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O00151

- PDLI1_HUMAN

UniProt

O00151 - PDLI1_HUMAN

Protein

PDZ and LIM domain protein 1

Gene

PDLIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi260 – 2601Zinc 1
    Metal bindingi263 – 2631Zinc 1
    Metal bindingi280 – 2801Zinc 1
    Metal bindingi283 – 2831Zinc 1
    Metal bindingi286 – 2861Zinc 2
    Metal bindingi289 – 2891Zinc 2
    Metal bindingi307 – 3071Zinc 2
    Metal bindingi310 – 3101Zinc 2

    GO - Molecular functioni

    1. transcription coactivator activity Source: Ensembl
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: Ensembl
    2. response to hypoxia Source: Ensembl
    3. response to oxidative stress Source: ProtInc

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PDZ and LIM domain protein 1
    Alternative name(s):
    C-terminal LIM domain protein 1
    Elfin
    LIM domain protein CLP-36
    Gene namesi
    Name:PDLIM1
    Synonyms:CLIM1, CLP36
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2067. PDLIM1.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity
    Note: Associates with the actin stress fibers.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. cytoskeleton Source: UniProtKB-SubCell
    3. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33158.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 329328PDZ and LIM domain protein 1PRO_0000075859Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine3 Publications
    Modified residuei90 – 901Phosphoserine5 Publications
    Modified residuei130 – 1301Phosphoserine1 Publication
    Modified residuei144 – 1441Phosphotyrosine1 Publication
    Modified residuei321 – 3211Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00151.
    PaxDbiO00151.
    PeptideAtlasiO00151.
    PRIDEiO00151.

    2D gel databases

    OGPiO00151.
    UCD-2DPAGEO00151.

    PTM databases

    PhosphoSiteiO00151.

    Expressioni

    Tissue specificityi

    Strongly expressed in the heart and skeletal muscle, moderately expressed in the spleen, small intestine, colon, placenta, and lung. A lower level expression is seen in liver, thymus, kidney, prostate and pancreas and is not found in the brain, testis, ovary, and peripheral blood leukocytes.

    Gene expression databases

    BgeeiO00151.
    CleanExiHS_PDLIM1.
    GenevestigatoriO00151.

    Organism-specific databases

    HPAiHPA017010.

    Interactioni

    Subunit structurei

    Interacts with alpha-actinins 1, 2 and 4.2 Publications

    Protein-protein interaction databases

    BioGridi114572. 19 interactions.
    IntActiO00151. 11 interactions.
    MINTiMINT-5005794.
    STRINGi9606.ENSP00000360305.

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1211
    Beta strandi15 – 217
    Helixi22 – 243
    Beta strandi26 – 338
    Helixi38 – 414
    Beta strandi49 – 535
    Helixi63 – 719
    Beta strandi74 – 8411
    Beta strandi261 – 2633
    Turni281 – 2844
    Beta strandi287 – 2893
    Helixi293 – 2964
    Beta strandi299 – 3035
    Helixi308 – 3158

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X62NMR-A250-315[»]
    2PKTX-ray1.50A1-86[»]
    ProteinModelPortaliO00151.
    SMRiO00151. Positions 1-87, 251-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00151.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8583PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini258 – 31760LIM 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

    eggNOGiNOG250485.
    HOGENOMiHOG000290704.
    HOVERGENiHBG061371.
    InParanoidiO00151.
    OMAiNLCIGDI.
    OrthoDBiEOG77DJ69.
    PhylomeDBiO00151.
    TreeFamiTF106408.

    Family and domain databases

    Gene3Di2.10.110.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR028537. PDLIM1.
    IPR001478. PDZ.
    IPR006643. ZASP.
    IPR001781. Znf_LIM.
    [Graphical view]
    PANTHERiPTHR24214:SF5. PTHR24214:SF5. 1 hit.
    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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O00151-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTQQIDLQG PGPWGFRLVG GKDFEQPLAI SRVTPGSKAA LANLCIGDVI    50
    TAIDGENTSN MTHLEAQNRI KGCTDNLTLT VARSEHKVWS PLVTEEGKRH 100
    PYKMNLASEP QEVLHIGSAH NRSAMPFTAS PASSTTARVI TNQYNNPAGL 150
    YSSENISNFN NALESKTAAS GVEANSRPLD HAQPPSSLVI DKESEVYKML 200
    QEKQELNEPP KQSTSFLVLQ EILESEEKGD PNKPSGFRSV KAPVTKVAAS 250
    IGNAQKLPMC DKCGTGIVGV FVKLRDRHRH PECYVCTDCG TNLKQKGHFF 300
    VEDQIYCEKH ARERVTPPEG YEVVTVFPK 329
    Length:329
    Mass (Da):36,072
    Last modified:January 23, 2007 - v4
    Checksum:iC85881A04D63D314
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211G → R in AAC05580. (PubMed:10022510)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751N → S.2 Publications
    Corresponds to variant rs2296961 [ dbSNP | Ensembl ].
    VAR_022271

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90878 mRNA. Translation: AAC05580.1.
    AJ310549 mRNA. Translation: CAC32846.1.
    AK314792 mRNA. Translation: BAG37323.1.
    AY923052 Genomic DNA. Translation: AAW82438.1.
    AL160288, AL157834 Genomic DNA. Translation: CAH70720.1.
    AL157834, AL160288 Genomic DNA. Translation: CAH72341.1.
    BC000915 mRNA. Translation: AAH00915.1.
    BC018755 mRNA. Translation: AAH18755.1.
    CCDSiCCDS7441.1.
    RefSeqiNP_066272.1. NM_020992.3.
    UniGeneiHs.368525.

    Genome annotation databases

    EnsembliENST00000329399; ENSP00000360305; ENSG00000107438.
    GeneIDi9124.
    KEGGihsa:9124.
    UCSCiuc001kkh.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90878 mRNA. Translation: AAC05580.1 .
    AJ310549 mRNA. Translation: CAC32846.1 .
    AK314792 mRNA. Translation: BAG37323.1 .
    AY923052 Genomic DNA. Translation: AAW82438.1 .
    AL160288 , AL157834 Genomic DNA. Translation: CAH70720.1 .
    AL157834 , AL160288 Genomic DNA. Translation: CAH72341.1 .
    BC000915 mRNA. Translation: AAH00915.1 .
    BC018755 mRNA. Translation: AAH18755.1 .
    CCDSi CCDS7441.1.
    RefSeqi NP_066272.1. NM_020992.3.
    UniGenei Hs.368525.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X62 NMR - A 250-315 [» ]
    2PKT X-ray 1.50 A 1-86 [» ]
    ProteinModelPortali O00151.
    SMRi O00151. Positions 1-87, 251-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114572. 19 interactions.
    IntActi O00151. 11 interactions.
    MINTi MINT-5005794.
    STRINGi 9606.ENSP00000360305.

    PTM databases

    PhosphoSitei O00151.

    2D gel databases

    OGPi O00151.
    UCD-2DPAGE O00151.

    Proteomic databases

    MaxQBi O00151.
    PaxDbi O00151.
    PeptideAtlasi O00151.
    PRIDEi O00151.

    Protocols and materials databases

    DNASUi 9124.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329399 ; ENSP00000360305 ; ENSG00000107438 .
    GeneIDi 9124.
    KEGGi hsa:9124.
    UCSCi uc001kkh.4. human.

    Organism-specific databases

    CTDi 9124.
    GeneCardsi GC10M096997.
    HGNCi HGNC:2067. PDLIM1.
    HPAi HPA017010.
    MIMi 605900. gene.
    neXtProti NX_O00151.
    PharmGKBi PA33158.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250485.
    HOGENOMi HOG000290704.
    HOVERGENi HBG061371.
    InParanoidi O00151.
    OMAi NLCIGDI.
    OrthoDBi EOG77DJ69.
    PhylomeDBi O00151.
    TreeFami TF106408.

    Miscellaneous databases

    ChiTaRSi PDLIM1. human.
    EvolutionaryTracei O00151.
    GeneWikii PDLIM1.
    GenomeRNAii 9124.
    NextBioi 34201.
    PROi O00151.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00151.
    CleanExi HS_PDLIM1.
    Genevestigatori O00151.

    Family and domain databases

    Gene3Di 2.10.110.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR028537. PDLIM1.
    IPR001478. PDZ.
    IPR006643. ZASP.
    IPR001781. Znf_LIM.
    [Graphical view ]
    PANTHERi PTHR24214:SF5. PTHR24214:SF5. 1 hit.
    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. "Characterization of the human 36-kDa carboxyl terminal LIM domain protein (hCLIM1)."
      Kotaka M., Ngai S.M., Garcia-Barcelo M., Tsui S.K.W., Fung K.P., Lee C.Y., Waye M.M.Y.
      J. Cell. Biochem. 72:279-285(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "Human CLP-36, 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."
      Bauer K., Kratzer M., Otte M., Luber de Quintana K., Hagmann J., Arnold G.J., Eckerskorn C., Lottspeich F., Siess W.
      Blood 96:4236-4245(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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], VARIANT SER-175.
    4. NIEHS SNPs program
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-175.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Pancreas and Placenta.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-17.
      Tissue: Platelet.
    8. Bienvenut W.V., Claeys D.
      Submitted (NOV-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17; 23-32; 139-166; 212-238 AND 247-256, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    9. Cited for: INTERACTION WITH ALPHA-ACTININ-2.
    10. "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4."
      Vallenius T., Luukko K., Makela T.P.
      J. Biol. Chem. 275:11100-11105(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALPHA-ACTININ-1 AND ALPHA-ACTININ-4.
    11. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Solution structure of the LIM domain of carboxyl terminal LIM domain protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 250-315, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiPDLI1_HUMAN
    AccessioniPrimary (citable) accession number: O00151
    Secondary accession number(s): B2RBS6, Q5VZH5, Q9BPZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 4 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 10
      Human chromosome 10: 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