Q5H9F3 · BCORL_HUMAN
- ProteinBCL-6 corepressor-like protein 1
- GeneBCORL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1785 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | transcription corepressor activity | |
Biological Process | chromatin organization | |
Biological Process | negative regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBCL-6 corepressor-like protein 1
- Short namesBCoR-L1; BCoR-like protein 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5H9F3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Shukla-Vernon syndrome (SHUVER)
- Note
- DescriptionAn X-linked neurodevelopmental disorder manifesting in affected males with intellectual and learning disability, motor and language delay, autism spectrum disorder, attention deficit and hyperactivity disorder, and dysmorphic features. Some patients may have seizures and/or cerebellar atrophy on brain imaging. Carrier females may have mild disease manifestations.
- See alsoMIM:301029
Natural variants in SHUVER
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_082288 | 32 | P>L | in SHUVER; uncertain significance; dbSNP:rs1603105985 | |
VAR_082289 | 496 | S>F | in SHUVER; uncertain significance; dbSNP:rs1057521638 | |
VAR_082290 | 782 | V>E | in SHUVER; uncertain significance; dbSNP:rs1488781894 | |
VAR_070559 | 820 | N>S | in SHUVER; uncertain significance; dbSNP:rs398123004 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_082288 | 32 | in SHUVER; uncertain significance; dbSNP:rs1603105985 | |||
Sequence: P → L | ||||||
Natural variant | VAR_061020 | 111 | in dbSNP:rs4830173 | |||
Sequence: L → F | ||||||
Natural variant | VAR_037467 | 209 | in dbSNP:rs5932715 | |||
Sequence: G → S | ||||||
Natural variant | VAR_080909 | 327 | found in a patient with Uruguay faciocardiomusculoskeletal syndrome; uncertain significance | |||
Sequence: T → I | ||||||
Natural variant | VAR_082289 | 496 | in SHUVER; uncertain significance; dbSNP:rs1057521638 | |||
Sequence: S → F | ||||||
Mutagenesis | 623-624 | Strongly reduced repressor activity. Interferes with CTBP1 binding. | ||||
Sequence: DL → AS | ||||||
Natural variant | VAR_082290 | 782 | in SHUVER; uncertain significance; dbSNP:rs1488781894 | |||
Sequence: V → E | ||||||
Natural variant | VAR_070559 | 820 | in SHUVER; uncertain significance; dbSNP:rs398123004 | |||
Sequence: N → S | ||||||
Natural variant | VAR_037468 | 832 | in a breast cancer sample; somatic mutation | |||
Sequence: G → D | ||||||
Mutagenesis | 1739 | Slightly inhibits interaction with PCGF1. | ||||
Sequence: L → D or R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,211 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
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_0000312268 | 1-1785 | UniProt | BCL-6 corepressor-like protein 1 | |||
Sequence: MISTAPLYSGVHNWTSSDRIRMCGINEERRAPLSDEESTTGDCQHFGSQEFCVSSSFSKVELTAVGSGSNARGADPDGSATEKLGHKSEDKPDDPQPKMDYAGNVAEAEGLLVPLSSPGDGLKLPASDSAEASNSRADCSWTPLNTQMSKQVDCSPAGVKALDSRQGVGEKNTFILATLGTGVPVEGTLPLVTTNFSPLPAPICPPAPGSASVPHSVPDAFQVPLSVPAPVPHSGLVPVQVATSVPAPSPPLAPVPALAPAPPSVPTLISDSNPLSVSASVLVPVPASAPPSGPVPLSAPAPAPLSVPVSAPPLALIQAPVPPSAPTLVLAPVPTPVLAPMPASTPPAAPAPPSVPMPTPTPSSGPPSTPTLIPAFAPTPVPAPTPAPIFTPAPTPMPAATPAAIPTSAPIPASFSLSRVCFPAAQAPAMQKVPLSFQPGTVLTPSQPLVYIPPPSCGQPLSVATLPTTLGVSSTLTLPVLPSYLQDRCLPGVLASPELRSYPYAFSVARPLTSDSKLVSLEVNRLPCTSPSGSTTTQPAPDGVPGPLADTSLVTASAKVLPTPQPLLPAPSGSSAPPHPAKMPSGTEQQTEGTSVTFSPLKSPPQLEREMASPPECSEMPLDLSSKSNRQKLPLPNQRKTPPMPVLTPVHTSSKALLSTVLSRSQRTTQAAGGNVTSCLGSTSSPFVIFPEIVRNGDPSTWVKNSTALISTIPGTYVGVANPVPASLLLNKDPNLGLNRDPRHLPKQEPISIIDQGEPKGTGATCGKKGSQAGAEGQPSTVKRYTPARIAPGLPGCQTKELSLWKPTGPANIYPRCSVNGKPTSTQVLPVGWSPYHQASLLSIGISSAGQLTPSQGAPIRPTSVVSEFSGVPSLSSSEAVHGLPEGQPRPGGSFVPEQDPVTKNKTCRIAAKPYEEQVNPVLLTLSPQTGTLALSVQPSGGDIRMNQGPEESESHLCSDSTPKMEGPQGACGLKLAGDTKPKNQVLATYMSHELVLATPQNLPKMPELPLLPHDSHPKELILDVVPSSRRGSSTERPQLGSQVDLGRVKMEKVDGDVVFNLATCFRADGLPVAPQRGQAEVRAKAGQARVKQESVGVFACKNKWQPDDVTESLPPKKMKCGKEKDSEEQQLQPQAKAVVRSSHRPKCRKLPSDPQESTKKSPRGASDSGKEHNGVRGKHKHRKPTKPESQSPGKRADSHEEGSLEKKAKSSFRDFIPVVLSTRTRSQSGSICSSFAGMADSDMGSQEVFPTEEEEEVTPTPAKRRKVRKTQRDTQYRSHHAQDKSLLSQGRRHLWRAREMPWRTEAARQMWDTNEEEEEEEEEGLLKRKKRRRQKSRKYQTGEYLTEQEDEQRRKGRADLKARKQKTSSSQSLEHRLRNRNLLLPNKVQGISDSPNGFLPNNLEEPACLENSEKPSGKRKCKTKHMATVSEEAKGKGRWSQQKTRSPKSPTPVKPTEPCTPSKSRSASSEEASESPTARQIPPEARRLIVNKNAGETLLQRAARLGYKDVVLYCLQKDSEDVNHRDNAGYTALHEACSRGWTDILNILLEHGANVNCSAQDGTRPVHDAVVNDNLETIWLLLSYGADPTLATYSGQTAMKLASSDTMKRFLSDHLSDLQGRAEGDPGVSWDFYSSSVLEEKDGFACDLLHNPPGSSDQEGDDPMEEDDFMFELSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEITTMPKAEFYRQVASSQLLTPAERPGGLDDRSPPGSSETVELVRYEPDLLRLLGSEVEFQSCNS | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 496 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 496 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 599 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 599 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 603 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 613 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 613 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 747 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 927 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 961 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 962 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1016 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1028 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1029 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1029 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1033 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1033 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1034 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1092 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1162 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1450 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1452 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1461 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1467 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1469 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1474 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1476 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1476 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1478 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1753 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
The PCGF1-BCORL1 heterodimeric complex interacts with the KDM2B-SKP1 heterodimeric complex to form a homotetrameric polycomb repression complex 1 (PRC1.1) (PubMed:27568929).
Interacts with CTBP1, HDAC4, HDAC5 and HDAC7 (PubMed:17379597).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5H9F3-1 | PCGF1 Q9BSM1-1 | 6 | EBI-16041827, EBI-16041863 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 65-101 | Disordered | ||||
Sequence: VGSGSNARGADPDGSATEKLGHKSEDKPDDPQPKMDY | ||||||
Compositional bias | 79-97 | Basic and acidic residues | ||||
Sequence: SATEKLGHKSEDKPDDPQP | ||||||
Region | 113-137 | Disordered | ||||
Sequence: VPLSSPGDGLKLPASDSAEASNSRA | ||||||
Region | 343-368 | Disordered | ||||
Sequence: ASTPPAAPAPPSVPMPTPTPSSGPPS | ||||||
Compositional bias | 527-541 | Polar residues | ||||
Sequence: PCTSPSGSTTTQPAP | ||||||
Region | 527-550 | Disordered | ||||
Sequence: PCTSPSGSTTTQPAPDGVPGPLAD | ||||||
Region | 562-646 | Disordered | ||||
Sequence: PTPQPLLPAPSGSSAPPHPAKMPSGTEQQTEGTSVTFSPLKSPPQLEREMASPPECSEMPLDLSSKSNRQKLPLPNQRKTPPMPV | ||||||
Compositional bias | 564-578 | Pro residues | ||||
Sequence: PQPLLPAPSGSSAPP | ||||||
Compositional bias | 584-602 | Polar residues | ||||
Sequence: PSGTEQQTEGTSVTFSPLK | ||||||
Compositional bias | 622-636 | Polar residues | ||||
Sequence: LDLSSKSNRQKLPLP | ||||||
Region | 753-781 | Disordered | ||||
Sequence: IIDQGEPKGTGATCGKKGSQAGAEGQPST | ||||||
Region | 876-901 | Disordered | ||||
Sequence: SSSEAVHGLPEGQPRPGGSFVPEQDP | ||||||
Region | 937-977 | Disordered | ||||
Sequence: VQPSGGDIRMNQGPEESESHLCSDSTPKMEGPQGACGLKLA | ||||||
Region | 1107-1293 | Disordered | ||||
Sequence: PDDVTESLPPKKMKCGKEKDSEEQQLQPQAKAVVRSSHRPKCRKLPSDPQESTKKSPRGASDSGKEHNGVRGKHKHRKPTKPESQSPGKRADSHEEGSLEKKAKSSFRDFIPVVLSTRTRSQSGSICSSFAGMADSDMGSQEVFPTEEEEEVTPTPAKRRKVRKTQRDTQYRSHHAQDKSLLSQGRR | ||||||
Compositional bias | 1111-1131 | Basic and acidic residues | ||||
Sequence: TESLPPKKMKCGKEKDSEEQQ | ||||||
Compositional bias | 1187-1213 | Basic and acidic residues | ||||
Sequence: KPESQSPGKRADSHEEGSLEKKAKSSF | ||||||
Compositional bias | 1221-1236 | Polar residues | ||||
Sequence: LSTRTRSQSGSICSSF | ||||||
Compositional bias | 1275-1293 | Basic and acidic residues | ||||
Sequence: TQYRSHHAQDKSLLSQGRR | ||||||
Region | 1312-1487 | Disordered | ||||
Sequence: WDTNEEEEEEEEEGLLKRKKRRRQKSRKYQTGEYLTEQEDEQRRKGRADLKARKQKTSSSQSLEHRLRNRNLLLPNKVQGISDSPNGFLPNNLEEPACLENSEKPSGKRKCKTKHMATVSEEAKGKGRWSQQKTRSPKSPTPVKPTEPCTPSKSRSASSEEASESPTARQIPPEAR | ||||||
Motif | 1328-1336 | Nuclear localization signal | ||||
Sequence: KRKKRRRQK | ||||||
Compositional bias | 1339-1374 | Basic and acidic residues | ||||
Sequence: KYQTGEYLTEQEDEQRRKGRADLKARKQKTSSSQSL | ||||||
Compositional bias | 1386-1400 | Polar residues | ||||
Sequence: PNKVQGISDSPNGFL | ||||||
Compositional bias | 1425-1440 | Basic and acidic residues | ||||
Sequence: KHMATVSEEAKGKGRW | ||||||
Compositional bias | 1459-1477 | Polar residues | ||||
Sequence: PCTPSKSRSASSEEASESP | ||||||
Repeat | 1529-1558 | ANK 1 | ||||
Sequence: AGYTALHEACSRGWTDILNILLEHGANVNC | ||||||
Repeat | 1562-1591 | ANK 2 | ||||
Sequence: DGTRPVHDAVVNDNLETIWLLLSYGADPTL | ||||||
Repeat | 1595-1623 | ANK 3 | ||||
Sequence: SGQTAMKLASSDTMKRFLSDHLSDLQGRA | ||||||
Region | 1668-1785 | PCGF Ub-like fold domain (PUFD); required for the interaction with the KDM2B-SKP1 heterodimeric complex | ||||
Sequence: DDFMFELSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEITTMPKAEFYRQVASSQLLTPAERPGGLDDRSPPGSSETVELVRYEPDLLRLLGSEVEFQSCNS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q5H9F3-3
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.
- Name3
- Length1,785
- Mass (Da)190,561
- Last updated2022-02-23 v2
- ChecksumDD62FFFEC2DE1E9C
Q5H9F3-1
- Name1
- Differences from canonical
- 1436-1509: Missing
Q5H9F3-4
- Name4
- Differences from canonical
- 1230-1359: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
V9GYD4 | V9GYD4_HUMAN | BCORL1 | 45 | ||
H7C4B2 | H7C4B2_HUMAN | BCORL1 | 741 | ||
A0A087X1F0 | A0A087X1F0_HUMAN | BCORL1 | 28 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 79-97 | Basic and acidic residues | ||||
Sequence: SATEKLGHKSEDKPDDPQP | ||||||
Compositional bias | 527-541 | Polar residues | ||||
Sequence: PCTSPSGSTTTQPAP | ||||||
Compositional bias | 564-578 | Pro residues | ||||
Sequence: PQPLLPAPSGSSAPP | ||||||
Compositional bias | 584-602 | Polar residues | ||||
Sequence: PSGTEQQTEGTSVTFSPLK | ||||||
Compositional bias | 622-636 | Polar residues | ||||
Sequence: LDLSSKSNRQKLPLP | ||||||
Compositional bias | 1111-1131 | Basic and acidic residues | ||||
Sequence: TESLPPKKMKCGKEKDSEEQQ | ||||||
Compositional bias | 1187-1213 | Basic and acidic residues | ||||
Sequence: KPESQSPGKRADSHEEGSLEKKAKSSF | ||||||
Compositional bias | 1221-1236 | Polar residues | ||||
Sequence: LSTRTRSQSGSICSSF | ||||||
Alternative sequence | VSP_061439 | 1230-1359 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 1275-1293 | Basic and acidic residues | ||||
Sequence: TQYRSHHAQDKSLLSQGRR | ||||||
Compositional bias | 1339-1374 | Basic and acidic residues | ||||
Sequence: KYQTGEYLTEQEDEQRRKGRADLKARKQKTSSSQSL | ||||||
Compositional bias | 1386-1400 | Polar residues | ||||
Sequence: PNKVQGISDSPNGFL | ||||||
Compositional bias | 1425-1440 | Basic and acidic residues | ||||
Sequence: KHMATVSEEAKGKGRW | ||||||
Alternative sequence | VSP_061440 | 1436-1509 | in isoform 1 | |||
Sequence: Missing | ||||||
Compositional bias | 1459-1477 | Polar residues | ||||
Sequence: PCTPSKSRSASSEEASESP | ||||||
Sequence conflict | 1638 | in Ref. 4; BAC85922 | ||||
Sequence: V → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL034405 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL136450 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF459398 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF459400 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF510634 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z82208 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK074089 EMBL· GenBank· DDBJ | BAB84915.1 EMBL· GenBank· DDBJ | mRNA | ||
AL096777 EMBL· GenBank· DDBJ | CAB46626.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK124676 EMBL· GenBank· DDBJ | BAC85922.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |