Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P42167 (LAP2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Thymopoietin
    Short name=TP
    Alternative name(s):
    Splenin
  2. Thymopentin
    Alternative name(s):
    TP5
Gene names
Name:TMPO
Synonyms:LAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.

Subunit structure

Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and chromosomes By similarity. Ref.5 Ref.6

Subcellular location

Nucleus inner membrane; Single-pass type II membrane protein. Note: Tightly associated with the nuclear lamina.

Tissue specificity

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

Domain

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.

Post-translational modification

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

Citrullinated by PADI4 By similarity.

Pharmaceutical use

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

Sequence similarities

Belongs to the LEM family.

Contains 1 LEM domain.

Contains 1 LEM-like domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-455283,EBI-389883

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Beta (identifier: P42167-1)

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.
Isoform Alpha (identifier: P42166-1)

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.
Isoform Gamma (identifier: P42167-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Lamina-associated polypeptide 2, isoforms beta/gamma
PRO_0000045841
Peptide1 – 5050Thymopoietin
PRO_0000017677
Peptide33 – 375Thymopentin
PRO_0000017678

Regions

Transmembrane411 – 43424Helical; Signal-anchor for type II membrane protein; Potential
Topological domain435 – 45420Lumenal Potential
Domain5 – 4844LEM-like
Domain109 – 15345LEM
Region1 – 410410Nucleoplasmic Potential
Region49 – 10860Linker
Region138 – 243106NAKAP95-binding N
Region299 – 37173Binds lamins B
Region300 – 37475NAKAP95-binding C

Amino acid modifications

Modified residue571Phosphothreonine Ref.15
Modified residue591Phosphoserine Ref.21
Modified residue661Phosphoserine Ref.15 Ref.18
Modified residue671Phosphoserine Ref.15 Ref.18
Modified residue741Phosphothreonine Ref.12 Ref.14 Ref.15 Ref.18 Ref.19 Ref.21
Modified residue791Phosphoserine Ref.15 Ref.18
Modified residue1541Phosphothreonine Ref.18
Modified residue1561Phosphoserine Ref.19
Modified residue1601Phosphothreonine Ref.15 Ref.18 Ref.19
Modified residue1641Phosphothreonine Ref.15
Modified residue1771Phosphoserine Ref.15
Modified residue1801Phosphoserine Ref.15
Modified residue1841Phosphoserine Ref.21
Modified residue2071N6-acetyllysine By similarity
Modified residue2111Phosphothreonine Ref.19
Modified residue2651Phosphoserine Ref.19
Modified residue2921Phosphoserine Ref.18
Modified residue3061Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18 Ref.19
Modified residue3121Phosphothreonine Ref.19
Modified residue3151Phosphoserine Ref.12 Ref.15 Ref.19
Modified residue3201Citrulline By similarity
Modified residue3621Phosphoserine Ref.15
Modified residue3851Phosphoserine Ref.15
Modified residue3891N6-acetyllysine By similarity

Natural variations

Alternative sequence222 – 330109Missing in isoform Gamma.
VSP_004456
Natural variant2871A → P.
Corresponds to variant rs7133258 [ dbSNP | Ensembl ].
VAR_049779
Natural variant4271L → F.
Corresponds to variant rs1058288 [ dbSNP | Ensembl ].
VAR_014786

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 03277C5723117909

FASTA45450,670
        10         20         30         40         50         60 
MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK 

        70         80         90        100        110        120 
GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL 

       130        140        150        160        170        180 
LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS 

       190        200        210        220        230        240 
DRYSDNEEDS KIELKLEKRE PLKGRAKTPV TLKQRRVEHN QSYSQAGITE TEWTSGSSKG 

       250        260        270        280        290        300 
GPLQALTRES TRGSRRTPRK RVETSEHFRI DGPVISESTP IAETIMASSN ESLVVNRVTG 

       310        320        330        340        350        360 
NFKHASPILP ITEFSDIPRR APKKPLTRAE VGEKTEERRV ERDILKEMFP YEASTPTGIS 

       370        380        390        400        410        420 
ASCRRPIKGA AGRPLELSDF RMEESFSSKY VPKYVPLADV KSEKTKKGRS IPVWIKILLF 

       430        440        450 
VVVAVFLFLV YQAMETNQVN PFSNFLHVDP RKSN 

« Hide

Isoform Alpha [UniParc].

See P42166.

Isoform Gamma [UniParc].

Checksum: F0669D9AEF97B32E
Show »

FASTA34538,738

References

« Hide 'large scale' references
[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]"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.
[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]"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).
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
[16]"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.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-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.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; THR-74 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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.
[23]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09087 mRNA. Translation: AAB60330.1.
U09088 mRNA. Translation: AAB60331.1.
BC053675 mRNA. Translation: AAH53675.1.
AF070631 mRNA. Translation: AAC25390.1.
U18269 expand/collapse EMBL AC list , U18266, U18267, U18268, U18270 Genomic DNA. Translation: AAB60434.1.
U18271 Genomic DNA. Translation: AAB60435.1.
CCDSCCDS31879.1. [P42167-1]
CCDS31880.1. [P42167-2]
PIRB55741.
C55741.
RefSeqNP_001027454.1. NM_001032283.2. [P42167-1]
NP_001027455.1. NM_001032284.2. [P42167-2]
UniGeneHs.11355.

3D structure databases

ProteinModelPortalP42167.
SMRP42167. Positions 2-57, 103-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112967. 47 interactions.
IntActP42167. 8 interactions.
MINTMINT-2839042.

PTM databases

PhosphoSiteP42167.

Polymorphism databases

DMDM1174690.

Proteomic databases

MaxQBP42167.
PeptideAtlasP42167.
PRIDEP42167.

Protocols and materials databases

DNASU7112.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393053; ENSP00000376773; ENSG00000120802. [P42167-2]
ENST00000556029; ENSP00000450627; ENSG00000120802. [P42167-1]
GeneID7112.
KEGGhsa:7112.
UCSCuc001tfj.3. human. [P42167-1]
uc001tfk.3. human. [P42167-2]

Organism-specific databases

CTD7112.
GeneCardsGC12P098909.
GeneReviewsTMPO.
HGNCHGNC:11875. TMPO.
HPACAB009847.
HPA008150.
MIM188380. gene.
neXtProtNX_P42167.
PharmGKBPA36576.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000113280.
HOVERGENHBG000166.
OMATGNFKHA.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressP42167.
BgeeP42167.
CleanExHS_TMPO.
GenevestigatorP42167.

Family and domain databases

Gene3D1.10.720.40. 2 hits.
InterProIPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamPF03020. LEM. 1 hit.
PF08198. Thymopoietin. 1 hit.
[Graphical view]
SMARTSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMSSF63451. SSF63451. 2 hits.
PROSITEPS50954. LEM. 1 hit.
PS50955. LEM_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTMPO. human.
GenomeRNAi7112.
NextBio27839.
PMAP-CutDBP42167.
PROP42167.
SOURCESearch...

Entry information

Entry nameLAP2B_HUMAN
AccessionPrimary (citable) accession number: P42167
Secondary accession number(s): Q14861
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM