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P42166 (LAP2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.26

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 694693Lamina-associated polypeptide 2, isoform alpha
PRO_0000017674
Peptide2 – 5049Thymopoietin
PRO_0000017675
Peptide33 – 375Thymopentin
PRO_0000017676

Regions

Domain5 – 4844LEM-like
Domain109 – 15345LEM
Region49 – 10860Linker
Coiled coil558 – 657100 By similarity
Motif190 – 1967Nuclear localization signal Potential

Amino acid modifications

Modified residue571Phosphothreonine Ref.16
Modified residue591Phosphoserine Ref.23
Modified residue661Phosphoserine Ref.16 Ref.19
Modified residue671Phosphoserine Ref.16 Ref.19
Modified residue741Phosphothreonine Ref.13 Ref.15 Ref.16 Ref.19 Ref.21 Ref.23
Modified residue791Phosphoserine Ref.16 Ref.19
Modified residue1541Phosphothreonine Ref.19
Modified residue1561Phosphoserine Ref.21
Modified residue1601Phosphothreonine Ref.16 Ref.19 Ref.21
Modified residue1641Phosphothreonine Ref.16
Modified residue1841Phosphoserine Ref.23
Modified residue3511Phosphoserine Ref.10 Ref.12 Ref.15 Ref.16 Ref.19 Ref.21 Ref.23
Modified residue3541Phosphoserine Ref.21 Ref.23
Modified residue3701Phosphoserine Ref.16 Ref.21
Modified residue4241Phosphoserine Ref.12 Ref.13 Ref.15 Ref.16 Ref.19 Ref.21
Modified residue6561N6-acetyllysine Ref.20

Natural variations

Natural variant2381L → R.
Corresponds to variant rs35998138 [ dbSNP | Ensembl ].
VAR_049773
Natural variant2931S → A.
Corresponds to variant rs35645287 [ dbSNP | Ensembl ].
VAR_049774
Natural variant3171T → S.
Corresponds to variant rs35969221 [ dbSNP | Ensembl ].
VAR_049775
Natural variant4161K → E.
Corresponds to variant rs11838270 [ dbSNP | Ensembl ].
VAR_049776
Natural variant4781K → N.
Corresponds to variant rs35761089 [ dbSNP | Ensembl ].
VAR_049777
Natural variant5991Q → E. Ref.2
Corresponds to variant rs17459334 [ dbSNP | Ensembl ].
VAR_005635
Natural variant6901R → C in CMD1T; affects the interaction with LMNA. Ref.26
Corresponds to variant rs17028450 [ dbSNP | Ensembl ].
VAR_049778

Secondary structure

....................... 694
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: 1B514B0FB61D0D75

FASTA69475,492
        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 

« Hide

Isoform Beta [UniParc].

See P42167.

Isoform Gamma [UniParc].

See P42167.

References

« Hide '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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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.
[25]"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.
[26]"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 expand/collapse EMBL AC list , U18266, U18267, U18268 Genomic DNA. Translation: AAB60433.1.
S76736 mRNA. Translation: AAB33958.1.
PIRG01161.
RefSeqNP_003267.1. NM_003276.2.
UniGeneHs.11355.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GJJNMR-A1-168[»]
1H9ENMR-A2-57[»]
1H9FNMR-A103-159[»]
ProteinModelPortalP42166.
SMRP42166. Positions 1-159, 467-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112967. 43 interactions.
IntActP42166. 18 interactions.
MINTMINT-2863664.
STRING9606.ENSP00000266732.

Polymorphism databases

DMDM1174689.

Proteomic databases

PaxDbP42166.
PeptideAtlasP42166.
PRIDEP42166.

Protocols and materials databases

DNASU7112.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266732; ENSP00000266732; ENSG00000120802. [P42166-1]
GeneID7112.
KEGGhsa:7112.
UCSCuc001tfh.2. human. [P42166-1]

Organism-specific databases

CTD7112.
GeneCardsGC12P098909.
HGNCHGNC:11875. TMPO.
HPACAB009847.
MIM188380. gene.
613740. phenotype.
neXtProtNX_P42166.
Orphanet154. Familial isolated dilated cardiomyopathy.
PharmGKBPA36576.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87051.
HOGENOMHOG000060228.
HOVERGENHBG081890.
InParanoidP42166.
OrthoDBEOG7KWSGZ.
PhylomeDBP42166.
TreeFamTF328426.

Gene expression databases

ArrayExpressP42166.
BgeeP42166.
CleanExHS_TMPO.
GenevestigatorP42166.

Family and domain databases

Gene3D1.10.720.40. 2 hits.
InterProIPR021623. LAP2alpha.
IPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamPF11560. LAP2alpha. 1 hit.
PF03020. 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. human.
EvolutionaryTraceP42166.
GeneWikiThymopoietin.
GenomeRNAi7112.
NextBio27839.
PMAP-CutDBP42166.
PROP42166.
SOURCESearch...

Entry information

Entry nameLAP2A_HUMAN
AccessionPrimary (citable) accession number: P42166
Secondary accession number(s): P08918 expand/collapse secondary AC list , P08919, Q14860, Q16295
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM