O60706 · ABCC9_HUMAN
- ProteinATP-binding cassette sub-family C member 9
- GeneABCC9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1549 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Sleep duration is influenced both by environmental and genetic factors, with an estimated heritability of about 40%. Numerous genes are expected to contribute to the regulation of sleep duration
Features
Showing features for binding site.
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
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-binding cassette sub-family C member 9
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60706
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-30 | Extracellular | ||||
Sequence: MSLSFCGNNISSYNINDGVLQNSCFVDALN | ||||||
Transmembrane | 31-51 | Helical; Name=1 | ||||
Sequence: LVPHVFLLFITFPILFIGWGS | ||||||
Topological domain | 52-72 | Cytoplasmic | ||||
Sequence: QSSKVQIHHNTWLHFPGHNLR | ||||||
Transmembrane | 73-93 | Helical; Name=2 | ||||
Sequence: WILTFALLFVHVCEIAEGIVS | ||||||
Topological domain | 94-101 | Extracellular | ||||
Sequence: DSRRESRH | ||||||
Transmembrane | 102-122 | Helical; Name=3 | ||||
Sequence: LHLFMPAVMGFVATTTSIVYY | ||||||
Topological domain | 123-132 | Cytoplasmic | ||||
Sequence: HNIETSNFPK | ||||||
Transmembrane | 133-153 | Helical; Name=4 | ||||
Sequence: LLLALFLYWVMAFITKTIKLV | ||||||
Topological domain | 154-167 | Extracellular | ||||
Sequence: KYCQSGLDISNLRF | ||||||
Transmembrane | 168-188 | Helical; Name=5 | ||||
Sequence: CITGMMVILNGLLMAVEINVI | ||||||
Topological domain | 189-301 | Cytoplasmic | ||||
Sequence: RVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSS | ||||||
Transmembrane | 302-322 | Helical; Name=6 | ||||
Sequence: TFRYLADLLGFAGPLCISGIV | ||||||
Topological domain | 323-350 | Extracellular | ||||
Sequence: QRVNETQNGTNNTTGISETLSSKEFLEN | ||||||
Transmembrane | 351-371 | Helical; Name=7 | ||||
Sequence: AYVLAVLLFLALILQRTFLQA | ||||||
Topological domain | 372-423 | Cytoplasmic | ||||
Sequence: SYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQ | ||||||
Transmembrane | 424-444 | Helical; Name=8 | ||||
Sequence: LMWFLFLCPNLWAMPVQIIMG | ||||||
Topological domain | 445-455 | Extracellular | ||||
Sequence: VILLYNLLGSS | ||||||
Transmembrane | 456-476 | Helical; Name=9 | ||||
Sequence: ALVGAAVIVLLAPIQYFIATK | ||||||
Topological domain | 477-531 | Cytoplasmic | ||||
Sequence: LAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKT | ||||||
Transmembrane | 532-552 | Helical; Name=10 | ||||
Sequence: FALYTSLSIFMNAAIPIAAVL | ||||||
Topological domain | 553-571 | Extracellular | ||||
Sequence: ATFVTHAYASGNNLKPAEA | ||||||
Transmembrane | 572-592 | Helical; Name=11 | ||||
Sequence: FASLSLFHILVTPLFLLSTVV | ||||||
Topological domain | 593-990 | Cytoplasmic | ||||
Sequence: RFAVKAIISVQKLNEFLLSDEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPGRYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWRYLTSGG | ||||||
Transmembrane | 991-1011 | Helical; Name=12 | ||||
Sequence: FFLLILMIFSKLLKHSVIVAI | ||||||
Topological domain | 1012-1034 | Extracellular | ||||
Sequence: DYWLATWTSEYSINNTGKADQTY | ||||||
Transmembrane | 1035-1055 | Helical; Name=13 | ||||
Sequence: YVAGFSILCGAGIFLCLVTSL | ||||||
Topological domain | 1056-1127 | Cytoplasmic | ||||
Sequence: TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGM | ||||||
Transmembrane | 1128-1148 | Helical; Name=14 | ||||
Sequence: ISYATPVFLVALLPLGVAFYF | ||||||
Topological domain | 1149-1245 | Extracellular | ||||
Sequence: IQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNS | ||||||
Transmembrane | 1246-1266 | Helical; Name=15 | ||||
Sequence: GLVGLGLLYALTITNYLNWVV | ||||||
Topological domain | 1267-1549 | Cytoplasmic | ||||
Sequence: RNLADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cardiomyopathy, dilated, 1O (CMD1O)
- Note
- DescriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
- See alsoMIM:608569
Natural variants in CMD1O
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_018483 | 1513 | A>T | in CMD1O; dbSNP:rs72559751 |
Atrial fibrillation, familial, 12 (ATFB12)
- Note
- DescriptionA familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure.
- See alsoMIM:614050
Natural variants in ATFB12
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_066210 | 1547 | T>I | in ATFB12; compromises adenine nucleotide-dependent induction of KATP current; mutant ABCC9 that is coexpressed with KCNJ11 pore generates an aberrant channel that retains ATP-induced inhibition of potassium current, but shows a blunted response to ADP; dbSNP:rs387906805 |
Hypertrichotic osteochondrodysplasia (HTOCD)
- Note
- DescriptionA rare disorder characterized by congenital hypertrichosis, neonatal macrosomia, a distinct osteochondrodysplasia, and cardiomegaly. The hypertrichosis leads to thick scalp hair, which extends onto the forehead, and a general increase in body hair. In addition, macrocephaly and coarse facial features, including a broad nasal bridge, epicanthal folds, a wide mouth, and full lips, can be suggestive of a storage disorder. About half of affected individuals are macrosomic and edematous at birth, whereas in childhood they usually have a muscular appearance with little subcutaneous fat. Thickened calvarium, narrow thorax, wide ribs, flattened or ovoid vertebral bodies, coxa valga, osteopenia, enlarged medullary canals, and metaphyseal widening of long bones have been reported. Cardiac manifestations such as patent ductus arteriosus, ventricular hypertrophy, pulmonary hypertension, and pericardial effusions are present in approximately 80% of cases. Motor development is usually delayed due to hypotonia. Most patients have a mild speech delay, and a small percentage have learning difficulties or intellectual disability.
- See alsoMIM:239850
Natural variants in HTOCD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_068485 | 60 | H>Y | in HTOCD; dbSNP:rs387907230 | |
VAR_068486 | 207 | D>E | in HTOCD; dbSNP:rs2137921501 | |
VAR_068487 | 380 | G>C | in HTOCD; dbSNP:rs1165205076 | |
VAR_068488 | 432 | P>L | in HTOCD; mutant channels show reduced ATP sensitivity; rat ABCC9 construct containing this mutation shows gain of function | |
VAR_068489 | 478 | A>V | in HTOCD; rat ABCC9 construct containing this mutation shows gain of function; dbSNP:rs387907211 | |
VAR_068490 | 1020 | S>P | in HTOCD; dbSNP:rs387907229 | |
VAR_068491 | 1039 | F>S | in HTOCD | |
VAR_068492 | 1043 | C>Y | in HTOCD; rat ABCC9 construct containing this mutation shows gain of function; dbSNP:rs387907210 | |
VAR_068493 | 1054 | S>Y | in HTOCD | |
VAR_068494 | 1116 | R>C | in HTOCD; dbSNP:rs387907228 | |
VAR_068495 | 1116 | R>H | in HTOCD; mutant channels show reduced ATP sensitivity; dbSNP:rs387907227 | |
VAR_068496 | 1154 | R>Q | in HTOCD; mutant channels show reduced ATP sensitivity; dbSNP:rs387907209 | |
VAR_068497 | 1154 | R>W | in HTOCD; dbSNP:rs387907208 |
Intellectual disability and myopathy syndrome (IDMYS)
- Note
- DescriptionAn autosomal recessive disorder characterized by global developmental delay, mildly impaired intellectual development, hypotonia, muscle weakness and fatigue, and white matter abnormalities on brain imaging. Variable additional features may include sensorineural hearing loss, dysmorphic facies, and progressive heart disease.
- See alsoMIM:619719
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_068485 | 60 | in HTOCD; dbSNP:rs387907230 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_068486 | 207 | in HTOCD; dbSNP:rs2137921501 | |||
Sequence: D → E | ||||||
Natural variant | VAR_068487 | 380 | in HTOCD; dbSNP:rs1165205076 | |||
Sequence: G → C | ||||||
Natural variant | VAR_068488 | 432 | in HTOCD; mutant channels show reduced ATP sensitivity; rat ABCC9 construct containing this mutation shows gain of function | |||
Sequence: P → L | ||||||
Natural variant | VAR_068489 | 478 | in HTOCD; rat ABCC9 construct containing this mutation shows gain of function; dbSNP:rs387907211 | |||
Sequence: A → V | ||||||
Natural variant | VAR_068490 | 1020 | in HTOCD; dbSNP:rs387907229 | |||
Sequence: S → P | ||||||
Natural variant | VAR_068491 | 1039 | in HTOCD | |||
Sequence: F → S | ||||||
Natural variant | VAR_068492 | 1043 | in HTOCD; rat ABCC9 construct containing this mutation shows gain of function; dbSNP:rs387907210 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_068493 | 1054 | in HTOCD | |||
Sequence: S → Y | ||||||
Natural variant | VAR_048143 | 1108 | in dbSNP:rs35404804 | |||
Sequence: P → S | ||||||
Natural variant | VAR_068494 | 1116 | in HTOCD; dbSNP:rs387907228 | |||
Sequence: R → C | ||||||
Natural variant | VAR_068495 | 1116 | in HTOCD; mutant channels show reduced ATP sensitivity; dbSNP:rs387907227 | |||
Sequence: R → H | ||||||
Natural variant | VAR_068496 | 1154 | in HTOCD; mutant channels show reduced ATP sensitivity; dbSNP:rs387907209 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_068497 | 1154 | in HTOCD; dbSNP:rs387907208 | |||
Sequence: R → W | ||||||
Natural variant | VAR_083082 | 1160 | in dbSNP:rs780799175 | |||
Sequence: L → R | ||||||
Natural variant | VAR_018483 | 1513 | in CMD1O; dbSNP:rs72559751 | |||
Sequence: A → T | ||||||
Natural variant | VAR_066210 | 1547 | in ATFB12; compromises adenine nucleotide-dependent induction of KATP current; mutant ABCC9 that is coexpressed with KCNJ11 pore generates an aberrant channel that retains ATP-induced inhibition of potassium current, but shows a blunted response to ADP; dbSNP:rs387906805 | |||
Sequence: T → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,877 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, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000093402 | 1-1549 | UniProt | ATP-binding cassette sub-family C member 9 | |||
Sequence: MSLSFCGNNISSYNINDGVLQNSCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYCQSGLDISNLRFCITGMMVILNGLLMAVEINVIRVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPGRYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK | |||||||
Glycosylation | 9 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 326 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 330 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 333 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 334 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 630 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 658 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 297-597 | ABC transmembrane type-1 1 | ||||
Sequence: ILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVK | ||||||
Domain | 672-912 | ABC transporter 1 | ||||
Sequence: IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKT | ||||||
Region | 944-967 | Disordered | ||||
Sequence: REAKAQMEDEDEEEEEEEDEDDNM | ||||||
Compositional bias | 950-966 | Acidic residues | ||||
Sequence: MEDEDEEEEEEEDEDDN | ||||||
Domain | 994-1274 | ABC transmembrane type-1 2 | ||||
Sequence: LILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEV | ||||||
Domain | 1312-1546 | ABC transporter 2 | ||||
Sequence: IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVM |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O60706-1
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.
- NameSUR2A
- Length1,549
- Mass (Da)174,223
- Last updated2008-11-25 v2
- Checksum55508C9343AB1218
O60706-2
- NameSUR2B
- Differences from canonical
- 1508-1549: SSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK → HTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YFV4 | H0YFV4_HUMAN | ABCC9 | 1176 | ||
G3V1N6 | G3V1N6_HUMAN | ABCC9 | 170 | ||
A0A804HHX2 | A0A804HHX2_HUMAN | ABCC9 | 1284 | ||
A0A804HIU2 | A0A804HIU2_HUMAN | ABCC9 | 1235 | ||
A0A804HK56 | A0A804HK56_HUMAN | ABCC9 | 163 | ||
A0A804HL58 | A0A804HL58_HUMAN | ABCC9 | 162 | ||
A0A804HL22 | A0A804HL22_HUMAN | ABCC9 | 1480 | ||
A0A804HKB7 | A0A804HKB7_HUMAN | ABCC9 | 1532 | ||
Q8N4N7 | Q8N4N7_HUMAN | ABCC9 | 149 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 586 | in Ref. 1; AAC16057/AAC16058 | ||||
Sequence: F → S | ||||||
Sequence conflict | 589 | in Ref. 1; AAC16057/AAC16058 | ||||
Sequence: S → F | ||||||
Compositional bias | 950-966 | Acidic residues | ||||
Sequence: MEDEDEEEEEEEDEDDN | ||||||
Sequence conflict | 1503 | in Ref. 1; AAC16057/AAC16058 | ||||
Sequence: I → M | ||||||
Alternative sequence | VSP_000058 | 1508-1549 | in isoform SUR2B | |||
Sequence: SSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK → HTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF061323 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061289 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061290 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061291 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061292 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061293 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061294 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061295 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061296 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061297 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061298 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061299 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061300 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061301 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061302 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061303 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061304 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061305 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061306 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061307 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061308 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061309 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061310 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061311 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061312 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061313 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061314 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061315 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061316 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061317 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061318 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061319 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061320 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061321 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061322 EMBL· GenBank· DDBJ | AAC16057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061324 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061289 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061290 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061291 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061292 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061293 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061294 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061295 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061296 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061297 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061298 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061299 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061300 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061301 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061302 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061303 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061304 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061305 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061306 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061307 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061308 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061309 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061310 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061311 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061312 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061313 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061314 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061315 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061316 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061317 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061318 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061319 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061320 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061321 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF061322 EMBL· GenBank· DDBJ | AAC16058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC008250 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC084806 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |