Q61029 (LAP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma

Alternative name(s):
Thymopoietin isoforms beta/delta/epsilon/gamma
Short name=TP beta/delta/epsilon/gamma

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	452 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
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 By similarity. Chromosome By similarity. Note: Tightly associated with the nuclear lamina 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	Mitosis-specific phosphorylation specifically abolishes its binding to lamin B and chromosomes By similarity.
Sequence similarities	Belongs to the LEM family. Contains 1 LEM domain. Contains 1 LEM-like domain.

Ontologies

Keywords
Cellular component	Chromosome Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from direct assay Ref.6. Source: MGI
Cellular_component	chromatin Inferred from sequence orthology PubMed 17284516. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelope Inferred from direct assay Ref.6PubMed 18809722. Source: MGI nuclear inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Zbtb7b	Q64321	2	EBI-6172136,EBI-642868

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform Beta (identifier: Q61029-1)

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: Q61033-1)

The sequence of this isoform can be found in the external entry Q61033.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform Zeta (identifier: Q61033-2)

The sequence of this isoform can be found in the external entry Q61033.
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 differs from the canonical sequence as follows:
     221-292: Missing.

Isoform Epsilon (identifier: Q61029-3)

The sequence of this isoform differs from the canonical sequence as follows:
     221-260: Missing.

Isoform Gamma (identifier: Q61029-4)

The sequence of this isoform differs from the canonical sequence as follows:
     221-329: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 452	452	Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma		PRO_0000206146
Regions
	Transmembrane	410 – 430	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	431 – 452	22	Lumenal Potential
	Domain	5 – 48	44	LEM-like
	Domain	109 – 153	45	LEM
	Region	1 – 409	409	Nucleoplasmic Potential
	Region	49 – 108	60	Linker
	Region	137 – 242	106	NAKAP95-binding N
	Region	298 – 370	73	Binds lamins B
	Region	299 – 373	75	NAKAP95-binding C
Amino acid modifications
	Modified residue	66	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	67	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	74	1	Phosphothreonine Ref.4 Ref.8
	Modified residue	155	1	Phosphoserine Ref.7 Ref.9
	Modified residue	159	1	Phosphothreonine Ref.4
	Modified residue	176	1	Phosphoserine Ref.4
	Modified residue	179	1	Phosphoserine; by PKC Ref.4
	Modified residue	183	1	Phosphoserine Ref.9
	Modified residue	207	1	Phosphothreonine Ref.9 Ref.10
	Modified residue	210	1	Phosphothreonine By similarity
	Modified residue	264	1	Phosphoserine By similarity
	Modified residue	291	1	Phosphoserine By similarity
	Modified residue	305	1	Phosphoserine By similarity
	Modified residue	311	1	Phosphothreonine By similarity
	Modified residue	314	1	Phosphoserine By similarity
	Modified residue	361	1	Phosphoserine By similarity
	Modified residue	384	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	221 – 329	109	Missing in isoform Gamma.		VSP_010132
	Alternative sequence	221 – 292	72	Missing in isoform Delta.		VSP_010131
	Alternative sequence	221 – 260	40	Missing in isoform Epsilon.		VSP_010130
Experimental info
	Sequence conflict	72 – 73	2	EP → DA in AAC52574. Ref.1
	Sequence conflict	72 – 73	2	EP → DA in AAC52575. Ref.1
	Sequence conflict	72 – 73	2	EP → DA in AAC52576. Ref.1
	Sequence conflict	72 – 73	2	EP → DA in AAC52577. Ref.1
	Sequence conflict	422 – 424	3	VAV → GAC in AAC52574. Ref.1
	Sequence conflict	422 – 424	3	VAV → GAC in AAC52575. Ref.1
	Sequence conflict	422 – 424	3	VAV → GAC in AAC52576. Ref.1
	Sequence conflict	422 – 424	3	VAV → GAC in AAC52577. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 132AF11B458DCFBA	FASTA	452	50,373
	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 RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRTEHNQ SYSQAGVTET EWTSGSSTGG 250 260 270 280 290 300 PLQALTREST RGSRRTPRKR VETSQHFRID GAVISESTPI AETIKASSNE SLVANRLTGN 310 320 330 340 350 360 FKHASSILPI TEFSDITRRT PKKPLTRAEV GEKTEERRVD RDILKEMFPY EASTPTGISA 370 380 390 400 410 420 SCRRPIKGAA GRPLELSDFR MEESFSSKYV PKYAPLADVK SEKTKKRRSV PMWIKMLLFA 430 440 450 LVAVFLFLVY QAMETNQGNP FTNFLQDTKI SN
	Isoform Alpha [UniParc]. See Q61033.		–	–
	Isoform Zeta [UniParc]. See Q61033.		–	–
	Isoform Delta [UniParc]. Checksum: F2BE6B5556030A49	FASTA	380	42,650
	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 RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRTEHNQ VANRLTGNFK HASSILPITE 250 260 270 280 290 300 FSDITRRTPK KPLTRAEVGE KTEERRVDRD ILKEMFPYEA STPTGISASC RRPIKGAAGR 310 320 330 340 350 360 PLELSDFRME ESFSSKYVPK YAPLADVKSE KTKKRRSVPM WIKMLLFALV AVFLFLVYQA 370 380 METNQGNPFT NFLQDTKISN
	Isoform Epsilon [UniParc]. Checksum: C54639DAB8788CEE	FASTA	412	46,050
	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 RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRTEHNQ VETSQHFRID GAVISESTPI 250 260 270 280 290 300 AETIKASSNE SLVANRLTGN FKHASSILPI TEFSDITRRT PKKPLTRAEV GEKTEERRVD 310 320 330 340 350 360 RDILKEMFPY EASTPTGISA SCRRPIKGAA GRPLELSDFR MEESFSSKYV PKYAPLADVK 370 380 390 400 410 SEKTKKRRSV PMWIKMLLFA LVAVFLFLVY QAMETNQGNP FTNFLQDTKI SN
	Isoform Gamma [UniParc]. Checksum: BA62B6D869B0FDAD	FASTA	343	38,502
	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 RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRTEHNQ VGEKTEERRV DRDILKEMFP 250 260 270 280 290 300 YEASTPTGIS ASCRRPIKGA AGRPLELSDF RMEESFSSKY VPKYAPLADV KSEKTKKRRS 310 320 330 340 VPMWIKMLLF ALVAVFLFLV YQAMETNQGN PFTNFLQDTK ISN

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]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow and Lung.
[3]	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].
[4]	"Identification of phosphorylation sites in native lamina-associated polypeptide 2 beta." Dreger M., Otto H., Neubauer G., Mann M., Hucho F. Biochemistry 38:9426-9434(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 61-85 AND 173-194 (ISOFORM BETA), PHOSPHORYLATION AT THR-74; THR-159; SER-176 AND SER-179, MASS SPECTROMETRY.
[5]	"LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction." Furukawa K. J. Cell Sci. 112:2485-2492(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BANF1.
[6]	"Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less)." Nili E., Cojocaru G.S., Kalma Y., Ginsberg D., Copeland N.G., Gilbert D.J., Jenkins N.A., Berger R., Shaklai S., Amariglio N., Brok-Simoni F., Simon A.J., Rechavi G. J. Cell Sci. 114:3297-3307(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GMCL.
[7]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, MASS SPECTROMETRY. Tissue: Brain.
[8]	"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 AND THR-74, MASS SPECTROMETRY. Tissue: Liver.
[9]	"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-66; SER-67; SER-155; SER-183 AND THR-207, MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-207, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U39074 mRNA. Translation: AAC52574.1. U39075 mRNA. Translation: AAC52575.1. U39076 mRNA. Translation: AAC52576.1. U39077 mRNA. Translation: AAC52577.1. AK150305 mRNA. Translation: BAE29455.1. AK150515 mRNA. Translation: BAE29627.1. AK153281 mRNA. Translation: BAE31865.1. AK165851 mRNA. Translation: BAE38413.1. CH466539 Genomic DNA. Translation: EDL21533.1.
IPI	IPI00320399. IPI00466738. IPI00466817. IPI00623133.
RefSeq	NP_001073598.1. NM_001080129.1. NP_001073600.1. NM_001080131.1. NP_001073601.1. NM_001080132.1.
UniGene	Mm.159684. Mm.439157.
3D structure databases
ProteinModelPortal	Q61029.
SMR	Q61029. Positions 2-56, 102-158.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61029. 2 interactions.
Proteomic databases
PRIDE	Q61029.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000072239; ENSMUSP00000072092; ENSMUSG00000019961. ENSMUST00000092219; ENSMUSP00000089864; ENSMUSG00000019961. ENSMUST00000099355; ENSMUSP00000096956; ENSMUSG00000019961. ENSMUST00000105293; ENSMUSP00000100930; ENSMUSG00000019961.
GeneID	21917.
KEGG	mmu:21917.
Organism-specific databases
CTD	7112.
MGI	MGI:106920. Tmpo.
Phylogenomic databases
GeneTree	ENSGT00510000048934.
HOGENOM	HOG000113280.
HOVERGEN	HBG000166.
OMA	TGNFKHA.
Gene expression databases
ArrayExpress	Q61029.
Bgee	Q61029.
CleanEx	MM_TMPO.
Genevestigator	Q61029.
GermOnline	ENSMUSG00000019961. Mus musculus.
Family and domain databases
Gene3D	1.10.720.40. 2 hits.
InterPro	IPR013146. LEM-like_dom. IPR011015. LEM/LEM-like_dom. IPR003887. LEM_dom. [Graphical view]
Pfam	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.
NextBio	301476.
SOURCE	Search...

Entry information

Entry name

LAP2B_MOUSE

Accession

Primary (citable) accession number: Q61029
Secondary accession number(s): Q3UCI5 , Q61030, Q61031, Q61032

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 111 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program