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P42166

- LAP2A_HUMAN

UniProt

P42166 - LAP2A_HUMAN

Protein

Lamina-associated polypeptide 2, isoform alpha

Gene

TMPO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.
    TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. lamin binding Source: ProtInc

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: Ensembl

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lamina-associated polypeptide 2, isoform alpha
    Alternative name(s):
    Thymopoietin isoform alpha
    Short name:
    TP alpha
    Thymopoietin-related peptide isoform alpha
    Short name:
    TPRP isoform alpha
    Cleaved into the following 2 chains:
    Thymopoietin
    Short name:
    TP
    Alternative name(s):
    Splenin
    Alternative name(s):
    TP5
    Gene namesi
    Name:TMPO
    Synonyms:LAP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11875. TMPO.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Expressed diffusely throughout the nucleus.

    GO - Cellular componenti

    1. chromatin Source: MGI
    2. nuclear envelope Source: ProtInc
    3. nuclear inner membrane Source: Ensembl
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Cardiomyopathy, dilated 1T (CMD1T) [MIM:613740]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti690 – 6901R → C in CMD1T; affects the interaction with LMNA. 1 Publication
    Corresponds to variant rs17028450 [ dbSNP | Ensembl ].
    VAR_049778

    Pharmaceutical usei

    TP5 is available under the names Timunox (Cilag), Sintomodulina (Italofarmaco) and Mepentil (Recordati). Used in primary and secondary immune deficiencies, autoimmunity, infections and cancer.

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi613740. phenotype.
    Orphaneti154. Familial isolated dilated cardiomyopathy.
    PharmGKBiPA36576.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 694693Lamina-associated polypeptide 2, isoform alphaPRO_0000017674Add
    BLAST
    Peptidei2 – 5049ThymopoietinPRO_0000017675Add
    BLAST
    Peptidei33 – 375ThymopentinPRO_0000017676

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571Phosphothreonine2 Publications
    Modified residuei59 – 591Phosphoserine2 Publications
    Modified residuei66 – 661Phosphoserine3 Publications
    Modified residuei67 – 671Phosphoserine3 Publications
    Modified residuei74 – 741Phosphothreonine7 Publications
    Modified residuei79 – 791Phosphoserine3 Publications
    Modified residuei154 – 1541Phosphothreonine2 Publications
    Modified residuei156 – 1561Phosphoserine2 Publications
    Modified residuei160 – 1601Phosphothreonine4 Publications
    Modified residuei164 – 1641Phosphothreonine2 Publications
    Modified residuei184 – 1841Phosphoserine2 Publications
    Modified residuei351 – 3511Phosphoserine8 Publications
    Modified residuei354 – 3541Phosphoserine3 Publications
    Modified residuei370 – 3701Phosphoserine3 Publications
    Modified residuei424 – 4241Phosphoserine7 Publications
    Modified residuei656 – 6561N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated in a mitose-specific manner.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP42166.
    PeptideAtlasiP42166.
    PRIDEiP42166.

    Miscellaneous databases

    PMAP-CutDBP42166.

    Expressioni

    Tissue specificityi

    Expressed in many tissues. Most abundant in adult thymus and fetal liver.

    Gene expression databases

    ArrayExpressiP42166.
    BgeeiP42166.
    CleanExiHS_TMPO.
    GenevestigatoriP42166.

    Organism-specific databases

    HPAiCAB009847.

    Interactioni

    Subunit structurei

    Interacts with LMNA, BANF1 and RB1 and with chromosomes. Associates directly or indirectly with lamins at specific cell-cycle stages.3 Publications

    Protein-protein interaction databases

    BioGridi112967. 49 interactions.
    IntActiP42166. 18 interactions.
    MINTiMINT-2863664.
    STRINGi9606.ENSP00000266732.

    Structurei

    Secondary structure

    1
    694
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 114
    Helixi13 – 2210
    Beta strandi29 – 313
    Helixi34 – 396
    Turni40 – 423
    Beta strandi43 – 453
    Turni46 – 483
    Beta strandi113 – 1153
    Helixi117 – 1226
    Beta strandi123 – 1253
    Turni126 – 1283
    Beta strandi136 – 1383
    Helixi139 – 1457
    Helixi147 – 1526

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GJJNMR-A1-168[»]
    1H9ENMR-A2-57[»]
    1H9FNMR-A103-159[»]
    ProteinModelPortaliP42166.
    SMRiP42166. Positions 2-57, 103-159, 467-690.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42166.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 4844LEM-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini109 – 15345LEMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 10860LinkerAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili558 – 657100By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi190 – 1967Nuclear localization signalSequence Analysis

    Domaini

    The N-terminal part contains two structurally independent, non-interacting domains: LEM-like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C or LEM-B). LEM-like binds DNA while LEM interacts with BANF1.
    The C-terminal domain forms a four-stranded coiled coil.By similarity

    Sequence similaritiesi

    Belongs to the LEM family.Curated
    Contains 1 LEM domain.PROSITE-ProRule annotation
    Contains 1 LEM-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG87051.
    HOGENOMiHOG000060228.
    HOVERGENiHBG081890.
    InParanoidiP42166.
    OMAiCCSSGRP.
    OrthoDBiEOG7KWSGZ.
    PhylomeDBiP42166.
    TreeFamiTF328426.

    Family and domain databases

    Gene3Di1.10.720.40. 2 hits.
    InterProiIPR021623. LAP2alpha.
    IPR013146. LEM-like_dom.
    IPR011015. LEM/LEM-like_dom.
    IPR003887. LEM_dom.
    [Graphical view]
    PfamiPF11560. LAP2alpha. 1 hit.
    PF03020. LEM. 1 hit.
    PF08198. Thymopoietin. 1 hit.
    [Graphical view]
    SMARTiSM00540. LEM. 1 hit.
    [Graphical view]
    SUPFAMiSSF63451. SSF63451. 2 hits.
    PROSITEiPS50954. LEM. 1 hit.
    PS50955. LEM_LIKE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform Alpha (identifier: P42166-1) [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

    MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR    50
    PPLPAGTNSK GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD 100
    KPRQEDKDDL DVTELTNEDL LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR 150
    EQGTESRSST PLPTISSSAE NTRQNGSNDS DRYSDNEEGK KKEHKKVKST 200
    RDIVPFSELG TTPSGGGFFQ GISFPEISTR PPLGSTELQA AKKVHTSKGD 250
    LPREPLVATN LPGRGQLQKL ASERNLFISC KSSHDRCLEK SSSSSSQPEH 300
    SAMLVSTAAS PSLIKETTTG YYKDIVENIC GREKSGIQPL CPERSHISDQ 350
    SPLSSKRKAL EESESSQLIS PPLAQAIRDY VNSLLVQGGV GSLPGTSNSM 400
    PPLDVENIQK RIDQSKFQET EFLSPPRKVP RLSEKSVEER DSGSFVAFQN 450
    IPGSELMSSF AKTVVSHSLT TLGLEVAKQS QHDKIDASEL SFPFHESILK 500
    VIEEEWQQVD RQLPSLACKY PVSSREATQI LSVPKVDDEI LGFISEATPL 550
    GGIQAASTES CNQQLDLALC RAYEAAASAL QIATHTAFVA KAMQADISQA 600
    AQILSSDPSR THQALGILSK TYDAASYICE AAFDEVKMAA HTMGNATVGR 650
    RYLWLKDCKI NLASKNKLAS TPFKGGTLFG GEVCKVIKKR GNKH 694
    Length:694
    Mass (Da):75,492
    Last modified:January 23, 2007 - v2
    Checksum:i1B514B0FB61D0D75
    GO
    Isoform Beta (identifier: P42167-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P42167.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:454
    Mass (Da):50,670
    GO
    Isoform Gamma (identifier: P42167-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P42167.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:345
    Mass (Da):38,738
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti238 – 2381L → R.
    Corresponds to variant rs35998138 [ dbSNP | Ensembl ].
    VAR_049773
    Natural varianti293 – 2931S → A.
    Corresponds to variant rs35645287 [ dbSNP | Ensembl ].
    VAR_049774
    Natural varianti317 – 3171T → S.
    Corresponds to variant rs35969221 [ dbSNP | Ensembl ].
    VAR_049775
    Natural varianti416 – 4161K → E.
    Corresponds to variant rs11838270 [ dbSNP | Ensembl ].
    VAR_049776
    Natural varianti478 – 4781K → N.
    Corresponds to variant rs35761089 [ dbSNP | Ensembl ].
    VAR_049777
    Natural varianti599 – 5991Q → E.1 Publication
    Corresponds to variant rs17459334 [ dbSNP | Ensembl ].
    VAR_005635
    Natural varianti690 – 6901R → C in CMD1T; affects the interaction with LMNA. 1 Publication
    Corresponds to variant rs17028450 [ dbSNP | Ensembl ].
    VAR_049778

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09086 mRNA. Translation: AAB60329.1.
    U18270
    , U18266, U18267, U18268 Genomic DNA. Translation: AAB60433.1.
    S76736 mRNA. Translation: AAB33958.1.
    CCDSiCCDS9064.1. [P42166-1]
    PIRiG01161.
    RefSeqiNP_003267.1. NM_003276.2. [P42166-1]
    UniGeneiHs.11355.

    Genome annotation databases

    EnsembliENST00000266732; ENSP00000266732; ENSG00000120802. [P42166-1]
    GeneIDi7112.
    KEGGihsa:7112.
    UCSCiuc001tfh.2. human. [P42166-1]

    Polymorphism databases

    DMDMi1174689.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09086 mRNA. Translation: AAB60329.1 .
    U18270
    , U18266 , U18267 , U18268 Genomic DNA. Translation: AAB60433.1 .
    S76736 mRNA. Translation: AAB33958.1 .
    CCDSi CCDS9064.1. [P42166-1 ]
    PIRi G01161.
    RefSeqi NP_003267.1. NM_003276.2. [P42166-1 ]
    UniGenei Hs.11355.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GJJ NMR - A 1-168 [» ]
    1H9E NMR - A 2-57 [» ]
    1H9F NMR - A 103-159 [» ]
    ProteinModelPortali P42166.
    SMRi P42166. Positions 2-57, 103-159, 467-690.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112967. 49 interactions.
    IntActi P42166. 18 interactions.
    MINTi MINT-2863664.
    STRINGi 9606.ENSP00000266732.

    Polymorphism databases

    DMDMi 1174689.

    Proteomic databases

    PaxDbi P42166.
    PeptideAtlasi P42166.
    PRIDEi P42166.

    Protocols and materials databases

    DNASUi 7112.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266732 ; ENSP00000266732 ; ENSG00000120802 . [P42166-1 ]
    GeneIDi 7112.
    KEGGi hsa:7112.
    UCSCi uc001tfh.2. human. [P42166-1 ]

    Organism-specific databases

    CTDi 7112.
    GeneCardsi GC12P098909.
    GeneReviewsi TMPO.
    HGNCi HGNC:11875. TMPO.
    HPAi CAB009847.
    MIMi 188380. gene.
    613740. phenotype.
    neXtProti NX_P42166.
    Orphaneti 154. Familial isolated dilated cardiomyopathy.
    PharmGKBi PA36576.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87051.
    HOGENOMi HOG000060228.
    HOVERGENi HBG081890.
    InParanoidi P42166.
    OMAi CCSSGRP.
    OrthoDBi EOG7KWSGZ.
    PhylomeDBi P42166.
    TreeFami TF328426.

    Miscellaneous databases

    ChiTaRSi TMPO. human.
    EvolutionaryTracei P42166.
    GeneWikii Thymopoietin.
    GenomeRNAii 7112.
    NextBioi 27839.
    PMAP-CutDB P42166.
    PROi P42166.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42166.
    Bgeei P42166.
    CleanExi HS_TMPO.
    Genevestigatori P42166.

    Family and domain databases

    Gene3Di 1.10.720.40. 2 hits.
    InterProi IPR021623. LAP2alpha.
    IPR013146. LEM-like_dom.
    IPR011015. LEM/LEM-like_dom.
    IPR003887. LEM_dom.
    [Graphical view ]
    Pfami PF11560. LAP2alpha. 1 hit.
    PF03020. LEM. 1 hit.
    PF08198. Thymopoietin. 1 hit.
    [Graphical view ]
    SMARTi SM00540. LEM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63451. SSF63451. 2 hits.
    PROSITEi PS50954. LEM. 1 hit.
    PS50955. LEM_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Three distinct human thymopoietins are derived from alternatively spliced mRNAs."
      Harris C.A., Andryuk P.J., Cline S.W., Chan H.K., Natarajan A., Siekierka J.J., Goldstein G.
      Proc. Natl. Acad. Sci. U.S.A. 91:6283-6287(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
      Tissue: Thymus.
    2. "Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2."
      Harris C.A., Andryuk P.J., Cline S.W., Siekierka J.J., Goldstein G.
      Genomics 28:198-205(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA; BETA AND GAMMA), VARIANT GLU-599.
    3. "A new thymopoietin precursor gene from human thymus."
      Hara H., Hayashi K., Ohta K., Itoh N., Ohta M.
      Biochem. Mol. Biol. Int. 34:927-933(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-526.
      Tissue: Thymus.
    4. Bienvenut W.V., Vousden K.H., Lukashchuk N.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 127-139; 254-264; 417-427 AND 526-535, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Lung carcinoma.
    5. "Isolation and complete amino acid sequence of human thymopoietin and splenin."
      Audhya T., Schlesinger D.H., Goldstein G.
      Proc. Natl. Acad. Sci. U.S.A. 84:3545-3549(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    6. Cited for: RETRACTION.
    7. "Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics."
      Dechat T., Gotzmann J., Stockinger A., Harris C.A., Talle M.A., Siekierka J.J., Foisner R.
      EMBO J. 17:4887-4902(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHROMOSOMES, PHOSPHORYLATION.
    8. "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins."
      Dechat T., Korbei B., Vaughan O.A., Vlcek S., Hutchison C.J., Foisner R.
      J. Cell Sci. 113:3473-3484(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LMNA.
    9. "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein."
      Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J.
      Mol. Biol. Cell 13:4401-4413(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LMNA AND RB1.
    10. "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-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    12. "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-351 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    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 THR-74; SER-351 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-66; SER-67; THR-74; SER-79; THR-160; THR-164; SER-351; SER-370 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "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].
    19. "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-66; SER-67; THR-74; SER-79; THR-154; THR-160; SER-351 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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 THR-74; SER-156; THR-160; SER-351; SER-354; SER-370 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-59; THR-74; SER-184; SER-351 AND SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA."
      Cai M., Huang Y., Ghirlando R., Wilson K.L., Craigie R., Clore G.M.
      EMBO J. 20:4399-4407(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-169.
    25. "Structural characterization of the LEM motif common to three human inner nuclear membrane proteins."
      Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K., Callebaut I., Worman H.J., Zinn-Justin S.
      Structure 9:503-511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-57 AND 103-159.
    26. Cited for: VARIANT CMD1T CYS-690, CHARACTERIZATION OF VARIANT CMD1T CYS-690.

    Entry informationi

    Entry nameiLAP2A_HUMAN
    AccessioniPrimary (citable) accession number: P42166
    Secondary accession number(s): P08918
    , P08919, Q14860, Q16295
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 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, Pharmaceutical, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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