P42166 (LAP2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lamina-associated polypeptide 2, isoform alpha

Alternative name(s):
Thymopoietin isoform alpha
Short name=TP alpha
Thymopoietin-related peptide isoform alpha
Short name=TPRP isoform alpha

Cleaved into the following 2 chains:

1. Thymopoietin
   Short name=TP
   Alternative name(s):
   Splenin
2. Thymopentin
   Alternative name(s):
   TP5

Gene names

Name:	TMPO
Synonyms:	LAP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	694 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. TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.
Subunit structure	Interacts with LMNA, BANF1 and RB1 and with chromosomes. Associates directly or indirectly with lamins at specific cell-cycle stages. Ref.7 Ref.8 Ref.9
Subcellular location	Nucleus. Chromosome. Note: Expressed diffusely throughout the nucleus.
Tissue specificity	Expressed in many tissues. Most abundant in adult thymus and fetal liver.
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. The C-terminal domain forms a four-stranded coiled coil By similarity.
Post-translational modification	Phosphorylated in a mitose-specific manner. Ref.7
Involvement in disease	Cardiomyopathy, dilated 1T (CMD1T) [MIM:613740]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25
Pharmaceutical use	TP5 is available under the names Timunox (Cilag), Sintomodulina (Italofarmaco) and Mepentil (Recordati). Used in primary and secondary immune deficiencies, autoimmunity, infections and cancer.
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 Polymorphism
Disease	Cardiomyopathy Disease mutation
Domain	Coiled coil
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara
Cellular_component	chromatin Inferred from direct assay PubMed 17284516. Source: MGI nuclear envelope Traceable author statement Ref.2. Source: ProtInc nuclear inner membrane Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW lamin binding Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform Alpha (identifier: P42166-1)

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 Beta (identifier: P42167-1)

The sequence of this isoform can be found in the external entry P42167.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform Gamma (identifier: P42167-2)

The sequence of this isoform can be found in the external entry P42167.
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 Ref.4

Chain

2 – 694

693

Lamina-associated polypeptide 2, isoform alpha

PRO_0000017674

Peptide

2 – 50

49

Thymopoietin

PRO_0000017675

Peptide

33 – 37

5

Thymopentin

PRO_0000017676

Regions

Domain

5 – 48

44

LEM-like

Domain

109 – 153

45

LEM

Region

49 – 108

60

Linker

Coiled coil

558 – 657

100

By similarity

Motif

190 – 196

7

Nuclear localization signal Potential

Amino acid modifications

Modified residue

57

1

Phosphothreonine Ref.16

Modified residue

59

1

Phosphoserine Ref.22

Modified residue

66

1

Phosphoserine Ref.16 Ref.18

Modified residue

67

1

Phosphoserine Ref.16 Ref.18

Modified residue

74

1

Phosphothreonine Ref.13 Ref.15 Ref.16 Ref.18 Ref.20 Ref.22

Modified residue

79

1

Phosphoserine Ref.16 Ref.18

Modified residue

154

1

Phosphothreonine Ref.18

Modified residue

156

1

Phosphoserine Ref.20

Modified residue

160

1

Phosphothreonine Ref.16 Ref.18 Ref.20

Modified residue

164

1

Phosphothreonine Ref.16

Modified residue

184

1

Phosphoserine Ref.22

Modified residue

351

1

Phosphoserine Ref.10 Ref.12 Ref.15 Ref.16 Ref.18 Ref.20 Ref.22

Modified residue

354

1

Phosphoserine Ref.20 Ref.22

Modified residue

370

1

Phosphoserine Ref.16 Ref.20

Modified residue

424

1

Phosphoserine Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.20

Modified residue

656

1

N6-acetyllysine Ref.19

Natural variations

Natural variant

238

1

L → R.
Corresponds to variant rs35998138 [ dbSNP | Ensembl ].

VAR_049773

Natural variant

293

1

S → A.
Corresponds to variant rs35645287 [ dbSNP | Ensembl ].

VAR_049774

Natural variant

317

1

T → S.
Corresponds to variant rs35969221 [ dbSNP | Ensembl ].

VAR_049775

Natural variant

416

1

K → E.
Corresponds to variant rs11838270 [ dbSNP | Ensembl ].

VAR_049776

Natural variant

478

1

K → N.
Corresponds to variant rs35761089 [ dbSNP | Ensembl ].

VAR_049777

Natural variant

599

1

Q → E. Ref.2
Corresponds to variant rs17459334 [ dbSNP | Ensembl ].

VAR_005635

Natural variant

690

1

R → C in CMD1T; affects the interaction with LMNA. Ref.25
Corresponds to variant rs17028450 [ dbSNP | Ensembl ].

VAR_049778

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

694

Helix Strand Turn

Details...

Beta strand

8 – 11

4

Helix

13 – 22

10

Beta strand

29 – 31

3

Helix

34 – 39

6

Turn

40 – 42

3

Beta strand

43 – 45

3

Turn

46 – 48

3

Beta strand

113 – 115

3

Helix

117 – 122

6

Beta strand

123 – 125

3

Turn

126 – 128

3

Beta strand

136 – 138

3

Helix

139 – 145

7

Helix

147 – 152

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 1B514B0FB61D0D75	FASTA	694	75,492
	10 20 30 40 50 60 MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK 70 80 90 100 110 120 GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL 130 140 150 160 170 180 LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS 190 200 210 220 230 240 DRYSDNEEGK KKEHKKVKST RDIVPFSELG TTPSGGGFFQ GISFPEISTR PPLGSTELQA 250 260 270 280 290 300 AKKVHTSKGD LPREPLVATN LPGRGQLQKL ASERNLFISC KSSHDRCLEK SSSSSSQPEH 310 320 330 340 350 360 SAMLVSTAAS PSLIKETTTG YYKDIVENIC GREKSGIQPL CPERSHISDQ SPLSSKRKAL 370 380 390 400 410 420 EESESSQLIS PPLAQAIRDY VNSLLVQGGV GSLPGTSNSM PPLDVENIQK RIDQSKFQET 430 440 450 460 470 480 EFLSPPRKVP RLSEKSVEER DSGSFVAFQN IPGSELMSSF AKTVVSHSLT TLGLEVAKQS 490 500 510 520 530 540 QHDKIDASEL SFPFHESILK VIEEEWQQVD RQLPSLACKY PVSSREATQI LSVPKVDDEI 550 560 570 580 590 600 LGFISEATPL GGIQAASTES CNQQLDLALC RAYEAAASAL QIATHTAFVA KAMQADISQA 610 620 630 640 650 660 AQILSSDPSR THQALGILSK TYDAASYICE AAFDEVKMAA HTMGNATVGR RYLWLKDCKI 670 680 690 NLASKNKLAS TPFKGGTLFG GEVCKVIKKR GNKH
	Isoform Beta [UniParc]. See P42167.		–	–
	Isoform Gamma [UniParc]. See P42167.		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three distinct human thymopoietins are derived from alternatively spliced mRNAs." Harris C.A., Andryuk P.J., Cline S.W., Chan H.K., Natarajan A., Siekierka J.J., Goldstein G. Proc. Natl. Acad. Sci. U.S.A. 91:6283-6287(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA). Tissue: Thymus.
[2]	"Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2." Harris C.A., Andryuk P.J., Cline S.W., Siekierka J.J., Goldstein G. Genomics 28:198-205(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA; BETA AND GAMMA), VARIANT GLU-599.
[3]	"A new thymopoietin precursor gene from human thymus." Hara H., Hayashi K., Ohta K., Itoh N., Ohta M. Biochem. Mol. Biol. Int. 34:927-933(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-526. Tissue: Thymus.
[4]	Bienvenut W.V., Vousden K.H., Lukashchuk N. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 127-139; 254-264; 417-427 AND 526-535, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[5]	"Isolation and complete amino acid sequence of human thymopoietin and splenin." Audhya T., Schlesinger D.H., Goldstein G. Proc. Natl. Acad. Sci. U.S.A. 84:3545-3549(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[6]	Erratum Goldstein G., Schlesinger D.H., Audhya T. Proc. Natl. Acad. Sci. U.S.A. 91:6249-6249(1994) [PubMed] [Europe PMC] [Abstract] Cited for: RETRACTION.
[7]	"Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics." Dechat T., Gotzmann J., Stockinger A., Harris C.A., Talle M.A., Siekierka J.J., Foisner R. EMBO J. 17:4887-4902(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHROMOSOMES, PHOSPHORYLATION.
[8]	"Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins." Dechat T., Korbei B., Vaughan O.A., Vlcek S., Hutchison C.J., Foisner R. J. Cell Sci. 113:3473-3484(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LMNA.
[9]	"Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein." Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J. Mol. Biol. Cell 13:4401-4413(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LMNA AND RB1.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Prostate cancer.
[12]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[15]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-351 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-66; SER-67; THR-74; SER-79; THR-160; THR-164; SER-351; SER-370 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; SER-79; THR-154; THR-160; SER-351 AND SER-424, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656, MASS SPECTROMETRY.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-156; THR-160; SER-351; SER-354; SER-370 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; THR-74; SER-184; SER-351 AND SER-354, MASS SPECTROMETRY.
[23]	"Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA." Cai M., Huang Y., Ghirlando R., Wilson K.L., Craigie R., Clore G.M. EMBO J. 20:4399-4407(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-169.
[24]	"Structural characterization of the LEM motif common to three human inner nuclear membrane proteins." Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K., Callebaut I., Worman H.J., Zinn-Justin S. Structure 9:503-511(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-57 AND 103-159.
[25]	"Thymopoietin (lamina-associated polypeptide 2) gene mutation associated with dilated cardiomyopathy." Taylor M.R., Slavov D., Gajewski A., Vlcek S., Ku L., Fain P.R., Carniel E., Di Lenarda A., Sinagra G., Boucek M.M., Cavanaugh J., Graw S.L., Ruegg P., Feiger J., Zhu X., Ferguson D.A., Bristow M.R., Gotzmann J., Foisner R., Mestroni L. Hum. Mutat. 26:566-574(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMD1T CYS-690, CHARACTERIZATION OF VARIANT CMD1T CYS-690.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U09086 mRNA. Translation: AAB60329.1.
U18270 , U18266, U18267, U18268 Genomic DNA. Translation: AAB60433.1.
S76736 mRNA. Translation: AAB33958.1.

IPI

IPI00216230.

PIR

G01161.

RefSeq

NP_003267.1. NM_003276.2.

UniGene

Hs.11355.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GJJ	NMR	-	A	1-168	[»]
1H9E	NMR	-	A	2-57	[»]
1H9F	NMR	-	A	103-159	[»]

ProteinModelPortal

P42166.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42166. 14 interactions.

MINT

MINT-2863664.

STRING

9606.ENSP00000266732.

Polymorphism databases

DMDM

1174689.

Proteomic databases

PaxDb

P42166.

PeptideAtlas

P42166.

PRIDE

P42166.

Protocols and materials databases

DNASU

7112.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266732; ENSP00000266732; ENSG00000120802.

GeneID

7112.

KEGG

hsa:7112.

UCSC

uc001tfh.2. human.

Organism-specific databases

CTD

7112.

GeneCards

GC12P098909.

HGNC

HGNC:11875. TMPO.

HPA

CAB009847.

MIM

188380. gene.
613740. phenotype.

neXtProt

NX_P42166.

Orphanet

154. Familial isolated dilated cardiomyopathy.

PharmGKB

PA36576.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG87051.

HOGENOM

HOG000060228.

HOVERGEN

HBG081890.

InParanoid

P42166.

OrthoDB

EOG428214.

PhylomeDB

P42166.

Gene expression databases

ArrayExpress

P42166.

Bgee

P42166.

CleanEx

HS_TMPO.

Genevestigator

P42166.

GermOnline

ENSG00000120802. Homo sapiens.

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. human.

EvolutionaryTrace

P42166.

GenomeRNAi

7112.

NextBio

27839.

PMAP-CutDB

P42166.

SOURCE

Search...

Entry information

Entry name

LAP2A_HUMAN

Accession

Primary (citable) accession number: P42166
Secondary accession number(s): P08918 , P08919, Q14860, Q16295

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.