Q86U86 · PB1_HUMAN
- ProteinProtein polybromo-1
- GenePBRM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1689 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 1379-1447 | HMG box | ||||
Sequence: RKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEERAAKVAEQQERERAAQQ |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein polybromo-1
- Short nameshPB1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86U86
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Renal cell carcinoma (RCC)
- Note
- DescriptionRenal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype.
- See alsoMIM:144700
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_064653 | 49 | found in a lung cancer cell line; dbSNP:rs542945393 | |||
Sequence: V → L | ||||||
Natural variant | VAR_064654 | 56 | found in a brain cancer cell line; dbSNP:rs923060956 | |||
Sequence: T → A | ||||||
Natural variant | VAR_064655 | 57 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: Missing | ||||||
Natural variant | VAR_064656 | 66 | found in a colon cancer cell line; dbSNP:rs368888772 | |||
Sequence: R → G | ||||||
Natural variant | VAR_064657 | 90 | found in a bladder cancer cell line | |||
Sequence: Q → E | ||||||
Natural variant | VAR_064658 | 144 | found in a malignant melanoma cell line; dbSNP:rs2153927262 | |||
Sequence: Y → F | ||||||
Natural variant | VAR_064659 | 160 | found in a malignant melanoma cell line | |||
Sequence: E → A | ||||||
Natural variant | VAR_064660 | 202 | found in a endometrial cancer cell line; dbSNP:rs765525545 | |||
Sequence: R → C | ||||||
Natural variant | VAR_064661 | 206 | found in hematopoietic and lymphoid cancer cell lines; dbSNP:rs1359676390 | |||
Sequence: E → K | ||||||
Natural variant | VAR_064662 | 226 | found in hematopoietic and lymphoid cancer cell lines | |||
Sequence: E → G | ||||||
Natural variant | VAR_064663 | 228 | found in a breast cancer cell line; dbSNP:rs201022657 | |||
Sequence: I → V | ||||||
Natural variant | VAR_064664 | 232 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: T → P | ||||||
Natural variant | VAR_064665 | 233 | found in a renal carcinoma cell line | |||
Sequence: I → T | ||||||
Natural variant | VAR_064666 | 256 | found in an ovary carcinoma cell line; dbSNP:rs776146971 | |||
Sequence: A → T | ||||||
Natural variant | VAR_064667 | 340 | found in a malignant melanoma cell line; dbSNP:rs200106731 | |||
Sequence: G → A | ||||||
Natural variant | VAR_064668 | 523 | found in a case of clear cell renal carcinoma; somatic mutation; dbSNP:rs2153490743 | |||
Sequence: M → I | ||||||
Natural variant | VAR_064669 | 540 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: R → S | ||||||
Natural variant | VAR_064670 | 597 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: A → D | ||||||
Natural variant | VAR_064671 | 621 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: K → E | ||||||
Natural variant | VAR_064672 | 661 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: K → N | ||||||
Natural variant | VAR_064673 | 674 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: D → E | ||||||
Natural variant | VAR_064674 | 678 | in dbSNP:rs1422119249 | |||
Sequence: R → C | ||||||
Natural variant | VAR_064675 | 893 | found in hematopoietic, lymphoid, lung and liver cancer cell lines; dbSNP:rs753344888 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_064676 | 895 | found in a lung cancer cell line | |||
Sequence: T → S | ||||||
Natural variant | VAR_064677 | 922 | found in a breast cancer cell line | |||
Sequence: E → Q | ||||||
Natural variant | VAR_064678 | 925 | found in a colon cancer cell line | |||
Sequence: K → Q | ||||||
Natural variant | VAR_064679 | 1079 | found in a colon cancer cell line; requires 2 nucleotide substitutions | |||
Sequence: P → Y | ||||||
Natural variant | VAR_064680 | 1098 | found in hematopoietic and lymphoid cancer cell lines; dbSNP:rs201156614 | |||
Sequence: A → S | ||||||
Natural variant | VAR_064681 | 1120 | found in hematopoietic and lymphoid cancer cell lines; dbSNP:rs35102895 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_064682 | 1177 | found in a kidney cancer cell line | |||
Sequence: G → S | ||||||
Natural variant | VAR_064683 | 1204 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: H → P | ||||||
Natural variant | VAR_064684 | 1209-1214 | found in a case of clear cell renal carcinoma; somatic mutation | |||
Sequence: Missing | ||||||
Natural variant | VAR_064685 | 1287 | found in a breast cancer cell line; dbSNP:rs2084387436 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_064686 | 1414 | found in a lung cancer cell line; dbSNP:rs2153489547 | |||
Sequence: G → E | ||||||
Natural variant | VAR_064687 | 1503 | found in a stomach cancer cell line | |||
Sequence: G → C | ||||||
Natural variant | VAR_064688 | 1560 | found in an endometrial cancer cell line | |||
Sequence: Q → H | ||||||
Natural variant | VAR_064689 | 1614 | found in a case of clear cell renal carcinoma; somatic mutation; dbSNP:rs2080680257 | |||
Sequence: I → N | ||||||
Natural variant | VAR_064690 | 1647 | found in a breast cancer cell line; dbSNP:rs200020801 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4,661 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000211207 | 1-1689 | UniProt | Protein polybromo-1 | |||
Sequence: MGSKRRRATSPSSSVSGDFDDGHHSVSTPGPSRKRRRLSNLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDVNLLTADFQLLFNNAKSYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTVTEGSSPAYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVFKDANSIKKIFYMKKAEIEHHEMAKSSLRMRTPSNLAAARLTGPSHSKGSLGEERNPTSKYYRNKRAVQGGRLSAITMALQYGSESEEDAALAAARYEEGESEAESITSFMDVSNPFYQLYDTVRSCRNNQGQLIAEPFYHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIYKRVLKLQQVMQAKKKELARRDDIEDGDSMISSATSDTGSAKRKSKKNIRKQRMKILFNVVLEAREPGSGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMIEDMKLMFRNARHYNEEGSQVYNDAHILEKLLKEKRKELGPLPDDDDMASPKLKLSRKSGISPKKSKYMTPMQQKLNEVYEAVKNYTDKRGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIYKDALVLHKVLLETRRDLEGDEDSHVPNVTLLIQELIHNLFVSVMSHQDDEGRCYSDSLAEIPAVDPNFPNKPPLTFDIIRKNVENNRYRRLDLFQEHMFEVLERARRMNRTDSEIYEDAVELQQFFIKIRDELCKNGEILLSPALSYTTKHLHNDVEKERKEKLPKEIEEDKLKREEEKREAEKSEDSSGAAGLSGLHRTYSQDCSFKNSMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPENFRDEDVFVCESRYSAKTKSFKKIKLWTMPISSVRFVPRDVPLPVVRVASVFANADKGDDEKNTDNSEDSRAEDNFNLEKEKEDVPVEMSNGEPGCHYFEQLHYNDMWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMTCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFKGLKRFSLSAKVVDDEIYYFRKPIVPQKEPSPLLEKKIQLLEAKFAELEGGDDDIEEMGEEDSEVIEPPSLPQLQTPLASELDLMPYTPPQSTPKSAKGSAKKEGSKRKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEERAAKVAEQQERERAAQQQQPSASPRAGTPVGALMGVVPPPTPMGMLNQQLTPVAGMMGGYPPGLPPLQGPVDGLVSMGSMQPLHPGGPPPHHLPPGVPGLPGIPPPGVMNQGVAPMVGTPAPGGSPYGQQVGVLGPPGQQAPPPYPGPHPAGPPVIQQPTTPMFVAPPPKTQRLLHSEAYLKYIEGLSAESNSISKWDQTLAARRRDVHLSKEQESRLPSHWLKSKGAHTTMADALWRLRDLMLRDTLNIRQAYNLENV | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 10 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 16 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 39 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 96 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 131 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 134 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 154 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 178 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 210 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 316 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 316 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 319 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 351 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 353 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 355 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 371 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 375 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 414 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 425 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 471 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 498 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 498 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 502 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 505 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 509 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 509 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 511 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 591 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 636 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 636 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 638 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 648 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 648 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 653 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 689 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 931 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 934 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 935 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 946 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 948 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 948 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 952 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 987 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 987 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1099 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1106 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1111 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1119 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1119 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1167 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1289 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 1293 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 1293 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 1308 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1398 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1405 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1405 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1410 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1453 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1642 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1654 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1656 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with acetylated 'Lys-14' of histone H3 (H3K14ac), and may also interact with other acetylated or methylated Lys residues on histone H3
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86U86 | ARID2 Q68CP9 | 5 | EBI-637807, EBI-637818 | |
BINARY | Q86U86 | BRD1 O95696-1 | 2 | EBI-637807, EBI-11700916 | |
BINARY | Q86U86 | BRD1 O95696-2 | 2 | EBI-637807, EBI-11017508 | |
BINARY | Q86U86 | CHD7 Q9P2D1 | 4 | EBI-637807, EBI-3951683 | |
BINARY | Q86U86 | SMARCA4 P51532 | 7 | EBI-637807, EBI-302489 | |
XENO | Q86U86 | tat P04608 | 2 | EBI-637807, EBI-6164389 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MGSKRRRATSPSSSVSGDFDD | ||||||
Region | 1-39 | Disordered | ||||
Sequence: MGSKRRRATSPSSSVSGDFDDGHHSVSTPGPSRKRRRLS | ||||||
Domain | 64-134 | Bromo 1 | ||||
Sequence: QGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDVNLLTADFQLLFNNAKSYYKPDSPEY | ||||||
Region | 155-177 | Disordered | ||||
Sequence: GEADDEDDDEDGQDNQGTVTEGS | ||||||
Domain | 200-270 | Bromo 2 | ||||
Sequence: SGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVF | ||||||
Domain | 400-470 | Bromo 3 | ||||
Sequence: QGQLIAEPFYHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIY | ||||||
Region | 487-517 | Disordered | ||||
Sequence: LARRDDIEDGDSMISSATSDTGSAKRKSKKN | ||||||
Domain | 538-608 | Bromo 4 | ||||
Sequence: SGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMIEDMKLMFRNARHYNEEGSQVY | ||||||
Compositional bias | 625-639 | Basic and acidic residues | ||||
Sequence: LGPLPDDDDMASPKL | ||||||
Region | 625-646 | Disordered | ||||
Sequence: LGPLPDDDDMASPKLKLSRKSG | ||||||
Domain | 676-746 | Bromo 5 | ||||
Sequence: RGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIY | ||||||
Domain | 792-862 | Bromo 6 | ||||
Sequence: HQDDEGRCYSDSLAEIPAVDPNFPNKPPLTFDIIRKNVENNRYRRLDLFQEHMFEVLERARRMNRTDSEIY | ||||||
Compositional bias | 902-933 | Basic and acidic residues | ||||
Sequence: VEKERKEKLPKEIEEDKLKREEEKREAEKSED | ||||||
Region | 902-941 | Disordered | ||||
Sequence: VEKERKEKLPKEIEEDKLKREEEKREAEKSEDSSGAAGLS | ||||||
Domain | 956-1074 | BAH 1 | ||||
Sequence: SMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPENFRDEDVFVCESRYSAKTKSFKKIK | ||||||
Region | 1106-1133 | Disordered | ||||
Sequence: KGDDEKNTDNSEDSRAEDNFNLEKEKED | ||||||
Domain | 1156-1272 | BAH 2 | ||||
Sequence: MWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMTCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFK | ||||||
Region | 1354-1378 | Disordered | ||||
Sequence: DLMPYTPPQSTPKSAKGSAKKEGSK | ||||||
Region | 1431-1460 | Disordered | ||||
Sequence: RAAKVAEQQERERAAQQQQPSASPRAGTPV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 9 isoforms produced by Alternative splicing.
Q86U86-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,689
- Mass (Da)192,948
- Last updated2003-06-01 v1
- Checksum0A656E319C4FC748
Q86U86-2
- Name2
- Differences from canonical
- 1430-1484: Missing
Q86U86-3
- Name3
- Differences from canonical
- 300-332: RTPSNLAAARLTGPSHSKGSLGEERNPTSKYYR → S
- 1430-1484: Missing
Q86U86-4
- Name4
- Differences from canonical
- 989-1013: Missing
- 1336-1362: Missing
- 1430-1484: Missing
Q86U86-5
- Name5
- Differences from canonical
- 1430-1484: Missing
- 1485-1536: Missing
Q86U86-6
- Name6
- Differences from canonical
- 857-1689: Missing
Q86U86-7
- Name7
- Differences from canonical
- 513-513: K → KRNTHDSEMLGLRRLS
- 1430-1484: Missing
- 1485-1536: Missing
Q86U86-8
- Name8
- Differences from canonical
- 513-513: K → KRNTHDSEMLGLRRLS
- 1485-1536: Missing
Q86U86-9
- Name9
- Differences from canonical
- 989-1013: Missing
- 1430-1484: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1 | in Ref. 4; AAI15011 | ||||
Sequence: M → T | ||||||
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MGSKRRRATSPSSSVSGDFDD | ||||||
Sequence conflict | 65 | in Ref. 4; AAI15011 | ||||
Sequence: G → S | ||||||
Sequence conflict | 242 | in Ref. 4; AAI15012 | ||||
Sequence: Y → C | ||||||
Sequence conflict | 251 | in Ref. 4; AAI15011 | ||||
Sequence: D → V | ||||||
Alternative sequence | VSP_015231 | 300-332 | in isoform 3 | |||
Sequence: RTPSNLAAARLTGPSHSKGSLGEERNPTSKYYR → S | ||||||
Sequence conflict | 430 | in Ref. 4; AAI15012 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_035499 | 513 | in isoform 7 and isoform 8 | |||
Sequence: K → KRNTHDSEMLGLRRLS | ||||||
Sequence conflict | 553 | in Ref. 1; AAG34760 | ||||
Sequence: K → R | ||||||
Sequence conflict | 567 | in Ref. 4; AAI15012 | ||||
Sequence: D → Y | ||||||
Compositional bias | 625-639 | Basic and acidic residues | ||||
Sequence: LGPLPDDDDMASPKL | ||||||
Sequence conflict | 750 | in Ref. 4; AAI15012 | ||||
Sequence: L → P | ||||||
Sequence conflict | 792 | in Ref. 4; AAI15012 | ||||
Sequence: H → R | ||||||
Alternative sequence | VSP_015232 | 857-1689 | in isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 902-933 | Basic and acidic residues | ||||
Sequence: VEKERKEKLPKEIEEDKLKREEEKREAEKSED | ||||||
Sequence conflict | 927 | in Ref. 4; AAI15010 and 5; BAB71210 | ||||
Sequence: Missing | ||||||
Sequence conflict | 963 | in Ref. 5; BAB71210 | ||||
Sequence: Y → H | ||||||
Alternative sequence | VSP_015233 | 989-1013 | in isoform 4 and isoform 9 | |||
Sequence: Missing | ||||||
Sequence conflict | 1144 | in Ref. 1; AAG34760 | ||||
Sequence: G → V | ||||||
Sequence conflict | 1245 | in Ref. 1; AAG34760 | ||||
Sequence: R → K | ||||||
Sequence conflict | 1306 | in Ref. 1; AAG34760 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_015234 | 1336-1362 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 1349 | in Ref. 4; AAI15010 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_015235 | 1430-1484 | in isoform 2, isoform 3, isoform 4, isoform 5, isoform 7 and isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015236 | 1485-1536 | in isoform 5, isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 1488 | in Ref. 4; AAI15012 | ||||
Sequence: G → D | ||||||
Sequence conflict | 1568 | in Ref. 1; AAG34760 | ||||
Sequence: G → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF197569 EMBL· GenBank· DDBJ | AAG34760.1 EMBL· GenBank· DDBJ | mRNA | ||
AF225870 EMBL· GenBank· DDBJ | AAG48939.1 EMBL· GenBank· DDBJ | mRNA | ||
AF225871 EMBL· GenBank· DDBJ | AAG48940.1 EMBL· GenBank· DDBJ | mRNA | ||
AF225872 EMBL· GenBank· DDBJ | AAG48941.1 EMBL· GenBank· DDBJ | mRNA | ||
AF177387 EMBL· GenBank· DDBJ | AAG48933.1 EMBL· GenBank· DDBJ | mRNA | ||
AY281068 EMBL· GenBank· DDBJ | AAP34197.1 EMBL· GenBank· DDBJ | mRNA | ||
BC115009 EMBL· GenBank· DDBJ | AAI15010.1 EMBL· GenBank· DDBJ | mRNA | Different termination. | |
BC115010 EMBL· GenBank· DDBJ | AAI15011.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC115011 EMBL· GenBank· DDBJ | AAI15012.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC129934 EMBL· GenBank· DDBJ | AAI29935.1 EMBL· GenBank· DDBJ | mRNA | ||
BC129935 EMBL· GenBank· DDBJ | AAI29936.1 EMBL· GenBank· DDBJ | mRNA | ||
AK056541 EMBL· GenBank· DDBJ | BAB71210.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |