A0A499FJI4 · A0A499FJI4_HUMAN
- ProteinRCR-type E3 ubiquitin transferase
- GeneMYCBP2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids4738 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
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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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytosol | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleoplasm | |
Molecular Function | metal ion binding | |
Biological Process | protein ubiquitination |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRCR-type E3 ubiquitin transferase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A499FJI4
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4,454 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 69 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 183 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1624 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1625 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2334 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2683 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2687 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2690 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2699 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2701 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2712 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2787 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2843 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2847 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2849 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2854 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2868 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2872 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2892 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2893 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2895 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2898 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2899 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2904 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2929 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2931 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2933 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2971 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2980 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3005 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3009 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3014 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3045 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3246 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3499 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3516 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3519 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 3520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3538 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3549 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3568 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 3573 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3579 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3981 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 3991 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3992 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4003 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 4004 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4189 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 4191 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Proteomic databases
Expression
Gene expression databases
Family & Domains
Features
Showing features for region, compositional bias, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 87-127 | Disordered | ||||
Sequence: DRDQGGGSAGHPASRNKKILNKKKLKRKQKSKSKVKTRSKS | ||||||
Compositional bias | 102-121 | Basic residues | ||||
Sequence: NKKILNKKKLKRKQKSKSKV | ||||||
Region | 172-192 | Disordered | ||||
Sequence: SKNSVQSGESDSDEEEESKEP | ||||||
Repeat | 601-656 | RCC1 | ||||
Sequence: GSIFFTGSASKGEDGESTKSRRQSKPYKPKKIIKMEGKIVVYTACNNGSSSVISKD | ||||||
Region | 609-628 | Disordered | ||||
Sequence: ASKGEDGESTKSRRQSKPYK | ||||||
Compositional bias | 614-628 | Basic and acidic residues | ||||
Sequence: DGESTKSRRQSKPYK | ||||||
Region | 898-928 | Disordered | ||||
Sequence: RSHPAQLKHKRDKHKDGSGERGEKDASKITT | ||||||
Compositional bias | 908-924 | Basic and acidic residues | ||||
Sequence: RDKHKDGSGERGEKDAS | ||||||
Repeat | 959-1009 | RCC1 | ||||
Sequence: GDVYTFGYGQHGQLGHGDVNSRGCPTLVQALPGPSTQVTAGSNHTAVLLMD | ||||||
Repeat | 1010-1067 | RCC1 | ||||
Sequence: GQVFTFGSFSKGQLGRPILDVPYWNAKPAPMPNIGSKYGRKATWIGASGDQTFLRIDE | ||||||
Region | 1993-2012 | Disordered | ||||
Sequence: FNPNQSTDSTTGNQPEQGLS | ||||||
Region | 2321-2340 | Disordered | ||||
Sequence: QQDQAKKPQRIPGSPAVTAA | ||||||
Repeat | 2341-2434 | Filamin | ||||
Sequence: SSNTDMTYGGLASPKLDVSYEPMIVKEARYIAITMMKVYENYSFEELRFASPTPKRPSENMLIRVNNDGTYCANWTPGAIGLYTLHVTIDGIEI | ||||||
Compositional bias | 2769-2795 | Polar residues | ||||
Sequence: QPQLQSDRGNISTSSKPASTSGKSELS | ||||||
Region | 2769-2991 | Disordered | ||||
Sequence: QPQLQSDRGNISTSSKPASTSGKSELSSKHSRSLKPDGRMSRTTADQKKPRGTESLSASESLILKSDAAKLRSDSHSRSLSPNHNTLQTLKSDGRMPSSSRAESPGPGSRLSSPKPKTLPANRSSPSGASSPRSSSPHDKNLPQKSTAPVKTKLDPPRERSKSDSYTLDPDTLRKKKMPLTEPLRGRSTSPKPKSVPKDSTDSPGSENRAPSPHVVQENLHSE | ||||||
Compositional bias | 2796-2817 | Basic and acidic residues | ||||
Sequence: SKHSRSLKPDGRMSRTTADQKK | ||||||
Compositional bias | 2843-2875 | Polar residues | ||||
Sequence: SHSRSLSPNHNTLQTLKSDGRMPSSSRAESPGP | ||||||
Compositional bias | 2883-2916 | Polar residues | ||||
Sequence: KPKTLPANRSSPSGASSPRSSSPHDKNLPQKSTA | ||||||
Compositional bias | 2920-2950 | Basic and acidic residues | ||||
Sequence: TKLDPPRERSKSDSYTLDPDTLRKKKMPLTE | ||||||
Compositional bias | 2961-2983 | Polar residues | ||||
Sequence: PKSVPKDSTDSPGSENRAPSPHV | ||||||
Region | 3003-3080 | Disordered | ||||
Sequence: TNSLTDSTCDDSSEFKSVDEGSNKVHFSIGKAPLKDEQEMRASPKISRKCANRHTRPKKEKSSFLFKGDGSKPLEPAK | ||||||
Compositional bias | 3032-3048 | Basic and acidic residues | ||||
Sequence: GKAPLKDEQEMRASPKI | ||||||
Region | 3126-3146 | Disordered | ||||
Sequence: APIRSSLNSQQPTEEKETKLK | ||||||
Region | 3665-3691 | Disordered | ||||
Sequence: PVEPEEEEDEENKTSKENSEQEKDTRV | ||||||
Domain | 3778-3956 | DOC | ||||
Sequence: FSISIQSGFEAMSQELCIVMCLKDLTSIVDIKTSSRPAMIGSLTDGSTETFWESGDEDKNKTKNITINCVKGINARYVSVHVDNSRDLGNKVTSMTFLTGKAVEDLCRIKQVDLDSRHIGWVTSELPGGDNHIIKIELKGPENTLRVRQVKVLGWKDGESTKIAGQISASVAQQRNCEA | ||||||
Region | 3975-3994 | Disordered | ||||
Sequence: SGDAEPTPEQEEKALLSSPE | ||||||
Compositional bias | 3979-3993 | Basic and acidic residues | ||||
Sequence: EPTPEQEEKALLSSP | ||||||
Domain | 4488-4539 | RING-type | ||||
Sequence: CMICFTEALSAAPAIQLDCSHIFHLQCCRRVLENRWLGPRITFGFISCPICK |
Sequence similarities
Belongs to the RING-Cys relay (RCR) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length4,738
- Mass (Da)520,043
- Last updated2021-09-29 v2
- Checksum2A7ADCF48F115567
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
O75592 | MYCB2_HUMAN | MYCBP2 | 4678 | ||
A0A804HIR9 | A0A804HIR9_HUMAN | MYCBP2 | 4700 | ||
A0A804HJ25 | A0A804HJ25_HUMAN | MYCBP2 | 4634 | ||
A0A804HKQ1 | A0A804HKQ1_HUMAN | MYCBP2 | 4752 | ||
A0A804HL12 | A0A804HL12_HUMAN | MYCBP2 | 4772 | ||
H7C3U4 | H7C3U4_HUMAN | MYCBP2 | 1061 | ||
A0A8Q3SHQ6 | A0A8Q3SHQ6_HUMAN | MYCBP2 | 4537 | ||
A0A8Q3SHK7 | A0A8Q3SHK7_HUMAN | MYCBP2 | 4665 | ||
A0A8Q3SHQ2 | A0A8Q3SHQ2_HUMAN | MYCBP2 | 4609 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 102-121 | Basic residues | ||||
Sequence: NKKILNKKKLKRKQKSKSKV | ||||||
Compositional bias | 614-628 | Basic and acidic residues | ||||
Sequence: DGESTKSRRQSKPYK | ||||||
Compositional bias | 908-924 | Basic and acidic residues | ||||
Sequence: RDKHKDGSGERGEKDAS | ||||||
Compositional bias | 2769-2795 | Polar residues | ||||
Sequence: QPQLQSDRGNISTSSKPASTSGKSELS | ||||||
Compositional bias | 2796-2817 | Basic and acidic residues | ||||
Sequence: SKHSRSLKPDGRMSRTTADQKK | ||||||
Compositional bias | 2843-2875 | Polar residues | ||||
Sequence: SHSRSLSPNHNTLQTLKSDGRMPSSSRAESPGP | ||||||
Compositional bias | 2883-2916 | Polar residues | ||||
Sequence: KPKTLPANRSSPSGASSPRSSSPHDKNLPQKSTA | ||||||
Compositional bias | 2920-2950 | Basic and acidic residues | ||||
Sequence: TKLDPPRERSKSDSYTLDPDTLRKKKMPLTE | ||||||
Compositional bias | 2961-2983 | Polar residues | ||||
Sequence: PKSVPKDSTDSPGSENRAPSPHV | ||||||
Compositional bias | 3032-3048 | Basic and acidic residues | ||||
Sequence: GKAPLKDEQEMRASPKI | ||||||
Compositional bias | 3979-3993 | Basic and acidic residues | ||||
Sequence: EPTPEQEEKALLSSP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC001226 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL159154 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL159158 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL359257 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF455798 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |