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Q9UHB6

- LIMA1_HUMAN

UniProt

Q9UHB6 - LIMA1_HUMAN

Protein

LIM domain and actin-binding protein 1

Gene

LIMA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Binds to actin monomers and filaments. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments.1 Publication

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. actin monomer binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament bundle assembly Source: UniProtKB
    2. negative regulation of actin filament depolymerization Source: UniProtKB
    3. ruffle organization Source: UniProtKB

    Keywords - Ligandi

    Actin-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LIM domain and actin-binding protein 1
    Alternative name(s):
    Epithelial protein lost in neoplasm
    Gene namesi
    Name:LIMA1
    Synonyms:EPLIN, SREBP3
    ORF Names:PP624
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:24636. LIMA1.

    Subcellular locationi

    Cytoplasm. Cell junctionfocal adhesion. Cytoplasmcytoskeleton
    Note: This cytoskeletal protein co-localizes with actin stress fibers and focal adhesion plaques.

    GO - Cellular componenti

    1. actin cytoskeleton Source: LIFEdb
    2. cytoplasm Source: HPA
    3. focal adhesion Source: UniProtKB
    4. plasma membrane Source: HPA
    5. stress fiber Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485527.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 759759LIM domain and actin-binding protein 1PRO_0000075730Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei4 – 41Phosphoserine1 Publication
    Modified residuei15 – 151Phosphoserine1 Publication
    Modified residuei132 – 1321Phosphoserine3 Publications
    Modified residuei225 – 2251Phosphoserine2 Publications
    Modified residuei229 – 2291Phosphotyrosine1 Publication
    Modified residuei230 – 2301PhosphoserineBy similarity
    Modified residuei263 – 2631Phosphoserine1 Publication
    Modified residuei343 – 3431Phosphoserine1 Publication
    Modified residuei350 – 3501Phosphoserine1 Publication
    Modified residuei362 – 3621Phosphoserine5 Publications
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei369 – 3691Phosphoserine1 Publication
    Modified residuei374 – 3741Phosphoserine3 Publications
    Modified residuei439 – 4391N6-succinyllysineBy similarity
    Modified residuei490 – 4901Phosphoserine7 Publications
    Modified residuei604 – 6041Phosphoserine3 Publications
    Modified residuei609 – 6091Phosphoserine1 Publication
    Modified residuei617 – 6171Phosphoserine2 Publications
    Modified residuei686 – 6861Phosphoserine6 Publications
    Modified residuei692 – 6921Phosphoserine4 Publications
    Modified residuei698 – 6981Phosphoserine3 Publications
    Modified residuei726 – 7261Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHB6.
    PaxDbiQ9UHB6.
    PRIDEiQ9UHB6.

    PTM databases

    PhosphoSiteiQ9UHB6.

    Expressioni

    Tissue specificityi

    Highly expressed in placenta, kidney, pancreas, prostate, ovary, spleen and heart. Also detected in lung, liver, brain, skeletal muscle, thymus, testis and intestine. Not detected in leukocytes. Isoform Beta expressed generally at very low levels. Isoform Alpha abundant in epithelial cells from mammary gland, prostate and in normal oral keratinocytes. Low levels in aortic endothelial cells and dermal fibroblasts. Not detectable in myocardium.

    Inductioni

    Down-regulated in some cancer cell lines. Isoform Alpha is induced by serum. Isoform Beta is constitutively expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHB6.
    BgeeiQ9UHB6.
    GenevestigatoriQ9UHB6.

    Organism-specific databases

    HPAiHPA023871.
    HPA052645.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SVILO463853EBI-351479,EBI-6995105From a different organism.

    Protein-protein interaction databases

    BioGridi119559. 22 interactions.
    DIPiDIP-29633N.
    IntActiQ9UHB6. 12 interactions.
    MINTiMINT-1132272.

    Structurei

    Secondary structure

    1
    759
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi384 – 3874
    Turni391 – 3933
    Beta strandi401 – 4044
    Beta strandi406 – 4116
    Turni412 – 4143
    Turni418 – 4203
    Turni426 – 4283
    Beta strandi432 – 4343
    Helixi439 – 4457

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D8YNMR-A381-457[»]
    ProteinModelPortaliQ9UHB6.
    SMRiQ9UHB6. Positions 381-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHB6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini388 – 44861LIM zinc-bindingPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Sequence similaritiesi

    Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain

    Phylogenomic databases

    eggNOGiNOG238020.
    HOGENOMiHOG000059621.
    HOVERGENiHBG051492.
    OMAiDEISKPE.
    OrthoDBiEOG7PCJH8.
    PhylomeDBiQ9UHB6.
    TreeFamiTF350273.

    Family and domain databases

    Gene3Di2.10.110.10. 1 hit.
    InterProiIPR028740. EPLIN.
    IPR001781. Znf_LIM.
    [Graphical view]
    PANTHERiPTHR24206:SF27. PTHR24206:SF27. 1 hit.
    PfamiPF00412. LIM. 1 hit.
    [Graphical view]
    SMARTiSM00132. LIM. 1 hit.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform Beta (identifier: Q9UHB6-1) [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

    MESSPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEETNM    50
    EKKRSNTENL SQHFRKGTLT VLKKKWENPG LGAESHTDSL RNSSTEIRHR 100
    ADHPPAEVTS HAASGAKADQ EEQIHPRSRL RSPPEALVQG RYPHIKDGED 150
    LKDHSTESKK MENCLGESRH EVEKSEISEN TDASGKIEKY NVPLNRLKMM 200
    FEKGEPTQTK ILRAQSRSAS GRKISENSYS LDDLEIGPGQ LSSSTFDSEK 250
    NESRRNLELP RLSETSIKDR MAKYQAAVSK QSSSTNYTNE LKASGGEIKI 300
    HKMEQKENVP PGPEVCITHQ EGEKISANEN SLAVRSTPAE DDSRDSQVKS 350
    EVQQPVHPKP LSPDSRASSL SESSPPKAMK KFQAPARETC VECQKTVYPM 400
    ERLLANQQVF HISCFRCSYC NNKLSLGTYA SLHGRIYCKP HFNQLFKSKG 450
    NYDEGFGHRP HKDLWASKNE NEEILERPAQ LANARETPHS PGVEDAPIAK 500
    VGVLAASMEA KASSQQEKED KPAETKKLRI AWPPPTELGS SGSALEEGIK 550
    MSKPKWPPED EISKPEVPED VDLDLKKLRR SSSLKERSRP FTVAASFQST 600
    SVKSPKTVSP PIRKGWSMSE QSEESVGGRV AERKQVENAK ASKKNGNVGK 650
    TTWQNKESKG ETGKRSKEGH SLEMENENLV ENGADSDEDD NSFLKQQSPQ 700
    EPKSLNWSSF VDNTFAEEFT TQNQKSQDVE LWEGEVVKEL SVEEQIKRNR 750
    YYDEDEDEE 759

    Note: Produced by alternative promoter usage.

    Length:759
    Mass (Da):85,226
    Last modified:May 1, 2000 - v1
    Checksum:i996378AFD3B003D5
    GO
    Isoform Alpha (identifier: Q9UHB6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-160: Missing.

    Note: Produced by alternative promoter usage.

    Show »
    Length:599
    Mass (Da):67,119
    Checksum:iDE0AE1D7A916BE30
    GO
    Isoform 3 (identifier: Q9UHB6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-302: Missing.

    Note: Produced by alternative splicing of isoform Beta.

    Show »
    Length:457
    Mass (Da):51,219
    Checksum:iDD730BA1D2FB8E2E
    GO
    Isoform 4 (identifier: Q9UHB6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         344-344: R → PG

    Note: Produced by alternative splicing.

    Show »
    Length:760
    Mass (Da):85,224
    Checksum:i5FD64F6E2ECEFAE2
    GO
    Isoform 5 (identifier: Q9UHB6-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-160: Missing.
         344-344: R → PG

    Note: No experimental confirmation available.

    Show »
    Length:600
    Mass (Da):67,117
    Checksum:iDAE126F756B45C5F
    GO

    Sequence cautioni

    The sequence AAG17267.1 differs from that shown. Reason: Frameshift at positions 365 and 662.
    The sequence BAA91120.1 differs from that shown. Reason: Frameshift at position 697.
    The sequence BAD92749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti381 – 3811Missing in BAA90914. (PubMed:14702039)Curated
    Sequence conflicti381 – 3811Missing in AAH01247. (PubMed:15489334)Curated
    Sequence conflicti415 – 4151F → L in AAG17267. (PubMed:15498874)Curated
    Sequence conflicti463 – 4631D → G in BAA90914. (PubMed:14702039)Curated
    Sequence conflicti491 – 4911P → Q in AAF67491. (PubMed:10931946)Curated
    Sequence conflicti520 – 5212DK → NR in AAF67491. (PubMed:10931946)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 302302Missing in isoform 3. 2 PublicationsVSP_003117Add
    BLAST
    Alternative sequencei1 – 160160Missing in isoform Alpha and isoform 5. 2 PublicationsVSP_003116Add
    BLAST
    Alternative sequencei344 – 3441R → PG in isoform 4 and isoform 5. 2 PublicationsVSP_040136

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF198454 mRNA. Translation: AAF23755.1.
    AF198455 mRNA. Translation: AAF23756.1.
    AF157325 mRNA. Translation: AAF67491.1.
    AL136911 mRNA. Translation: CAB66845.1.
    AK000372 mRNA. Translation: BAA91120.1. Frameshift.
    AK000335 mRNA. Translation: BAA91092.1.
    AK023649 mRNA. Translation: BAB14625.1.
    AK000057 mRNA. Translation: BAA90914.1.
    AK314447 mRNA. Translation: BAG37056.1.
    AB209512 mRNA. Translation: BAD92749.1. Different initiation.
    CH471111 Genomic DNA. Translation: EAW58135.1.
    BC001247 mRNA. Translation: AAH01247.2.
    BC010664 mRNA. Translation: AAH10664.1.
    BC110815 mRNA. Translation: AAI10816.1.
    BC136763 mRNA. Translation: AAI36764.1.
    AF218025 mRNA. Translation: AAG17267.1. Frameshift.
    CCDSiCCDS44877.1. [Q9UHB6-4]
    CCDS55826.1. [Q9UHB6-5]
    CCDS58230.1. [Q9UHB6-3]
    CCDS8802.1. [Q9UHB6-1]
    RefSeqiNP_001107018.1. NM_001113546.1. [Q9UHB6-4]
    NP_001107019.1. NM_001113547.1. [Q9UHB6-5]
    NP_001230704.1. NM_001243775.1. [Q9UHB6-3]
    NP_057441.1. NM_016357.4. [Q9UHB6-1]
    UniGeneiHs.525419.

    Genome annotation databases

    GeneIDi51474.
    KEGGihsa:51474.
    UCSCiuc001rwg.4. human. [Q9UHB6-1]
    uc001rwi.4. human. [Q9UHB6-4]

    Polymorphism databases

    DMDMi20138067.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF198454 mRNA. Translation: AAF23755.1 .
    AF198455 mRNA. Translation: AAF23756.1 .
    AF157325 mRNA. Translation: AAF67491.1 .
    AL136911 mRNA. Translation: CAB66845.1 .
    AK000372 mRNA. Translation: BAA91120.1 . Frameshift.
    AK000335 mRNA. Translation: BAA91092.1 .
    AK023649 mRNA. Translation: BAB14625.1 .
    AK000057 mRNA. Translation: BAA90914.1 .
    AK314447 mRNA. Translation: BAG37056.1 .
    AB209512 mRNA. Translation: BAD92749.1 . Different initiation.
    CH471111 Genomic DNA. Translation: EAW58135.1 .
    BC001247 mRNA. Translation: AAH01247.2 .
    BC010664 mRNA. Translation: AAH10664.1 .
    BC110815 mRNA. Translation: AAI10816.1 .
    BC136763 mRNA. Translation: AAI36764.1 .
    AF218025 mRNA. Translation: AAG17267.1 . Frameshift.
    CCDSi CCDS44877.1. [Q9UHB6-4 ]
    CCDS55826.1. [Q9UHB6-5 ]
    CCDS58230.1. [Q9UHB6-3 ]
    CCDS8802.1. [Q9UHB6-1 ]
    RefSeqi NP_001107018.1. NM_001113546.1. [Q9UHB6-4 ]
    NP_001107019.1. NM_001113547.1. [Q9UHB6-5 ]
    NP_001230704.1. NM_001243775.1. [Q9UHB6-3 ]
    NP_057441.1. NM_016357.4. [Q9UHB6-1 ]
    UniGenei Hs.525419.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D8Y NMR - A 381-457 [» ]
    ProteinModelPortali Q9UHB6.
    SMRi Q9UHB6. Positions 381-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119559. 22 interactions.
    DIPi DIP-29633N.
    IntActi Q9UHB6. 12 interactions.
    MINTi MINT-1132272.

    PTM databases

    PhosphoSitei Q9UHB6.

    Polymorphism databases

    DMDMi 20138067.

    Proteomic databases

    MaxQBi Q9UHB6.
    PaxDbi Q9UHB6.
    PRIDEi Q9UHB6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 51474.
    KEGGi hsa:51474.
    UCSCi uc001rwg.4. human. [Q9UHB6-1 ]
    uc001rwi.4. human. [Q9UHB6-4 ]

    Organism-specific databases

    CTDi 51474.
    GeneCardsi GC12M050569.
    H-InvDB HIX0171649.
    HGNCi HGNC:24636. LIMA1.
    HPAi HPA023871.
    HPA052645.
    MIMi 608364. gene.
    neXtProti NX_Q9UHB6.
    PharmGKBi PA143485527.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238020.
    HOGENOMi HOG000059621.
    HOVERGENi HBG051492.
    OMAi DEISKPE.
    OrthoDBi EOG7PCJH8.
    PhylomeDBi Q9UHB6.
    TreeFami TF350273.

    Miscellaneous databases

    ChiTaRSi LIMA1. human.
    EvolutionaryTracei Q9UHB6.
    GeneWikii LIMA1.
    GenomeRNAii 51474.
    NextBioi 55109.
    PROi Q9UHB6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHB6.
    Bgeei Q9UHB6.
    Genevestigatori Q9UHB6.

    Family and domain databases

    Gene3Di 2.10.110.10. 1 hit.
    InterProi IPR028740. EPLIN.
    IPR001781. Znf_LIM.
    [Graphical view ]
    PANTHERi PTHR24206:SF27. PTHR24206:SF27. 1 hit.
    Pfami PF00412. LIM. 1 hit.
    [Graphical view ]
    SMARTi SM00132. LIM. 1 hit.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "EPLIN, epithelial protein lost in neoplasm."
      Maul R.S., Chang D.D.
      Oncogene 18:7838-7841(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
      Tissue: Hypothalamus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
      Tissue: Uterus.
    4. "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 ALPHA; BETA AND 3).
      Tissue: Colon, Hepatoma and Placenta.
    5. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    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] (ISOFORM BETA).
      Tissue: Brain, Cervix, Colon and Placenta.
    8. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-759.
    9. "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing."
      Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.
      EMBO Rep. 1:287-292(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Characterization of the human EPLIN (Epithelial protein lost in neoplasm) gene reveals distinct promoters for the two EPLIN isoforms."
      Chen S., Maul R.S., Kim H.R., Chang D.D.
      Gene 248:69-76(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE, INDUCTION.
    11. "EPLIN regulates actin dynamics by cross-linking and stabilizing filaments."
      Maul R.S., Song Y., Amann K.J., Gerbin S.C., Pollard T.D., Chang D.D.
      J. Cell Biol. 160:399-407(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-490; SER-686 AND SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-132; SER-362 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-686 AND SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-225; TYR-229; SER-362; SER-374; SER-490; SER-604; SER-609; SER-617; SER-686; SER-692 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; SER-617 AND SER-686, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-132; SER-225; SER-263; SER-343; SER-362; SER-374; SER-490; SER-604; SER-686; SER-692 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-132; SER-350; SER-362; SER-365; SER-369; SER-374; SER-490; SER-686; SER-698 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Solution structure of the LIM domain of epithelial protein lost in neoplasm."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 381-460.

    Entry informationi

    Entry nameiLIMA1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHB6
    Secondary accession number(s): B2RB09
    , Q2TAN7, Q59FE8, Q9BVF2, Q9H8J1, Q9HBN5, Q9NX96, Q9NXC3, Q9NXU6, Q9P0H8, Q9UHB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 140 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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