Q62671 · UBR5_RAT
- ProteinE3 ubiquitin-protein ligase UBR5
- GeneUbr5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2788 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm and nucleus (By similarity).
Mainly acts as a ubiquitin chain elongator that extends pre-ubiquitinated substrates (By similarity).
Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (By similarity).
Recognizes type-1 N-degrons, containing positively charged amino acids (Arg, Lys and His) (By similarity).
Together with UBR4, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR5 is probably branching multiple 'Lys-48'-linked chains of substrates initially modified with mixed conjugates by UBR4 (By similarity).
Together with ITCH, catalyzes 'Lys-48'-/'Lys-63'-branched ubiquitination of TXNIP, leading to its degradation: UBR5 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by ITCH (By similarity).
Catalytic component of a nuclear protein quality control pathway that mediates ubiquitination and degradation of unpaired transcription factors (i.e. transcription factors that are not assembled into functional multiprotein complexes): specifically recognizes and binds degrons that are not accessible when transcription regulators are associated with their coactivators (By similarity).
Ubiquitinates various unpaired transcription regulator (MYC, SUPT4H1, SUPT5H, CDC20 and MCRS1), as well as ligand-bound nuclear receptors (ESR1, NR1H3, NR3C1, PGR, RARA, RXRA AND VDR) that are not associated with their nuclear receptor coactivators (NCOAs) (By similarity).
Involved in maturation and/or transcriptional regulation of mRNA by mediating polyubiquitination and activation of CDK9 (By similarity).
Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (By similarity).
Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response (By similarity).
Ubiquitinates acetylated PCK1 (By similarity).
Acts as a positive regulator of the canonical Wnt signaling pathway by mediating 1 ubiquitination and stabilization of CTNNB1, and 2 'Lys-48'-linked ubiquitination and degradation of TLE3 (By similarity).
Promotes disassembly of the mitotic checkpoint complex (MCC) from the APC/C complex by catalyzing ubiquitination of BUB1B, BUB3 and CDC20 (By similarity).
Plays an essential role in extraembryonic development (By similarity).
Required for the maintenance of skeletal tissue homeostasis by acting as an inhibitor of hedgehog (HH) signaling (By similarity).
Mainly acts as a ubiquitin chain elongator that extends pre-ubiquitinated substrates (By similarity).
Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (By similarity).
Recognizes type-1 N-degrons, containing positively charged amino acids (Arg, Lys and His) (By similarity).
Together with UBR4, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR5 is probably branching multiple 'Lys-48'-linked chains of substrates initially modified with mixed conjugates by UBR4 (By similarity).
Together with ITCH, catalyzes 'Lys-48'-/'Lys-63'-branched ubiquitination of TXNIP, leading to its degradation: UBR5 mediates branching of 'Lys-48'-linked chains of substrates initially modified with 'Lys-63'-linked conjugates by ITCH (By similarity).
Catalytic component of a nuclear protein quality control pathway that mediates ubiquitination and degradation of unpaired transcription factors (i.e. transcription factors that are not assembled into functional multiprotein complexes): specifically recognizes and binds degrons that are not accessible when transcription regulators are associated with their coactivators (By similarity).
Ubiquitinates various unpaired transcription regulator (MYC, SUPT4H1, SUPT5H, CDC20 and MCRS1), as well as ligand-bound nuclear receptors (ESR1, NR1H3, NR3C1, PGR, RARA, RXRA AND VDR) that are not associated with their nuclear receptor coactivators (NCOAs) (By similarity).
Involved in maturation and/or transcriptional regulation of mRNA by mediating polyubiquitination and activation of CDK9 (By similarity).
Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (By similarity).
Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response (By similarity).
Ubiquitinates acetylated PCK1 (By similarity).
Acts as a positive regulator of the canonical Wnt signaling pathway by mediating 1 ubiquitination and stabilization of CTNNB1, and 2 'Lys-48'-linked ubiquitination and degradation of TLE3 (By similarity).
Promotes disassembly of the mitotic checkpoint complex (MCC) from the APC/C complex by catalyzing ubiquitination of BUB1B, BUB3 and CDC20 (By similarity).
Plays an essential role in extraembryonic development (By similarity).
Required for the maintenance of skeletal tissue homeostasis by acting as an inhibitor of hedgehog (HH) signaling (By similarity).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 2757 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase UBR5
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ62671
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086933 | 1-2788 | E3 ubiquitin-protein ligase UBR5 | |||
Sequence: MNKQAVKRLHMLREVSEKLNKYNLNSHPPLNVLEQATIKQCVVGPNHAAFLLEDGRICRIGFSVQPDRLELGKPDNNDGSKLNSSSGTGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGARDSRRQTRVIRTGRDRGSGLLGSQPQPVIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDEDGDDGDDTASESYLPGEDLMSLLDADIHSAHPSVIIDADAMFSEDISYFGYPSFRRSSLSRLGSSRVLLLPLERDSELLRERESVLRLRERRWLDGASFDNERGSTSKEGEPNPDKKNTPVQSPVSLGEDLQWWPDKDGTKFTCIGALYSELVAVSSKGELYQWKWTESEPYRNAQNPSLHHPRATFLGLTNEKIVLLSANSIRATVATENNKVATWVDETLSSVASKLEHTAQTYSELQGERIVSLHCCALYTCAQLENNLYWWGVVPFSQRKKMLEKARAKNKKPKSSAGVQSLNVRGGRQVCLRNNPLYHAGAVAFSISAGIPKVGVLMESVWNMNDSCRFQLRSPESLKSMEKASKTIETKPESKQEPVKTEMGPPPSPASTCSDASSIASSASMPYKRRRSTPAPKEEEKVNEEQWSLREVVFVEDVKNVPVGKVLKVDGAYVAVKFPGTSSNTNCQNSSGPDADPSSLLQDCRLLRIDELQVVKTGGTPKVPDCFQRTPKKLCIPEKTEILAVNVDSKGVHAVLKTGNWVRYCIFDLATGKAEQENNFPTSSVAFLGQNERSVAIFTAGQESPIILRDGNGTIYPMAKDCMGGIRDPDWLDLPPISSLGMGVHSLINLPANSTIKKKAAIIIMAVEKQTLMQHILRCDYEACRQYLVNLEQAVVLEQNLQMLQTFISHRCDGNRNILHACVSVCFPTSNKETKEEEEAERSERNTFAERLSAVEAIANAISVVSSNGPGNRAGSSSSRSLRLREMMRRSLRAAGLGRHEAGASSSDHQDPVSPPIAPPSWVPDPPSMDPDGDIDFILAPAVGSLTTAATGGGQGPSTSTIPGPSTEPSVVESKDRKANAHFILKLLCDSAVLQPYLRELLSAKDARGMTPFMSAVSGRAYPAAITILETAQKIAKAEVSGSEKEEDVFMGMVCPSGTNPDDSPLYVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAGQKSARLDLLYRLLTATNLVTLPNSRGEHLLLFLVQTVARQTVEHCQYRPPRIREDRNRKTASPDDSDMPDHDLEPPRFAQLALERVLQDWNALRSMIMFGSQENKDPLSASSRIGHLLPEEQVYLNQQSGTIRLDCFTHCLIVKCTADILLLDTLLGTLVKELQNKYTPGRREEAIAVTMRFLRSVARVFVILSVEMASSKKKNNFIPQPIGKCKRVFQALLPYAVEELCNVAESLIVPVRMGIARPTAPFTLASTSIDAMQGSEELFSVEPLPPRPSSDQSSSSSQSQSSYIIRNPQQRRISQSQPVRGREEEQDDIVSADVEEVEVVEGVAGEEDHHDEQEEHGEENAEAEGHHDEHDEDGSDMELDLLAAAETESDSESNHSNQDNASGRRSVVTAATAGSEAGASSVPAFFSEDDSQSNDSSDSDSSSSQSDDIEQETFMLDEPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAASSAGLIYIDPSNLRRSGTISTSAAAAAAALEASNASSYLTSASSLARAYSIVIRQISDLMGLIPKYNHLVYSQIPAAVKLTYQDAVNLQNYVEEKLIPTWNWMVSIMDSTEAQLRYGSALASAGDPGHPNHPLHASQNSARRERMTAREEASLRTLEGRRRRATLLSARQGMMSARGDFLNYALSLMRSHNDEHSDVLPVLDVCSLKHVAYVFQALIYWIKAMNQQTTLDTPQLERKRTRELLELGIDNEDSEHENDDDTSQSATLNDKDDESLPAETGQNHPFFRRSDSMTFLGCIPPNPFEVPLAEAIPLADQPHLLQPNARKEDLFGRPSQGLYSSSAGSGKCLVEVTMDRNCLEVLPTKMSYAANLKNVMNMQNRQKKAGEDQSMLAEEADSSKPGPSAHDVAAQLKSSLLAEIGLTESEGPPLTSFRPQCSFMGMVISHDMLLGRWRLSLELFGRVFMEDVGAEPGSILTELGGFEVKESKFRREMEKLRNQQSRDLSLEVDRDRDLLIQQTMRQLNNHFGRRCATTPMAVHRVKVTFKDEPGEGSGVARSFYTAIAQAFLSNEKLPNLDCIQNANKGTHTSLMQRLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSIDTRPFRPASEGNPSDDPDPLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVEEAMELIVAHGRENGADSILDLGLLDSSEKVQENRKRHGSSRSVVDMDLDDTDDGDDNAPLFYQPGKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDADAVFSAMDLAFAVDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLLQFKRWFWSIVERMSMTERQDLVYFWTSSPSLPASEEGFQPMPSITIRPPDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIKTKNFGFV | ||||||
Modified residue | 100 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 317 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 342 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 567 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 601 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 626 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 797 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 917 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1007 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1104 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1124 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1216 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1297 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1344 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1364 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1470 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1538 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1725 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1730 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1735 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1769 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1959 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1980 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2016 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2018 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2020 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2066 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2203 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2231 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2279 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2459 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2473 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2475 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highest levels found in testis. Also present in liver, kidney, lung and brain.
Developmental stage
In early postnatal life, expression in the testis increases to reach a maximum around day 28.
Interaction
Subunit
Homotetramer; composed of a dimer of dimers. Associates with CDK9 and TFIIS/TCEA1 and forms a transcription regulatory complex made of CDK9, RNAP II, UBR5 and TFIIS/TCEA1 that can stimulate target gene transcription (e.g. gamma fibrinogen/FGG) by recruiting their promoters. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Binds TOPBP1. Interacts with PIH1D1. Interacts with CIB1.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 68-165 | Disordered | ||||
Sequence: RLELGKPDNNDGSKLNSSSGTGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGARDSRRQTRVIRTGRDRGSGLLGSQ | ||||||
Compositional bias | 77-141 | Polar residues | ||||
Sequence: NDGSKLNSSSGTGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGA | ||||||
Domain | 174-216 | UBA | ||||
Sequence: VIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSR | ||||||
Compositional bias | 318-334 | Basic and acidic residues | ||||
Sequence: FDNERGSTSKEGEPNPD | ||||||
Region | 318-343 | Disordered | ||||
Sequence: FDNERGSTSKEGEPNPDKKNTPVQSP | ||||||
Compositional bias | 572-591 | Basic and acidic residues | ||||
Sequence: KSMEKASKTIETKPESKQEP | ||||||
Region | 572-636 | Disordered | ||||
Sequence: KSMEKASKTIETKPESKQEPVKTEMGPPPSPASTCSDASSIASSASMPYKRRRSTPAPKEEEKVN | ||||||
Compositional bias | 600-621 | Polar residues | ||||
Sequence: PSPASTCSDASSIASSASMPYK | ||||||
Region | 988-1024 | Disordered | ||||
Sequence: AGLGRHEAGASSSDHQDPVSPPIAPPSWVPDPPSMDP | ||||||
Compositional bias | 1006-1020 | Pro residues | ||||
Sequence: VSPPIAPPSWVPDPP | ||||||
Compositional bias | 1041-1061 | Polar residues | ||||
Sequence: TAATGGGQGPSTSTIPGPSTE | ||||||
Region | 1041-1064 | Disordered | ||||
Sequence: TAATGGGQGPSTSTIPGPSTEPSV | ||||||
Zinc finger | 1166-1234 | UBR-type | ||||
Sequence: DTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIA | ||||||
Region | 1288-1308 | Disordered | ||||
Sequence: REDRNRKTASPDDSDMPDHDL | ||||||
Region | 1504-1729 | Disordered | ||||
Sequence: SVEPLPPRPSSDQSSSSSQSQSSYIIRNPQQRRISQSQPVRGREEEQDDIVSADVEEVEVVEGVAGEEDHHDEQEEHGEENAEAEGHHDEHDEDGSDMELDLLAAAETESDSESNHSNQDNASGRRSVVTAATAGSEAGASSVPAFFSEDDSQSNDSSDSDSSSSQSDDIEQETFMLDEPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAAS | ||||||
Compositional bias | 1510-1540 | Polar residues | ||||
Sequence: PRPSSDQSSSSSQSQSSYIIRNPQQRRISQS | ||||||
Compositional bias | 1552-1566 | Acidic residues | ||||
Sequence: DIVSADVEEVEVVEG | ||||||
Compositional bias | 1567-1597 | Basic and acidic residues | ||||
Sequence: VAGEEDHHDEQEEHGEENAEAEGHHDEHDED | ||||||
Compositional bias | 1611-1640 | Polar residues | ||||
Sequence: TESDSESNHSNQDNASGRRSVVTAATAGSE | ||||||
Compositional bias | 1649-1674 | Polar residues | ||||
Sequence: FFSEDDSQSNDSSDSDSSSSQSDDIE | ||||||
Compositional bias | 1682-1729 | Polar residues | ||||
Sequence: EPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAAS | ||||||
Region | 1848-1881 | Disordered | ||||
Sequence: LASAGDPGHPNHPLHASQNSARRERMTAREEASL | ||||||
Compositional bias | 1865-1881 | Basic and acidic residues | ||||
Sequence: QNSARRERMTAREEASL | ||||||
Region | 1974-2011 | Disordered | ||||
Sequence: GIDNEDSEHENDDDTSQSATLNDKDDESLPAETGQNHP | ||||||
Compositional bias | 1986-2004 | Basic and acidic residues | ||||
Sequence: DDTSQSATLNDKDDESLPA | ||||||
Region | 2106-2132 | Disordered | ||||
Sequence: NRQKKAGEDQSMLAEEADSSKPGPSAH | ||||||
Region | 2313-2383 | Disordered | ||||
Sequence: HTSLMQRLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSIDTRPFRPASEGNPSDDPDPLPAH | ||||||
Compositional bias | 2319-2360 | Basic and acidic residues | ||||
Sequence: RLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSI | ||||||
Domain | 2367-2444 | PABC | ||||
Sequence: PASEGNPSDDPDPLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVEEAMELIVAHGR | ||||||
Domain | 2451-2788 | HECT | ||||
Sequence: ILDLGLLDSSEKVQENRKRHGSSRSVVDMDLDDTDDGDDNAPLFYQPGKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDADAVFSAMDLAFAVDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLLQFKRWFWSIVERMSMTERQDLVYFWTSSPSLPASEEGFQPMPSITIRPPDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIKTKNFGFV | ||||||
Compositional bias | 2463-2480 | Basic and acidic residues | ||||
Sequence: VQENRKRHGSSRSVVDMD | ||||||
Region | 2463-2490 | Disordered | ||||
Sequence: VQENRKRHGSSRSVVDMDLDDTDDGDDN |
Domain
The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons.
The UBA domain recognizes and binds ubiquitin. It acts as an ubiquitin acceptor required to place 'Lys-48' of ubiquitin into the HECT domain activie site, thereby potentiating the E3 ubiquitin-protein ligase activity.
Sequence similarities
Belongs to the UBR5 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,788
- Mass (Da)308,027
- Last updated2012-02-22 v3
- ChecksumC2EA68B962627231
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6ARZ1 | A0A8I6ARZ1_RAT | Ubr5 | 2798 | ||
H9KVE3 | H9KVE3_RAT | Ubr5 | 2386 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 77-141 | Polar residues | ||||
Sequence: NDGSKLNSSSGTGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGA | ||||||
Compositional bias | 318-334 | Basic and acidic residues | ||||
Sequence: FDNERGSTSKEGEPNPD | ||||||
Compositional bias | 572-591 | Basic and acidic residues | ||||
Sequence: KSMEKASKTIETKPESKQEP | ||||||
Compositional bias | 600-621 | Polar residues | ||||
Sequence: PSPASTCSDASSIASSASMPYK | ||||||
Compositional bias | 1006-1020 | Pro residues | ||||
Sequence: VSPPIAPPSWVPDPP | ||||||
Compositional bias | 1041-1061 | Polar residues | ||||
Sequence: TAATGGGQGPSTSTIPGPSTE | ||||||
Compositional bias | 1510-1540 | Polar residues | ||||
Sequence: PRPSSDQSSSSSQSQSSYIIRNPQQRRISQS | ||||||
Compositional bias | 1552-1566 | Acidic residues | ||||
Sequence: DIVSADVEEVEVVEG | ||||||
Compositional bias | 1567-1597 | Basic and acidic residues | ||||
Sequence: VAGEEDHHDEQEEHGEENAEAEGHHDEHDED | ||||||
Compositional bias | 1611-1640 | Polar residues | ||||
Sequence: TESDSESNHSNQDNASGRRSVVTAATAGSE | ||||||
Compositional bias | 1649-1674 | Polar residues | ||||
Sequence: FFSEDDSQSNDSSDSDSSSSQSDDIE | ||||||
Compositional bias | 1682-1729 | Polar residues | ||||
Sequence: EPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAAS | ||||||
Compositional bias | 1865-1881 | Basic and acidic residues | ||||
Sequence: QNSARRERMTAREEASL | ||||||
Sequence conflict | 1890 | in Ref. 2; CAA45756 | ||||
Sequence: Missing | ||||||
Compositional bias | 1986-2004 | Basic and acidic residues | ||||
Sequence: DDTSQSATLNDKDDESLPA | ||||||
Compositional bias | 2319-2360 | Basic and acidic residues | ||||
Sequence: RLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSI | ||||||
Compositional bias | 2463-2480 | Basic and acidic residues | ||||
Sequence: VQENRKRHGSSRSVVDMD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X64411 EMBL· GenBank· DDBJ | CAA45756.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |