Details for: TMPO

Gene ID: 7112

Symbol: TMPO

Ensembl ID: ENSG00000120802

Description: thymopoietin

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: ovarian surface epithelial cell (CL2000064)
    Fold Change: 2.15
    Marker Score: 5840.5
  • Cell Name: type I NK T cell (CL0000921)
    Fold Change: 2.08
    Marker Score: 1630
  • Cell Name: Unknown (CL0002371)
    Fold Change: 2
    Marker Score: 2130
  • Cell Name: large pre-B-II cell (CL0000957)
    Fold Change: 2
    Marker Score: 5446
  • Cell Name: migratory enteric neural crest cell (CL0002607)
    Fold Change: 1.94
    Marker Score: 1821
  • Cell Name: DN3 thymocyte (CL0000807)
    Fold Change: 1.8
    Marker Score: 900
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 1.78
    Marker Score: 5294
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 1.77
    Marker Score: 17782
  • Cell Name: Leydig cell (CL0000178)
    Fold Change: 1.73
    Marker Score: 1860
  • Cell Name: neural crest cell (CL0011012)
    Fold Change: 1.7
    Marker Score: 1820
  • Cell Name: fraction A pre-pro B cell (CL0002045)
    Fold Change: 1.67
    Marker Score: 1681
  • Cell Name: Unknown (CL0000548)
    Fold Change: 1.65
    Marker Score: 1205
  • Cell Name: erythroblast (CL0000765)
    Fold Change: 1.63
    Marker Score: 1018
  • Cell Name: oogonial cell (CL0000024)
    Fold Change: 1.53
    Marker Score: 2206
  • Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
    Fold Change: 1.52
    Marker Score: 2156
  • Cell Name: epithelial cell of nephron (CL1000449)
    Fold Change: 1.52
    Marker Score: 3172
  • Cell Name: IgG plasmablast (CL0000982)
    Fold Change: 1.51
    Marker Score: 417
  • Cell Name: myeloid leukocyte (CL0000766)
    Fold Change: 1.5
    Marker Score: 1809
  • Cell Name: cortical thymic epithelial cell (CL0002364)
    Fold Change: 1.49
    Marker Score: 5507
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: 1.48
    Marker Score: 2518
  • Cell Name: memory regulatory T cell (CL0002678)
    Fold Change: 1.46
    Marker Score: 508
  • Cell Name: cerebral cortex endothelial cell (CL1001602)
    Fold Change: 1.44
    Marker Score: 857
  • Cell Name: primordial germ cell (CL0000670)
    Fold Change: 1.42
    Marker Score: 1785
  • Cell Name: CD8-positive, alpha-beta cytokine secreting effector T cell (CL0000908)
    Fold Change: 1.42
    Marker Score: 613
  • Cell Name: naive regulatory T cell (CL0002677)
    Fold Change: 1.41
    Marker Score: 428
  • Cell Name: DN1 thymic pro-T cell (CL0000894)
    Fold Change: 1.4
    Marker Score: 435
  • Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
    Fold Change: 1.4
    Marker Score: 878
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: 1.38
    Marker Score: 1458
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 1.35
    Marker Score: 8800
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: 1.35
    Marker Score: 8627
  • Cell Name: CD38-negative naive B cell (CL0002102)
    Fold Change: 1.33
    Marker Score: 2793
  • Cell Name: small pre-B-II cell (CL0000954)
    Fold Change: 1.32
    Marker Score: 1580.5
  • Cell Name: plasmablast (CL0000980)
    Fold Change: 1.31
    Marker Score: 1741.5
  • Cell Name: non-classical monocyte (CL0000875)
    Fold Change: 1.29
    Marker Score: 3122
  • Cell Name: CD14-positive monocyte (CL0001054)
    Fold Change: 1.29
    Marker Score: 3220
  • Cell Name: promyelocyte (CL0000836)
    Fold Change: 1.26
    Marker Score: 624
  • Cell Name: B-1 B cell (CL0000819)
    Fold Change: 1.25
    Marker Score: 2186
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 1.25
    Marker Score: 12694.5
  • Cell Name: common lymphoid progenitor (CL0000051)
    Fold Change: 1.25
    Marker Score: 849
  • Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
    Fold Change: 1.24
    Marker Score: 2424.5
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: 1.24
    Marker Score: 69352
  • Cell Name: mesodermal cell (CL0000222)
    Fold Change: 1.22
    Marker Score: 16114.5
  • Cell Name: mesangial cell (CL0000650)
    Fold Change: 1.21
    Marker Score: 1465.5
  • Cell Name: blood cell (CL0000081)
    Fold Change: 1.21
    Marker Score: 14032.5
  • Cell Name: primitive red blood cell (CL0002355)
    Fold Change: 1.2
    Marker Score: 903
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 1.19
    Marker Score: 1287
  • Cell Name: IgG-negative class switched memory B cell (CL0002117)
    Fold Change: 1.19
    Marker Score: 1168
  • Cell Name: mucous neck cell (CL0000651)
    Fold Change: 1.18
    Marker Score: 2682
  • Cell Name: stem cell (CL0000034)
    Fold Change: 1.16
    Marker Score: 2761
  • Cell Name: memory B cell (CL0000787)
    Fold Change: 1.16
    Marker Score: 878
  • Cell Name: taste receptor cell (CL0000209)
    Fold Change: 1.15
    Marker Score: 997
  • Cell Name: stromal cell (CL0000499)
    Fold Change: 1.15
    Marker Score: 1348
  • Cell Name: pro-T cell (CL0000827)
    Fold Change: 1.15
    Marker Score: 4688.5
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 1.13
    Marker Score: 39208
  • Cell Name: mesenchymal stem cell (CL0000134)
    Fold Change: 1.13
    Marker Score: 1740
  • Cell Name: granulocyte (CL0000094)
    Fold Change: 1.13
    Marker Score: 506
  • Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
    Fold Change: 1.12
    Marker Score: 3147
  • Cell Name: chromaffin cell (CL0000166)
    Fold Change: 1.1
    Marker Score: 1554
  • Cell Name: male germ cell (CL0000015)
    Fold Change: 1.1
    Marker Score: 318
  • Cell Name: mature B cell (CL0000785)
    Fold Change: 1.1
    Marker Score: 804.5
  • Cell Name: respiratory epithelial cell (CL0002368)
    Fold Change: 1.1
    Marker Score: 604
  • Cell Name: hematopoietic precursor cell (CL0008001)
    Fold Change: 1.09
    Marker Score: 383
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 1.09
    Marker Score: 260
  • Cell Name: hepatocyte (CL0000182)
    Fold Change: 1.09
    Marker Score: 741
  • Cell Name: exhausted T cell (CL0011025)
    Fold Change: 1.08
    Marker Score: 623
  • Cell Name: hematopoietic cell (CL0000988)
    Fold Change: 1.08
    Marker Score: 718
  • Cell Name: mature T cell (CL0002419)
    Fold Change: 1.08
    Marker Score: 10658
  • Cell Name: epithelial cell of lower respiratory tract (CL0002632)
    Fold Change: 1.07
    Marker Score: 4481
  • Cell Name: innate lymphoid cell (CL0001065)
    Fold Change: 1.07
    Marker Score: 384
  • Cell Name: glial cell (CL0000125)
    Fold Change: 1.07
    Marker Score: 1172
  • Cell Name: Sertoli cell (CL0000216)
    Fold Change: 1.07
    Marker Score: 6318
  • Cell Name: cerebellar granule cell precursor (CL0002362)
    Fold Change: 1.06
    Marker Score: 595.5
  • Cell Name: enteric smooth muscle cell (CL0002504)
    Fold Change: 1.06
    Marker Score: 2496
  • Cell Name: respiratory goblet cell (CL0002370)
    Fold Change: 1.06
    Marker Score: 306
  • Cell Name: kidney cell (CL1000497)
    Fold Change: 1.06
    Marker Score: 707
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 1.05
    Marker Score: 9249.5
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: 1.05
    Marker Score: 9998
  • Cell Name: early lymphoid progenitor (CL0000936)
    Fold Change: 1.05
    Marker Score: 515
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 1.05
    Marker Score: 313
  • Cell Name: leukocyte (CL0000738)
    Fold Change: 1.05
    Marker Score: 601
  • Cell Name: type EC enteroendocrine cell (CL0000577)
    Fold Change: 1.04
    Marker Score: 981.5
  • Cell Name: CD4-positive helper T cell (CL0000492)
    Fold Change: 1.04
    Marker Score: 1133
  • Cell Name: naive thymus-derived CD8-positive, alpha-beta T cell (CL0000900)
    Fold Change: 1.03
    Marker Score: 1845
  • Cell Name: basal cell (CL0000646)
    Fold Change: 1.03
    Marker Score: 1328
  • Cell Name: glandular epithelial cell (CL0000150)
    Fold Change: 1.03
    Marker Score: 2524
  • Cell Name: choroid plexus epithelial cell (CL0000706)
    Fold Change: 1.03
    Marker Score: 943
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 1.02
    Marker Score: 2162
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: 1.02
    Marker Score: 1063
  • Cell Name: mature alpha-beta T cell (CL0000791)
    Fold Change: 1.02
    Marker Score: 53767
  • Cell Name: ependymal cell (CL0000065)
    Fold Change: 1.02
    Marker Score: 354
  • Cell Name: enteric neuron (CL0007011)
    Fold Change: 1.01
    Marker Score: 538.5
  • Cell Name: extravillous trophoblast (CL0008036)
    Fold Change: 1.01
    Marker Score: 901
  • Cell Name: vein endothelial cell (CL0002543)
    Fold Change: 1.01
    Marker Score: 911
  • Cell Name: Bergmann glial cell (CL0000644)
    Fold Change: 1.01
    Marker Score: 411
  • Cell Name: effector memory CD4-positive, alpha-beta T cell (CL0000905)
    Fold Change: 1.01
    Marker Score: 737
  • Cell Name: malignant cell (CL0001064)
    Fold Change: 1.01
    Marker Score: 13505
  • Cell Name: fibroblast of connective tissue of prostate (CL1000299)
    Fold Change: 1
    Marker Score: 250
  • Cell Name: prostate stromal cell (CL0002622)
    Fold Change: 1
    Marker Score: 250
  • Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
    Fold Change: 1
    Marker Score: 71579
  • Cell Name: forebrain radial glial cell (CL0013000)
    Fold Change: 0.99
    Marker Score: 47800

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Other Information

**Key Characteristics** 1. **Cell-type specific expression**: TMPO is expressed in a range of cell types, including thymocytes, NK T cells, granulosa cells, and neural crest cells, highlighting its potential role in diverse cellular processes. 2. **Regulation of cell cycle**: TMPO is involved in the regulation of the cell cycle, particularly in the transition from mitosis to the G1 phase, suggesting its role in controlling cellular proliferation. 3. **Nuclear envelope dynamics**: TMPO is implicated in the regulation of nuclear envelope dynamics, including its assembly and disassembly, which is essential for cell cycle progression and cellular differentiation. 4. **Signaling pathways**: TMPO is involved in various signaling pathways, including those mediated by Rho GTPases, which are critical for cell migration, proliferation, and differentiation. **Pathways and Functions** TMPO's involvement in various cellular processes can be attributed to its participation in the following pathways and functions: 1. **Cadherin binding**: TMPO interacts with cadherins, which are essential adhesion molecules that regulate cell-cell interactions and tissue organization. 2. **Cdc42 GTPase cycle**: TMPO regulates the activity of Cdc42, a key GTPase involved in cell cycle progression, cell migration, and cytoskeletal organization. 3. **Cell cycle regulation**: TMPO modulates the cell cycle by regulating the transition from mitosis to the G1 phase, ensuring proper cellular proliferation and differentiation. 4. **Nuclear envelope reassembly**: TMPO is involved in the reassembly of the nuclear envelope after mitosis, which is essential for maintaining nuclear integrity and regulating gene expression. 5. **Rho GTPase signaling**: TMPO regulates the activity of Rho GTPases, which are critical for cell migration, proliferation, and differentiation. **Clinical Significance** TMPO's involvement in immune cell development and function has significant implications for the understanding and treatment of various diseases, including: 1. **Immunodeficiency disorders**: TMPO's role in thymocyte development and function makes it a potential target for the treatment of immunodeficiency disorders, such as thymic dysplasia and severe combined immunodeficiency. 2. **Cancer**: TMPO's involvement in cell cycle regulation and nuclear envelope dynamics positions it as a potential regulator of cancer cell proliferation and differentiation. 3. **Reproductive disorders**: TMPO's expression in granulosa cells and Leydig cells makes it a potential target for the treatment of reproductive disorders, such as infertility and testicular dysfunction. In conclusion, TMPO is a multifunctional gene that plays a critical role in regulating cellular processes, including cell cycle progression, nuclear envelope dynamics, and signaling pathways. Its involvement in immune cell development and function has significant implications for the understanding and treatment of various diseases, making it an attractive target for further research and therapeutic intervention.

Genular Protein ID: 1189690402

Symbol: LAP2A_HUMAN

Name: Lamina-associated polypeptide 2, isoform alpha

UniProtKB Accession Codes:

P42166 P08918 P08919 Q14860 Q16295

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CDD 2 CPTAC 1 CTD 1 ChiTaRS 1 DMDM 1 DNASU 1 DisGeNET 1 EMBL 6 EPD 1 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 6 Gene3D 2 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 4 MIM 1 MINT 1 MalaCards 1 MassIVE 1 MetOSite 1 NCBI Taxonomy 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 17 PDBsum 14 PIR 1 PROSITE 2 PROSITE-ProRule 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 3 PharmGKB 1 Pharos 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 Pumba 1 RNAct 1 RefSeq 1 SAM 1 SMART 2 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TreeFam 1 UCSC 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 7517549

Title: Three distinct human thymopoietins are derived from alternatively spliced mRNAs.

PubMed ID: 7517549

DOI: 10.1073/pnas.91.14.6283

PubMed ID: 8530026

Title: Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2.

PubMed ID: 8530026

DOI: 10.1006/geno.1995.1131

PubMed ID: 7703909

Title: A new thymopoietin precursor gene from human thymus.

PubMed ID: 7703909

PubMed ID: 3473468

Title: Isolation and complete amino acid sequence of human thymopoietin and splenin.

PubMed ID: 3473468

DOI: 10.1073/pnas.84.11.3545

PubMed ID: 8016147

Title:

PubMed ID: 8016147

DOI: 10.1073/pnas.91.13.6249

PubMed ID: 9707448

Title: Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics.

PubMed ID: 9707448

DOI: 10.1093/emboj/17.16.4887

PubMed ID: 10984438

Title: Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins.

PubMed ID: 10984438

DOI: 10.1242/jcs.113.19.3473

PubMed ID: 12475961

Title: Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein.

PubMed ID: 12475961

DOI: 10.1091/mbc.e02-07-0450

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17487921

Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

PubMed ID: 17487921

DOI: 10.1002/elps.200600782

PubMed ID: 17924679

Title: 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.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28813417

Title: CMTM6 maintains the expression of PD-L1 and regulates anti-tumour immunity.

PubMed ID: 28813417

DOI: 10.1038/nature23643

PubMed ID: 11500367

Title: Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA.

PubMed ID: 11500367

DOI: 10.1093/emboj/20.16.4399

PubMed ID: 11435115

Title: Structural characterization of the LEM motif common to three human inner nuclear membrane proteins.

PubMed ID: 11435115

DOI: 10.1016/s0969-2126(01)00611-6

PubMed ID: 16247757

Title: Thymopoietin (lamina-associated polypeptide 2) gene mutation associated with dilated cardiomyopathy.

PubMed ID: 16247757

DOI: 10.1002/humu.20250

PubMed ID: 27896284

Title: Analyses of more than 60,000 exomes questions the role of numerous genes previously associated with dilated cardiomyopathy.

PubMed ID: 27896284

DOI: 10.1002/mgg3.245

Sequence Information:

  • Length: 694
  • Mass: 75492
  • Checksum: 1B514B0FB61D0D75
  • Sequence:
    • MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK 
GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL 
LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS 
DRYSDNEEGK KKEHKKVKST RDIVPFSELG TTPSGGGFFQ GISFPEISTR PPLGSTELQA 
AKKVHTSKGD LPREPLVATN LPGRGQLQKL ASERNLFISC KSSHDRCLEK SSSSSSQPEH 
SAMLVSTAAS PSLIKETTTG YYKDIVENIC GREKSGIQPL CPERSHISDQ SPLSSKRKAL 
EESESSQLIS PPLAQAIRDY VNSLLVQGGV GSLPGTSNSM PPLDVENIQK RIDQSKFQET 
EFLSPPRKVP RLSEKSVEER DSGSFVAFQN IPGSELMSSF AKTVVSHSLT TLGLEVAKQS 
QHDKIDASEL SFPFHESILK VIEEEWQQVD RQLPSLACKY PVSSREATQI LSVPKVDDEI 
LGFISEATPL GGIQAASTES CNQQLDLALC RAYEAAASAL QIATHTAFVA KAMQADISQA 
AQILSSDPSR THQALGILSK TYDAASYICE AAFDEVKMAA HTMGNATVGR RYLWLKDCKI 
NLASKNKLAS TPFKGGTLFG GEVCKVIKKR GNKH

Genular Protein ID: 1814914812

Symbol: LAP2B_HUMAN

Name: Lamina-associated polypeptide 2, isoforms beta/gamma

UniProtKB Accession Codes:

P42167 A2T926 Q14861

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 2 CORUM 1 CTD 1 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 EMBL 11 EPD 1 Ensembl 3 ExpressionAtlas 1 GO 8 Gene3D 1 GeneCards 1 GeneReviews 1 GeneTree 1 Genevisible 1 GenomeRNAi 1 HGNC 1 HOGENOM 1 HPA 1 IntAct 1 InterPro 3 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MalaCards 1 MassIVE 1 MaxQB 1 MetOSite 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PIR 2 PROSITE 2 PROSITE-ProRule 2 PathwayCommons 1 PeptideAtlas 1 Pfam 2 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 Proteomes 1 ProteomicsDB 2 Pumba 1 Reactome 13 RefSeq 3 SAM 1 SMART 2 SMR 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TopDownProteomics 2 UCSC 1 UniProtKB 1 VEuPathDB 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 7517549

Title: Three distinct human thymopoietins are derived from alternatively spliced mRNAs.

PubMed ID: 7517549

DOI: 10.1073/pnas.91.14.6283

PubMed ID: 18403046

Title: LAP2zeta binds BAF and suppresses LAP2beta-mediated transcriptional repression.

PubMed ID: 18403046

DOI: 10.1016/j.ejcb.2008.01.014

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8530026

Title: Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2.

PubMed ID: 8530026

DOI: 10.1006/geno.1995.1131

PubMed ID: 9490046

Title: Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin.

PubMed ID: 9490046

DOI: 10.1046/j.1432-1327.1998.2510729.x

PubMed ID: 12538639

Title: HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication.

PubMed ID: 12538639

DOI: 10.1083/jcb.200210026

PubMed ID: 10806084

Title: Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics.

PubMed ID: 10806084

DOI: 10.1006/jsbi.2000.4212

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17487921

Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

PubMed ID: 17487921

DOI: 10.1002/elps.200600782

PubMed ID: 17924679

Title: 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.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17693683

Title: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.

PubMed ID: 17693683

DOI: 10.1074/mcp.m700120-mcp200

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 11500367

Title: Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA.

PubMed ID: 11500367

DOI: 10.1093/emboj/20.16.4399

PubMed ID: 11435115

Title: Structural characterization of the LEM motif common to three human inner nuclear membrane proteins.

PubMed ID: 11435115

DOI: 10.1016/s0969-2126(01)00611-6

Sequence Information:

  • Length: 454
  • Mass: 50670
  • Checksum: 03277C5723117909
  • Sequence:
    • MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK 
GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL 
LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS 
DRYSDNEEDS KIELKLEKRE PLKGRAKTPV TLKQRRVEHN QSYSQAGITE TEWTSGSSKG 
GPLQALTRES TRGSRRTPRK RVETSEHFRI DGPVISESTP IAETIMASSN ESLVVNRVTG 
NFKHASPILP ITEFSDIPRR APKKPLTRAE VGEKTEERRV ERDILKEMFP YEASTPTGIS 
ASCRRPIKGA AGRPLELSDF RMEESFSSKY VPKYVPLADV KSEKTKKGRS IPVWIKILLF 
VVVAVFLFLV YQAMETNQVN PFSNFLHVDP RKSN

Genular Protein ID: 1118450729

Symbol: Q59G12_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q59G12

Database IDs:

ARBA 5 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 2 CTD 1 DNASU 1 EMBL 2 GO 3 Gene3D 1 Genevisible 1 GenomeRNAi 1 IntAct 1 InterPro 3 KEGG 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 4 PeptideAtlas 1 Pfam 2 RefSeq 2 SAM 2 SMART 2 SUPFAM 1

Sequence Information:

  • Length: 378
  • Mass: 41806
  • Checksum: D73087A941C65F75
  • Sequence:
    • GSEAAARSPA RSKRAGVSGG GKGCGEGASQ IPEMPEFLED PSVLTKDKLK SELVANNVTL 
PAGEQRKDVY VQLYLQHLTA RNRPPLPAGT NSKGPPDFSS DEEREPTPVL GSGAAAAGRS 
RAAVGRKATK KTDKPRQEDK DDLDVTELTN EDLLDQLVKY GVNPGPIVGT TRKLYEKKLL 
KLREQGTESR SSTPLPTISS SAENTRQNGS NDSDRYSDNE EDSKIELKLE KREPLKGRAK 
TPVTLKQRRV EHNQVGEKTE ERRVERDILK EMFPYEASTP TGISASCRRP IKGAAGRPLE 
LSDFRMEESF SSKYVPKYVP LADVKSEKTK KGRSIPVWIK ILLFVVVAVF LFLVYQAMET 
NQVNPFSNFL HVDPRKSN

Genular Protein ID: 2309660591

Symbol: G5E972_HUMAN

Name: N/A

UniProtKB Accession Codes:

G5E972

Database IDs:

ARBA 5 Antibodypedia 1 Bgee 1 BioGRID-ORCS 1 CDD 2 CTD 1 ChiTaRS 1 DNASU 1 EMBL 3 EPD 1 Ensembl 2 GO 2 Gene3D 1 GeneTree 1 GenomeRNAi 1 HGNC 1 InterPro 3 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 4 Pfam 2 Proteomes 2 ProteomicsDB 1 RefSeq 1 SAM 2 SMART 2 SUPFAM 1 UCSC 1 VEuPathDB 1

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 17487921

Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

PubMed ID: 17487921

DOI: 10.1002/elps.200600782

PubMed ID: 17924679

Title: 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.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17693683

Title: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.

PubMed ID: 17693683

DOI: 10.1074/mcp.M700120-MCP200

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 414
  • Mass: 46306
  • Checksum: D36CC78A5EEE7679
  • Sequence:
    • MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK 
GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL 
LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS 
DRYSDNEEDS KIELKLEKRE PLKGRAKTPV TLKQRRVEHN QVETSEHFRI DGPVISESTP 
IAETIMASSN ESLVVNRVTG NFKHASPILP ITEFSDIPRR APKKPLTRAE VGEKTEERRV 
ERDILKEMFP YEASTPTGIS ASCRRPIKGA AGRPLELSDF RMEESFSSKY VPKYVPLADV 
KSEKTKKGRS IPVWIKILLF VVVAVFLFLV YQAMETNQVN PFSNFLHVDP RKSN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.