| UniProt ID | RUVB1_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y265 | |
| Protein Name | RuvB-like 1 | |
| Gene Name | RUVBL1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 456 | |
| Subcellular Localization | Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol, although it is also present in t | |
| Protein Description | Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.; Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.; Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation.; May be able to bind plasminogen at cell surface and enhance plasminogen activation.. | |
| Protein Sequence | MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKKMAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKINGKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Sumoylation | ------MKIEEVKST ------CCHHHCCCC | 59.84 | - | |
| 2 | Sumoylation | ------MKIEEVKST ------CCHHHCCCC | 59.84 | 28112733 | |
| 2 | Acetylation | ------MKIEEVKST ------CCHHHCCCC | 59.84 | 19608861 | |
| 2 | Ubiquitination | ------MKIEEVKST ------CCHHHCCCC | 59.84 | 19608861 | |
| 7 (in isoform 2) | Ubiquitination | - | 45.42 | - | |
| 7 | Ubiquitination | -MKIEEVKSTTKTQR -CCHHHCCCCCCHHH | 45.42 | - | |
| 17 | Phosphorylation | TKTQRIASHSHVKGL CCHHHHHHCCCCCCC | 24.13 | 30266825 | |
| 19 | Phosphorylation | TQRIASHSHVKGLGL HHHHHHCCCCCCCCC | 27.72 | 30266825 | |
| 22 | Ubiquitination | IASHSHVKGLGLDES HHHCCCCCCCCCCCC | 42.89 | 21890473 | |
| 22 (in isoform 1) | Ubiquitination | - | 42.89 | 21890473 | |
| 22 (in isoform 2) | Ubiquitination | - | 42.89 | 21890473 | |
| 29 | Phosphorylation | KGLGLDESGLAKQAA CCCCCCCCHHHHHHH | 38.48 | 21815630 | |
| 33 | Ubiquitination | LDESGLAKQAASGLV CCCCHHHHHHHHHHC | 45.58 | 21906983 | |
| 33 (in isoform 2) | Ubiquitination | - | 45.58 | 21890473 | |
| 33 | Acetylation | LDESGLAKQAASGLV CCCCHHHHHHHHHHC | 45.58 | 25953088 | |
| 33 (in isoform 1) | Ubiquitination | - | 45.58 | 21890473 | |
| 49 | Glutathionylation | QENAREACGVIVELI HHHHHHHHHHHHHHH | 3.71 | 22555962 | |
| 57 | Ubiquitination | GVIVELIKSKKMAGR HHHHHHHHCCCCCCC | 69.70 | - | |
| 74 | Phosphorylation | LLAGPPGTGKTALAL EECCCCCCHHHHHHH | 41.08 | 23911959 | |
| 76 (in isoform 2) | Ubiquitination | - | 30.38 | 21890473 | |
| 76 | Ubiquitination | AGPPGTGKTALALAI CCCCCCHHHHHHHHH | 30.38 | 21906983 | |
| 76 (in isoform 1) | Ubiquitination | - | 30.38 | 21890473 | |
| 77 | Phosphorylation | GPPGTGKTALALAIA CCCCCHHHHHHHHHH | 28.40 | 21712546 | |
| 89 | Phosphorylation | AIAQELGSKVPFCPM HHHHHHCCCCCCCCC | 43.00 | 21712546 | |
| 113 | Sulfoxidation | IKKTEVLMENFRRAI CCHHHHHHHHHHHHH | 4.83 | 21406390 | |
| 128 | Acetylation | GLRIKETKEVYEGEV CCEEEECCEEECCCC | 46.40 | 26051181 | |
| 141 | Glutathionylation | EVTELTPCETENPMG CCEEECCCCCCCCCC | 9.47 | 22555962 | |
| 143 | Phosphorylation | TELTPCETENPMGGY EEECCCCCCCCCCCC | 48.02 | 22210691 | |
| 147 | Sulfoxidation | PCETENPMGGYGKTI CCCCCCCCCCCCHHH | 11.10 | 28465586 | |
| 152 | Acetylation | NPMGGYGKTISHVII CCCCCCCHHHEEEEE | 33.91 | 26051181 | |
| 152 | Ubiquitination | NPMGGYGKTISHVII CCCCCCCHHHEEEEE | 33.91 | - | |
| 153 | Phosphorylation | PMGGYGKTISHVIIG CCCCCCHHHEEEEEE | 24.29 | 20068231 | |
| 155 | Phosphorylation | GGYGKTISHVIIGLK CCCCHHHEEEEEECC | 19.55 | 20068231 | |
| 162 | Acetylation | SHVIIGLKTAKGTKQ EEEEEECCCCCCCCE | 41.02 | 25953088 | |
| 162 (in isoform 2) | Ubiquitination | - | 41.02 | - | |
| 162 | Ubiquitination | SHVIIGLKTAKGTKQ EEEEEECCCCCCCCE | 41.02 | - | |
| 163 | Phosphorylation | HVIIGLKTAKGTKQL EEEEECCCCCCCCEE | 38.35 | 20068231 | |
| 167 | Phosphorylation | GLKTAKGTKQLKLDP ECCCCCCCCEEECCH | 18.21 | 20068231 | |
| 171 | Ubiquitination | AKGTKQLKLDPSIFE CCCCCEEECCHHHHH | 48.64 | 21890473 | |
| 171 (in isoform 2) | Ubiquitination | - | 48.64 | 21890473 | |
| 171 (in isoform 1) | Ubiquitination | - | 48.64 | 21890473 | |
| 171 | Acetylation | AKGTKQLKLDPSIFE CCCCCEEECCHHHHH | 48.64 | 23954790 | |
| 179 | Phosphorylation | LDPSIFESLQKERVE CCHHHHHHHHHHHHC | 25.92 | 21712546 | |
| 182 | Acetylation | SIFESLQKERVEAGD HHHHHHHHHHHCCCC | 53.43 | 25953088 | |
| 182 (in isoform 1) | Ubiquitination | - | 53.43 | 21890473 | |
| 182 (in isoform 2) | Ubiquitination | - | 53.43 | 21890473 | |
| 182 | Ubiquitination | SIFESLQKERVEAGD HHHHHHHHHHHCCCC | 53.43 | 21906983 | |
| 192 | Phosphorylation | VEAGDVIYIEANSGA HCCCCEEEEECCCCC | 7.80 | - | |
| 201 (in isoform 2) | Ubiquitination | - | 38.17 | 21890473 | |
| 201 | Acetylation | EANSGAVKRQGRCDT ECCCCCCEECCCCCC | 38.17 | 26051181 | |
| 201 (in isoform 1) | Ubiquitination | - | 38.17 | 21890473 | |
| 201 | Ubiquitination | EANSGAVKRQGRCDT ECCCCCCEECCCCCC | 38.17 | 21906983 | |
| 205 | Methylation | GAVKRQGRCDTYATE CCCEECCCCCCEEEE | 13.55 | 126257617 | |
| 225 | Ubiquitination | EEYVPLPKGDVHKKK HHHCCCCCCCCCCCH | 75.36 | - | |
| 225 | Sumoylation | EEYVPLPKGDVHKKK HHHCCCCCCCCCCCH | 75.36 | - | |
| 225 | Sumoylation | EEYVPLPKGDVHKKK HHHCCCCCCCCCCCH | 75.36 | 25114211 | |
| 232 | Acetylation | KGDVHKKKEIIQDVT CCCCCCCHHHEECCC | 59.97 | 11791605 | |
| 239 | Phosphorylation | KEIIQDVTLHDLDVA HHHEECCCHHHHHHH | 27.02 | - | |
| 274 | Ubiquitination | KKTEITDKLRGEINK CCCCCHHHHHHHHHH | 31.28 | - | |
| 274 | Acetylation | KKTEITDKLRGEINK CCCCCHHHHHHHHHH | 31.28 | 25953088 | |
| 281 (in isoform 2) | Ubiquitination | - | 53.90 | 21890473 | |
| 281 (in isoform 1) | Ubiquitination | - | 53.90 | 21890473 | |
| 281 | Ubiquitination | KLRGEINKVVNKYID HHHHHHHHHHHHHHH | 53.90 | 21906983 | |
| 281 | Acetylation | KLRGEINKVVNKYID HHHHHHHHHHHHHHH | 53.90 | 27452117 | |
| 321 | Phosphorylation | YLHRALESSIAPIVI HHHHHHHCCCCCEEE | 28.09 | 27050516 | |
| 322 | Phosphorylation | LHRALESSIAPIVIF HHHHHHCCCCCEEEE | 17.25 | 25693802 | |
| 331 | Phosphorylation | APIVIFASNRGNCVI CCEEEEECCCCCEEE | 19.13 | 21712546 | |
| 346 | Phosphorylation | RGTEDITSPHGIPLD ECCCCCCCCCCCCHH | 18.42 | - | |
| 363 | Phosphorylation | DRVMIIRTMLYTPQE HHHHHHHHHHCCHHH | 10.91 | 20068231 | |
| 366 | Phosphorylation | MIIRTMLYTPQEMKQ HHHHHHHCCHHHHHH | 12.93 | 24043423 | |
| 367 | Phosphorylation | IIRTMLYTPQEMKQI HHHHHHCCHHHHHHH | 17.97 | 24043423 | |
| 372 | Ubiquitination | LYTPQEMKQIIKIRA HCCHHHHHHHHHHHH | 37.28 | - | |
| 372 | Acetylation | LYTPQEMKQIIKIRA HCCHHHHHHHHHHHH | 37.28 | 25953088 | |
| 387 | Phosphorylation | QTEGINISEEALNHL HCCCCCCCHHHHHHH | 25.54 | 24719451 | |
| 400 | Ubiquitination | HLGEIGTKTTLRYSV HHHHCCCHHHHHEEE | 34.01 | 21890473 | |
| 400 (in isoform 1) | Ubiquitination | - | 34.01 | 21890473 | |
| 411 | Phosphorylation | RYSVQLLTPANLLAK HEEEEECCHHHHHHH | 29.02 | - | |
| 418 | Ubiquitination | TPANLLAKINGKDSI CHHHHHHHHCCCCCC | 36.35 | - | |
| 427 | Ubiquitination | NGKDSIEKEHVEEIS CCCCCCCHHHHHHHH | 51.99 | - | |
| 438 | Phosphorylation | EEISELFYDAKSSAK HHHHHHHCHHHHHHH | 27.84 | - | |
| 441 | Ubiquitination | SELFYDAKSSAKILA HHHHCHHHHHHHHHH | 41.88 | - | |
| 445 | Sumoylation | YDAKSSAKILADQQD CHHHHHHHHHHHHHH | 39.95 | 28112733 | |
| 445 (in isoform 1) | Ubiquitination | - | 39.95 | 21890473 | |
| 445 | Ubiquitination | YDAKSSAKILADQQD CHHHHHHHHHHHHHH | 39.95 | 2190698 | |
| 453 | Acetylation | ILADQQDKYMK---- HHHHHHHHHCC---- | 42.79 | 19608861 | |
| 454 | Phosphorylation | LADQQDKYMK----- HHHHHHHHCC----- | 20.58 | 25106551 | |
| 456 | Acetylation | DQQDKYMK------- HHHHHHCC------- | 54.84 | 61239 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 239 | T | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RUVB1_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RUVB1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2 AND LYS-453, AND MASSSPECTROMETRY. | |
