PDLIM1

Protein-coding gene in the species Homo sapiens
PDLIM1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1X62, 2PKT

Identifiers
AliasesPDLIM1, CLIM1, CLP-36, CLP36, HEL-S-112, hCLIM1, PDZ and LIM domain 1
External IDsOMIM: 605900; MGI: 1860611; HomoloGene: 9643; GeneCards: PDLIM1; OMA:PDLIM1 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for PDLIM1
Genomic location for PDLIM1
Band10q23.33Start95,237,572 bp[1]
End95,291,012 bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for PDLIM1
Genomic location for PDLIM1
Band19|19 C3Start40,209,617 bp[2]
End40,260,286 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • lower lobe of lung

  • nasal epithelium

  • mucosa of urinary bladder

  • right lung

  • pericardium

  • gingival epithelium

  • upper lobe of lung

  • olfactory zone of nasal mucosa

  • palpebral conjunctiva

  • upper lobe of left lung
Top expressed in
  • ileum

  • placenta

  • jejunum

  • duodenum

  • esophagus

  • colon

  • uterus

  • zygote

  • lens

  • genital tubercle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transcription coactivator activity
  • metal ion binding
  • cadherin binding involved in cell-cell adhesion
  • actin binding
  • muscle alpha-actinin binding
Cellular component
  • cytoplasm
  • cytoskeleton
  • focal adhesion
  • transcription regulator complex
  • Z discdkac
  • stress fiber
  • filamentous actin
Biological process
  • response to hypoxia
  • regulation of transcription, DNA-templated
  • response to oxidative stress
  • cell-cell adhesion
  • positive regulation of nucleic acid-templated transcription
  • heart development
  • actin cytoskeleton organization
  • muscle structure development
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9124

54132

Ensembl

ENSG00000107438

ENSMUSG00000055044

UniProt

O00151

O70400

RefSeq (mRNA)

NM_020992

NM_016861

RefSeq (protein)

NP_066272

NP_058557

Location (UCSC)Chr 10: 95.24 – 95.29 MbChr 19: 40.21 – 40.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

PDZ and LIM domain protein 1 is a protein that in humans is encoded by the PDLIM1 gene.[5][6]

Interactions

PDLIM1 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000107438 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000055044 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kotaka M, Kostin S, Ngai S, Chan K, Lau Y, Lee SM, Li Hy, Ng EK, Schaper J, Tsui SK, Fung Kp, Lee Cy, Waye MM (October 2000). "Interaction of hCLIM1, an enigma family protein, with alpha-actinin 2". J Cell Biochem. 78 (4): 558–65. doi:10.1002/1097-4644(20000915)78:4<558::AID-JCB5>3.0.CO;2-I. PMID 10861853. S2CID 84122657.
  6. ^ "Entrez Gene: PDLIM1 PDZ and LIM domain 1 (elfin)".
  7. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  8. ^ a b Vallenius T, Luukko K, Mäkelä TP (April 2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. PMID 10753915.
  9. ^ Bauer K, Kratzer M, Otte M, de Quintana KL, Hagmann J, Arnold GJ, Eckerskorn C, Lottspeich F, Siess W (December 2000). "Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells". Blood. 96 (13): 4236–45. doi:10.1182/blood.V96.13.4236. PMID 11110697.
  10. ^ a b Johnsen SA, Güngör C, Prenzel T, Riethdorf S, Riethdorf L, Taniguchi-Ishigaki N, Rau T, Tursun B, Furlow JD, Sauter G, Scheffner M, Pantel K, Gannon F, Bach I (January 2009). "Regulation of estrogen-dependent transcription by the LIM cofactors CLIM and RLIM in breast cancer". Cancer Res. 69 (1): 128–36. doi:10.1158/0008-5472.CAN-08-1630. PMC 2713826. PMID 19117995.

Further reading

  • Wang H, Harrison-Shostak DC, Lemasters JJ, Herman B (1996). "Cloning of a rat cDNA encoding a novel LIM domain protein with high homology to rat RIL". Gene. 165 (2): 267–71. doi:10.1016/0378-1119(95)00542-E. PMID 8522188.
  • Kotaka M, Ngai SM, Garcia-Barcelo M, Tsui SK, Fung KP, Lee CY, Waye MM (1999). "Characterization of the human 36-kDa carboxyl terminal LIM domain protein (hCLIM1)". J. Cell. Biochem. 72 (2): 279–85. doi:10.1002/(SICI)1097-4644(19990201)72:2<279::AID-JCB12>3.0.CO;2-7. PMID 10022510. S2CID 23811125.
  • Vallenius T, Luukko K, Mäkelä TP (2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. PMID 10753915.
  • Bauer K, Kratzer M, Otte M, de Quintana KL, Hagmann J, Arnold GJ, Eckerskorn C, Lottspeich F, Siess W (2001). "Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells". Blood. 96 (13): 4236–45. doi:10.1182/blood.V96.13.4236. PMID 11110697.
  • Ostendorff HP, Peirano RI, Peters MA, Schlüter A, Bossenz M, Scheffner M, Bach I (2002). "Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors". Nature. 416 (6876): 99–103. Bibcode:2002Natur.416...99O. doi:10.1038/416099a. PMID 11882901. S2CID 4426785.
  • Vallenius T, Mäkelä TP (2003). "Clik1: a novel kinase targeted to actin stress fibers by the CLP-36 PDZ-LIM protein". J. Cell Sci. 115 (Pt 10): 2067–73. doi:10.1242/jcs.115.10.2067. PMID 11973348.
  • Kioussi C, Briata P, Baek SH, Rose DW, Hamblet NS, Herman T, Ohgi KA, Lin C, Gleiberman A, Wang J, Brault V, Ruiz-Lozano P, Nguyen HD, Kemler R, Glass CK, Wynshaw-Boris A, Rosenfeld MG (2003). "Identification of a Wnt/Dvl/beta-Catenin --> Pitx2 pathway mediating cell-type-specific proliferation during development". Cell. 111 (5): 673–85. doi:10.1016/S0092-8674(02)01084-X. PMID 12464179. S2CID 16108479.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
  • Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Miehe U, Kadyrov M, Neumaier-Wagner P, Bartz C, Rath W, Huppertz B (2007). "Expression of the actin stress fiber-associated protein CLP36 in the human placenta". Histochem. Cell Biol. 126 (4): 465–71. doi:10.1007/s00418-006-0182-5. PMID 16609848. S2CID 22394948.
  • v
  • t
  • e
  • 1x62: Solution structure of the LIM domain of carboxyl terminal LIM domain protein 1
    1x62: Solution structure of the LIM domain of carboxyl terminal LIM domain protein 1
  • 2pkt: Crystal structure of the human CLP-36 (PDLIM1) bound to the C-terminal peptide of human alpha-actinin-1
    2pkt: Crystal structure of the human CLP-36 (PDLIM1) bound to the C-terminal peptide of human alpha-actinin-1


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