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P48059

- LIMS1_HUMAN

UniProt

P48059 - LIMS1_HUMAN

Protein

LIM and senescent cell antigen-like-containing domain protein 1

Gene

LIMS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell aging Source: ProtInc
    2. cell junction assembly Source: Reactome
    3. cellular response to transforming growth factor beta stimulus Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_20649. Cell-extracellular matrix interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LIM and senescent cell antigen-like-containing domain protein 1
    Alternative name(s):
    Particularly interesting new Cys-His protein 1
    Short name:
    PINCH-1
    Renal carcinoma antigen NY-REN-48
    Gene namesi
    Name:LIMS1
    Synonyms:PINCH, PINCH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6616. LIMS1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. focal adhesion Source: UniProtKB
    3. perinuclear region of cytoplasm Source: UniProtKB
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421F → A: Loss of interaction with ILK and loss of localization to focal adhesion. 2 Publications
    Mutagenesisi56 – 561R → A: Alters interaction with ILK. 1 Publication
    Mutagenesisi61 – 611H → D: Alters interaction with ILK. 1 Publication
    Mutagenesisi62 – 621D → A: Alters interaction with ILK. 1 Publication
    Mutagenesisi66 – 661L → D: Alters interaction with ILK. 1 Publication

    Organism-specific databases

    PharmGKBiPA30389.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 325324LIM and senescent cell antigen-like-containing domain protein 1PRO_0000075888Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48059.
    PaxDbiP48059.
    PRIDEiP48059.

    2D gel databases

    OGPiP48059.

    PTM databases

    PhosphoSiteiP48059.

    Expressioni

    Tissue specificityi

    Expressed in most tissues except in the brain.

    Gene expression databases

    ArrayExpressiP48059.
    BgeeiP48059.
    CleanExiHS_LIMS1.
    GenevestigatoriP48059.

    Interactioni

    Subunit structurei

    Interacts (via LIM zinc-binding 5) with TGFB1I1 By similarity. Interacts with integrin-linked protein kinase 1 (ILK) via the first LIM domain, and in competition with LIMS2. Part of the heterotrimeric IPP complex composed of integrin-linked kinase (ILK), LIMS1 or LIMS2, and PARVA. Interacts with SH3/SH2 adapter NCK2, thereby linking the complex to cell surface receptors.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hoxa1P090223EBI-306928,EBI-3957603From a different organism.
    ILKQ134185EBI-306928,EBI-747644
    IlkO552223EBI-306928,EBI-6690138From a different organism.
    NCK2O436392EBI-306928,EBI-713635

    Protein-protein interaction databases

    BioGridi110175. 16 interactions.
    DIPiDIP-40671N.
    IntActiP48059. 29 interactions.
    MINTiMINT-5004275.
    STRINGi9606.ENSP00000331775.

    Structurei

    Secondary structure

    1
    325
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni11 – 133
    Beta strandi22 – 265
    Beta strandi29 – 324
    Turni33 – 353
    Turni39 – 413
    Helixi46 – 483
    Beta strandi51 – 533
    Beta strandi56 – 583
    Helixi60 – 667
    Beta strandi72 – 743
    Beta strandi83 – 853
    Beta strandi88 – 903
    Turni92 – 943
    Beta strandi98 – 1003
    Beta strandi105 – 1073
    Beta strandi110 – 1123
    Beta strandi115 – 1173
    Helixi119 – 1268
    Turni136 – 1383
    Beta strandi150 – 1523
    Turni156 – 1583
    Beta strandi162 – 1643
    Beta strandi173 – 1753
    Beta strandi178 – 1803
    Helixi182 – 1865
    Turni194 – 1974
    Beta strandi210 – 2134
    Turni214 – 2163
    Turni220 – 2223
    Beta strandi227 – 2293
    Beta strandi232 – 2343
    Beta strandi237 – 2393
    Helixi241 – 2477

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G47NMR-A1-70[»]
    1NYPNMR-A188-251[»]
    1U5SNMR-B188-251[»]
    2CORNMR-A125-190[»]
    2D8XNMR-A71-127[»]
    2KBXNMR-B1-70[»]
    3F6QX-ray1.60B6-68[»]
    4HI8X-ray1.20B6-68[»]
    4HI9X-ray1.20B6-68[»]
    ProteinModelPortaliP48059.
    SMRiP48059. Positions 6-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48059.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 6253LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini71 – 12151LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini135 – 18450LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini193 – 24351LIM zinc-binding 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini252 – 30352LIM zinc-binding 5PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 5 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG263350.
    HOGENOMiHOG000253950.
    HOVERGENiHBG000053.
    InParanoidiP48059.
    OMAiNQNRALC.
    PhylomeDBiP48059.
    TreeFamiTF314113.

    Family and domain databases

    Gene3Di2.10.110.10. 5 hits.
    InterProiIPR017351. PINCH.
    IPR001781. Znf_LIM.
    [Graphical view]
    PANTHERiPTHR24210. PTHR24210. 1 hit.
    PfamiPF00412. LIM. 5 hits.
    [Graphical view]
    PIRSFiPIRSF038003. PINCH. 1 hit.
    SMARTiSM00132. LIM. 5 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 5 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P48059-1) [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

    MANALASATC ERCKGGFAPA EKIVNSNGEL YHEQCFVCAQ CFQQFPEGLF    50
    YEFEGRKYCE HDFQMLFAPC CHQCGEFIIG RVIKAMNNSW HPECFRCDLC 100
    QEVLADIGFV KNAGRHLCRP CHNREKARGL GKYICQKCHA IIDEQPLIFK 150
    NDPYHPDHFN CANCGKELTA DARELKGELY CLPCHDKMGV PICGACRRPI 200
    EGRVVNAMGK QWHVEHFVCA KCEKPFLGHR HYERKGLAYC ETHYNQLFGD 250
    VCFHCNRVIE GDVVSALNKA WCVNCFACST CNTKLTLKNK FVEFDMKPVC 300
    KKCYEKFPLE LKKRLKKLAE TLGRK 325
    Length:325
    Mass (Da):37,251
    Last modified:January 23, 2007 - v4
    Checksum:iE665FEB11D849CAE
    GO
    Isoform 2 (identifier: P48059-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLGVAAGMTHSNM

    Note: No experimental confirmation available.

    Show »
    Length:337
    Mass (Da):38,422
    Checksum:i8577792E1A56418B
    GO
    Isoform 3 (identifier: P48059-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAFSGRARPCIIPENEEIPRAALNTVHEANGTEDERAVSKLQRRHSDVKVYKEFCDFYAKFNM

    Show »
    Length:387
    Mass (Da):44,390
    Checksum:i3AB2EDB2203CEBFF
    GO
    Isoform 4 (identifier: P48059-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTCNM

    Show »
    Length:329
    Mass (Da):37,701
    Checksum:iA69518B2E12F39A5
    GO
    Isoform 5 (identifier: P48059-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTALQLKELSHSGLYRRRRDRPDSLRVNGLPEEELSNM

    Show »
    Length:362
    Mass (Da):41,571
    Checksum:iB2123BE2DDC4736C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781I → T in AAH05341. (PubMed:15489334)Curated
    Sequence conflicti262 – 2621D → G in AAH05341. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MLGVAAGMTHSNM in isoform 2. 1 PublicationVSP_042672
    Alternative sequencei1 – 11M → MAFSGRARPCIIPENEEIPR AALNTVHEANGTEDERAVSK LQRRHSDVKVYKEFCDFYAK FNM in isoform 3. 1 PublicationVSP_043210
    Alternative sequencei1 – 11M → MTCNM in isoform 4. CuratedVSP_043211
    Alternative sequencei1 – 11M → MTALQLKELSHSGLYRRRRD RPDSLRVNGLPEEELSNM in isoform 5. 1 PublicationVSP_043212

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09284 mRNA. Translation: AAA20086.2.
    AK296992 mRNA. Translation: BAH12469.1.
    AK302411 mRNA. Translation: BAH13699.1.
    AK304260 mRNA. Translation: BAH14143.1.
    AK314217 mRNA. Translation: BAG36891.1.
    AC010095 Genomic DNA. Translation: AAY14983.1.
    AC012487 Genomic DNA. No translation available.
    BC005341 mRNA. Translation: AAH05341.1.
    CCDSiCCDS2078.1. [P48059-1]
    CCDS54382.1. [P48059-2]
    CCDS54383.1. [P48059-4]
    CCDS54384.1. [P48059-5]
    CCDS54385.1. [P48059-3]
    PIRiJC2324.
    RefSeqiNP_001180411.1. NM_001193482.1. [P48059-4]
    NP_001180412.1. NM_001193483.2. [P48059-2]
    NP_001180413.1. NM_001193484.1. [P48059-5]
    NP_001180414.1. NM_001193485.2. [P48059-3]
    NP_001180417.1. NM_001193488.1. [P48059-1]
    NP_004978.2. NM_004987.5. [P48059-1]
    UniGeneiHs.597715.
    Hs.613268.

    Genome annotation databases

    EnsembliENST00000332345; ENSP00000331775; ENSG00000169756. [P48059-1]
    ENST00000338045; ENSP00000337598; ENSG00000169756. [P48059-1]
    ENST00000393310; ENSP00000376987; ENSG00000169756. [P48059-1]
    ENST00000409441; ENSP00000387264; ENSG00000169756. [P48059-5]
    ENST00000410093; ENSP00000386926; ENSG00000169756. [P48059-4]
    ENST00000542845; ENSP00000446121; ENSG00000169756. [P48059-3]
    ENST00000544547; ENSP00000437912; ENSG00000169756. [P48059-2]
    GeneIDi3987.
    KEGGihsa:3987.
    UCSCiuc002teg.3. human. [P48059-1]
    uc002tei.3. human. [P48059-4]
    uc002tej.3. human. [P48059-5]
    uc002tek.4. human. [P48059-3]
    uc002tel.3. human. [P48059-2]

    Polymorphism databases

    DMDMi18266876.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09284 mRNA. Translation: AAA20086.2 .
    AK296992 mRNA. Translation: BAH12469.1 .
    AK302411 mRNA. Translation: BAH13699.1 .
    AK304260 mRNA. Translation: BAH14143.1 .
    AK314217 mRNA. Translation: BAG36891.1 .
    AC010095 Genomic DNA. Translation: AAY14983.1 .
    AC012487 Genomic DNA. No translation available.
    BC005341 mRNA. Translation: AAH05341.1 .
    CCDSi CCDS2078.1. [P48059-1 ]
    CCDS54382.1. [P48059-2 ]
    CCDS54383.1. [P48059-4 ]
    CCDS54384.1. [P48059-5 ]
    CCDS54385.1. [P48059-3 ]
    PIRi JC2324.
    RefSeqi NP_001180411.1. NM_001193482.1. [P48059-4 ]
    NP_001180412.1. NM_001193483.2. [P48059-2 ]
    NP_001180413.1. NM_001193484.1. [P48059-5 ]
    NP_001180414.1. NM_001193485.2. [P48059-3 ]
    NP_001180417.1. NM_001193488.1. [P48059-1 ]
    NP_004978.2. NM_004987.5. [P48059-1 ]
    UniGenei Hs.597715.
    Hs.613268.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G47 NMR - A 1-70 [» ]
    1NYP NMR - A 188-251 [» ]
    1U5S NMR - B 188-251 [» ]
    2COR NMR - A 125-190 [» ]
    2D8X NMR - A 71-127 [» ]
    2KBX NMR - B 1-70 [» ]
    3F6Q X-ray 1.60 B 6-68 [» ]
    4HI8 X-ray 1.20 B 6-68 [» ]
    4HI9 X-ray 1.20 B 6-68 [» ]
    ProteinModelPortali P48059.
    SMRi P48059. Positions 6-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110175. 16 interactions.
    DIPi DIP-40671N.
    IntActi P48059. 29 interactions.
    MINTi MINT-5004275.
    STRINGi 9606.ENSP00000331775.

    PTM databases

    PhosphoSitei P48059.

    Polymorphism databases

    DMDMi 18266876.

    2D gel databases

    OGPi P48059.

    Proteomic databases

    MaxQBi P48059.
    PaxDbi P48059.
    PRIDEi P48059.

    Protocols and materials databases

    DNASUi 3987.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332345 ; ENSP00000331775 ; ENSG00000169756 . [P48059-1 ]
    ENST00000338045 ; ENSP00000337598 ; ENSG00000169756 . [P48059-1 ]
    ENST00000393310 ; ENSP00000376987 ; ENSG00000169756 . [P48059-1 ]
    ENST00000409441 ; ENSP00000387264 ; ENSG00000169756 . [P48059-5 ]
    ENST00000410093 ; ENSP00000386926 ; ENSG00000169756 . [P48059-4 ]
    ENST00000542845 ; ENSP00000446121 ; ENSG00000169756 . [P48059-3 ]
    ENST00000544547 ; ENSP00000437912 ; ENSG00000169756 . [P48059-2 ]
    GeneIDi 3987.
    KEGGi hsa:3987.
    UCSCi uc002teg.3. human. [P48059-1 ]
    uc002tei.3. human. [P48059-4 ]
    uc002tej.3. human. [P48059-5 ]
    uc002tek.4. human. [P48059-3 ]
    uc002tel.3. human. [P48059-2 ]

    Organism-specific databases

    CTDi 3987.
    GeneCardsi GC02P109150.
    HGNCi HGNC:6616. LIMS1.
    MIMi 602567. gene.
    neXtProti NX_P48059.
    PharmGKBi PA30389.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263350.
    HOGENOMi HOG000253950.
    HOVERGENi HBG000053.
    InParanoidi P48059.
    OMAi NQNRALC.
    PhylomeDBi P48059.
    TreeFami TF314113.

    Enzyme and pathway databases

    Reactomei REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_20649. Cell-extracellular matrix interactions.

    Miscellaneous databases

    ChiTaRSi LIMS1. human.
    EvolutionaryTracei P48059.
    GeneWikii LIMS1.
    GenomeRNAii 3987.
    NextBioi 15640.
    PROi P48059.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48059.
    Bgeei P48059.
    CleanExi HS_LIMS1.
    Genevestigatori P48059.

    Family and domain databases

    Gene3Di 2.10.110.10. 5 hits.
    InterProi IPR017351. PINCH.
    IPR001781. Znf_LIM.
    [Graphical view ]
    PANTHERi PTHR24210. PTHR24210. 1 hit.
    Pfami PF00412. LIM. 5 hits.
    [Graphical view ]
    PIRSFi PIRSF038003. PINCH. 1 hit.
    SMARTi SM00132. LIM. 5 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new LIM protein containing an autoepitope homologous to 'senescent cell antigen'."
      Rearden A.
      Biochem. Biophys. Res. Commun. 201:1124-1131(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal liver.
    2. Rearden A.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    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] (ISOFORMS 1; 2; 3 AND 5).
      Tissue: Testis, Tongue and Trachea.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1).
      Tissue: Bone marrow.
    6. "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 2-12, ACETYLATION AT ALA-2.
      Tissue: Platelet.
    7. "Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways."
      Tu Y., Li F., Wu C.
      Mol. Biol. Cell 9:3367-3382(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCK2.
    8. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    9. "The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells."
      Tu Y., Li F., Goicoechea S., Wu C.
      Mol. Cell. Biol. 19:2425-2434(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ILK AND NCK2, SUBCELLULAR LOCATION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain."
      Velyvis A., Yang Y., Wu C., Qin J.
      J. Biol. Chem. 276:4932-4939(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-70.
    12. "Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling."
      Velyvis A., Vaynberg J., Yang Y., Vinogradova O., Zhang Y., Wu C., Qin J.
      Nat. Struct. Biol. 10:558-564(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 188-251.
    13. "Solution structure of the second and third LIM domain of particularly interesting new Cys-His protein (PINCH)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 71-190.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 6-68 IN COMPLEX WITH ILK, MUTAGENESIS OF PHE-42; HIS-61; ASP-62 AND LEU-66.
    15. "Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase."
      Yang Y., Wang X., Hawkins C.A., Chen K., Vaynberg J., Mao X., Tu Y., Zuo X., Wang J., Wang Y.-X., Wu C., Tjandra N., Qin J.
      J. Biol. Chem. 284:5836-5844(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-70 IN COMPLEX WITH ILK, MUTAGENESIS OF PHE-42 AND ARG-56, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiLIMS1_HUMAN
    AccessioniPrimary (citable) accession number: P48059
    Secondary accession number(s): B2RAJ4
    , B7Z483, B7Z7R3, B7Z907, Q53TE0, Q9BS44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 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 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3