Reviewed,
UniProtKB/Swiss-Prot Q61033 (LAP2A_MOUSE)
Last modified
May 26, 2009.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lamina-associated polypeptide 2, isoforms alpha/zeta Alternative name(s): Thymopoietin isoforms alpha/zeta Short name=TP alpha/zeta | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 693 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Play an important role, together with LMNA, in the nuclear anchorage of RB1 By similarity. |
| Subunit structure | Interacts with LMNA, BANF1 and RB1 and with chromosomes. Associates directly or indirectly with lamins at specific cell-cycle stages By similarity. |
| Subcellular location | Nucleus By similarity. Note: Expressed diffusely throughout the nucleus By similarity. |
| 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 By similarity. |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosomal protein Nucleus |
| Coding sequence diversity | Alternative splicing |
| Ligand | DNA-binding |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | regulation of transcription Inferred from direct assay. Source: MGI |
| Cellular component | chromosome Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelopeInferred from direct assay. Source: MGI |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: MGI |
| Complete GO annotation... | |
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. | ||||||
| Isoform Beta (identifier: Q61029-1) The sequence of this isoform can be found in the external entry Q61029-1. 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 Q61029-2. 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 Q61029-3. 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 Q61029-4. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | |||||||||||||||||||||||||
| Chain | 2 – 693 | 692 | Lamina-associated polypeptide 2, isoforms alpha/zeta | PRO_0000206145 | ||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||
| Domain | 5 – 48 | 44 | LEM-like | |||||||||||||||||||||||||
| Domain | 108 – 152 | 45 | LEM | |||||||||||||||||||||||||
| Region | 49 – 107 | 59 | Linker | |||||||||||||||||||||||||
| Motif | 190 – 196 | 7 | Nuclear localization signal Potential | |||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||
| Modified residue | 66 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 67 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 74 | 1 | Phosphothreonine By similarity | |||||||||||||||||||||||||
| Modified residue | 79 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 155 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 159 | 1 | Phosphothreonine Ref.2 | |||||||||||||||||||||||||
| Modified residue | 163 | 1 | Phosphothreonine Ref.2 | |||||||||||||||||||||||||
| Modified residue | 167 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 176 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 179 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 183 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 308 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 349 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 368 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||
| Modified residue | 422 | 1 | Phosphoserine Ref.2 | |||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||
| Alternative sequence | 188 – 225 | 38 | GKKKE…SFPEI → DSKIELKLEKREPLKGRAKT PVTLKQRRTEHNQVFVVL in isoform Zeta. | VSP_010128 | ||||||||||||||||||||||||
| Alternative sequence | 226 – 693 | 468 | Missing in isoform Zeta. | VSP_010129 | ||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||
| Helix | 495 – 504 | 10 | ||||||||||||||||||||||||||
| Helix | 505 – 507 | 3 | ||||||||||||||||||||||||||
| Beta strand | 508 – 510 | 3 | ||||||||||||||||||||||||||
| Turn | 516 – 518 | 3 | ||||||||||||||||||||||||||
| Helix | 524 – 530 | 7 | ||||||||||||||||||||||||||
| Helix | 537 – 541 | 5 | ||||||||||||||||||||||||||
| Helix | 558 – 604 | 47 | ||||||||||||||||||||||||||
| Helix | 610 – 654 | 45 | ||||||||||||||||||||||||||
| Beta strand | 655 – 657 | 3 | ||||||||||||||||||||||||||
| Helix | 661 – 669 | 9 | ||||||||||||||||||||||||||
| Beta strand | 674 – 678 | 5 | ||||||||||||||||||||||||||
Sequences
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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: 8743987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; GAMMA; DELTA; EPSILON AND ZETA). Strain: C57BL/6 X DBA/2. Tissue: Thymus. |
| [2] | "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: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159; THR-163 AND SER-422, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U39073 mRNA. Translation: AAC52573.1. U39078 mRNA. Translation: AAC52578.1. | |||||||||||||
| IPI | IPI00126338. IPI00798595. | ||||||||||||
| UniGene | Mm.159684 Mm.439157 | ||||||||||||
3D structure databases | |||||||||||||
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| SMR | Q61033. Positions 2-56, 102-158. | ||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q61033. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q61033. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUSG00000019961. Mus musculus. [Contig view] | ||||||||||||
Organism-specific databases | |||||||||||||
| MGI | MGI:106920. Tmpo. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | Q61033. | ||||||||||||
| HOVERGEN | Q61033. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q61033. | ||||||||||||
| Bgee | Q61033. | ||||||||||||
| CleanEx | MM_TMPO. | ||||||||||||
| GermOnline | ENSMUSG00000019961. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003887. LEM. IPR013146. Thymopoietin_LEM. [Graphical view] | ||||||||||||
| Pfam | PF03020. LEM. 1 hit. PF08198. Thymopoietin. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD004209. LEM. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| SMART | SM00540. LEM. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS50954. LEM. 1 hit. PS50955. LEM_LIKE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | LAP2A_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q61033 Secondary accession number(s): Q61028 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


