Q61033 (LAP2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Name:	Tmpo
Synonyms:	Lap2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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. 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.6
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.6 The C-terminal domain forms a four-stranded coiled coil. Ref.6
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	Chromosome Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from direct assay PubMed 11591818. Source: MGI
Cellular_component	chromatin Inferred from sequence orthology PubMed 17284516. Source: MGI nuclear envelope Inferred from direct assay PubMed 11591818PubMed 18809722. Source: MGI nuclear inner membrane Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
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.
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 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

Coiled coil

557 – 656

100

Motif

190 – 196

7

Nuclear localization signal Potential

Amino acid modifications

Modified residue

59

1

Phosphoserine By similarity

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

153

1

Phosphothreonine By similarity

Modified residue

155

1

Phosphoserine By similarity

Modified residue

159

1

Phosphothreonine Ref.4

Modified residue

163

1

Phosphothreonine Ref.4

Modified residue

183

1

Phosphoserine Ref.5

Modified residue

349

1

Phosphoserine By similarity

Modified residue

352

1

Phosphoserine By similarity

Modified residue

368

1

Phosphoserine By similarity

Modified residue

422

1

Phosphoserine Ref.4

Modified residue

655

1

N6-acetyllysine By similarity

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

Experimental info

Sequence conflict

72 – 73

2

EP → DA in AAC52573. Ref.1

Sequence conflict

72 – 73

2

EP → DA in AAC52578. Ref.1

Sequence conflict

262 – 265

4

KGQT → RGRP in AAC52578. Ref.1

Sequence conflict

280 – 281

2

SS → LC in AAC52578. Ref.1

Sequence conflict

322 – 324

3

DIV → EHS in AAC52578. Ref.1

Sequence conflict

393 – 394

2

GT → RS in AAC52578. Ref.1

Sequence conflict

606

1

D → I in AAC52578. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

693

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 00604F3B66FF63F3	FASTA	693	75,168
	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
	Isoform Zeta [UniParc]. Checksum: D980460C9CE89898	FASTA	225	24,990
	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 RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRTEHNQ VFVVL
	Isoform Beta [UniParc]. See Q61029.		–	–
	Isoform Delta [UniParc]. See Q61029.		–	–
	Isoform Epsilon [UniParc]. See Q61029.		–	–
	Isoform Gamma [UniParc]. See Q61029.		–	–

References

	« Hide 'large scale' referencesShow '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]	"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 THR-159; THR-163 AND SER-422, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"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, 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.

IPI

IPI00126338.
IPI00798595.

RefSeq

NP_001073603.1. NM_001080134.1.
NP_035735.2. NM_011605.2.

UniGene

Mm.159684.
Mm.439157.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V0X	X-ray	2.20	A/B	459-693	[»]

ProteinModelPortal

Q61033.

SMR

Q61033. Positions 2-56, 102-158, 465-689.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29323N.

IntAct

Q61033. 1 interaction.

MINT

MINT-4100192.

Proteomic databases

PaxDb

Q61033.

PRIDE

Q61033.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000020123; ENSMUSP00000020123; ENSMUSG00000019961.

GeneID

21917.

KEGG

mmu:21917.

UCSC

uc007gtu.1. mouse.
uc007gtv.1. mouse.

Organism-specific databases

CTD

7112.

MGI

MGI:106920. Tmpo.

Phylogenomic databases

eggNOG

NOG87051.

GeneTree

ENSGT00510000048934.

HOGENOM

HOG000113280.

HOVERGEN

HBG081890.

InParanoid

B2RUB9.

OrthoDB

EOG428214.

Gene expression databases

ArrayExpress

Q61033.

Bgee

Q61033.

CleanEx

MM_TMPO.

Genevestigator

Q61033.

GermOnline

ENSMUSG00000019961. Mus musculus.

Family and domain databases

Gene3D

1.10.720.40. 2 hits.

InterPro

IPR021623. LAP2alpha.
IPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]

Pfam

PF11560. LAP2alpha. 1 hit.
PF03020. LEM. 1 hit.
PF08198. Thymopoietin. 1 hit.
[Graphical view]

SMART

SM00540. LEM. 1 hit.
[Graphical view]

SUPFAM

SSF63451. LEM_like. 2 hits.

PROSITE

PS50954. LEM. 1 hit.
PS50955. LEM_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TMPO. mouse.

EvolutionaryTrace

Q61033.

NextBio

301476.

SOURCE

Search...

Entry information

Entry name

LAP2A_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 105 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program