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Q61033 (LAP2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lamina-associated polypeptide 2, isoforms alpha/zeta
Alternative name(s):
Thymopoietin isoforms alpha/zeta
Short name=TP alpha/zeta
Gene names
Name:Tmpo
Synonyms:Lap2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homooligomer. Interacts with LMNA, BANF1 and RB1 and with chromosomes. Associates directly or indirectly with lamins at specific cell-cycle stages By similarity. Ref.9

Subcellular location

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

Domain

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. Ref.9

The C-terminal domain forms a four-stranded coiled coil. Ref.9

Post-translational modification

Phosphorylated in a mitose-specific manner By similarity.

Sequence similarities

Belongs to the LEM family.

Contains 1 LEM domain.

Contains 1 LEM-like domain.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q61033-1)

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 Zeta (identifier: Q61033-2)

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.
Isoform Beta (identifier: Q61029-1)

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.
Isoform Delta (identifier: Q61029-2)

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.
Isoform Epsilon (identifier: Q61029-3)

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.
Isoform Gamma (identifier: Q61029-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 693692Lamina-associated polypeptide 2, isoforms alpha/zeta
PRO_0000206145

Regions

Domain5 – 4844LEM-like
Domain108 – 15245LEM
Region49 – 10759Linker
Coiled coil557 – 656100
Motif190 – 1967Nuclear localization signal Potential

Amino acid modifications

Modified residue591Phosphoserine By similarity
Modified residue661Phosphoserine Ref.5 Ref.7
Modified residue671Phosphoserine Ref.5 Ref.7
Modified residue741Phosphothreonine Ref.5 Ref.7
Modified residue791Phosphoserine By similarity
Modified residue1531Phosphothreonine By similarity
Modified residue1551Phosphoserine By similarity
Modified residue1591Phosphothreonine Ref.5
Modified residue1631Phosphothreonine By similarity
Modified residue1831Phosphoserine By similarity
Modified residue3491Phosphoserine By similarity
Modified residue3521Phosphoserine By similarity
Modified residue3681Phosphoserine By similarity
Modified residue4221Phosphoserine Ref.5
Modified residue6551N6-acetyllysine By similarity

Natural variations

Alternative sequence188 – 22538GKKKE…SFPEI → DSKIELKLEKREPLKGRAKT PVTLKQRRTEHNQVFVVL in isoform Zeta.
VSP_010128
Alternative sequence226 – 693468Missing in isoform Zeta.
VSP_010129

Experimental info

Sequence conflict72 – 732EP → DA in AAC52573. Ref.1
Sequence conflict72 – 732EP → DA in AAC52578. Ref.1
Sequence conflict262 – 2654KGQT → RGRP in AAC52578. Ref.1
Sequence conflict280 – 2812SS → LC in AAC52578. Ref.1
Sequence conflict322 – 3243DIV → EHS in AAC52578. Ref.1
Sequence conflict393 – 3942GT → RS in AAC52578. Ref.1
Sequence conflict6061D → I in AAC52578. Ref.1

Secondary structure

.................... 693
Helix Strand Turn

Details...

Sequences

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

Last modified July 27, 2011. Version 4.
Checksum: 00604F3B66FF63F3

FASTA69375,168
        10         20         30         40         50         60 
MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLAAGANSK 

        70         80         90        100        110        120 
GPPDFSSDEE REPTPVLGSG ASVGRGRGAV GRKATKKTDK PRLEDKDDLD VTELSNEELL 

       130        140        150        160        170        180 
DQLVRYGVNP GPIVGTTRKL YEKKLLKLRE QGTESRSSTP LPTVSSSAEN TRQNGSNDSD 

       190        200        210        220        230        240 
RYSDNDEGKK KEHKKVKSAR DCVPFSELAS TPSGAFFQGI SFPEISTRPP LGRTELQAAK 

       250        260        270        280        290        300 
KVQTTKRDPP RETCTDTALP GKGQTHKLAP GRSLFIPSES SYDRCVEKSS SPSSQREFAA 

       310        320        330        340        350        360 
RLVSAAASPS LIRETTTTYS KDIVENICRG GKSRAQPLRA EEPGVSDQSV FSSEREVLQE 

       370        380        390        400        410        420 
SERSQVISPP LAQAIRDYVN SLLVQGGVGS LPGTSDSVPT LDVENICKRL SQSSYQDSES 

       430        440        450        460        470        480 
LSPPRKVPRL SEKPARGGDS GSCVAFQNTP GSEHRSSFAK SVVSHSLTTL GVEVSKPPPQ 

       490        500        510        520        530        540 
HDKIEASEPS FPLHESILKV VEEEWQQIDR QLPSVACRYP VSSIEAARIL SVPKVDDEIL 

       550        560        570        580        590        600 
GFISEATPRA ATQASSTESC DKHLDLALCR SYEAAASALQ IAAHTAFVAK SLQADISQAA 

       610        620        630        640        650        660 
QIINSDPSDA QQALRILNRT YDAASYLCDA AFDEVRMSAC AMGSSTMGRR YLWLKDCKIS 

       670        680        690 
PASKNKLTVA PFKGGTLFGG EVHKVIKKRG NKQ 

« Hide

Isoform Zeta [UniParc].

Checksum: D980460C9CE89898
Show »

FASTA22524,990
Isoform Beta [UniParc].

See Q61029.

Isoform Delta [UniParc].

See Q61029.

Isoform Epsilon [UniParc].

See Q61029.

Isoform Gamma [UniParc].

See Q61029.

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39073 mRNA. Translation: AAC52573.1.
U39078 mRNA. Translation: AAC52578.1.
CH466539 Genomic DNA. Translation: EDL21530.1.
BC141062 mRNA. Translation: AAI41063.1.
RefSeqNP_035735.2. NM_011605.3.
UniGeneMm.159684.
Mm.439157.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V0XX-ray2.20A/B459-693[»]
ProteinModelPortalQ61033.
SMRQ61033. Positions 1-158, 465-689.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204234. 3 interactions.
DIPDIP-29323N.
IntActQ61033. 3 interactions.
MINTMINT-4100192.

Proteomic databases

PaxDbQ61033.
PRIDEQ61033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020123; ENSMUSP00000020123; ENSMUSG00000019961. [Q61033-1]
GeneID21917.
KEGGmmu:21917.
UCSCuc007gtu.1. mouse. [Q61033-2]
uc007gtv.1. mouse. [Q61033-1]

Organism-specific databases

CTD7112.
MGIMGI:106920. Tmpo.

Phylogenomic databases

eggNOGNOG87051.
GeneTreeENSGT00510000048934.
HOGENOMHOG000113280.
HOVERGENHBG081890.
InParanoidB2RUB9.
OrthoDBEOG7KWSGZ.
TreeFamTF328426.

Gene expression databases

ArrayExpressQ61033.
BgeeQ61033.
CleanExMM_TMPO.
GenevestigatorQ61033.

Family and domain databases

Gene3D1.10.720.40. 2 hits.
InterProIPR021623. LAP2alpha.
IPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamPF11560. LAP2alpha. 1 hit.
PF03020. 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. mouse.
EvolutionaryTraceQ61033.
NextBio301476.
PROQ61033.
SOURCESearch...

Entry information

Entry nameLAP2A_MOUSE
AccessionPrimary (citable) accession number: Q61033
Secondary accession number(s): B2RUB9, Q61028
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot