SUMO1 | ENSG00000116030 | NCBI 7341

Details for: SUMO1

Gene ID: 7341

Symbol: SUMO1

Ensembl ID: ENSG00000116030

Description: small ubiquitin like modifier 1

Associated with

Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cytokine signaling in immune system
(R-HSA-1280215)
Disease
(R-HSA-1643685)
Dna double-strand break repair
(R-HSA-5693532)
Dna double strand break response
(R-HSA-5693606)
Formation of incision complex in gg-ner
(R-HSA-5696395)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Global genome nucleotide excision repair (gg-ner)
(R-HSA-5696399)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Interferon gamma signaling
(R-HSA-877300)
Interferon signaling
(R-HSA-913531)
Late sars-cov-2 infection events
(R-HSA-9772573)
Maturation of nucleoprotein
(R-HSA-9694631)
Metabolism of proteins
(R-HSA-392499)
Mitotic anaphase
(R-HSA-68882)
Mitotic metaphase and anaphase
(R-HSA-2555396)
M phase
(R-HSA-68886)
Negative regulation of activity of tfap2 (ap-2) family transcription factors
(R-HSA-8866904)
Nuclear envelope (ne) reassembly
(R-HSA-2995410)
Nucleotide excision repair
(R-HSA-5696398)
Pkr-mediated signaling
(R-HSA-9833482)
Post-translational protein modification
(R-HSA-597592)
Postmitotic nuclear pore complex (npc) reformation
(R-HSA-9615933)
Processing and activation of sumo
(R-HSA-3215018)
Recruitment and atm-mediated phosphorylation of repair and signaling proteins at dna double strand breaks
(R-HSA-5693565)
Regulation of ifng signaling
(R-HSA-877312)
Rna polymerase ii transcription
(R-HSA-73857)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov infections
(R-HSA-9679506)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumo is conjugated to e1 (uba2:sae1)
(R-HSA-3065676)
Sumo is proteolytically processed
(R-HSA-3065679)
Sumo is transferred from e1 to e2 (ube2i, ubc9)
(R-HSA-3065678)
Sumoylation
(R-HSA-2990846)
Sumoylation of chromatin organization proteins
(R-HSA-4551638)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
Sumoylation of dna methylation proteins
(R-HSA-4655427)
Sumoylation of dna replication proteins
(R-HSA-4615885)
Sumoylation of immune response proteins
(R-HSA-4755510)
Sumoylation of intracellular receptors
(R-HSA-4090294)
Sumoylation of nuclear envelope proteins
(R-HSA-9793242)
Sumoylation of rna binding proteins
(R-HSA-4570464)
Sumoylation of sumoylation proteins
(R-HSA-4085377)
Sumoylation of transcription cofactors
(R-HSA-3899300)
Sumoylation of transcription factors
(R-HSA-3232118)
Sumoylation of ubiquitinylation proteins
(R-HSA-3232142)
Transcriptional regulation by the ap-2 (tfap2) family of transcription factors
(R-HSA-8864260)
Translation of structural proteins
(R-HSA-9694635)
Viral infection pathways
(R-HSA-9824446)
Cellular response to cadmium ion
(GO:0071276)
Cellular response to heat
(GO:0034605)
Cytosol
(GO:0005829)
Dna repair
(GO:0006281)
Enzyme binding
(GO:0019899)
Negative regulation of action potential
(GO:0045759)
Negative regulation of delayed rectifier potassium channel activity
(GO:1902260)
Negative regulation of dna-binding transcription factor activity
(GO:0043433)
Negative regulation of dna-templated transcription
(GO:0045892)
Negative regulation of dna binding
(GO:0043392)
Negative regulation of protein import into nucleus
(GO:0042308)
Negative regulation of transcription by transcription factor localization
(GO:0010621)
Nuclear pore
(GO:0005643)
Nucleolus
(GO:0005730)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Plasma membrane
(GO:0005886)
Pml body organization
(GO:0030578)
Positive regulation of atpase-coupled calcium transmembrane transporter activity
(GO:1901896)
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process
(GO:0032436)
Positive regulation of protein-containing complex assembly
(GO:0031334)
Potassium channel regulator activity
(GO:0015459)
Protein binding
(GO:0005515)
Protein localization to nuclear pore
(GO:0090204)
Protein stabilization
(GO:0050821)
Protein sumoylation
(GO:0016925)
Protein tag activity
(GO:0031386)
Regulation of cardiac muscle cell contraction
(GO:0086004)
Regulation of protein localization
(GO:0032880)
Rna binding
(GO:0003723)
Roof of mouth development
(GO:0060021)
Small protein activating enzyme binding
(GO:0044388)
Transcription factor binding
(GO:0008134)
Ubiquitin-like protein ligase binding
(GO:0044389)
Ubiquitin-specific protease binding
(GO:1990381)
Ubiquitin protein ligase binding
(GO:0031625)
Xy body
(GO:0001741)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 439.9364
Cell Significance Index: -68.4300
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 269.5123
Cell Significance Index: -68.3600
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 211.0827
Cell Significance Index: -86.9600
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 189.3576
Cell Significance Index: -89.4000
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 166.3636
Cell Significance Index: -85.5800
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 133.9002
Cell Significance Index: -89.8500
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 67.8613
Cell Significance Index: -83.6700
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 22.6987
Cell Significance Index: -89.5700
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 21.9683
Cell Significance Index: -58.8500
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 17.5552
Cell Significance Index: -53.9200
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 13.1500
Cell Significance Index: -28.7800
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 4.1765
Cell Significance Index: 145.1300
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 4.1578
Cell Significance Index: 87.0300
Cell Name: granulosa cell (CL0000501)
Fold Change: 4.0488
Cell Significance Index: 106.4600
Cell Name: kidney cell (CL1000497)
Fold Change: 3.6960
Cell Significance Index: 29.5100
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 3.2701
Cell Significance Index: 35.5500
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 3.0438
Cell Significance Index: 159.8100
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: 2.7167
Cell Significance Index: 22.8200
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 2.4766
Cell Significance Index: 116.4000
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: 2.3626
Cell Significance Index: 14.5400
Cell Name: cell in vitro (CL0001034)
Fold Change: 2.3050
Cell Significance Index: 1258.8300
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 2.2881
Cell Significance Index: 170.5300
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 2.1952
Cell Significance Index: 301.4600
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 1.9524
Cell Significance Index: 57.3400
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.8940
Cell Significance Index: 232.8900
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 1.7602
Cell Significance Index: 207.5800
Cell Name: theca cell (CL0000503)
Fold Change: 1.6885
Cell Significance Index: 9.9200
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 1.6777
Cell Significance Index: 22.8900
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 1.6745
Cell Significance Index: 740.3400
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 1.5893
Cell Significance Index: 43.2600
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 1.4863
Cell Significance Index: 267.9300
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 1.4709
Cell Significance Index: 16.7100
Cell Name: odontoblast (CL0000060)
Fold Change: 1.4094
Cell Significance Index: 180.6800
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 1.4007
Cell Significance Index: 99.0600
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.3687
Cell Significance Index: 271.6300
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.3073
Cell Significance Index: 262.2500
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 1.2241
Cell Significance Index: 57.0800
Cell Name: lactocyte (CL0002325)
Fold Change: 1.1901
Cell Significance Index: 153.7500
Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.1314
Cell Significance Index: 72.9900
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 1.1086
Cell Significance Index: 318.9700
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.9322
Cell Significance Index: 151.6200
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 0.8924
Cell Significance Index: 25.5800
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.6865
Cell Significance Index: 18.3300
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.5352
Cell Significance Index: 27.8000
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.4500
Cell Significance Index: 161.3900
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.3548
Cell Significance Index: 35.1000
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 0.2601
Cell Significance Index: 2.4000
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.1858
Cell Significance Index: 31.7300
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1198
Cell Significance Index: 22.7900
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.1112
Cell Significance Index: 5.0400
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.1034
Cell Significance Index: 1.7300
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.0793
Cell Significance Index: 60.0000
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.0623
Cell Significance Index: 45.7000
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.0531
Cell Significance Index: 3.3400
Cell Name: peg cell (CL4033014)
Fold Change: 0.0515
Cell Significance Index: 1.1900
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.0455
Cell Significance Index: 0.7800
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0371
Cell Significance Index: 69.9000
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.0046
Cell Significance Index: 0.1000
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0028
Cell Significance Index: -4.3400
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0063
Cell Significance Index: -11.6800
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0080
Cell Significance Index: -5.8900
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: -0.0154
Cell Significance Index: -10.6700
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0220
Cell Significance Index: -29.9500
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0506
Cell Significance Index: -31.6000
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0538
Cell Significance Index: -34.1400
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0677
Cell Significance Index: -6.9200
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.1047
Cell Significance Index: -59.0700
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.1127
Cell Significance Index: -51.1600
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.1409
Cell Significance Index: -1.6800
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.1520
Cell Significance Index: -9.3400
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1672
Cell Significance Index: -35.2200
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.1793
Cell Significance Index: -4.8000
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1866
Cell Significance Index: -21.3800
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -0.2781
Cell Significance Index: -4.9100
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -0.2812
Cell Significance Index: -16.8800
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.2830
Cell Significance Index: -15.8800
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -0.2975
Cell Significance Index: -3.8100
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.3570
Cell Significance Index: -51.9000
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.3779
Cell Significance Index: -44.0400
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.4067
Cell Significance Index: -11.3700
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.4095
Cell Significance Index: -13.1200
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.4223
Cell Significance Index: -48.2100
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.4310
Cell Significance Index: -11.0100
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.4796
Cell Significance Index: -36.8000
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.5390
Cell Significance Index: -42.6900
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.5451
Cell Significance Index: -36.6600
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -0.7326
Cell Significance Index: -13.5400
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.8181
Cell Significance Index: -85.1800
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.8501
Cell Significance Index: -18.1100
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.9882
Cell Significance Index: -29.1100
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -1.0302
Cell Significance Index: -26.4800
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -1.1815
Cell Significance Index: -52.2600
Cell Name: skeletal muscle fibroblast (CL0011027)
Fold Change: -1.3017
Cell Significance Index: -8.8200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -1.3323
Cell Significance Index: -46.8200
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.4239
Cell Significance Index: -87.3000
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -1.4532
Cell Significance Index: -8.7800
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -1.4589
Cell Significance Index: -55.2500
Cell Name: paneth cell of colon (CL0009009)
Fold Change: -1.5496
Cell Significance Index: -23.2200
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: -1.8195
Cell Significance Index: -18.8400
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -1.9435
Cell Significance Index: -63.6300

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.

**Key Characteristics** SUMO1 is a small protein that consists of 96 amino acids and is synthesized as a precursor protein. It is covalently attached to target proteins through a process called sumoylation, which involves the action of SUMO-specific E3 ligases. This modification can alter the function, localization, and stability of the target protein. SUMO1 is also involved in the regulation of transcriptional coactivators, such as p53, and can modulate the activity of transcription factors, including NF-κB and p53. **Pathways and Functions** SUMO1 is involved in various cellular pathways, including: 1. **Cell Cycle Regulation**: SUMO1 plays a crucial role in regulating the cell cycle by modulating the activity of key proteins, such as p53 and cyclin-dependent kinases (CDKs). 2. **DNA Repair**: SUMO1 is involved in the repair of DNA double-strand breaks by recruiting and activating repair proteins, such as ATM and ATR. 3. **Immune Response**: SUMO1 regulates the activity of immune response proteins, such as NF-κB and interferon-gamma (IFN-γ), which are involved in the regulation of immune cell function and cytokine production. 4. **Transcriptional Regulation**: SUMO1 modulates the activity of transcription factors, including p53 and NF-κB, which regulate the expression of genes involved in cell growth, differentiation, and survival. 5. **Protein Degradation**: SUMO1 can regulate the degradation of proteins by modifying the activity of ubiquitin ligases and proteasomes. **Clinical Significance** Dysregulation of SUMO1 has been implicated in various diseases, including: 1. **Cancer**: SUMO1 has been shown to play a role in the regulation of tumor suppressor proteins, such as p53, and can contribute to tumorigenesis. 2. **Autoimmune Disorders**: SUMO1 has been implicated in the regulation of immune response proteins, such as NF-κB, which can contribute to autoimmune diseases, such as rheumatoid arthritis. 3. **Viral Infections**: SUMO1 has been shown to regulate the activity of viral proteins, such as the nucleoprotein of SARS-CoV-2, which can contribute to viral replication and pathogenesis. 4. **Neurological Disorders**: SUMO1 has been implicated in the regulation of neurotransmitter receptors and can contribute to neurological disorders, such as Parkinson's disease. In conclusion, SUMO1 is a critical PTM player that regulates various cellular processes, including cell cycle regulation, DNA repair, and immune response. Its dysregulation has been linked to various diseases, including cancer, autoimmune disorders, and viral infections. Further studies are needed to fully understand the mechanisms by which SUMO1 regulates cellular processes and to explore its potential as a therapeutic target for various diseases.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Small ubiquitin-related modifier 1

Genular Protein ID: 333088824

Symbol: SUMO1_HUMAN

Name: Small ubiquitin-related modifier 1

UniProtKB Accession Codes:

P63165 A8MUS8 B2R4I5 P55856 Q6FGG0 Q6NZ62 Q93068

Database IDs:

Citations:

PubMed ID: 9119407

Title: SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family.

PubMed ID: 9119407

DOI: 10.1006/geno.1996.4556

PubMed ID: 8806687

Title: PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia.

PubMed ID: 8806687

PubMed ID: 8812453

Title: UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins.

PubMed ID: 8812453

DOI: 10.1006/geno.1996.0462

PubMed ID: 9019411

Title: A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2.

PubMed ID: 9019411

DOI: 10.1016/s0092-8674(00)81862-0

PubMed ID: 8978815

Title: A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.

PubMed ID: 8978815

DOI: 10.1083/jcb.135.6.1457

PubMed ID: 8906799

Title: Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin.

PubMed ID: 8906799

PubMed ID: 14702039

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

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15815621

Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

PubMed ID: 15815621

DOI: 10.1038/nature03466

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: 9162015

Title: Preferential modification of nuclear proteins by a novel ubiquitin-like molecule.

PubMed ID: 9162015

DOI: 10.1074/jbc.272.22.14001

PubMed ID: 10574707

Title: Cell cycle regulation of PML modification and ND10 composition.

PubMed ID: 10574707

DOI: 10.1242/jcs.112.24.4581

PubMed ID: 10961991

Title: Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif.

PubMed ID: 10961991

DOI: 10.1074/jbc.m004293200

PubMed ID: 12383504

Title: Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.

PubMed ID: 12383504

DOI: 10.1016/s0378-1119(02)00843-0

PubMed ID: 12924945

Title: Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation.

PubMed ID: 12924945

DOI: 10.1021/bi0345283

PubMed ID: 12565818

Title: The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML.

PubMed ID: 12565818

DOI: 10.1016/s0014-4827(02)00025-3

PubMed ID: 12606074

Title: Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitin-related modifier-1, SUMO-1.

PubMed ID: 12606074

DOI: 10.1016/s0168-1702(02)00312-x

PubMed ID: 12573574

Title: The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9).

PubMed ID: 12573574

DOI: 10.1006/viro.2002.1767

PubMed ID: 15487983

Title: Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1.

PubMed ID: 15487983

DOI: 10.1042/bj20041210

PubMed ID: 15608651

Title: Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection.

PubMed ID: 15608651

DOI: 10.1038/nsmb878

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: 16955485

Title: Functional modulation of parkin through physical interaction with SUMO-1.

PubMed ID: 16955485

DOI: 10.1002/jnr.21041

PubMed ID: 16990542

Title: SUMO1 haploinsufficiency leads to cleft lip and palate.

PubMed ID: 16990542

DOI: 10.1126/science.1128406

PubMed ID: 17956732

Title: RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia.

PubMed ID: 17956732

DOI: 10.1016/j.cell.2007.07.044

PubMed ID: 18707152

Title: Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution.

PubMed ID: 18707152

DOI: 10.1021/pr800368m

PubMed ID: 18538659

Title: Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25.

PubMed ID: 18538659

DOI: 10.1016/j.molcel.2008.03.021

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: 18408734

Title: RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation.

PubMed ID: 18408734

DOI: 10.1038/ncb1716

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: 19223394

Title: SUMOylation regulates Kv2.1 and modulates pancreatic beta-cell excitability.

PubMed ID: 19223394

DOI: 10.1242/jcs.036632

PubMed ID: 20388717

Title: In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.

PubMed ID: 20388717

DOI: 10.1074/jbc.m110.106955

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: 21965678

Title: SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function.

PubMed ID: 21965678

DOI: 10.1074/jbc.m111.267237

PubMed ID: 21829689

Title: SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability.

PubMed ID: 21829689

DOI: 10.1371/journal.pone.0023046

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: 22406621

Title: The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA.

PubMed ID: 22406621

DOI: 10.1158/0008-5472.can-11-3159

PubMed ID: 23086935

Title: PolySUMO-binding proteins identified through a string search.

PubMed ID: 23086935

DOI: 10.1074/jbc.m112.410985

PubMed ID: 22398289

Title: SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function.

PubMed ID: 22398289

DOI: 10.1128/jvi.00314-12

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: 25218447

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

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 24651376

Title: Characterization of nuclear localization and SUMOylation of the ATBF1 transcription factor in epithelial cells.

PubMed ID: 24651376

DOI: 10.1371/journal.pone.0092746

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: 27068747

Title: Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2alpha.

PubMed ID: 27068747

DOI: 10.1074/jbc.m115.713370

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: 9654451

Title: Structure determination of the small ubiquitin-related modifier SUMO-1.

PubMed ID: 9654451

DOI: 10.1006/jmbi.1998.1839

PubMed ID: 15296745

Title: A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex.

PubMed ID: 15296745

DOI: 10.1016/j.str.2004.05.023

PubMed ID: 15660128

Title: Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.

PubMed ID: 15660128

DOI: 10.1038/sj.emboj.7600552

PubMed ID: 16204249

Title: Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation.

PubMed ID: 16204249

DOI: 10.1074/jbc.m507059200

PubMed ID: 15931224

Title: Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.

PubMed ID: 15931224

DOI: 10.1038/nature03588

PubMed ID: 15959518

Title: Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.

PubMed ID: 15959518

DOI: 10.1038/nature03634

PubMed ID: 15723079

Title: SUMO modification of the ubiquitin-conjugating enzyme E2-25K.

PubMed ID: 15723079

DOI: 10.1038/nsmb903

PubMed ID: 16712526

Title: Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease.

PubMed ID: 16712526

DOI: 10.1042/bj20060526

PubMed ID: 17099698

Title: SUMO protease SENP1 induces isomerization of the scissile peptide bond.

PubMed ID: 17099698

DOI: 10.1038/nsmb1172

Sequence Information:

Length: 101
Mass: 11557
Checksum: 89BE97D2D054FB33
Sequence:

MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN 
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V

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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: SUMO1

Associated with

Cells (max top 100)

Other Information

SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family. PubMed ID: 9119407

PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. PubMed ID: 8806687

UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins. PubMed ID: 8812453

A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. PubMed ID: 9019411

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. PubMed ID: 8978815

Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin. PubMed ID: 8906799

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Generation and annotation of the DNA sequences of human chromosomes 2 and 4. PubMed ID: 15815621

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Preferential modification of nuclear proteins by a novel ubiquitin-like molecule. PubMed ID: 9162015

Cell cycle regulation of PML modification and ND10 composition. PubMed ID: 10574707

Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. PubMed ID: 10961991

Molecular features of human ubiquitin-like SUMO genes and their encoded proteins. PubMed ID: 12383504

Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation. PubMed ID: 12924945

The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML. PubMed ID: 12565818

Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitin-related modifier-1, SUMO-1. PubMed ID: 12606074

The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9). PubMed ID: 12573574

Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. PubMed ID: 15487983

Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. PubMed ID: 15608651

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Functional modulation of parkin through physical interaction with SUMO-1. PubMed ID: 16955485

SUMO1 haploinsufficiency leads to cleft lip and palate. PubMed ID: 16990542

RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia. PubMed ID: 17956732

Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution. PubMed ID: 18707152

Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. PubMed ID: 18538659

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. PubMed ID: 18408734

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

SUMOylation regulates Kv2.1 and modulates pancreatic beta-cell excitability. PubMed ID: 19223394

In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification. PubMed ID: 20388717

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function. PubMed ID: 21965678

SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability. PubMed ID: 21829689

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA. PubMed ID: 22406621

PolySUMO-binding proteins identified through a string search. PubMed ID: 23086935

SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function. PubMed ID: 22398289

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

Characterization of nuclear localization and SUMOylation of the ATBF1 transcription factor in epithelial cells. PubMed ID: 24651376

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

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

Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2alpha. PubMed ID: 27068747

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Structure determination of the small ubiquitin-related modifier SUMO-1. PubMed ID: 9654451

A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. PubMed ID: 15296745

Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. PubMed ID: 15660128

Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. PubMed ID: 16204249

Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. PubMed ID: 15931224

Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. PubMed ID: 15959518

SUMO modification of the ubiquitin-conjugating enzyme E2-25K. PubMed ID: 15723079

Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease. PubMed ID: 16712526

SUMO protease SENP1 induces isomerization of the scissile peptide bond. PubMed ID: 17099698