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P42166

- LAP2A_HUMAN

UniProt

P42166 - LAP2A_HUMAN

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Protein
Lamina-associated polypeptide 2, isoform alpha
Gene
TMPO, LAP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 alpha
PRO_0000017674Add
BLAST
Peptidei2 – 5049Thymopoietin
PRO_0000017675Add
BLAST
Peptidei33 – 375Thymopentin
PRO_0000017676

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 residuei184 – 1841Phosphoserine1 Publication
Modified residuei351 – 3511Phosphoserine7 Publications
Modified residuei354 – 3541Phosphoserine2 Publications
Modified residuei370 – 3701Phosphoserine2 Publications
Modified residuei424 – 4241Phosphoserine6 Publications
Modified residuei656 – 6561N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated in a mitose-specific manner.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP42166.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 4844LEM-like
Add
BLAST
Domaini109 – 15345LEM
Add
BLAST

Region

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

Coiled coil

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi190 – 1967Nuclear localization signal Reviewed prediction

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.
Contains 1 LEM domain.
Contains 1 LEM-like domain.

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 155 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

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