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P42167

- LAP2B_HUMAN

UniProt

P42167 - LAP2B_HUMAN

Protein

Lamina-associated polypeptide 2, isoforms beta/gamma

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 151 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95.
    Thymopoietin (TP) and Thymopentin (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
    3. protein binding Source: IntAct

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_200828. Depolymerisation of the Nuclear Lamina.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lamina-associated polypeptide 2, isoforms beta/gamma
    Alternative name(s):
    Thymopoietin, isoforms beta/gamma
    Short name:
    TP beta/gamma
    Thymopoietin-related peptide isoforms beta/gamma
    Short name:
    TPRP isoforms beta/gamma
    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 inner membrane; Single-pass type II membrane protein
    Note: Tightly associated with the nuclear lamina.
    Isoform Zeta : Cytoplasm 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: UniProtKB
    3. nuclear envelope Source: ProtInc
    4. nuclear inner membrane Source: UniProtKB-SubCell
    5. nuclear membrane Source: HPA
    6. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    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.

    Organism-specific databases

    PharmGKBiPA36576.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Lamina-associated polypeptide 2, isoforms beta/gammaPRO_0000045841Add
    BLAST
    Peptidei1 – 5050ThymopoietinPRO_0000017677Add
    BLAST
    Peptidei33 – 375ThymopentinPRO_0000017678

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571Phosphothreonine1 Publication
    Modified residuei59 – 591Phosphoserine1 Publication
    Modified residuei66 – 661Phosphoserine2 Publications
    Modified residuei67 – 671Phosphoserine2 Publications
    Modified residuei74 – 741Phosphothreonine6 Publications
    Modified residuei79 – 791Phosphoserine2 Publications
    Modified residuei154 – 1541Phosphothreonine1 Publication
    Modified residuei156 – 1561Phosphoserine1 Publication
    Modified residuei160 – 1601Phosphothreonine3 Publications
    Modified residuei164 – 1641Phosphothreonine1 Publication
    Modified residuei177 – 1771Phosphoserine1 Publication
    Modified residuei180 – 1801Phosphoserine1 Publication
    Modified residuei184 – 1841Phosphoserine1 Publication
    Modified residuei207 – 2071N6-acetyllysineBy similarity
    Modified residuei211 – 2111Phosphothreonine1 Publication
    Modified residuei265 – 2651Phosphoserine1 Publication
    Modified residuei292 – 2921Phosphoserine1 Publication
    Modified residuei306 – 3061Phosphoserine8 Publications
    Modified residuei312 – 3121Phosphothreonine1 Publication
    Modified residuei315 – 3151Phosphoserine3 Publications
    Modified residuei320 – 3201CitrullineBy similarity
    Modified residuei362 – 3621Phosphoserine1 Publication
    Modified residuei385 – 3851Phosphoserine1 Publication
    Modified residuei389 – 3891N6-acetyllysineBy similarity

    Post-translational modificationi

    Mitosis-specific phosphorylation specifically abolishes its binding to lamin B and chromosomes.By similarity
    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiP42167.
    PeptideAtlasiP42167.
    PRIDEiP42167.

    PTM databases

    PhosphoSiteiP42167.

    Miscellaneous databases

    PMAP-CutDBP42167.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP42167.
    BgeeiP42167.
    CleanExiHS_TMPO.
    GenevestigatoriP42167.

    Organism-specific databases

    HPAiCAB009847.
    HPA008150.

    Interactioni

    Subunit structurei

    Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and chromosomes By similarity. Isoform Zeta interacts with BANF1/BAF and may sequester it in the cytoplasm.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-455283,EBI-389883

    Protein-protein interaction databases

    BioGridi112967. 49 interactions.
    IntActiP42167. 8 interactions.
    MINTiMINT-2839042.

    Structurei

    3D structure databases

    ProteinModelPortaliP42167.
    SMRiP42167. Positions 2-57, 103-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini435 – 45420LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei411 – 43424Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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
    Regioni1 – 410410NucleoplasmicSequence AnalysisAdd
    BLAST
    Regioni49 – 10860LinkerAdd
    BLAST
    Regioni138 – 243106NAKAP95-binding NAdd
    BLAST
    Regioni299 – 37173Binds lamins BAdd
    BLAST
    Regioni300 – 37475NAKAP95-binding CAdd
    BLAST

    Domaini

    Has 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.

    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

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOGENOMiHOG000113280.
    HOVERGENiHBG000166.
    OMAiTGNFKHA.

    Family and domain databases

    Gene3Di1.10.720.40. 2 hits.
    InterProiIPR013146. LEM-like_dom.
    IPR011015. LEM/LEM-like_dom.
    IPR003887. LEM_dom.
    [Graphical view]
    PfamiPF03020. 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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform Beta (identifier: P42167-1) [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 DRYSDNEEDS KIELKLEKRE 200
    PLKGRAKTPV TLKQRRVEHN QSYSQAGITE TEWTSGSSKG GPLQALTRES 250
    TRGSRRTPRK RVETSEHFRI DGPVISESTP IAETIMASSN ESLVVNRVTG 300
    NFKHASPILP ITEFSDIPRR APKKPLTRAE VGEKTEERRV ERDILKEMFP 350
    YEASTPTGIS ASCRRPIKGA AGRPLELSDF RMEESFSSKY VPKYVPLADV 400
    KSEKTKKGRS IPVWIKILLF VVVAVFLFLV YQAMETNQVN PFSNFLHVDP 450
    RKSN 454
    Length:454
    Mass (Da):50,670
    Last modified:January 23, 2007 - v2
    Checksum:i03277C5723117909
    GO
    Isoform Alpha (identifier: P42166-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P42166.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:694
    Mass (Da):75,492
    GO
    Isoform Gamma (identifier: P42167-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         222-330: Missing.

    Show »
    Length:345
    Mass (Da):38,738
    Checksum:iF0669D9AEF97B32E
    GO
    Isoform Zeta (identifier: P42167-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         222-248: SYSQAGITETEWTSGSSKGGPLQALTR → VSLVLLPPCTGINNLLTTLIHVLAFNG
         249-454: Missing.

    Note: Inhibits LAP2beta-mediated repression.

    Show »
    Length:248
    Mass (Da):27,388
    Checksum:iC3CDE62D4C0B0590
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti287 – 2871A → P.
    Corresponds to variant rs7133258 [ dbSNP | Ensembl ].
    VAR_049779
    Natural varianti427 – 4271L → F.
    Corresponds to variant rs1058288 [ dbSNP | Ensembl ].
    VAR_014786

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei222 – 330109Missing in isoform Gamma. 2 PublicationsVSP_004456Add
    BLAST
    Alternative sequencei222 – 24827SYSQA…QALTR → VSLVLLPPCTGINNLLTTLI HVLAFNG in isoform Zeta. 1 PublicationVSP_056162Add
    BLAST
    Alternative sequencei249 – 454206Missing in isoform Zeta. 1 PublicationVSP_056163Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09087 mRNA. Translation: AAB60330.1.
    U09088 mRNA. Translation: AAB60331.1.
    EF028063 mRNA. Translation: ABL61272.1.
    AF070631 mRNA. Translation: AAC25390.1.
    BC053675 mRNA. Translation: AAH53675.1.
    U18269
    , U18266, U18267, U18268, U18270 Genomic DNA. Translation: AAB60434.1.
    U18271 Genomic DNA. Translation: AAB60435.1.
    CCDSiCCDS31879.1. [P42167-1]
    CCDS31880.1. [P42167-2]
    PIRiB55741.
    C55741.
    RefSeqiNP_001027454.1. NM_001032283.2. [P42167-1]
    NP_001027455.1. NM_001032284.2. [P42167-2]
    UniGeneiHs.11355.

    Genome annotation databases

    EnsembliENST00000261210; ENSP00000261210; ENSG00000120802.
    ENST00000393053; ENSP00000376773; ENSG00000120802. [P42167-2]
    ENST00000556029; ENSP00000450627; ENSG00000120802. [P42167-1]
    GeneIDi7112.
    KEGGihsa:7112.
    UCSCiuc001tfj.3. human. [P42167-1]
    uc001tfk.3. human. [P42167-2]

    Polymorphism databases

    DMDMi1174690.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09087 mRNA. Translation: AAB60330.1 .
    U09088 mRNA. Translation: AAB60331.1 .
    EF028063 mRNA. Translation: ABL61272.1 .
    AF070631 mRNA. Translation: AAC25390.1 .
    BC053675 mRNA. Translation: AAH53675.1 .
    U18269
    , U18266 , U18267 , U18268 , U18270 Genomic DNA. Translation: AAB60434.1 .
    U18271 Genomic DNA. Translation: AAB60435.1 .
    CCDSi CCDS31879.1. [P42167-1 ]
    CCDS31880.1. [P42167-2 ]
    PIRi B55741.
    C55741.
    RefSeqi NP_001027454.1. NM_001032283.2. [P42167-1 ]
    NP_001027455.1. NM_001032284.2. [P42167-2 ]
    UniGenei Hs.11355.

    3D structure databases

    ProteinModelPortali P42167.
    SMRi P42167. Positions 2-57, 103-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112967. 49 interactions.
    IntActi P42167. 8 interactions.
    MINTi MINT-2839042.

    PTM databases

    PhosphoSitei P42167.

    Polymorphism databases

    DMDMi 1174690.

    Proteomic databases

    MaxQBi P42167.
    PeptideAtlasi P42167.
    PRIDEi P42167.

    Protocols and materials databases

    DNASUi 7112.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261210 ; ENSP00000261210 ; ENSG00000120802 .
    ENST00000393053 ; ENSP00000376773 ; ENSG00000120802 . [P42167-2 ]
    ENST00000556029 ; ENSP00000450627 ; ENSG00000120802 . [P42167-1 ]
    GeneIDi 7112.
    KEGGi hsa:7112.
    UCSCi uc001tfj.3. human. [P42167-1 ]
    uc001tfk.3. human. [P42167-2 ]

    Organism-specific databases

    CTDi 7112.
    GeneCardsi GC12P098909.
    GeneReviewsi TMPO.
    HGNCi HGNC:11875. TMPO.
    HPAi CAB009847.
    HPA008150.
    MIMi 188380. gene.
    neXtProti NX_P42167.
    PharmGKBi PA36576.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000113280.
    HOVERGENi HBG000166.
    OMAi TGNFKHA.

    Enzyme and pathway databases

    Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_200828. Depolymerisation of the Nuclear Lamina.

    Miscellaneous databases

    ChiTaRSi TMPO. human.
    GenomeRNAii 7112.
    NextBioi 27839.
    PMAP-CutDB P42167.
    PROi P42167.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42167.
    Bgeei P42167.
    CleanExi HS_TMPO.
    Genevestigatori P42167.

    Family and domain databases

    Gene3Di 1.10.720.40. 2 hits.
    InterProi IPR013146. LEM-like_dom.
    IPR011015. LEM/LEM-like_dom.
    IPR003887. LEM_dom.
    [Graphical view ]
    Pfami 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA), SUBCELLULAR LOCATION (ISOFORM ZETA).
    3. Yu W., Gibbs R.A.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA).
      Tissue: Brain.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [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 BETA).
      Tissue: Eye.
    6. "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] OF 1-237 AND 313-454 (ISOFORMS BETA AND GAMMA).
    7. "Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin."
      Furukawa K., Kondo T.
      Eur. J. Biochem. 251:729-733(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LMNB1.
    8. "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication."
      Martins S., Eikvar S., Furukawa K., Collas P.
      J. Cell Biol. 160:177-188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKAP8L.
    9. "Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics."
      Dechat T., Vlcek S., Foisner R.
      J. Struct. Biol. 129:335-345(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    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-306, 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-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. "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; SER-306 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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.
    16. "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 AND SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-66; SER-67; THR-74; SER-79; THR-160; THR-164; SER-177; SER-180; SER-306; SER-315; SER-362 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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.
    19. "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].
    20. "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-292 AND SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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; THR-211; SER-265; SER-306; THR-312 AND SER-315, 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 AND SER-184, 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.

    Entry informationi

    Entry nameiLAP2B_HUMAN
    AccessioniPrimary (citable) accession number: P42167
    Secondary accession number(s): A2T926, Q14861
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 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

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

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