Details for: WIZ

Gene ID: 58525

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: WIZ

Ensembl ID: ENSG00000011451

Description: WIZ zinc finger

Cell Significance Landscape

Associated with

Significant Cells

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

  • melanocyte of skin CL1000458
    CSI 7.2
    rCSI 9.82%
    PRS 86.2
  • neural crest cell CL0011012
    CSI 3.56
    rCSI 2.81%
    PRS 98.08
  • club cell CL0000158
    CSI 2.07
    rCSI 3.03%
    PRS 98.59
  • caudal ganglionic eminence derived cortical interneuron CL4023064
    CSI 1.98
    rCSI 3.5%
    PRS 96.05
  • basal cell of epidermis CL0002187
    CSI 1.78
    rCSI 3.16%
    PRS 85.31

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 [WIZ](/details-gene/58525) (WIZ zinc finger) is a protein-coding gene located on chromosome 19p13.12. It encodes a nuclear protein characterized by multiple zinc finger domains, which are crucial for its function as a DNA-binding transcription factor. Functional annotations suggest that [WIZ](/details-gene/58525) is primarily involved in the negative regulation of gene expression. It acts by binding to DNA and recruiting transcriptional corepressors and histone modifying enzymes, such as histone methyltransferases, to silence target genes ([Link](https://doi.org/10.1016/j.molcel.2008.10.025)). Expression data highlights its significant role in specific cell lineages, particularly in [melanocyte of skin](/details-cell/CL1000458) and their developmental precursors, [neural crest cell](/details-cell/CL0011012), suggesting a key function in cell fate determination and maintenance within these populations. ## Cellular Roles and Expression Landscape The **Overall** expression profile of [WIZ](/details-gene/58525) indicates a highly cell-type-specific role rather than ubiquitous function. Its most significant expression is observed in [melanocyte of skin](/details-cell/CL1000458) (CSI: 7.20), followed by the multipotent embryonic population of [neural crest cell](/details-cell/CL0011012) (CSI: 3.56). This strong association with the neural crest lineage suggests a potential role for [WIZ](/details-gene/58525) in establishing or maintaining the identity of melanocytes. Beyond this primary lineage, [WIZ](/details-gene/58525) also shows notable significance in other diverse cell types, including secretory [club cell](/details-cell/CL0000158) in the lungs (CSI: 2.07), progenitor [basal cell of epidermis](/details-cell/CL0002187) (CSI: 1.78), and a specific neuronal subtype, the [caudal ganglionic eminence derived cortical interneuron](/details-cell/CL4023064) (CSI: 1.98). This pattern suggests that its regulatory functions, while prominent in melanocytes, are also employed in distinct developmental and homeostatic contexts across different tissues. ## Pathways and Molecular Function The functional profile of [WIZ](/details-gene/58525) is centered on its role as a nuclear regulator of transcription. Molecular function annotations confirm its capacity for [DNA-binding transcription factor activity, rna polymerase ii-specific](/details-go/GO:0000981) and [rna polymerase ii cis-regulatory region sequence-specific dna binding](/details-go/GO:0000978). The protein does not appear to act alone; rather, it functions as part of larger protein complexes, as indicated by its binding activities, including [protein binding](/details-go/GO:0005515), [histone methyltransferase binding](/details-go/GO:1990226), and [transcription corepressor binding](/details-go/GO:0001222). This suite of functions positions [WIZ](/details-gene/58525) as a scaffold protein that recruits enzymatic machinery to specific genomic loci to mediate gene silencing. This is consistent with its annotated involvement in the biological process of [regulation of transcription by rna polymerase ii](/details-go/GO:0006357). Additionally, its connection to [positive regulation of nuclear cell cycle dna replication](/details-go/GO:0010571) suggests its transcriptional targets may include key genes that control cell proliferation. The protein is localized to the [nucleus](/details-go/GO:0005634) and specifically the [nucleoplasm](/details-go/GO:0005654), which is consistent with its role in transcription. ## Research Directions The specific expression pattern and molecular function of [WIZ](/details-gene/58525) provide a foundation for several testable hypotheses regarding its biological and potential pathological roles. 1. **Hypothesis 1:** Given its high significance in [melanocyte of skin](/details-cell/CL1000458) and its function as a transcriptional corepressor, [WIZ](/details-gene/58525) may be a critical factor in maintaining melanocyte identity by repressing genes associated with alternative neural crest fates. Dysregulation or mutation of [WIZ](/details-gene/58525) could contribute to melanocyte dedifferentiation, a hallmark of melanoma progression. 2. **Hypothesis 2:** The significant expression of [WIZ](/details-gene/58525) in the mitotically active [basal cell of epidermis](/details-cell/CL0002187), combined with its annotated role in regulating the cell cycle, suggests that it functions as a gatekeeper for epidermal stratification. It may act by silencing pro-proliferative genes to permit terminal differentiation of keratinocytes. **Experimental Approach to Test Hypothesis 1:** To investigate the role of [WIZ](/details-gene/58525) in maintaining melanocyte identity, a CRISPR-Cas9-mediated knockout could be performed in primary human melanocytes or a human melanoma cell line. The resulting cellular phenotype could be assessed for changes in morphology, pigmentation, and proliferation. Transcriptomic analysis (RNA-seq) would identify genes that are derepressed upon [WIZ](/details-gene/58525) loss, while chromatin immunoprecipitation sequencing (ChIP-seq) for [WIZ](/details-gene/58525) and associated histone marks (e.g., H3K9me2, H3K27me3) would map its direct genomic targets and reveal its epigenetic mechanism of action. **Therapeutic Potential:** As an intracellular DNA-binding protein, [WIZ](/details-gene/58525) is a challenging direct target for conventional biologics like antibodies. However, its function appears to be dependent on protein-protein interactions, particularly with histone methyltransferases. If aberrant [WIZ](/details-gene/58525) activity is implicated in diseases like melanoma, developing small molecules to disrupt these critical interactions could represent a viable therapeutic strategy. Such an approach would aim for the **inhibition** of its repressive function, potentially reactivating tumor suppressor genes that it silences.

Genular Protein ID: 3053042663

Symbol: WIZ_HUMAN

Name: Protein Wiz

UniProtKB Accession Codes:

O95785 B3KVH1 B7ZM82 M0QY21 Q4G0E0 Q6P6B0 Q6ZN24 Q7LDY6 Q7LDZ1 Q96IG5 Q96SQ6 Q9BUR8 Q9NPT1

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CTD 1 ChEMBL 1 ChiTaRS 1 DNASU 1 EMBL 13 Ensembl 2 ExpressionAtlas 1 GO 13 Gene3D 1 GeneCards 1 GeneTree 1 GenomeRNAi 1 GlyGen 1 HGNC 1 HPA 1 InParanoid 1 IntAct 1 InterPro 3 KEGG 1 MIM 1 MINT 1 MassIVE 1 NCBI Taxonomy 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PIR 1 PRO 1 PROSITE 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 4 Pumba 1 RNAct 1 RefSeq 2 SMART 1 STRING 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TreeFam 1 UCSC 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

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: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

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: 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: 19061646

Title: CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation.

PubMed ID: 19061646

DOI: 10.1016/j.molcel.2008.10.025

PubMed ID: 18438403

Title: Protein lysine methyltransferase G9a acts on non-histone targets.

PubMed ID: 18438403

DOI: 10.1038/nchembio.88

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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: 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: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

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

Sequence Information:

  • Length: 1651
  • Mass: 178674
  • Checksum: 9DB0485964578310
  • Sequence:
    • MEGSLAGSLA APDRPQGPER LPGPAPRENI EGGAEAAEGE GGIFRSTRYL PVTKEGPRDI 
LDGRGGISGT PDGRGPWEHP LVQEAGEGIL SERRFEDSVI VRTMKPHAEL EGSRRFLHHR 
GEPRLLEKHA QGRPRFDWLQ DEDEQGSPQD AGLHLDLPAQ PPPLAPFRRV FVPVEDTPKT 
LDMAVVGGRE DLEDLEGLAQ PSEWGLPTSA SEVATQTWTV NSEASVERLQ PLLPPIRTGP 
YLCELLEEVA EGVASPDEDE DEEPAVFPCI ECSIYFKQKE HLLEHMSQHR RAPGQEPPAD 
LAPLACGECG WAFADPTALE QHRQLHQASR EKIIEEIQKL KQVPGDEGRE ARLQCPKCVF 
GTNSSRAYVQ HAKLHMREPP GQTTKEPFGG SSGAGSPSPE ASALLYQPYG AAVGLSACVF 
CGFPAPSESL LREHVRLVHA HPHWEEDGEA YEEDPASQPG TSQDAHACFP DTAVDYFGKA 
EPSLAPMWRE NPAGYDPSLA FGPGCQQLSI RDFPLSKPLL HGTGQRPLGR LAFPSTLAST 
PYSLQLGRNK STVHPQGLGE RRRPWSEEEE EEEEEEDVVL TSEMDFSPEN GVFSPLATPS 
LIPQAALELK QAFREALQAV EATQGQQQQL RGMVPIVLVA KLGPQVMAAA RVPPRLQPEE 
LGLAGAHPLD FLLLDAPLGG PLGLDTLLDG DPAMALKHEE RKCPYCPDRF HNGIGLANHV 
RGHLNRVGVS YNVRHFISAE EVKAIERRFS FQKKKKKVAN FDPGTFSLMR CDFCGAGFDT 
RAGLSSHARA HLRDFGITNW ELTVSPINIL QELLATSAAE QPPSPLGREP GGPPGSFLTS 
RRPRLPLTVP FPPTWAEDPG PAYGDAQSLT TCEVCGACFE TRKGLSSHAR SHLRQLGVAE 
SESSGAPIDL LYELVKQKGL PDAHLGLPPG LAKKSSSLKE VVAGAPRPGL LSLAKPLDAP 
AVNKAIKSPP GFSAKGLGHP PSSPLLKKTP LALAGSPTPK NPEDKSPQLS LSPRPASPKA 
QWPQSEDEGP LNLTSGPEPA RDIRCEFCGE FFENRKGLSS HARSHLRQMG VTEWYVNGSP 
IDTLREILKR RTQSRPGGPP NPPGPSPKAL AKMMGGAGPG SSLEARSPSD LHISPLAKKL 
PPPPGSPLGH SPTASPPPTA RKMFPGLAAP SLPKKLKPEQ IRVEIKREML PGALHGELHP 
SEGPWGAPRE DMTPLNLSSR AEPVRDIRCE FCGEFFENRK GLSSHARSHL RQMGVTEWSV 
NGSPIDTLRE ILKKKSKPCL IKKEPPAGDL APALAEDGPP TVAPGPVQSP LPLSPLAGRP 
GKPGAGPAQV PRELSLTPIT GAKPSATGYL GSVAAKRPLQ EDRLLPAEVK AKTYIQTELP 
FKAKTLHEKT SHSSTEACCE LCGLYFENRK ALASHARAHL RQFGVTEWCV NGSPIETLSE 
WIKHRPQKVG AYRSYIQGGR PFTKKFRSAG HGRDSDKRPS LGLAPGGLAV VGRSAGGEPG 
PEAGRAADGG ERPLAASPPG TVKAEEHQRQ NINKFERRQA RPPDASAARG GEDTNDLQQK 
LEEVRQPPPR VRPVPSLVPR PPQTSLVKFV GNIYTLKCRF CEVEFQGPLS IQEEWVRHLQ 
RHILEMNFSK ADPPPEESQA PQAQTAAAEA P

Genular Protein ID: 2931687639

Symbol: M0QXA7_HUMAN

Name: N/A

UniProtKB Accession Codes:

M0QXA7

Database IDs:

AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID-ORCS 1 CTD 1 ChiTaRS 1 DNASU 1 EMBL 3 Ensembl 2 ExpressionAtlas 1 GO 2 GeneTree 1 HGNC 1 IntAct 1 InterPro 3 MINT 1 MassIVE 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 3 PROSITE-ProRule 1 PeptideAtlas 2 Pfam 1 Proteomes 2 ProteomicsDB 1 RefSeq 3 SAM 1 SMART 1 SUPFAM 1 UCSC 1 VEuPathDB 1

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

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: 16964243

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

PubMed ID: 16964243

DOI: 10.1038/nbt1240

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: 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: 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: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.O114.044792

PubMed ID: 28112733

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

PubMed ID: 28112733

Sequence Information:

  • Length: 968
  • Mass: 103279
  • Checksum: AF8BB4E5A5BE125C
  • Sequence:
    • MVAMDLGSPS LPKKSLPVPG ALEQVASRLS SKVAAEVPHG SKQELQDLKA QSLTTCEVCG 
ACFETRKGLS SHARSHLRQL GVAESESSGA PIDLLYELVK QKGLPDAHLG LPPGLAKKSS 
SLKEVVAGAP RPGLLSLAKP LDAPAVNKAI KSPPGFSAKG LGHPPSSPLL KKTPLALAGS 
PTPKNPEDKS PQLSLSPRPA SPKAQWPQSE DEGPLNLTLD SDGGRELDCQ LCGAWFETRK 
GLSSHARAHL RHLGVSDPDA KGSPIDVLHG LIRRDGVQIR LPPRRGALAH PGRPPPTSAA 
LSLLPPPPPA KKAKLKAAGM ASPWGKQDLS AAAAAGIFWA SDVEPSPLNL SSGPEPARDI 
RCEFCGEFFE NRKGLSSHAR SHLRQMGVTE WYVNGSPIDT LREILKRRTQ SRPGGPPNPP 
GPSPKALAKM MGGAGPGSSL EARSPSDLHI SPLAKKLPPP PGSPLGHSPT ASPPPTARKM 
FPGLAAPSLP KKLKPEQIRV EIKREMLPGA LHGELHPSEG PWGAPREDMT PLNLSSRAEP 
VRDIRCEFCG EFFENRKGLS SHARSHLRQM GVTEWSVNGS PIDTLREILK KKSKPCLIKK 
EPPAGDLAPA LAEDGPPTVA PGPVQSPLPL SPLAGRPGKP GAGPAQVPRE LSLTPITGAK 
PSATGYLGSV AAKRPLQEDR LLPAEVKAKT YIQTELPFKA KTLHEKTSHS STEACCELCG 
LYFENRKALA SHARAHLRQF GVTEWCVNGS PIETLSEWIK HRPQKVGAYR SYIQGGRPFT 
KKFRSAGHGR DSDKRPSLGL APGGLAVVGR SAGGEPGPEA GRAADGGERP LAASPPGTVK 
AEEHQRQNIN KFERRQARPP DASAARGGED TNDLQQKLEE VRQPPPRVRP VPSLVPRPPQ 
TSLVKFVGNI YTLKCRFCEV EFQGPLSIQE EWVRHLQRHI LEMNFSKADP PPEESQAPQA 
QTAAAEAP

Genular Protein ID: 1370899787

Symbol: A0A2R8YFV2_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A2R8YFV2

Database IDs:

Antibodypedia 1 Bgee 1 CTD 1 ChiTaRS 1 DNASU 1 EMBL 3 Ensembl 2 ExpressionAtlas 1 GO 2 Gene3D 1 GeneTree 1 HGNC 1 InterPro 3 MassIVE 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 3 PROSITE-ProRule 1 PeptideAtlas 2 Pfam 1 Proteomes 2 ProteomicsDB 1 RefSeq 1 SAM 1 SMART 1 SUPFAM 1 VEuPathDB 1

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

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: 16964243

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

PubMed ID: 16964243

DOI: 10.1038/nbt1240

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: 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: 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: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.O114.044792

PubMed ID: 28112733

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

PubMed ID: 28112733

Sequence Information:

  • Length: 1699
  • Mass: 183745
  • Checksum: 93688CB1B8FBE529
  • Sequence:
    • MEGSLAGSLA APDRPQGPER LPGPAPRENI EGGAEAAEGE GGIFRSTRYL PVTKEGPRDI 
LDGRGGISDG QPHPGLSEAL PRVTSATHRI SSCCWDGGSL DFRPGSPPPH LLGHFPGTPD 
GRGPWEHPLV QEAGEGILSE RRFEDSVIVR TMKPHAELEG SRRFLHHRGE PRLLEKHAQG 
RPRFDWLQDE DEQGSPQDAG LHLDLPAQPP PLAPFRRVFV PVEDTPKTLD MAVVGGREDL 
EDLEGLAQPS EWGLPTSASE VATQTWTVNS EASVERLQPL LPPIRTGPYL CELLEEVAEG 
VASPDEDEDE EPAVFPCIEC SIYFKQKEHL LEHMSQHRRA PGQEPPADLA PLACGECGWA 
FADPTALEQH RQLHQASREK IIEEIQKLKQ VPGDEGREAR LQCPKCVFGT NSSRAYVQHA 
KLHMREPPGQ TTKEPFGGSS GAGSPSPEAS ALLYQPYGAA VGLSACVFCG FPAPSESLLR 
EHVRLVHAHP HWEEDGEAYE EDPASQPGTS QDAHACFPDT AVDYFGKAEP SLAPMWRENP 
AGYDPSLAFG PGCQQLSIRD FPLSKPLLHG TGQRPLGRLA FPSTLASTPY SLQLGRNKST 
VHPQGLGERR RPWSEEEEEE EEEEDVVLTS EMDFSPENGV FSPLATPSLI PQAALELKQA 
FREALQAVEA TQGQQQQLRG MVPIVLVAKL GPQVMAAARV PPRLQPEELG LAGAHPLDFL 
LLDAPLGGPL GLDTLLDGDP AMALKHEERK CPYCPDRFHN GIGLANHVRG HLNRVGVSYN 
VRHFISAEEV KAIERRFSFQ KKKKKVANFD PGTFSLMRCD FCGAGFDTRA GLSSHARAHL 
RDFGITNWEL TVSPINILQE LLATSAAEQP PSPLGREPGG PPGSFLTSRR PRLPLTVPFP 
PTWAEDPGPA YGDAQSLTTC EVCGACFETR KGLSSHARSH LRQLGVAESE SSGAPIDLLY 
ELVKQKGLPD AHLGLPPGLA KKSSSLKEVV AGAPRPGLLS LAKPLDAPAV NKAIKSPPGF 
SAKGLGHPPS SPLLKKTPLA LAGSPTPKNP EDKSPQLSLS PRPASPKAQW PQSEDEGPLN 
LTSGPEPARD IRCEFCGEFF ENRKGLSSHA RSHLRQMGVT EWYVNGSPID TLREILKRRT 
QSRPGGPPNP PGPSPKALAK MMGGAGPGSS LEARSPSDLH ISPLAKKLPP PPGSPLGHSP 
TASPPPTARK MFPGLAAPSL PKKLKPEQIR VEIKREMLPG ALHGELHPSE GPWGAPREDM 
TPLNLSSRAE PVRDIRCEFC GEFFENRKGL SSHARSHLRQ MGVTEWSVNG SPIDTLREIL 
KKKSKPCLIK KEPPAGDLAP ALAEDGPPTV APGPVQSPLP LSPLAGRPGK PGAGPAQVPR 
ELSLTPITGA KPSATGYLGS VAAKRPLQED RLLPAEVKAK TYIQTELPFK AKTLHEKTSH 
SSTEACCELC GLYFENRKAL ASHARAHLRQ FGVTEWCVNG SPIETLSEWI KHRPQKVGAY 
RSYIQGGRPF TKKFRSAGHG RDSDKRPSLG LAPGGLAVVG RSAGGEPGPE AGRAADGGER 
PLAASPPGTV KAEEHQRQNI NKFERRQARP PDASAARGGE DTNDLQQKLE EVRQPPPRVR 
PVPSLVPRPP QTSLVKFVGN IYTLKCRFCE VEFQGPLSIQ EEWVRHLQRH ILEMNFSKAD 
PPPEESQAPQ AQTAAAEAP