UniProt Accession

 LAP2B_HUMAN; P42167; Q14861 

Genbank Protein ID

 U09087; U09088; BC053675; AF070631; U18269; U18266; U18267; U18268; U18270; U18271 

Genbank Nucleotide ID

 AAB60330.1; AAB60331.1; AAH53675.1; AAC25390.1; AAB60434.1; AAB60434.1; AAB60434.1; AAB60434.1; AAB60434.1; AAB60435.1 

Protein Name

 Lamina-associated polypeptide 2, isoforms beta/gamma 

Protein Synonyms/Alias

 Thymopoietin, isoforms beta/gamma; TP beta/gamma; Thymopoietin-related peptide isoforms beta/gamma; TPRP isoforms beta/gamma; Thymopoietin; TP; Splenin; Thymopentin; TP5 

Gene Name

 TMPO 

Gene Synonyms/Alias

 LAP2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
60	LPAGTNSKGPPDFSS	ubiquitination	[1]
107	DKPRQEDKDDLDVTE	ubiquitination	[1]
126	DLLDQLVKYGVNPGP	ubiquitination	[1]
207	EPLKGRAKTPVTLKQ	acetylation	[2]
213	AKTPVTLKQRRVEHN	ubiquitination	[3]
303	NRVTGNFKHASPILP	ubiquitination	[1, 3, 4, 5, 6, 7]
334	TRAEVGEKTEERRVE	ubiquitination	[1, 3]
346	RVERDILKEMFPYEA	ubiquitination	[1, 3, 4, 5, 6, 7, 8]
368	ASCRRPIKGAAGRPL	ubiquitination	[1, 3]
389	MEESFSSKYVPKYVP	ubiquitination	[1, 3, 4, 5, 6, 7, 8, 9]
393	FSSKYVPKYVPLADV	ubiquitination	[1, 3, 4, 5, 6, 7]
401	YVPLADVKSEKTKKG	ubiquitination	[1, 3, 4, 6, 7, 8]
404	LADVKSEKTKKGRSI	ubiquitination	[6]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 5 48 LEM-like.
 DOMAIN 109 153 LEM.
 REGION 1 410 Nucleoplasmic (Potential).
 REGION 49 108 Linker.
 REGION 138 243 NAKAP95-binding N.
 REGION 299 371 Binds lamins B.
 REGION 300 374 NAKAP95-binding C.
 MOD_RES 57 57 Phosphothreonine.
 MOD_RES 59 59 Phosphoserine.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 74 74 Phosphothreonine.
 MOD_RES 79 79 Phosphoserine.
 MOD_RES 154 154 Phosphothreonine.
 MOD_RES 156 156 Phosphoserine.
 MOD_RES 160 160 Phosphothreonine.
 MOD_RES 164 164 Phosphothreonine.
 MOD_RES 177 177 Phosphoserine.
 MOD_RES 180 180 Phosphoserine.
 MOD_RES 184 184 Phosphoserine.
 MOD_RES 208 208 Phosphothreonine (By similarity).
 MOD_RES 211 211 Phosphothreonine.
 MOD_RES 265 265 Phosphoserine.
 MOD_RES 292 292 Phosphoserine.
 MOD_RES 306 306 Phosphoserine.
 MOD_RES 312 312 Phosphothreonine.
 MOD_RES 315 315 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.
 MOD_RES 385 385 Phosphoserine.  

Keyword

 Alternative splicing; Complete proteome; DNA-binding; Membrane; Nucleus; Pharmaceutical; Phosphoprotein; Polymorphism; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 454 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005635; C:nuclear envelope; TAS:ProtInc.
 GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0005521; F:lamin binding; TAS:ProtInc. 

Interpro

 IPR013146; LEM-like_dom.
 IPR011015; LEM/LEM-like_dom.
 IPR003887; LEM_dom. 

Pfam

 PF03020; LEM
 PF08198; Thymopoietin 

SMART

 SM00540; LEM 

PROSITE

 PS50954; LEM
 PS50955; LEM_LIKE 

PRINTS