Details for: TRIP10

Gene ID: 9322

Gene Type:  Protein-coding  - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.

Symbol: TRIP10

Ensembl ID: ENSG00000125733

Description: thyroid hormone receptor interactor 10

Cell Significance Landscape

Associated with

Significant Cells

Cell Significance Index (CSI) scores for the chosen context(s)

  • squamous epithelial cell CL0000076
    CSI 23.4
    rCSI 55.54%
    PRS 68.06
  • keratinocyte CL0000312
    CSI 10.25
    rCSI 8.59%
    PRS 68.9
  • nasal mucosa goblet cell CL0002480
    CSI 6.27
    rCSI 7.27%
    PRS 72.17
  • interstitial cell of Cajal CL0002088
    CSI 4.11
    rCSI 5.23%
    PRS 71.18
  • CD8-positive, alpha-beta memory T cell, CD45RO-positive CL0001203
    CSI 4
    rCSI 4.85%
    PRS 50.61
  • secretory cell CL0000151
    CSI 3.95
    rCSI 4.12%
    PRS 65.14
  • ependymal cell CL0000065
    CSI 3.61
    rCSI 7.33%
    PRS 43.71
  • skin fibroblast CL0002620
    CSI 3.59
    rCSI 3.1%
    PRS 69.68
  • brush cell of tracheobronchial tree CL0002075
    CSI 3.1
    rCSI 9.18%
    PRS 74.5
  • helper T cell CL0000912
    CSI 2.96
    rCSI 4.19%
    PRS 68.91
  • epithelial cell of lower respiratory tract CL0002632
    CSI 2.83
    rCSI 2.19%
    PRS 67.38
  • ON-bipolar cell CL0000749
    CSI 2.74
    rCSI 4.08%
    PRS 66.13
  • mesodermal cell CL0000222
    CSI 2.65
    rCSI 3.18%
    PRS 63.01
  • club cell CL0000158
    CSI 2.64
    rCSI 3.87%
    PRS 60.34
  • conjunctival epithelial cell CL1000432
    CSI 2.57
    rCSI 3.93%
    PRS 65.57
  • mesenchymal cell CL0008019
    CSI 2.57
    rCSI 6.52%
    PRS 58.9
  • subcutaneous adipocyte CL0002521
    CSI 2.52
    rCSI 12.9%
    PRS 69.66
  • perivascular cell CL4033054
    CSI 2.52
    rCSI 3.44%
    PRS 70.66
  • alveolar type 1 fibroblast cell CL4028004
    CSI 2.46
    rCSI 2.7%
    PRS 68.48
  • melanocyte CL0000148
    CSI 2.45
    rCSI 1.82%
    PRS 57.48
  • stem cell CL0000034
    CSI 2.44
    rCSI 2.35%
    PRS 55.74
  • pulmonary capillary endothelial cell CL4028001
    CSI 2.38
    rCSI 4.54%
    PRS 79.04
  • fibroblast of lung CL0002553
    CSI 2.35
    rCSI 2.18%
    PRS 65.43
  • lung secretory cell CL1000272
    CSI 2.33
    rCSI 5.78%
    PRS 63.39
  • kidney loop of Henle thin ascending limb epithelial cell CL1001107
    CSI 2.32
    rCSI 6.01%
    PRS 59.89
  • transit amplifying cell CL0009010
    CSI 2.31
    rCSI 3.54%
    PRS 77.56
  • epithelial cell of lung CL0000082
    CSI 2.3
    rCSI 1.9%
    PRS 64.34
  • blood vessel endothelial cell CL0000071
    CSI 2.28
    rCSI 4.73%
    PRS 61.98
  • extravillous trophoblast CL0008036
    CSI 2.27
    rCSI 2.81%
    PRS 61.5
  • respiratory hillock cell CL4030023
    CSI 2.27
    rCSI 4.04%
    PRS 77.64
  • retinal blood vessel endothelial cell CL0002585
    CSI 2.27
    rCSI 3.62%
    PRS 69.02
  • transit amplifying cell of colon CL0009011
    CSI 2.19
    rCSI 2.57%
    PRS 67.02
  • myoepithelial cell CL0000185
    CSI 2.17
    rCSI 5.5%
    PRS 72.62
  • bronchus fibroblast of lung CL2000093
    CSI 2.12
    rCSI 1.72%
    PRS 65.15
  • duct epithelial cell CL0000068
    CSI 2.11
    rCSI 3.08%
    PRS 69.9
  • respiratory suprabasal cell CL4033048
    CSI 2.07
    rCSI 2.66%
    PRS 69.51
  • lung endothelial cell CL1001567
    CSI 2.07
    rCSI 4.83%
    PRS 81.7
  • parietal epithelial cell CL1000452
    CSI 2
    rCSI 5.35%
    PRS 55.84
  • hepatic stellate cell CL0000632
    CSI 2
    rCSI 7.48%
    PRS 56.68
  • enteric smooth muscle cell CL0002504
    CSI 2
    rCSI 2.85%
    PRS 66.87
  • pulmonary artery endothelial cell CL1001568
    CSI 1.96
    rCSI 2.67%
    PRS 76.2
  • fibroblast of cardiac tissue CL0002548
    CSI 1.95
    rCSI 9.34%
    PRS 64.79
  • cerebral cortex endothelial cell CL1001602
    CSI 1.93
    rCSI 3.33%
    PRS 54.98
  • retinal bipolar neuron CL0000748
    CSI 1.91
    rCSI 3.59%
    PRS 53.01
  • intestine goblet cell CL0019031
    CSI 1.91
    rCSI 1.69%
    PRS 62.72
  • alveolar adventitial fibroblast CL4028006
    CSI 1.85
    rCSI 2.92%
    PRS 67.3
  • muscle cell CL0000187
    CSI 1.84
    rCSI 3.78%
    PRS 81.57
  • colonocyte CL1000347
    CSI 1.8
    rCSI 2.58%
    PRS 67.85
  • myeloid leukocyte CL0000766
    CSI 1.8
    rCSI 1.66%
    PRS 66.38
  • multi-ciliated epithelial cell CL0005012
    CSI 1.79
    rCSI 1.78%
    PRS 58.25
  • tracheal goblet cell CL1000329
    CSI 1.74
    rCSI 3.8%
    PRS 77.28
  • adventitial cell CL0002503
    CSI 1.74
    rCSI 4.15%
    PRS 72.85
  • mucous neck cell CL0000651
    CSI 1.73
    rCSI 2.49%
    PRS 75.12
  • pancreatic acinar cell CL0002064
    CSI 1.72
    rCSI 2.29%
    PRS 71.27
  • acinar cell CL0000622
    CSI 1.71
    rCSI 2.51%
    PRS 76.35
  • colon epithelial cell CL0011108
    CSI 1.7
    rCSI 1.78%
    PRS 61.26
  • glandular epithelial cell CL0000150
    CSI 1.68
    rCSI 4.42%
    PRS 81.9
  • vascular associated smooth muscle cell CL0000359
    CSI 1.62
    rCSI 5.27%
    PRS 64.61
  • Langerhans cell CL0000453
    CSI 1.62
    rCSI 2.47%
    PRS 79.82
  • keratocyte CL0002363
    CSI 1.55
    rCSI 3.71%
    PRS 71.9
  • dendritic cell, human CL0001056
    CSI 1.53
    rCSI 2.34%
    PRS 73.99
  • retinal cone cell CL0000573
    CSI 1.52
    rCSI 2.45%
    PRS 54.37
  • stratified epithelial cell CL0000079
    CSI 1.47
    rCSI 9.1%
    PRS 81.13
  • lung pericyte CL0009089
    CSI 1.45
    rCSI 3.84%
    PRS 73.41
  • corneal epithelial cell CL0000575
    CSI 1.43
    rCSI 4.09%
    PRS 75.96
  • cardiac endothelial cell CL0010008
    CSI 1.41
    rCSI 5.67%
    PRS 63.81
  • basal cell of prostate epithelium CL0002341
    CSI 1.4
    rCSI 4.04%
    PRS 76.11
  • tracheobronchial smooth muscle cell CL0019019
    CSI 1.37
    rCSI 2.41%
    PRS 72.83
  • lung ciliated cell CL1000271
    CSI 1.36
    rCSI 1.57%
    PRS 55.22
  • basal cell of epidermis CL0002187
    CSI 1.34
    rCSI 2.38%
    PRS 38.06
  • intestinal tuft cell CL0019032
    CSI 1.29
    rCSI 1.97%
    PRS 69.07
  • intestinal epithelial cell CL0002563
    CSI 1.23
    rCSI 1.28%
    PRS 62.81
  • smooth muscle cell of prostate CL1000487
    CSI 1.16
    rCSI 6.83%
    PRS 77.67
  • chondrocyte CL0000138
    CSI 1.15
    rCSI 1.84%
    PRS 57.25
  • regular ventricular cardiac myocyte CL0002131
    CSI 1.12
    rCSI 6.98%
    PRS 56.61
  • mucus secreting cell CL0000319
    CSI 1.09
    rCSI 1.73%
    PRS 75.72
  • luminal cell of prostate epithelium CL0002340
    CSI 0.98
    rCSI 5.26%
    PRS 76.19
  • syncytiotrophoblast cell CL0000525
    CSI 0.94
    rCSI 2.7%
    PRS 77.22
  • stromal cell of ovary CL0002132
    CSI 0.87
    rCSI 2.38%
    PRS 76.78
  • microcirculation associated smooth muscle cell CL0008035
    CSI 0.83
    rCSI 2.4%
    PRS 66.05
  • melanocyte of skin CL1000458
    CSI 0.79
    rCSI 1.07%
    PRS 34.48
  • blood vessel smooth muscle cell CL0019018
    CSI 0.65
    rCSI 5.25%
    PRS 58.13
  • vein endothelial cell of respiratory system CL4033008
    CSI 0.39
    rCSI 2.68%
    PRS 76.96
  • epithelial cell of esophagus CL0002252
    CSI 0.34
    rCSI 3.39%
    PRS 80.15
  • epithelial cell of urethra CL1000296
    CSI 0.17
    rCSI 4.27%
    PRS 80.08

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration

Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.

Comma-separated if multiple.
Comma-separated if multiple.

Legend:
  • Query Gene
  • Node Color (Target Cell CSI, relative to current network):
    • Very High
    • High
    • Medium
    • Low
    • Very Low
    • CSI N/A
  • Node Size: Proportional to Target Cell CSI magnitude
  • STRING PPI Edge
  • Shared Pathway Edge (ONTOLOGY)

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Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

## Summary Thyroid Hormone Receptor Interactor 10 ([TRIP10](/details-gene/9322)), also known as Cdc42-interacting protein 4, is an adaptor protein centrally involved in the regulation of cellular architecture and membrane dynamics. Its primary function is to link Rho GTPase signaling, particularly from Cdc42, to the organization of the actin cytoskeleton and to processes such as endocytosis and vesicle trafficking. Expression data from the **Overall** context indicates that [TRIP10](/details-gene/9322) is a highly significant gene in barrier and structural tissues, with its most prominent expression observed in [squamous epithelial cell](/details-cell/CL0000076) and [keratinocyte](/details-cell/CL0000312). This suggests a critical role in maintaining the integrity and function of epithelial layers throughout the body. ## Cellular Roles and Expression Landscape **Overall**, the expression profile of [TRIP10](/details-gene/9322) underscores its importance in epithelial and secretory cell biology. The gene shows its highest significance in [squamous epithelial cell](/details-cell/CL0000076) (CSI: 23.40) and [keratinocyte](/details-cell/CL0000312) (CSI: 10.25), cell types that rely on a highly organized cytoskeleton for structural integrity and barrier function. This pattern is extended to other specialized epithelial and secretory cells, including [nasal mucosa goblet cell](/details-cell/CL0002480), [secretory cell](/details-cell/CL0000151), and [club cell](/details-cell/CL0000158), suggesting its involvement in processes related to cellular secretion and defense at mucosal surfaces. Beyond its dominant role in epithelia, [TRIP10](/details-gene/9322) also shows notable significance in diverse cell types requiring dynamic cytoskeletal remodeling. These include [interstitial cell of Cajal](/details-cell/CL0002088), which are pacemaker cells in the gut, and components of the adaptive immune system such as [CD8-positive, alpha-beta memory T cell, CD45RO-positive](/details-cell/CL0001203) and [helper T cell](/details-cell/CL0000912). This broader expression is consistent with its fundamental role as a cytoskeletal regulator, adapting its function to the specific needs of different cell lineages, from maintaining structural barriers to enabling immune cell migration and interaction. ## Pathways and Molecular Function The molecular functions of [TRIP10](/details-gene/9322) are tightly linked to the regulation of small GTPases and their downstream effects on the cytoskeleton. Functional annotation places the protein at the center of the [Rho gtpase cycle](/details-cell/R-HSA-9012999), as part of the broader [Signaling by rho gtpases](/details-cell/R-HSA-194315) pathway. Its discovery as a Cdc42-interacting protein provides a direct mechanistic link to its role in [Actin cytoskeleton organization](/details-cell/GO:0030036) [Link](https://doi.org/10.1016/s0960-9822(06)00219-3). This function is critical for forming cellular structures such as the [Cell cortex](/details-cell/GO:0005938) and [Cell projection](/details-cell/GO:0042995), which is highly relevant to its expression in structurally demanding [keratinocytes](/details-cell/CL0000312). Furthermore, [TRIP10](/details-gene/9322) is a key component of membrane trafficking machinery. Its involvement in [Clathrin-mediated endocytosis](/details-cell/R-HSA-8856828) and the more general process of [Vesicle-mediated transport](/details-cell/R-HSA-5653656) explains its high significance in secretory cell types like [nasal mucosa goblet cell](/details-cell/CL0002480). Research has also specifically localized a TRIP10-related protein to the [Phagocytic cup](/details-cell/GO:0001891) [Link](https://doi.org/10.1182/blood-2002-03-0851), connecting its function in membrane remodeling to specialized immune processes. The protein's ability to engage in [Lipid binding](/details-cell/GO:0008289) and [Protein binding](/details-cell/GO:0005515) allows it to act as a scaffold, coordinating the assembly of protein complexes required for these dynamic cellular events. ## Research Directions Based on its defined molecular roles and distinct expression pattern, [TRIP10](/details-gene/9322) presents several avenues for future investigation. Its function appears critical at the intersection of structural maintenance and dynamic cellular remodeling. 1. **Hypothesis 1:** The high expression of [TRIP10](/details-gene/9322) in keratinocytes and squamous epithelial cells is essential for the formation and maintenance of cell-cell adhesion junctions. Its disruption would compromise epithelial barrier integrity and impair the collective cell migration required for wound healing. This is supported by evidence that a splicing variant can disrupt beta-catenin-mediated adhesion [Link](https://doi.org/10.1016/j.bbrc.2005.11.117). 2. **Hypothesis 2:** In secretory cells such as goblet cells, [TRIP10](/details-gene/9322) acts as a critical adaptor protein that couples extracellular signals, transduced via the Rho GTPase pathway, to the machinery of vesicle transport and exocytosis, thereby regulating mucin secretion at mucosal surfaces. To test the role of [TRIP10](/details-gene/9322) in epithelial barrier function (Hypothesis 1), a conditional knockout mouse model could be generated with [TRIP10](/details-gene/9322) specifically deleted in epidermal keratinocytes. The barrier function of the skin could be assessed *in vivo* using transepidermal water loss (TEWL) measurements and by challenging the mice with skin irritants. *In vitro* studies using primary keratinocytes from these mice could involve scratch-wound assays to monitor cell migration and immunofluorescence staining for key junctional proteins (e.g., E-cadherin, ZO-1) to assess the integrity of adherens and tight junctions. Given its function as an intracellular scaffolding protein essential for fundamental cytoskeletal processes, [TRIP10](/details-gene/9322) is a challenging direct therapeutic target. However, its dysregulation has been implicated in pathologies involving altered cell adhesion, such as renal cell carcinoma [Link](https://doi.org/10.1016/j.bbrc.2005.11.117). This suggests that inhibiting its specific protein-protein interactions or targeting the downstream signaling pathways it regulates could be a viable indirect strategy to counter invasive phenotypes in certain cancers.

Genular Protein ID: 3322401314

Symbol: CIP4_HUMAN

Name: Cdc42-interacting protein 4

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9210375

Title: A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton.

PubMed ID: 9210375

DOI: 10.1016/s0960-9822(06)00219-3

PubMed ID: 12054674

Title: Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms.

PubMed ID: 12054674

DOI: 10.1016/s0006-291x(02)00398-4

PubMed ID: 16343437

Title: Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell-cell adhesion: expression and function in renal cell carcinoma.

PubMed ID: 16343437

DOI: 10.1016/j.bbrc.2005.11.117

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15057824

Title: The DNA sequence and biology of human chromosome 19.

PubMed ID: 15057824

DOI: 10.1038/nature02399

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: 7776974

Title: Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor.

PubMed ID: 7776974

DOI: 10.1210/mend.9.2.7776974

PubMed ID: 11294612

Title: Molecular cloning and chromosomal localization of human salt-tolerant protein.

PubMed ID: 11294612

DOI: 10.1023/a:1004132919896

PubMed ID: 10713100

Title: Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules.

PubMed ID: 10713100

DOI: 10.1074/jbc.275.11.7854

PubMed ID: 11069762

Title: Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages.

PubMed ID: 11069762

DOI: 10.1242/jcs.113.23.4165

PubMed ID: 11691828

Title: Altered gene expression pattern in cultured human breast cancer cells treated with hepatocyte growth factor/scatter factor in the setting of DNA damage.

PubMed ID: 11691828

PubMed ID: 11431473

Title: Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1.

PubMed ID: 11431473

DOI: 10.1074/jbc.m103540200

PubMed ID: 12456510

Title: Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup.

PubMed ID: 12456510

DOI: 10.1182/blood-2002-03-0851

PubMed ID: 12604778

Title: Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease.

PubMed ID: 12604778

DOI: 10.1073/pnas.0437967100

PubMed ID: 15047863

Title: AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus.

PubMed ID: 15047863

DOI: 10.1091/mbc.e03-10-0757

PubMed ID: 16326391

Title: Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins.

PubMed ID: 16326391

DOI: 10.1016/j.devcel.2005.11.005

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: 16318909

Title: Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL.

PubMed ID: 16318909

DOI: 10.1016/j.cellsig.2005.10.015

PubMed ID: 16630611

Title: The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics.

PubMed ID: 16630611

DOI: 10.1016/j.yexcr.2006.03.013

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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: 17512409

Title: Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.

PubMed ID: 17512409

DOI: 10.1016/j.cell.2007.03.040

PubMed ID: 19387844

Title: The NMR structure of the TC10- and Cdc42-interacting domain of CIP4.

PubMed ID: 19387844

DOI: 10.1007/s10858-009-9317-z

Sequence Information:

  • Length: 601
  • Mass: 68352
  • Checksum: A9BFE85520C7ABC5
  • Sequence:
  • MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV KKYLPKRPAK 
    DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL ELTKYSQEMK QERKMHFQEG 
    RRAQQQLENG FKQLENSKRK FERDCREAEK AAQTAERLDQ DINATKADVE KAKQQAHLRS 
    HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE 
    VVPIIAKCLE GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL 
    GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP SPRSGRDPLA 
    ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR KRLQQQLEER SRELQKEVDQ 
    REALKKMKDV YEKTPQMGDP ASLEPQIAET LSNIERLKLE VQKYEAWLAE AESRVLSNRG 
    DSLSRHARPP DPPASAPPDS SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS 
    PIGHCVAIYH FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL 
    N

Genular Protein ID: 3954564866

Symbol: W4VSQ9_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 15057824

Title: The DNA sequence and biology of human chromosome 19.

PubMed ID: 15057824

DOI: 10.1038/nature02399

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

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: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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

Sequence Information:

  • Length: 593
  • Mass: 67731
  • Checksum: 888861C16B47568B
  • Sequence:
  • MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV KKYLPKRPAK 
    DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL ELTKYSQEMK QERKMHFQEG 
    RRAQQQLENG FKQLENSKRK FERDCREAEK AAQTAERLDQ DINATKADVE KAKQQAHLRS 
    HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE 
    VVPIIAKCLE GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL 
    GTPSDGRPEL RGPGRSRTKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ LEERSRELQK 
    EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER LKLEVQKYEA WLAEAESRVL 
    SNRGDSLSRH ARPPDPPASA PPDSSSNSAS QDTKESSEEP PSEESQDTPI YTEFDEDFEE 
    EPTSPIGHCV AIYHFEDLGP PPPPSQGPAR ALSLWPRVKT SVLWKKTKGT AGPGSGGKRE 
    ARATCPPPTS ESRSIEPCQR REEGGCRLLL LGHGEPQDLC TLFLTPWLRL RPV