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Q61029 (LAP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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/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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
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 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.

Citrullinated by PADI4.

Sequence similarities

Belongs to the LEM family.

Contains 1 LEM domain.

Contains 1 LEM-like domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Zbtb7bQ643212EBI-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.
Note: Contains a N6-acetyllysine at position 206.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma
PRO_0000206146

Regions

Transmembrane410 – 43021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain431 – 45222Lumenal Potential
Domain5 – 4844LEM-like
Domain109 – 15345LEM
Region1 – 409409Nucleoplasmic Potential
Region49 – 10860Linker
Region137 – 242106NAKAP95-binding N
Region298 – 37073Binds lamins B
Region299 – 37375NAKAP95-binding C

Amino acid modifications

Modified residue591Phosphoserine By similarity
Modified residue661Phosphoserine Ref.8 Ref.10
Modified residue671Phosphoserine Ref.8 Ref.10
Modified residue741Phosphothreonine Ref.4 Ref.8 Ref.10
Modified residue791Phosphoserine By similarity
Modified residue1531Phosphothreonine By similarity
Modified residue1551Phosphoserine By similarity
Modified residue1591Phosphothreonine Ref.4 Ref.8
Modified residue1631Phosphothreonine By similarity
Modified residue1761Phosphoserine Ref.4
Modified residue1791Phosphoserine; by PKC Ref.4
Modified residue1831Phosphoserine By similarity
Modified residue2061N6-acetyllysine Ref.12
Modified residue2101Phosphothreonine By similarity
Modified residue2641Phosphoserine By similarity
Modified residue2911Phosphoserine By similarity
Modified residue3051Phosphoserine By similarity
Modified residue3111Phosphothreonine By similarity
Modified residue3141Phosphoserine By similarity
Modified residue3191Citrulline
Modified residue3611Phosphoserine By similarity
Modified residue3841Phosphoserine By similarity
Modified residue3881N6-acetyllysine Ref.12

Natural variations

Alternative sequence221 – 329109Missing in isoform Gamma.
VSP_010132
Alternative sequence221 – 29272Missing in isoform Delta.
VSP_010131
Alternative sequence221 – 26040Missing in isoform Epsilon.
VSP_010130

Experimental info

Sequence conflict72 – 732EP → DA in AAC52574. Ref.1
Sequence conflict72 – 732EP → DA in AAC52575. Ref.1
Sequence conflict72 – 732EP → DA in AAC52576. Ref.1
Sequence conflict72 – 732EP → DA in AAC52577. Ref.1
Sequence conflict422 – 4243VAV → GAC in AAC52574. Ref.1
Sequence conflict422 – 4243VAV → GAC in AAC52575. Ref.1
Sequence conflict422 – 4243VAV → GAC in AAC52576. Ref.1
Sequence conflict422 – 4243VAV → GAC in AAC52577. Ref.1

Sequences

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

Last modified July 27, 2011. Version 4.
Checksum: 132AF11B458DCFBA

FASTA45250,373
        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 

« Hide

Isoform Alpha [UniParc].

See Q61033.

Isoform Zeta [UniParc].

See Q61033.

Isoform Delta [UniParc].

Checksum: F2BE6B5556030A49
Show »

FASTA38042,650
Isoform Epsilon [UniParc].

Checksum: C54639DAB8788CEE
Show »

FASTA41246,050
Isoform Gamma [UniParc].

Checksum: BA62B6D869B0FDAD
Show »

FASTA34338,502

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]"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. expand/collapse author list , 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, IDENTIFICATION BY 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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; THR-74 AND THR-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"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].
[10]"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.
[11]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.
Nature 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-319.
[12]"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 AND LYS-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+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.
RefSeqNP_001073598.1. NM_001080129.2.
NP_001073600.1. NM_001080131.2.
NP_001073601.1. NM_001080132.2.
UniGeneMm.159684.
Mm.439157.

3D structure databases

ProteinModelPortalQ61029.
SMRQ61029. Positions 1-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204234. 3 interactions.
IntActQ61029. 3 interactions.
MINTMINT-4109431.

Proteomic databases

PRIDEQ61029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072239; ENSMUSP00000072092; ENSMUSG00000019961. [Q61029-1]
ENSMUST00000092219; ENSMUSP00000089864; ENSMUSG00000019961. [Q61029-3]
ENSMUST00000099355; ENSMUSP00000096956; ENSMUSG00000019961. [Q61029-2]
ENSMUST00000105293; ENSMUSP00000100930; ENSMUSG00000019961. [Q61029-4]
GeneID21917.
KEGGmmu:21917.
UCSCuc007gtq.1. mouse. [Q61029-1]
uc007gts.1. mouse. [Q61029-2]
uc007gtt.1. mouse. [Q61029-4]

Organism-specific databases

CTD7112.
MGIMGI:106920. Tmpo.

Phylogenomic databases

GeneTreeENSGT00510000048934.
HOGENOMHOG000113280.
HOVERGENHBG000166.
OMATGNFKHA.

Gene expression databases

ArrayExpressQ61029.
BgeeQ61029.
CleanExMM_TMPO.
GenevestigatorQ61029.

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. mouse.
NextBio301476.
PROQ61029.
SOURCESearch...

Entry information

Entry nameLAP2B_MOUSE
AccessionPrimary (citable) accession number: Q61029
Secondary accession number(s): Q3UCI5 expand/collapse secondary AC list , Q61030, Q61031, Q61032
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 121 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

MGD cross-references

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