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Q61033

- LAP2A_MOUSE

UniProt

Q61033 - LAP2A_MOUSE

Protein

Lamina-associated polypeptide 2, isoforms alpha/zeta

Gene

Tmpo

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: MGI

    GO - Biological processi

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

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lamina-associated polypeptide 2, isoforms alpha/zeta
    Alternative name(s):
    Thymopoietin isoforms alpha/zeta
    Short name:
    TP alpha/zeta
    Gene namesi
    Name:Tmpo
    Synonyms:Lap2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:106920. Tmpo.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity
    Note: Expressed diffusely throughout the nucleus.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 693692Lamina-associated polypeptide 2, isoforms alpha/zetaPRO_0000206145Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591PhosphoserineBy similarity
    Modified residuei66 – 661Phosphoserine2 Publications
    Modified residuei67 – 671Phosphoserine2 Publications
    Modified residuei74 – 741Phosphothreonine2 Publications
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei153 – 1531PhosphothreonineBy similarity
    Modified residuei155 – 1551PhosphoserineBy similarity
    Modified residuei159 – 1591Phosphothreonine1 Publication
    Modified residuei163 – 1631PhosphothreonineBy similarity
    Modified residuei183 – 1831PhosphoserineBy similarity
    Modified residuei349 – 3491PhosphoserineBy similarity
    Modified residuei352 – 3521PhosphoserineBy similarity
    Modified residuei368 – 3681PhosphoserineBy similarity
    Modified residuei422 – 4221Phosphoserine1 Publication
    Modified residuei655 – 6551N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated in a mitose-specific manner.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ61033.
    PaxDbiQ61033.
    PRIDEiQ61033.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61033.
    BgeeiQ61033.
    CleanExiMM_TMPO.
    GenevestigatoriQ61033.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi204234. 3 interactions.
    DIPiDIP-29323N.
    IntActiQ61033. 3 interactions.
    MINTiMINT-4100192.

    Structurei

    Secondary structure

    1
    693
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi495 – 50410
    Helixi505 – 5073
    Beta strandi508 – 5103
    Turni516 – 5183
    Helixi524 – 5307
    Helixi537 – 5415
    Helixi558 – 60447
    Helixi610 – 65445
    Beta strandi655 – 6573
    Helixi661 – 6699
    Beta strandi674 – 6785

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V0XX-ray2.20A/B459-693[»]
    ProteinModelPortaliQ61033.
    SMRiQ61033. Positions 2-56, 102-158, 465-689.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61033.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 4844LEM-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini108 – 15245LEMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 10759LinkerAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili557 – 656100Add
    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 By similarity.By similarity
    The C-terminal domain forms a four-stranded coiled coil.1 Publication

    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.
    GeneTreeiENSGT00510000048934.
    HOGENOMiHOG000113280.
    HOVERGENiHBG081890.
    InParanoidiB2RUB9.
    OMAiPRYRESK.
    OrthoDBiEOG7KWSGZ.
    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 (6)i

    Sequence statusi: Complete.

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

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q61033-1) [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
    PPLAAGANSK GPPDFSSDEE REPTPVLGSG ASVGRGRGAV GRKATKKTDK 100
    PRLEDKDDLD VTELSNEELL DQLVRYGVNP GPIVGTTRKL YEKKLLKLRE 150
    QGTESRSSTP LPTVSSSAEN TRQNGSNDSD RYSDNDEGKK KEHKKVKSAR 200
    DCVPFSELAS TPSGAFFQGI SFPEISTRPP LGRTELQAAK KVQTTKRDPP 250
    RETCTDTALP GKGQTHKLAP GRSLFIPSES SYDRCVEKSS SPSSQREFAA 300
    RLVSAAASPS LIRETTTTYS KDIVENICRG GKSRAQPLRA EEPGVSDQSV 350
    FSSEREVLQE SERSQVISPP LAQAIRDYVN SLLVQGGVGS LPGTSDSVPT 400
    LDVENICKRL SQSSYQDSES LSPPRKVPRL SEKPARGGDS GSCVAFQNTP 450
    GSEHRSSFAK SVVSHSLTTL GVEVSKPPPQ HDKIEASEPS FPLHESILKV 500
    VEEEWQQIDR QLPSVACRYP VSSIEAARIL SVPKVDDEIL GFISEATPRA 550
    ATQASSTESC DKHLDLALCR SYEAAASALQ IAAHTAFVAK SLQADISQAA 600
    QIINSDPSDA QQALRILNRT YDAASYLCDA AFDEVRMSAC AMGSSTMGRR 650
    YLWLKDCKIS PASKNKLTVA PFKGGTLFGG EVHKVIKKRG NKQ 693
    Length:693
    Mass (Da):75,168
    Last modified:July 27, 2011 - v4
    Checksum:i00604F3B66FF63F3
    GO
    Isoform Zeta (identifier: Q61033-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         188-225: GKKKEHKKVK...FFQGISFPEI → DSKIELKLEK...TEHNQVFVVL
         226-693: Missing.

    Note: Contains a N6-acetyllysine at position 206.

    Show »
    Length:225
    Mass (Da):24,990
    Checksum:iD980460C9CE89898
    GO
    Isoform Beta (identifier: Q61029-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q61029.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:452
    Mass (Da):50,373
    GO
    Isoform Delta (identifier: Q61029-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q61029.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:380
    Mass (Da):42,650
    GO
    Isoform Epsilon (identifier: Q61029-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q61029.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:412
    Mass (Da):46,050
    GO
    Isoform Gamma (identifier: Q61029-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q61029.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:343
    Mass (Da):38,502
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 732EP → DA in AAC52573. (PubMed:8743987)Curated
    Sequence conflicti72 – 732EP → DA in AAC52578. (PubMed:8743987)Curated
    Sequence conflicti262 – 2654KGQT → RGRP in AAC52578. (PubMed:8743987)Curated
    Sequence conflicti280 – 2812SS → LC in AAC52578. (PubMed:8743987)Curated
    Sequence conflicti322 – 3243DIV → EHS in AAC52578. (PubMed:8743987)Curated
    Sequence conflicti393 – 3942GT → RS in AAC52578. (PubMed:8743987)Curated
    Sequence conflicti606 – 6061D → I in AAC52578. (PubMed:8743987)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei188 – 22538GKKKE…SFPEI → DSKIELKLEKREPLKGRAKT PVTLKQRRTEHNQVFVVL in isoform Zeta. 1 PublicationVSP_010128Add
    BLAST
    Alternative sequencei226 – 693468Missing in isoform Zeta. 1 PublicationVSP_010129Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39073 mRNA. Translation: AAC52573.1.
    U39078 mRNA. Translation: AAC52578.1.
    CH466539 Genomic DNA. Translation: EDL21530.1.
    BC141062 mRNA. Translation: AAI41063.1.
    CCDSiCCDS24122.1. [Q61033-1]
    RefSeqiNP_035735.2. NM_011605.3. [Q61033-1]
    UniGeneiMm.159684.
    Mm.439157.

    Genome annotation databases

    EnsembliENSMUST00000020123; ENSMUSP00000020123; ENSMUSG00000019961. [Q61033-1]
    GeneIDi21917.
    KEGGimmu:21917.
    UCSCiuc007gtu.1. mouse. [Q61033-2]
    uc007gtv.1. mouse. [Q61033-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39073 mRNA. Translation: AAC52573.1 .
    U39078 mRNA. Translation: AAC52578.1 .
    CH466539 Genomic DNA. Translation: EDL21530.1 .
    BC141062 mRNA. Translation: AAI41063.1 .
    CCDSi CCDS24122.1. [Q61033-1 ]
    RefSeqi NP_035735.2. NM_011605.3. [Q61033-1 ]
    UniGenei Mm.159684.
    Mm.439157.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V0X X-ray 2.20 A/B 459-693 [» ]
    ProteinModelPortali Q61033.
    SMRi Q61033. Positions 2-56, 102-158, 465-689.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204234. 3 interactions.
    DIPi DIP-29323N.
    IntActi Q61033. 3 interactions.
    MINTi MINT-4100192.

    Proteomic databases

    MaxQBi Q61033.
    PaxDbi Q61033.
    PRIDEi Q61033.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020123 ; ENSMUSP00000020123 ; ENSMUSG00000019961 . [Q61033-1 ]
    GeneIDi 21917.
    KEGGi mmu:21917.
    UCSCi uc007gtu.1. mouse. [Q61033-2 ]
    uc007gtv.1. mouse. [Q61033-1 ]

    Organism-specific databases

    CTDi 7112.
    MGIi MGI:106920. Tmpo.

    Phylogenomic databases

    eggNOGi NOG87051.
    GeneTreei ENSGT00510000048934.
    HOGENOMi HOG000113280.
    HOVERGENi HBG081890.
    InParanoidi B2RUB9.
    OMAi PRYRESK.
    OrthoDBi EOG7KWSGZ.
    TreeFami TF328426.

    Miscellaneous databases

    ChiTaRSi TMPO. mouse.
    EvolutionaryTracei Q61033.
    NextBioi 301476.
    PROi Q61033.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61033.
    Bgeei Q61033.
    CleanExi MM_TMPO.
    Genevestigatori Q61033.

    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. "The characterization and localization of the mouse thymopoietin/lamina-associated polypeptide 2 gene and its alternatively spliced products."
      Berger R., Theodor L., Shoham J., Gokkel E., Brok-Simoni F., Avraham K.B., Copeland N.G., Jenkins N.A., Rechavi G., Simon A.J.
      Genome Res. 6:361-370(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; GAMMA; DELTA; EPSILON AND ZETA).
      Strain: C57BL/6 X DBA/2.
      Tissue: Thymus.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Brain.
    4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; THR-159 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 (ISOFORM ZETA), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    9. "Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina."
      Bradley C.M., Jones S., Huang Y., Suzuki Y., Kvaratskhelia M., Hickman A.B., Craigie R., Dyda F.
      Structure 15:643-653(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 459-693, IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, INTERACTION WITH LMNA, SUBUNIT.

    Entry informationi

    Entry nameiLAP2A_MOUSE
    AccessioniPrimary (citable) accession number: Q61033
    Secondary accession number(s): B2RUB9, Q61028
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 118 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3