Details for: LMO7

Gene ID: 4008

Symbol: LMO7

Ensembl ID: ENSG00000136153

Description: LIM domain 7

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: type I pneumocyte (CL0002062)
    Fold Change: 4.78
    Marker Score: 5753
  • Cell Name: regular ventricular cardiac myocyte (CL0002131)
    Fold Change: 4.16
    Marker Score: 92942
  • Cell Name: epithelial cell of lower respiratory tract (CL0002632)
    Fold Change: 3.43
    Marker Score: 14294.5
  • Cell Name: renal alpha-intercalated cell (CL0005011)
    Fold Change: 3.14
    Marker Score: 1655
  • Cell Name: lung goblet cell (CL1000143)
    Fold Change: 3.11
    Marker Score: 897
  • Cell Name: squamous epithelial cell (CL0000076)
    Fold Change: 2.92
    Marker Score: 1991.5
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 2.88
    Marker Score: 46295
  • Cell Name: nasal mucosa goblet cell (CL0002480)
    Fold Change: 2.8
    Marker Score: 1869
  • Cell Name: luminal cell of prostate epithelium (CL0002340)
    Fold Change: 2.68
    Marker Score: 1562
  • Cell Name: renal principal cell (CL0005009)
    Fold Change: 2.67
    Marker Score: 2060
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: 2.61
    Marker Score: 16660
  • Cell Name: epithelial cell of urethra (CL1000296)
    Fold Change: 2.43
    Marker Score: 1911
  • Cell Name: epithelial cell of lung (CL0000082)
    Fold Change: 2.42
    Marker Score: 12738
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 2.39
    Marker Score: 2516
  • Cell Name: type II pneumocyte (CL0002063)
    Fold Change: 2.39
    Marker Score: 15574
  • Cell Name: kidney interstitial fibroblast (CL1000692)
    Fold Change: 2.31
    Marker Score: 4453
  • Cell Name: regular atrial cardiac myocyte (CL0002129)
    Fold Change: 2.3
    Marker Score: 8190
  • Cell Name: bronchial goblet cell (CL1000312)
    Fold Change: 2.25
    Marker Score: 1111
  • Cell Name: ciliated cell (CL0000064)
    Fold Change: 2.23
    Marker Score: 7662
  • Cell Name: colon epithelial cell (CL0011108)
    Fold Change: 2.2
    Marker Score: 6921
  • Cell Name: epithelial cell of alveolus of lung (CL0010003)
    Fold Change: 2.2
    Marker Score: 985
  • Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
    Fold Change: 2.18
    Marker Score: 2215
  • Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
    Fold Change: 2.13
    Marker Score: 18508.5
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: 2.1
    Marker Score: 31380
  • Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
    Fold Change: 2.09
    Marker Score: 5610
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: 2.09
    Marker Score: 19650
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 2.09
    Marker Score: 3071
  • Cell Name: enterocyte (CL0000584)
    Fold Change: 2.08
    Marker Score: 9968
  • Cell Name: respiratory goblet cell (CL0002370)
    Fold Change: 2.07
    Marker Score: 597
  • Cell Name: pneumocyte (CL0000322)
    Fold Change: 2.04
    Marker Score: 3275
  • Cell Name: cardiac endothelial cell (CL0010008)
    Fold Change: 2.02
    Marker Score: 3831
  • Cell Name: corneal epithelial cell (CL0000575)
    Fold Change: 1.98
    Marker Score: 2191
  • Cell Name: lung ciliated cell (CL1000271)
    Fold Change: 1.93
    Marker Score: 917
  • Cell Name: secretory cell (CL0000151)
    Fold Change: 1.92
    Marker Score: 3504
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: 1.88
    Marker Score: 17868
  • Cell Name: parietal epithelial cell (CL1000452)
    Fold Change: 1.87
    Marker Score: 678
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: 1.87
    Marker Score: 4676
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: 1.83
    Marker Score: 15752
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 1.83
    Marker Score: 112432
  • Cell Name: multi-ciliated epithelial cell (CL0005012)
    Fold Change: 1.82
    Marker Score: 3455.5
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: 1.81
    Marker Score: 66785
  • Cell Name: cell of skeletal muscle (CL0000188)
    Fold Change: 1.75
    Marker Score: 1330
  • Cell Name: neuron (CL0000540)
    Fold Change: 1.74
    Marker Score: 7095
  • Cell Name: respiratory epithelial cell (CL0002368)
    Fold Change: 1.74
    Marker Score: 958
  • Cell Name: mucous neck cell (CL0000651)
    Fold Change: 1.72
    Marker Score: 3900
  • Cell Name: basal cell of epithelium of trachea (CL1000348)
    Fold Change: 1.71
    Marker Score: 12729
  • Cell Name: sst GABAergic cortical interneuron (CL4023017)
    Fold Change: 1.7
    Marker Score: 33907
  • Cell Name: renal interstitial pericyte (CL1001318)
    Fold Change: 1.7
    Marker Score: 1623
  • Cell Name: club cell (CL0000158)
    Fold Change: 1.7
    Marker Score: 1985.5
  • Cell Name: sncg GABAergic cortical interneuron (CL4023015)
    Fold Change: 1.7
    Marker Score: 13033
  • Cell Name: preosteoblast (CL0007010)
    Fold Change: 1.69
    Marker Score: 480
  • Cell Name: cerebral cortex neuron (CL0010012)
    Fold Change: 1.65
    Marker Score: 4709
  • Cell Name: pyramidal neuron (CL0000598)
    Fold Change: 1.65
    Marker Score: 2765
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 1.62
    Marker Score: 3969
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: 1.62
    Marker Score: 2506
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 1.62
    Marker Score: 402
  • Cell Name: caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 1.57
    Marker Score: 6063
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 1.57
    Marker Score: 1690
  • Cell Name: duct epithelial cell (CL0000068)
    Fold Change: 1.51
    Marker Score: 705
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: 1.5
    Marker Score: 5321
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 1.49
    Marker Score: 870
  • Cell Name: vip GABAergic cortical interneuron (CL4023016)
    Fold Change: 1.49
    Marker Score: 56420
  • Cell Name: basal cell (CL0000646)
    Fold Change: 1.47
    Marker Score: 1896
  • Cell Name: syncytiotrophoblast cell (CL0000525)
    Fold Change: 1.47
    Marker Score: 1205
  • Cell Name: mural cell (CL0008034)
    Fold Change: 1.46
    Marker Score: 167296
  • Cell Name: renal beta-intercalated cell (CL0002201)
    Fold Change: 1.45
    Marker Score: 458
  • Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
    Fold Change: 1.43
    Marker Score: 3377
  • Cell Name: enterocyte of colon (CL1000347)
    Fold Change: 1.42
    Marker Score: 2184
  • Cell Name: kidney collecting duct intercalated cell (CL1001432)
    Fold Change: 1.42
    Marker Score: 2347
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: 1.42
    Marker Score: 1470
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: 1.41
    Marker Score: 2245
  • Cell Name: kidney collecting duct principal cell (CL1001431)
    Fold Change: 1.41
    Marker Score: 3554
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 1.38
    Marker Score: 1374.5
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: 1.33
    Marker Score: 8564
  • Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
    Fold Change: 1.31
    Marker Score: 5432
  • Cell Name: osteoblast (CL0000062)
    Fold Change: 1.31
    Marker Score: 701
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 1.3
    Marker Score: 20420
  • Cell Name: epithelial cell of prostate (CL0002231)
    Fold Change: 1.28
    Marker Score: 887
  • Cell Name: midzonal region hepatocyte (CL0019028)
    Fold Change: 1.28
    Marker Score: 5508
  • Cell Name: immature innate lymphoid cell (CL0001082)
    Fold Change: 1.27
    Marker Score: 2590
  • Cell Name: epithelial cell of esophagus (CL0002252)
    Fold Change: 1.27
    Marker Score: 10956
  • Cell Name: mucus secreting cell (CL0000319)
    Fold Change: 1.27
    Marker Score: 323
  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 1.25
    Marker Score: 4088
  • Cell Name: intestine goblet cell (CL0019031)
    Fold Change: 1.25
    Marker Score: 1196
  • Cell Name: periportal region hepatocyte (CL0019026)
    Fold Change: 1.22
    Marker Score: 6534
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: 1.2
    Marker Score: 9403
  • Cell Name: germ cell (CL0000586)
    Fold Change: 1.2
    Marker Score: 2098
  • Cell Name: papillary tips cell (CL1000597)
    Fold Change: 1.14
    Marker Score: 230
  • Cell Name: taste receptor cell (CL0000209)
    Fold Change: 1.13
    Marker Score: 975
  • Cell Name: pulmonary ionocyte (CL0017000)
    Fold Change: 1.12
    Marker Score: 689
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 1.12
    Marker Score: 1186
  • Cell Name: stem cell (CL0000034)
    Fold Change: 1.11
    Marker Score: 2642
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 1.11
    Marker Score: 38342.5
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: 1.1
    Marker Score: 36989
  • Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
    Fold Change: 1.09
    Marker Score: 657
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 1.08
    Marker Score: 4227
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 1.07
    Marker Score: 1518
  • Cell Name: type G enteroendocrine cell (CL0000508)
    Fold Change: 1.06
    Marker Score: 367
  • Cell Name: thyroid follicular cell (CL0002258)
    Fold Change: 1.06
    Marker Score: 829
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 1.05
    Marker Score: 308

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Other Information

**Key characteristics**: * LMO7 is a transmembrane protein that is expressed in a variety of cell types. * It is a member of the LIM domain family of proteins. * It is involved in the regulation of cell adhesion, signaling, and proliferation. * It is also involved in the processing and presentation of antigens. **Pathways and functions**: * LMO7 is involved in the adaptive immune system. * It is expressed in immune cells, including dendritic cells, T cells, and B cells. * It plays a role in the recognition of foreign antigens by immune cells. * It is also involved in the processing and presentation of antigens by antigen-presenting cells. * It is involved in the regulation of cell adhesion, signaling, and proliferation. **Clinical significance**: * Mutations in the LMO7 gene have been linked to a number of human diseases, including cancer and autoimmune disorders. * LMO7 is a promising target for cancer immunotherapy. * Inhibition of LMO7 has been shown to inhibit cancer growth and metastasis. **Additional information**: * The LMO7 gene is located on chromosome 17p13.3. * It is a member of the LIM domain family of proteins. * It is a relatively novel protein that has not been well-studied.

Genular Protein ID: 286314314

Symbol: LMO7_HUMAN

Name: LIM domain only protein 7

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11935316

Title: A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer development: identification and characterization of candidate genes.

PubMed ID: 11935316

DOI: 10.1007/s00439-001-0646-6

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

PubMed ID: 10048485

Title: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.

PubMed ID: 10048485

DOI: 10.1093/dnares/5.6.355

PubMed ID: 12168954

Title: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.

PubMed ID: 12168954

DOI: 10.1093/dnares/9.3.99

PubMed ID: 10531035

Title: Identification of a family of human F-box proteins.

PubMed ID: 10531035

DOI: 10.1016/s0960-9822(00)80020-2

PubMed ID: 9826547

Title: Analysis of a human cDNA containing a tissue-specific alternatively spliced LIM domain.

PubMed ID: 9826547

DOI: 10.1006/bbrc.1998.9656

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: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

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: 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: 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: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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: 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: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

Sequence Information:

  • Length: 1683
  • Mass: 192696
  • Checksum: 3E79B2AEAC67F6F5
  • Sequence:
  • MKKIRICHIF TFYSWMSYDV LFQRTELGAL EIWRQLICAH VCICVGWLYL RDRVCSKKDI 
    ILRTEQNSGR TILIKAVTEK NFETKDFRAS LENGVLLCDL INKLKPGVIK KINRLSTPIA 
    GLDNINVFLK ACEQIGLKEA QLFHPGDLQD LSNRVTVKQE ETDRRVKNVL ITLYWLGRKA 
    QSNPYYNGPH LNLKAFENLL GQALTKALED SSFLKRSGRD SGYGDIWCPE RGEFLAPPRH 
    HKREDSFESL DSLGSRSLTS CSSDITLRGG REGFESDTDS EFTFKMQDYN KDDMSYRRIS 
    AVEPKTALPF NRFLPNKSRQ PSYVPAPLRK KKPDKHEDNR RSWASPVYTE ADGTFSSNQR 
    RIWGTNVENW PTVQGTSKSS CYLEEEKAKT RSIPNIVKDD LYVRKLSPVM PNPGNAFDQF 
    LPKCWTPEDV NWKRIKRETY KPWYKEFQGF SQFLLLQALQ TYSDDILSSE THTKIDPTSG 
    PRLITRRKNL SYAPGYRRDD LEMAALDPDL ENDDFFVRKT GVFHANPYVL RAFEDFRKFS 
    EQDDSVERDI ILQCREGELV LPDLEKDDMI VRRIPAQKKE VPLSGAPDRY HPVPFPEPWT 
    LPPEIQAKFL CVFERTCPSK EKSNSCRILV PSYRQKKDDM LTRKIQSWKL GTTVPPISFT 
    PGPCSEADLK RWEAIREASR LRHKKRLMVE RLFQKIYGEN GSKSMSDVSA EDVQNLRQLR 
    YEEMQKIKSQ LKEQDQKWQD DLAKWKDRRK SYTSDLQKKK EEREEIEKQA LEKSKRSSKT 
    FKEMLQDRES QNQKSTVPSR RRMYSFDDVL EEGKRPPTMT VSEASYQSER VEEKGATYPS 
    EIPKEDSTTF AKREDRVTTE IQLPSQSPVE EQSPASLSSL RSRSTQMEST RVSASLPRSY 
    RKTDTVRLTS VVTPRPFGSQ TRGISSLPRS YTMDDAWKYN GDVEDIKRTP NNVVSTPAPS 
    PDASQLASSL SSQKEVAATE EDVTRLPSPT SPFSSLSQDQ AATSKATLSS TSGLDLMSES 
    GEGEISPQRE VSRSQDQFSD MRISINQTPG KSLDFGFTIK WDIPGIFVAS VEAGSPAEFS 
    QLQVDDEIIA INNTKFSYND SKEWEEAMAK AQETGHLVMD VRRYGKAGSP ETKWIDATSG 
    IYNSEKSSNL SVTTDFSESL QSSNIESKEI NGIHDESNAF ESKASESISL KNLKRRSQFF 
    EQGSSDSVVP DLPVPTISAP SRWVWDQEEE RKRQERWQKE QDRLLQEKYQ REQEKLREEW 
    QRAKQEAERE NSKYLDEELM VLSSNSMSLT TREPSLATWE ATWSEGSKSS DREGTRAGEE 
    ERRQPQEEVV HEDQGKKPQD QLVIERERKW EQQLQEEQEQ KRLQAEAEEQ KRPAEEQKRQ 
    AEIERETSVR IYQYRRPVDS YDIPKTEEAS SGFLPGDRNK SRSTTELDDY STNKNGNNKY 
    LDQIGNMTSS QRRSKKEQVP SGAELERQQI LQEMRKRTPL HNDNSWIRQR SASVNKEPVS 
    LPGIMRRGES LDNLDSPRSN SWRQPPWLNQ PTGFYASSSV QDFSRPPPQL VSTSNRAYMR 
    NPSSSVPPPS AGSVKTSTTG VATTQSPTPR SHSPSASQSG SQLRNRSVSG KRICSYCNNI 
    LGKGAAMIIE SLGLCYHLHC FKCVACECDL GGSSSGAEVR IRNHQLYCND CYLRFKSGRP 
    TAM

Genular Protein ID: 1068293739

Symbol: F8WD26_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

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: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

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: 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: 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: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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: 28112733

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

PubMed ID: 28112733

Sequence Information:

  • Length: 1631
  • Mass: 186179
  • Checksum: FAB88F8504297121
  • Sequence:
  • MEGLEEAEAN CSVAFAEAQR WVEAVTEKNF ETKDFRASLE NGVLLCDLIN KLKPGVIKKI 
    NRLSTPIAGL DNINVFLKAC EQIGLKEAQL FHPGDLQDLS NRVTVKQEET DRRVKNVLIT 
    LYWLGRKAQS NPYYNGPHLN LKAFENLLGQ ALTKALEDSS FLKRSGRDSG YGDIWCPERG 
    EFLAPPRHHK REDSFESLDS LGSRSLTSCS SDITLRGGRE GFESDTDSEF TFKMQDYNKD 
    DMSYRRISAV EPKTALPFNR FLPNKSRQPS YVPAPLRKKK PDKHEDNRRS WASPVYTEAD 
    GTFSSNQRRI WGTNVENWPT VQGTSKSSCY LEEEKAKTRS IPNIVKDDLY VRKLSPVMPN 
    PGNAFDQFLP KCWTPEDVNW KRIKRETYKP WYKEFQGFSQ FLLLQALQTY SDDILSSETH 
    TKIDPTSGPR LITRRKNLSY APGYRRDDLE MAALDPDLEN DDFFVRKTGA FHANPYVLRA 
    FEDFRKFSEQ DDSVERDIIL QCREGELVLP DLEKDDMIVR RIPAQKKEVP LSGAPDRYHP 
    VPFPEPWTLP PEIQAKFLCV LERTCPSKEK SNSCRILVPS YRQKKDDMLT RKIQSWKLGT 
    TVPPISFTPG PCSEADLKRW EAIREASRLR HKKRLMVERL FQKIYGENGS KSMSDVSAED 
    VQNLRQLRYE EMQKIKSQLK EQDQKWQDDL AKWKDRRKSY TSDLQKKKEE REEIEKQALE 
    KSKRSSKTFK EMLQDRESQN QKSTVPSRRR MYSFDDVLEE GKRPPTMTVS EASYQSERVE 
    EKGATYPSEI PKEDSTTFAK REDRVTTEIQ LPSQSPVEEQ SPASLSSLRS RSTQMESTRV 
    SASLPRSYRK TDTVRLTSVV TPRPFGSQTR GISSLPRSYT MDDAWKYNGD VEDIKRTPNN 
    VVSTPAPSPD ASQLASSLSS QKEVAATEED VTRLPSPTSP FSSLSQDQAA TSKATLSSTS 
    GLDLMSESGE GEISPQREVS RSQDQFSDMR ISINQTPGKS LDFGFTIKWD IPGIFVASVE 
    AGSPAEFSQL QVDDEIIAIN NTKFSYNDSK EWEEAMAKAQ ETGHLVMDVR RYGKAGSPET 
    KWIDATSGIY NSEKSSNLSV TTDFSESLQS SNIESKEING IHDESNAFES KASESISLKN 
    LKRRSQFFEQ GSSDSVVPDL PVPTISAPSR WVWDQEEERK RQERWQKEQD RLLQEKYQRE 
    QEKLREEWQR AKQEAERENS KYLDEELMVL SSNSMSLTTR EPSLATWEAT WSEGSKSSDR 
    EGTRAGEEER RQPQEEVVHE DQGKKPQDQL VIERERKWEQ QLQEEQEQKR LQAEAEEQKR 
    PAEEQKRQAE IERETSVRIY QYRRPVDSYD IPKTEEASSG FLPGDRNKSR STTELDDYST 
    NKNGNNKYLD QIGNMTSSQR RSKKEQVPSG AELERQQILQ EMRKRTPLHN DNSWIRQRSA 
    SVNKEPVSLP GIMRRGESLD NLDSPRSNSW RQPPWLNQPT GFYASSSVQD FSRPPPQLVS 
    TSNRAYMRNP SSSVPPPSAG SVKTSTTGVA TTQSPTPRSH SPSASQSGSQ LRNRSVSGKR 
    ICSYCNNILG KGAAMIIESL GLCYHLHCFK CVACECDLGG SSSGAEVRIR NHQLYCNDCY 
    LRFKSGRPTA M

Genular Protein ID: 1348366939

Symbol: F8J2B5_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 21670154

Title: LMO7 mediates cell-specific activation of the Rho-myocardin-related transcription factor-serum response factor pathway and plays an important role in breast cancer cell migration.

PubMed ID: 21670154

DOI: 10.1128/MCB.01365-10

Sequence Information:

  • Length: 1631
  • Mass: 186241
  • Checksum: 5FC1483913806856
  • Sequence:
  • MEGLEEAEAN CSVAFAEAQR WVEAVTEKNF ETKDFRASLE NGVLLCDLIN KLKPGVIKKI 
    NRLSTPIAGL DNINVFLKAC EQIGLKEAQL FHPGDLQDLS NRVTVKQEET DRRVKNVLIT 
    LYWLGRKAQS NPYYNGPHLN LKAFENLLGQ ALTKALEDSS FLKRSGRDSG YGDIWCPERG 
    EFLAPPRHHK REDSFESLDS LGSRSLTSCS SDITLRGGRE GFESDTDSEF TFKMQDYNKD 
    DMSYRRISAV EPKTALPFNR FLPNKSRQPS YVPAPLRKKK PDKHEDNRRS WASPVYTEAD 
    GTFSSNQRRI WGTNVENWPT VQGTSKSSCY LEEEKAKTRS IPNIVKDDLY VRKLSPVMPN 
    PGNAFDQFLP KCWTPEDVNW KRIKRETYKP WYKEFQGFSQ FLLLQALQTY SDDILSSETH 
    TKIDPTSGPR LITRRKNLSY APGYRRDDLE MAALDPDLEN DDFFVRKTGV FHANPYVLRA 
    FEDFRKFSEQ DDSVERDIIL QCREGELVLP DLEKDDMIVR RIPAQKKEVP LSGAPDRYHP 
    VPFPEPWTLP PEIQAKFLCV FERTCPSKEK SNSCRILVPS YRQKKDDMLT RKIQSWKLGT 
    TVPPISFTPG PCSEADLKRW EAIREASRLR HKKRLMVERL FQKIYGENGS KSMSDVSAED 
    VQNLRQLRYE EMQKIKSQLK EQDQKWQDDL AKWKDRRKSY TSDLQKKKEE REEIEKQALE 
    KSKRSSKTFK EMLQDRESQN QKSTVPSRRR MYSFDDVLEE GKRPPTMTVS EASYQSERVE 
    EKGATYPSEI PKEDSTTFAK REDRVTTEIQ LPSQSPVEEQ SPASLSSLRS RSTQMESTRV 
    SASLPRSYRK TDTVRLTSVV TPRPFGSQTR GISSLPRSYT MDDAWKYNGD VEDIKRTPNN 
    VVSTPAPSPD ASQLASSLSS QKEVAATEED VTRLPSPTSP FSSLSQDQAA TSKATLSSTS 
    GLDLMSESGE GEISPQREVS RSQDQFSDMR ISINQTPGKS LDFGFTIKWD IPGIFVASVE 
    AGSPAEFSQL QVDDEIIAIN NTKFSYNDSK EWEEAMAKAQ ETGHLVMDVR RYGKAGSPET 
    KWIDATSGIY NSEKSSNLSV TTDFSESLQS SNIESKEING IHDESNAFES KASESISLKN 
    LKRRSQFFEQ GSSDSVVPDL PVPTISAPSR WVWDQEEERK RQERWQKEQD RLLQEKYQRE 
    QEKLREEWQR AKQEAERENS KYLDEELMVL SSNSMSLTTR EPSLATWEAT WSEGSKSSDR 
    EGTRAGEEER RQPQEEVVHE DQGKKPQDQL VIERERKWEQ QLQEEQEQKR LQAEAEEQKR 
    PAEEQKRQAE IERETSVRIY QYRRPVDSYD IPKTEEASSG FLPGDRNKSR STTELDDYST 
    NKNGNNKYLD QIGNMTSSQR RSKKEQVPSG AELERQQILQ EMRKRTPLHN DNSWIRQRSA 
    SVNKEPVSLP GIMRRGESLD NLDSPRSNSW RQPPWLNQPT GFYASSSVQD FSRPPPQLVS 
    TSNRAYMRNP SSSVPPPSAG SVKTSTTGVA TTQSPTPRSH SPSASQSGSQ LRNRSVSGKR 
    ICSYCNNILG KGAAMIIESL GLCYHLHCFK CVACECDLGG SSSGAEVRIR NHQLYCNDCY 
    LRFKSGRPTA M

Genular Protein ID: 3653551670

Symbol: E9PMT2_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

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: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

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: 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: 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: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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: 28112733

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

PubMed ID: 28112733

Sequence Information:

  • Length: 1398
  • Mass: 160022
  • Checksum: 1F6FF3E6124190AF
  • Sequence:
  • MQDYNKDDMS YRRISAVEPK TALPFNRFLP NKSRQPSYVP APLRKKKPDK HEDNRRSWAS 
    PVYTEADGTF SSNQRRIWGT NVENWPTVQG TSKSSCYLEE EKAKTRSIPN IVKDDLYVRK 
    LSPVMPNPGN AFDQFLPKCW TPEDVNWKRI KRETYKPWYK EFQGFSQFLL LQALQTYSDD 
    ILSSETHTKI DPTSGPRLIT RRKNLSYAPG YRRDDLEMAA LDPDLENDDF FVRKTGAFHA 
    NPYVLRAFED FRKFSEQDDS VERDIILQCR EGELVLPDLE KDDMIVRRIP AQKKEVPLSG 
    APDRYHPVPF PEPWTLPPEI QAKFLCVLER TCPSKEKSNS CRILVPSYRQ KKDDMLTRKI 
    QSWKLGTTVP PISFTPGPCS EADLKRWEAI REASRLRHKK RLMVERLFQK IYGENGSKSM 
    SDVSAEDVQN LRQLRYEEMQ KIKSQLKEQD QKWQDDLAKW KDRRKSYTSD LQKKKEEREE 
    IEKQALEKSK RSSKTFKEML QDRESQNQKS TVPSRRRMYS FDDVLEEGKR PPTMTVSEAS 
    YQSERVEEKG ATYPSEIPKE DSTTFAKRED RVTTEIQLPS QSPVEEQSPA SLSSLRSRST 
    QMESTRVSAS LPRSYRKTDT VRLTSVVTPR PFGSQTRGIS SLPRSYTMDD AWKYNGDVED 
    IKRTPNNVVS TPAPSPDASQ LASSLSSQKE VAATEEDVTR LPSPTSPFSS LSQDQAATSK 
    ATLSSTSGLD LMSESGEGEI SPQREVSRSQ DQFSDMRISI NQTPGKSLDF GFTIKWDIPG 
    IFVASVEAGS PAEFSQLQVD DEIIAINNTK FSYNDSKEWE EAMAKAQETG HLVMDVRRYG 
    KAGSPETKWI DATSGIYNSE KSSNLSVTTD FSESLQSSNI ESKEINGIHD ESNAFESKAS 
    ESISLKNLKR RSQFFEQGSS DSVVPDLPVP TISAPSRWVW DQEEERKRQE RWQKEQDRLL 
    QEKYQREQEK LREEWQRAKQ EAERENSKYL DEELMVLSSN SMSLTTREPS LATWEATWSE 
    GSKSSDREGT RAGEEERRQP QEEVVHEDQG KKPQDQLVIE RERKWEQQLQ EEQEQKRLQA 
    EAEEQKRPAE EQKRQAEIER ETSVRIYQYR RPVDSYDIPK TEEASSGFLP GDRNKSRSTT 
    ELDDYSTNKN GNNKYLDQIG NMTSSQRRSK KEQVPSGAEL ERQQILQEMR KRTPLHNDNS 
    WIRQRSASVN KEPVSLPGIM RRGESLDNLD SPRSNSWRQP PWLNQPTGFY ASSSVQDFSR 
    PPPQLVSTSN RAYMRNPSSS VPPPSAGSVK TSTTGVATTQ SPTPRSHSPS ASQSGSQLRN 
    RSVSGKRICS YCNNILGKGA AMIIESLGLC YHLHCFKCVA CECDLGGSSS GAEVRIRNHQ 
    LYCNDCYLRF KSGRPTAM

Genular Protein ID: 849257810

Symbol: A0A0A0MTE2_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

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: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

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: 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: 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: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

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: 28112733

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

PubMed ID: 28112733

Sequence Information:

  • Length: 1385
  • Mass: 158203
  • Checksum: 885B4564E783EB43
  • Sequence:
  • MQDYNKDDMS YRRISAVEPK TALPFNRFLP NKSRQPSYVP APLRKKKPDK HEDNRRSWAS 
    PVYTEADGTF SSNQRRIWGT NVENWPTVQG TSKSSCYLEE EKAKTRSIPN IVKDDLYVRK 
    LSPVMPNPGN AFDQFLPKCW TPEDVNWKRI KRETYKPWYK EFQGFSQFLL LQALQTYSDD 
    ILSSETHTKI DPTSGPRLIT RRKNLSYAPG YRRDDLEMAA LDPDLENDDF FVRKTGAFHA 
    NPYVLRAFED FRKFSEQDDS VERDIILQCR EGELVLPDLE KDDMIVRRIP AQKKEVPLSG 
    APDRYHPVPF PEPWTLPPEI QAKFLCVLER TCPSKEKSNS CRILVPSYRQ KKDDMLTRKI 
    QSWKLGTTVP PISFTPGPCS EADLKRWEAI REASRLRHKK RLMVERLFQK IYGENGSKSM 
    SDVSAEDVQN LRQLRYEEMQ KIKSQLKEQD QKWQDDLAKW KDRRKSYTSD LQKKKEEREE 
    IEKQALEKSK RSSKTFKEML QDRESQNQKS TVPSRRRMYS FDDVLEEGKR PPTMTVSEAS 
    YQSERVEEKG ATYPSEIPKE DSTTFAKRED RVTTEIQLPS QSPVEEQSPA SLSSLRSRST 
    QMESTRVSAS LPRSYRKTDT VRLTSVVTPR PFGSQTRGIS SLPRSYTMDD AWKYNGDVED 
    IKRTPNNVVS TPAPSPDASQ LASSLSSQKE VAATEEDVTR LPSPTSPFSS LSQDQAATSK 
    ATLSSTSGLD LMSESGEGEI SPQREVSRSQ DQFSDMRISI NQTPGKSLDF GFTIKWDIPG 
    IFVASVEAGS PAEFSQLQVD DEIIAINNTK FSYNDSKEWE EAMAKAQETG HLVMDVRRYG 
    KAGSPETKWI DATSGIYNSE KSSNLSVTTD FSESLQSSNI ESKEINGIHD ESNAFESKAS 
    ESISLKNLKR RSQFFEQGSS DSVVPDLPVP TISAPSRWVW DQEEERKRQE RWQKEQDRLL 
    QEKYQREQEK LREEWQRAKQ EAERENSKYL DEELMVLSSN SMSLTTREPS LATWEATWSE 
    GSKSSDREGT RAGEEERRQP QEEVVHEDQG KKPQDQLVIE RERKWEQQLQ EEQEQKRLQA 
    EAEEQKRPAE EQKRQAEIER ETSVRIYQYR RPVDSYDIPK TEEASSGFLP GDRNKSRSTT 
    ELDDYSTNKN GNNKYLDQIG NMTSSQRRSK KEQVPSGAEL ERQQILQEMR KRTPLHNDNS 
    WIRQRSASVN KEPVSLPGIM RRGESLDNLD SPRSNSWRQP PWLNQPTGFY ASSSVQDFSR 
    PPPQLVSTSN RAYMRNPSSS VPPPSAGSVK TSTTGVATTQ SPTPRSHSPS ASQSGSQLRN 
    SVLPVSVTSE ALPQELKSGS ETTNCTATTA ISDSNLDGQP PCDVSLHTKA LLQIEEEVVA 
    AHVDL

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.