Q9UIF8 · BAZ2B_HUMAN
- ProteinBromodomain adjacent to zinc finger domain protein 2B
- GeneBAZ2B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2168 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535).
The BRF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin remodeling complex (PubMed:28801535).
Chromatin reader protein, which may play a role in transcriptional regulation via interaction with ISWI (By similarity) (PubMed:10662543).
Involved in positively modulating the rate of age-related behavioral deterioration (By similarity).
Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with histone methyltransferase EHMT1 (By similarity).
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 | chromatin | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | metal ion binding | |
Biological Process | chromatin remodeling | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
The subsequence CRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPDGDWFCPACIAKASGQTLKIKKLHVKGKKTNESKKGKKVTLTGDTED shows transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameBromodomain adjacent to zinc finger domain protein 2B
- Alternative names
Gene names
- Community suggested namesBAZ2B
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UIF8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055549 | 71 | in dbSNP:rs10202670 | |||
Sequence: M → T | ||||||
Natural variant | VAR_055550 | 422 | in dbSNP:rs3213790 | |||
Sequence: L → S | ||||||
Natural variant | VAR_055551 | 530 | in dbSNP:rs3732287 | |||
Sequence: P → L | ||||||
Natural variant | VAR_055552 | 702 | in dbSNP:rs2302924 | |||
Sequence: G → V | ||||||
Natural variant | VAR_055553 | 2024 | in dbSNP:rs415793 | |||
Sequence: S → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,234 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), cross-link, modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000211174 | 1-2168 | UniProt | Bromodomain adjacent to zinc finger domain protein 2B | |||
Sequence: MESGERLPSSAASSTTPTSSSTPSVASVVSKGGLSTGVASLSSTINPCGHLFRTAGDQPFNLSTVSSAFPMVSHPVFGLHSASSGHSEFGGLGTLGTPTALAAHPQLASFPGAEWWRTTDAHTRTGATFFPPLLGIPPLFAPPAQNHDSSSFHSRTSGKSNRNGPEKGVNGSINGSNTSSVIGINTSVLSTTASSSMGQTKSTSSGGGNRKCNQEQSKNQPLDARVDKIKDKKPRKKAMESSSNSDSDSGTSSDTSSEGISSSDSDDLEEDEEEEDQSIEESEDDDSDSESEAQHKSNNQVLLHGISDPKADGQKATEKAQEKRIHQPLPLASESQTHSFQSQQKQPQVLSQQLPFIFQSSQAKEESVNKHTSVIQSTGLVSNVKPLSLVNQAKKETYMKLIVPSPDVLKAGNKNTSEESSLLTSELRSKREQYKQAFPSQLKKQESSKSLKKVIAALSNPKATSSSPAHPKQTLENNHPNPFLTNALLGNHQPNGVIQSVIQEAPLALTTKTKMQSKINENIAAASSTPFSSPVNLSTSGRRTPGNQTPVMPSASPILHSQGKEKAVSNNVNPVKTQHHSHPAKSLVEQFRGTDSDIPSSKDSEDSNEDEEEDDEEEDEEDDEDDESDDSQSESDSNSESDTEGSEEEDDDDKDQDESDSDTEGEKTSMKLNKTTSSVKSPSMSLTGHSTPRNLHIAKAPGSAPAALCSESQSPAFLGTSSSTLTSSPHSGTSKRRRVTDERELRIPLEYGWQRETRIRNFGGRLQGEVAYYAPCGKKLRQYPEVIKYLSRNGIMDISRDNFSFSAKIRVGDFYEARDGPQGMQWCLLKEEDVIPRIRAMEGRRGRPPNPDRQRAREESRMRRRKGRPPNVGNAEFLDNADAKLLRKLQAQEIARQAAQIKLLRKLQKQEQARVAKEAKKQQAIMAAEEKRKQKEQIKIMKQQEKIKRIQQIRMEKELRAQQILEAKKKKKEEAANAKLLEAEKRIKEKEMRRQQAVLLKHQERERRRQHMMLMKAMEARKKAEEKERLKQEKRDEKRLNKERKLEQRRLELEMAKELKKPNEDMCLADQKPLPELPRIPGLVLSGSTFSDCLMVVQFLRNFGKVLGFDVNIDVPNLSVLQEGLLNIGDSMGEVQDLLVRLLSAAVCDPGLITGYKAKTALGEHLLNVGVNRDNVSEILQIFMEAHCGQTELTESLKTKAFQAHTPAQKASVLAFLINELACSKSVVSEIDKNIDYMSNLRRDKWVVEGKLRKLRIIHAKKTGKRDTSGGIDLGEEQHPLGTPTPGRKRRRKGGDSDYDDDDDDDSDDQGDEDDEDEEDKEDKKGKKTDICEDEDEGDQAASVEELEKQIEKLSKQQSQYRRKLFDASHSLRSVMFGQDRYRRRYWILPQCGGIFVEGMESGEGLEEIAKEREKLKKAESVQIKEEMFETSGDSLNCSNTDHCEQKEDLKEKDNTNLFLQKPGSFSKLSKLLEVAKMPPESEVMTPKPNAGANGCTLSYQNSGKHSLGSVQSTATQSNVEKADSNNLFNTGSSGPGKFYSPLPNDQLLKTLTEKNRQWFSLLPRTPCDDTSLTHADMSTASLVTPQSQPPSKSPSPTPAPLGSSAQNPVGLNPFALSPLQVKGGVSMMGLQFCGWPTGVVTSNIPFTSSVPSLGSGLGLSEGNGNSFLTSNVASSKSESPVPQNEKATSAQPAAVEVAKPVDFPSPKPIPEEMQFGWWRIIDPEDLKALLKVLHLRGIREKALQKQIQKHLDYITQACLKNKDVAIIELNENEENQVTRDIVENWSVEEQAMEMDLSVLQQVEDLERRVASASLQVKGWMCPEPASEREDLVYFEHKSFTKLCKEHDGEFTGEDESSAHALERKSDNPLDIAVTRLADLERNIERRIEEDIAPGLRVWRRALSEARSAAQVALCIQQLQKSIAWEKSIMKVYCQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPDGDWFCPACIAKASGQTLKIKKLHVKGKKTNESKKGKKVTLTGDTEDEDSASTSSSLKRGNKDLKKRKMEENTSINLSKQESFTSVKKPKRDDSKDLALCSMILTEMETHEDAWPFLLPVNLKLVPGYKKVIKKPMDFSTIREKLSSGQYPNLETFALDVRLVFDNCETFNEDDSDIGRAGHNMRKYFEKKWTDTFKVS | |||||||
Modified residue (large scale data) | 335 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 405 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 549 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 554 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 556 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 683 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1283 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1285 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1425 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1462 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1465 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1465 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1467 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1467 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1507 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1541 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1680 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1680 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2011 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2014 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2014 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2019 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2019 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Within the BRF-1 ISWI chromatin remodeling complex interacts with SMARCA1; the interaction is direct (PubMed:28801535).
Component of the BRF-5 ISWI chromatin remodeling complex, at least composed of SMARCA5/SNF2H and BAZ2B, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (PubMed:28801535).
Within the BRF-5 ISWI chromatin remodeling complex interacts with SMARCA5/SNF2H; the interaction is direct (PubMed:28801535).
Interacts with acetylated lysine residues on histone H1.4, H2A, H2B, H3 and H4 (in vitro). Interacts with EHMT1 (By similarity).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MESGERLPSSAASSTTPTSSSTPSVASVV | ||||||
Region | 140-348 | Disordered | ||||
Sequence: FAPPAQNHDSSSFHSRTSGKSNRNGPEKGVNGSINGSNTSSVIGINTSVLSTTASSSMGQTKSTSSGGGNRKCNQEQSKNQPLDARVDKIKDKKPRKKAMESSSNSDSDSGTSSDTSSEGISSSDSDDLEEDEEEEDQSIEESEDDDSDSESEAQHKSNNQVLLHGISDPKADGQKATEKAQEKRIHQPLPLASESQTHSFQSQQKQPQ | ||||||
Compositional bias | 144-220 | Polar residues | ||||
Sequence: AQNHDSSSFHSRTSGKSNRNGPEKGVNGSINGSNTSSVIGINTSVLSTTASSSMGQTKSTSSGGGNRKCNQEQSKNQ | ||||||
Compositional bias | 221-242 | Basic and acidic residues | ||||
Sequence: PLDARVDKIKDKKPRKKAMESS | ||||||
Compositional bias | 243-262 | Polar residues | ||||
Sequence: SNSDSDSGTSSDTSSEGISS | ||||||
Compositional bias | 263-288 | Acidic residues | ||||
Sequence: SDSDDLEEDEEEEDQSIEESEDDDSD | ||||||
Compositional bias | 311-325 | Basic and acidic residues | ||||
Sequence: ADGQKATEKAQEKRI | ||||||
Compositional bias | 330-348 | Polar residues | ||||
Sequence: PLASESQTHSFQSQQKQPQ | ||||||
Region | 409-428 | Disordered | ||||
Sequence: LKAGNKNTSEESSLLTSELR | ||||||
Region | 459-479 | Disordered | ||||
Sequence: SNPKATSSSPAHPKQTLENNH | ||||||
Compositional bias | 528-556 | Polar residues | ||||
Sequence: STPFSSPVNLSTSGRRTPGNQTPVMPSAS | ||||||
Region | 528-698 | Disordered | ||||
Sequence: STPFSSPVNLSTSGRRTPGNQTPVMPSASPILHSQGKEKAVSNNVNPVKTQHHSHPAKSLVEQFRGTDSDIPSSKDSEDSNEDEEEDDEEEDEEDDEDDESDDSQSESDSNSESDTEGSEEEDDDDKDQDESDSDTEGEKTSMKLNKTTSSVKSPSMSLTGHSTPRNLHIA | ||||||
Compositional bias | 563-580 | Polar residues | ||||
Sequence: GKEKAVSNNVNPVKTQHH | ||||||
Compositional bias | 604-660 | Acidic residues | ||||
Sequence: SEDSNEDEEEDDEEEDEEDDEDDESDDSQSESDSNSESDTEGSEEEDDDDKDQDESD | ||||||
Compositional bias | 670-692 | Polar residues | ||||
Sequence: MKLNKTTSSVKSPSMSLTGHSTP | ||||||
Compositional bias | 719-733 | Polar residues | ||||
Sequence: GTSSSTLTSSPHSGT | ||||||
Region | 719-740 | Disordered | ||||
Sequence: GTSSSTLTSSPHSGTSKRRRVT | ||||||
Domain | 739-810 | MBD | ||||
Sequence: VTDERELRIPLEYGWQRETRIRNFGGRLQGEVAYYAPCGKKLRQYPEVIKYLSRNGIMDISRDNFSFSAKIR | ||||||
Compositional bias | 841-870 | Basic and acidic residues | ||||
Sequence: MEGRRGRPPNPDRQRAREESRMRRRKGRPP | ||||||
Region | 841-872 | Disordered | ||||
Sequence: MEGRRGRPPNPDRQRAREESRMRRRKGRPPNV | ||||||
Coiled coil | 883-1061 | |||||
Sequence: AKLLRKLQAQEIARQAAQIKLLRKLQKQEQARVAKEAKKQQAIMAAEEKRKQKEQIKIMKQQEKIKRIQQIRMEKELRAQQILEAKKKKKEEAANAKLLEAEKRIKEKEMRRQQAVLLKHQERERRRQHMMLMKAMEARKKAEEKERLKQEKRDEKRLNKERKLEQRRLELEMAKELKK | ||||||
Region | 1021-1043 | Disordered | ||||
Sequence: RKKAEEKERLKQEKRDEKRLNKE | ||||||
Domain | 1087-1152 | DDT | ||||
Sequence: GSTFSDCLMVVQFLRNFGKVLGFDVNIDVPNLSVLQEGLLNIGDSMGEVQDLLVRLLSAAVCDPGL | ||||||
Region | 1265-1341 | Disordered | ||||
Sequence: KRDTSGGIDLGEEQHPLGTPTPGRKRRRKGGDSDYDDDDDDDSDDQGDEDDEDEEDKEDKKGKKTDICEDEDEGDQA | ||||||
Compositional bias | 1299-1320 | Acidic residues | ||||
Sequence: YDDDDDDDSDDQGDEDDEDEED | ||||||
Coiled coil | 1334-1375 | |||||
Sequence: DEDEGDQAASVEELEKQIEKLSKQQSQYRRKLFDASHSLRSV | ||||||
Region | 1503-1542 | Disordered | ||||
Sequence: SGKHSLGSVQSTATQSNVEKADSNNLFNTGSSGPGKFYSP | ||||||
Region | 1582-1607 | Disordered | ||||
Sequence: SLVTPQSQPPSKSPSPTPAPLGSSAQ | ||||||
Compositional bias | 1670-1691 | Polar residues | ||||
Sequence: TSNVASSKSESPVPQNEKATSA | ||||||
Region | 1670-1694 | Disordered | ||||
Sequence: TSNVASSKSESPVPQNEKATSAQPA | ||||||
Zinc finger | 1931-1981 | PHD-type | ||||
Sequence: KVYCQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPDGDWFCPACIAK | ||||||
Region | 1998-2040 | Disordered | ||||
Sequence: KTNESKKGKKVTLTGDTEDEDSASTSSSLKRGNKDLKKRKMEE | ||||||
Domain | 2077-2147 | Bromo | ||||
Sequence: ETHEDAWPFLLPVNLKLVPGYKKVIKKPMDFSTIREKLSSGQYPNLETFALDVRLVFDNCETFNEDDSDIG |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing. Experimental confirmation may be lacking for some isoforms.
Q9UIF8-1
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
- Length2,168
- Mass (Da)240,459
- Last updated2009-05-05 v3
- ChecksumC64EEEE6243CF779
Q9UIF8-2
- Name2
Q9UIF8-3
- Name3
- Differences from canonical
- 789-822: Missing
Q9UIF8-4
- Name4
- Differences from canonical
- 1-196: Missing
Q9UIF8-5
- Name5
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037114 | 1-196 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 95 | in Ref. 6; AAH12576 | ||||
Sequence: L → G | ||||||
Alternative sequence | VSP_037115 | 112-113 | in isoform 2 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 144-220 | Polar residues | ||||
Sequence: AQNHDSSSFHSRTSGKSNRNGPEKGVNGSINGSNTSSVIGINTSVLSTTASSSMGQTKSTSSGGGNRKCNQEQSKNQ | ||||||
Compositional bias | 221-242 | Basic and acidic residues | ||||
Sequence: PLDARVDKIKDKKPRKKAMESS | ||||||
Compositional bias | 243-262 | Polar residues | ||||
Sequence: SNSDSDSGTSSDTSSEGISS | ||||||
Compositional bias | 263-288 | Acidic residues | ||||
Sequence: SDSDDLEEDEEEEDQSIEESEDDDSD | ||||||
Compositional bias | 311-325 | Basic and acidic residues | ||||
Sequence: ADGQKATEKAQEKRI | ||||||
Compositional bias | 330-348 | Polar residues | ||||
Sequence: PLASESQTHSFQSQQKQPQ | ||||||
Sequence conflict | 333 | in Ref. 1; BAA89212 | ||||
Sequence: S → F | ||||||
Compositional bias | 528-556 | Polar residues | ||||
Sequence: STPFSSPVNLSTSGRRTPGNQTPVMPSAS | ||||||
Compositional bias | 563-580 | Polar residues | ||||
Sequence: GKEKAVSNNVNPVKTQHH | ||||||
Compositional bias | 604-660 | Acidic residues | ||||
Sequence: SEDSNEDEEEDDEEEDEEDDEDDESDDSQSESDSNSESDTEGSEEEDDDDKDQDESD | ||||||
Alternative sequence | VSP_000553 | 633-730 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 670-692 | Polar residues | ||||
Sequence: MKLNKTTSSVKSPSMSLTGHSTP | ||||||
Compositional bias | 719-733 | Polar residues | ||||
Sequence: GTSSSTLTSSPHSGT | ||||||
Alternative sequence | VSP_000554 | 789-822 | in isoform 3 and isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 823 | in Ref. 1; BAA89212 | ||||
Sequence: G → E | ||||||
Compositional bias | 841-870 | Basic and acidic residues | ||||
Sequence: MEGRRGRPPNPDRQRAREESRMRRRKGRPP | ||||||
Sequence conflict | 918 | in Ref. 6; AAH12576 | ||||
Sequence: E → K | ||||||
Sequence conflict | 986 | in Ref. 6; AAH12576 | ||||
Sequence: R → Q | ||||||
Compositional bias | 1299-1320 | Acidic residues | ||||
Sequence: YDDDDDDDSDDQGDEDDEDEED | ||||||
Sequence conflict | 1324 | in Ref. 1; BAA89212 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 1379 | in Ref. 1; BAA89212 | ||||
Sequence: Q → P | ||||||
Sequence conflict | 1391 | in Ref. 1; BAA89212 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 1649 | in Ref. 1; BAA89212 | ||||
Sequence: S → L | ||||||
Compositional bias | 1670-1691 | Polar residues | ||||
Sequence: TSNVASSKSESPVPQNEKATSA | ||||||
Sequence conflict | 2034 | in Ref. 1; BAA89212 | ||||
Sequence: K → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB032255 EMBL· GenBank· DDBJ | BAA89212.1 EMBL· GenBank· DDBJ | mRNA | ||
AB040909 EMBL· GenBank· DDBJ | BAA96000.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL080173 EMBL· GenBank· DDBJ | CAB45759.1 EMBL· GenBank· DDBJ | mRNA | ||
AL834381 EMBL· GenBank· DDBJ | CAD39044.2 EMBL· GenBank· DDBJ | mRNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11404.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11405.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11407.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC012576 EMBL· GenBank· DDBJ | AAH12576.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK027612 EMBL· GenBank· DDBJ | BAB55231.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |