
    HOVERGENi HBG051478.
    InParanoidi Q9NR12.
    OMAi WPGPTAP.
    OrthoDBi EOG7HXCQB.
    PhylomeDBi Q9NR12.
    TreeFami TF106408.

    Miscellaneous databases

    ChiTaRSi PDLIM7. human.
    EvolutionaryTracei Q9NR12.
    GeneWikii PDLIM7.
    GenomeRNAii 9260.
    NextBioi 34707.
    PROi Q9NR12.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NR12.
    Bgeei Q9NR12.
    CleanExi HS_PDLIM7.
    Genevestigatori Q9NR12.

    Family and domain databases

    Gene3Di 2.10.110.10. 3 hits.
    2.30.42.10. 1 hit.
    InterProi IPR001478. PDZ.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 3 hits.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM00132. LIM. 3 hits.
    SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "LIM domain recognition of a tyrosine-containing tight turn."
      Wu R.-Y., Gill G.N.
      J. Biol. Chem. 269:25085-25090(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH INSR.
    2. "Overexpressed LIM mineralization proteins do not require LIM domains to induce bone."
      Liu Y., Hair G.A., Boden S.D., Viggeswarapu M., Titus L.
      J. Bone Miner. Res. 17:406-414(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
      Tissue: Heart.
    3. "Enigma sequence and interaction with Ret."
      Borrello M.G., Billaud M., Mercalli E., Ghizzoni S., Bidaud C.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Neuroepithelium.
    4. "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 1; 4; 5 AND 6).
      Tissue: Brain, Kidney, Mammary gland and Uterus.
    5. Bienvenut W.V., Claeys D.
      Submitted (NOV-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-17; 94-103 AND 246-258, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    6. "Protein-protein interaction of zinc finger LIM domains with protein kinase C."
      Kuroda S., Tokunaga C., Kiyohara Y., Higuchi O., Konishi H., Mizuno K., Gill G.N., Kikkawa U.
      J. Biol. Chem. 271:31029-31032(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKC.
    7. "Shc and Enigma are both required for mitogenic signaling by Ret/ptc2."
      Durick K., Gill G.N., Taylor S.S.
      Mol. Cell. Biol. 18:2298-2308(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RET AND SHC1.
    8. "The PDZ domain of the LIM protein enigma binds to beta-tropomyosin."
      Guy P.M., Kenny D.A., Gill G.N.
      Mol. Biol. Cell 10:1973-1984(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TPM2, MUTAGENESIS OF 15-GLY-PHE-16 AND HIS-63.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure of the PDZ domain of human PDLIM7 bound to a C-terminal extension from human beta-tropomyosin."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 1-84.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-450.

    Entry informationi

    Entry nameiPDLI7_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR12
    Secondary accession number(s): Q14250
    , Q5XG82, Q6NVZ5, Q96C91, Q9BXB8, Q9BXB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 121 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3