Q9P281 · BAHC1_HUMAN
- ProteinBAH and coiled-coil domain-containing protein 1
- GeneBAHCC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2639 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
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 | |
---|---|---|
Molecular Function | chromatin binding |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBAH and coiled-coil domain-containing protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9P281
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_061559 | 272 | in dbSNP:rs12952981 | |||
Sequence: A → T | ||||||
Natural variant | VAR_059589 | 1168 | in dbSNP:rs7213444 | |||
Sequence: T → A | ||||||
Natural variant | VAR_061560 | 1434 | in dbSNP:rs35572189 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_061561 | 1678 | in dbSNP:rs12601317 | |||
Sequence: T → A | ||||||
Natural variant | VAR_061562 | 2029 | in dbSNP:rs34680524 | |||
Sequence: V → I | ||||||
Natural variant | VAR_050685 | 2510 | in dbSNP:rs8746 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,495 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000312118 | 1-2639 | UniProt | BAH and coiled-coil domain-containing protein 1 | |||
Sequence: MDGRDFAPPPHLLSERGSLGHRSAAAAARLAPAGPAAQPPAHFQPGKYFPSPLPMASHTASSRLMGSSPASSFMGSFLTSSLGSAASTHPSGPSSSPPEQAYRGSHPTTSQIWFSHSHEAPGYPRFSGSLASTFLPVSHLDHHGNSNVLYGQHRFYGTQKDNFYLRNLPPQPTLLPANHNFPSVARAAPAHPMGSCSRDRDRGEAGSLQKGPKDFDRFLVGKELGREKAGKAAEGKERPAAEEDGGKERHKLVLPVPADGHCREGGPAPRGACEGRPKHLTSCLLNTKVLNGEMGRAALASCAGGMLGRPGTGVVTSGRCAKEAAGPPEPGPAFSECLERRQMLHHTASYAGPPPPLSTAAGSFPCLQLHGGPDGLCPLQDKAPRDLKASGPTFVPSVGHLADKGRPFQAAEACAVAGEGKDRHLEGTMAPDHAAPYGVSYAHLKAEGKGERRPGGFEAALNPRLKGLDYLSSAGPEASFPGLPKSGLDKSGYFELPTSSQDCARPGHQDPLGGKAPQACCTLDKTVGKEAPAGPPGAQKVARIRHQQHLMAAEVEQGGIGAEAKRKSLELASLGYSGPHLPPWGVQAGQGTAMAISEERKAGAYLDPFGSGLQQAALLPQELPAPPDEVSAMKNLLKYSSQALVVGQKAPLVGLGGLKASCIQQEAKFLSSKGPGQSERPDCARSREHDTTHGDGEVRQPPVGIAVALARQKDTVSRSEAAYGTNTARQGRAAPAFKGGGGPRSTHALDLEAEEERTRLCDDRLGLASRELLLQDSKDRVEFARIHPPSSCPGDLAPHLMMQSGQLGGDPAPHTHPHPPWLPRTRSPSLWMGGHSYGLGHPALHQNLPPGFPASVAGPVPSVFPLPQDAPTQLVILPSEPTPHSAPHALADVMDQASLWPPMYGGRGPASHMQHPGQLPVYSRPQLLRQQELYALQQQRAAQFQRKPEDQHLDLEEPAQEKAPKSTHKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASSPTPPPRPSAPCTLNVCPASSPGPGSRVRSAEEKNGEGQQSTADIITSEPVARAHSVAHAGLEFLASNDPSTSASQSFGITDLPPGYLRPMAGLGFSLPSDVHSSNLEDPETMQTTAPGAQPEPTRTFLPGEPPPCSPRSLEEPGLLSGAREATQDLAATPYPTERGPQGKAADPSPLEGLQELQCAALLEAGGPEATGQAHSTQGGAREERSREEGEQGPSSGASSQVLEQRAGSPGALEDEGEQPAPEEDELEEDELGQQSMEDSEEDCGGAPDNSHPPRALPGLDALVAATINLGDLPSDSPPDPQPPAASGPPSTVPLPHSSGIHGIALLSELADLAIQRQRSERTVPEEEEDVLAFNLQHLATLATAWSLVEAAGLDSSTAPAQPPTANPCSGPRLTPRMQILQRKDTWTPKTKPVCPLKAAIDRLDTQEVGMRVRLAELQRRYKEKQRELARLQRKHDHERDESSRSPARRGPGRPRKRKHSSSLPAPRPTGPLPRSDGKKVKAVRTSLGLLCAELRGGSGGEPAKKRSKLERSVYAGLQTASVEKAQCKKSSCQGGLAPSVAHRVAQLKPKVKSKGLPTGLSSFQQKEATPGGRIREKLSRAKSAKVSGATRHPQPKGHGSRETPRCPAQPSVAASQEAGSGYDSEDCEGLLGTEAPPREAGLLLHTGASVAVLGPSPSSVVKMEANQKAKKKKERQGLLGACRLSSPESEVKIKRRSVKAKVGTTLERAPGQRPPGALGKKKAKGKAKGSLRAEPGATPSRDALFNPSRAFACREEGSQLASERLKRATRKGTVLQPVLRRKNGALSITLATRNAKAILGKGRKLSKVKHKAGKQGKGRAVSRLLESFAVEEDFEFDDNSSFSEEEEDEEEEEEDSGPLSAEQSAALARSCAIHKEDLRDGLPVLIPKEDSLLYAGSVRTLQPPDIYSIVIEGERGNRQRIYSLEQLLQEAVLDVRPQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASGDEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFKIQCTEPSPALLVSSSCRRTKKVSSEAPPPSEAATPSLSPKAQDGPEALKTPGKKSISKDKAGKAELLTSGAKSPTGASDHFLGRRGSPLLSWSAVAQTKRKAVAAASKGPGVLQNLFQLNGSSKKLRAREALFPVHSVATPIFGNGFRADSFSSLASSYAPFVGGTGPGLPRGAHKLLRAKKAERVEAEKGGRRRAGGEFLVKLDHEGVTSPKNKTCKALLMGDKDFSPKLGRPLPSPSYVHPALVGKDKKGRAPIPPLPMGLALRKYAGQAEFPLPYDSDCHSSFSDEDEDGPGLAAGVPSRFLARLSVSSSSSGSSTSSSSGSVSTSSLCSSDNEDSSYSSDDEDPALLLQTCLTHPVPTLLAQPEALRSKGSGPHAHAQRCFLSRATVAGTGAGSGPSSSSKSKLKRKEALSFSKAKELSRRQRPPSVENRPKISAFLPARQLWKWSGNPTQRRGMKGKARKLFYKAIVRGEETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHKCQVVAREQYEQMARSRKCQDRQDLYYLAGTYDPTTGRLVTADGVPILC | |||||||
Modified residue | 222 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 982 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1141 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1718 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2075 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2112 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2128 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2247 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2248 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2274 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2274 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2276 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 23-49 | Disordered | ||||
Sequence: SAAAAARLAPAGPAAQPPAHFQPGKYF | ||||||
Region | 84-107 | Disordered | ||||
Sequence: SAASTHPSGPSSSPPEQAYRGSHP | ||||||
Region | 188-249 | Disordered | ||||
Sequence: APAHPMGSCSRDRDRGEAGSLQKGPKDFDRFLVGKELGREKAGKAAEGKERPAAEEDGGKER | ||||||
Compositional bias | 195-249 | Basic and acidic residues | ||||
Sequence: SCSRDRDRGEAGSLQKGPKDFDRFLVGKELGREKAGKAAEGKERPAAEEDGGKER | ||||||
Region | 669-702 | Disordered | ||||
Sequence: FLSSKGPGQSERPDCARSREHDTTHGDGEVRQPP | ||||||
Compositional bias | 680-696 | Basic and acidic residues | ||||
Sequence: RPDCARSREHDTTHGDG | ||||||
Region | 716-746 | Disordered | ||||
Sequence: VSRSEAAYGTNTARQGRAAPAFKGGGGPRST | ||||||
Region | 939-1047 | Disordered | ||||
Sequence: QRAAQFQRKPEDQHLDLEEPAQEKAPKSTHKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASSPTPPPRPSAPCTLNVCPASSPGPGSRVRSAEEKNGEGQQSTA | ||||||
Compositional bias | 945-964 | Basic and acidic residues | ||||
Sequence: QRKPEDQHLDLEEPAQEKAP | ||||||
Compositional bias | 976-1016 | Pro residues | ||||
Sequence: TAPGAPSPAAGPTKLPPCCHPPDPKPPASSPTPPPRPSAPC | ||||||
Compositional bias | 1104-1126 | Polar residues | ||||
Sequence: SDVHSSNLEDPETMQTTAPGAQP | ||||||
Region | 1104-1331 | Disordered | ||||
Sequence: SDVHSSNLEDPETMQTTAPGAQPEPTRTFLPGEPPPCSPRSLEEPGLLSGAREATQDLAATPYPTERGPQGKAADPSPLEGLQELQCAALLEAGGPEATGQAHSTQGGAREERSREEGEQGPSSGASSQVLEQRAGSPGALEDEGEQPAPEEDELEEDELGQQSMEDSEEDCGGAPDNSHPPRALPGLDALVAATINLGDLPSDSPPDPQPPAASGPPSTVPLPHSSG | ||||||
Compositional bias | 1223-1237 | Polar residues | ||||
Sequence: QGPSSGASSQVLEQR | ||||||
Compositional bias | 1248-1275 | Acidic residues | ||||
Sequence: GEQPAPEEDELEEDELGQQSMEDSEEDC | ||||||
Compositional bias | 1307-1322 | Pro residues | ||||
Sequence: DSPPDPQPPAASGPPS | ||||||
Coiled coil | 1439-1473 | |||||
Sequence: EVGMRVRLAELQRRYKEKQRELARLQRKHDHERDE | ||||||
Compositional bias | 1457-1480 | Basic and acidic residues | ||||
Sequence: QRELARLQRKHDHERDESSRSPAR | ||||||
Region | 1457-1513 | Disordered | ||||
Sequence: QRELARLQRKHDHERDESSRSPARRGPGRPRKRKHSSSLPAPRPTGPLPRSDGKKVK | ||||||
Region | 1582-1666 | Disordered | ||||
Sequence: KVKSKGLPTGLSSFQQKEATPGGRIREKLSRAKSAKVSGATRHPQPKGHGSRETPRCPAQPSVAASQEAGSGYDSEDCEGLLGTE | ||||||
Region | 1722-1776 | Disordered | ||||
Sequence: EVKIKRRSVKAKVGTTLERAPGQRPPGALGKKKAKGKAKGSLRAEPGATPSRDAL | ||||||
Compositional bias | 1868-1890 | Acidic residues | ||||
Sequence: FDDNSSFSEEEEDEEEEEEDSGP | ||||||
Region | 1868-1893 | Disordered | ||||
Sequence: FDDNSSFSEEEEDEEEEEEDSGPLSA | ||||||
Region | 2057-2119 | Disordered | ||||
Sequence: KKVSSEAPPPSEAATPSLSPKAQDGPEALKTPGKKSISKDKAGKAELLTSGAKSPTGASDHFL | ||||||
Region | 2317-2336 | Disordered | ||||
Sequence: SDCHSSFSDEDEDGPGLAAG | ||||||
Compositional bias | 2348-2375 | Polar residues | ||||
Sequence: SSSSSGSSTSSSSGSVSTSSLCSSDNED | ||||||
Region | 2348-2383 | Disordered | ||||
Sequence: SSSSSGSSTSSSSGSVSTSSLCSSDNEDSSYSSDDE | ||||||
Region | 2432-2472 | Disordered | ||||
Sequence: GAGSGPSSSSKSKLKRKEALSFSKAKELSRRQRPPSVENRP | ||||||
Compositional bias | 2442-2468 | Basic and acidic residues | ||||
Sequence: KSKLKRKEALSFSKAKELSRRQRPPSV | ||||||
Domain | 2513-2633 | BAH | ||||
Sequence: ETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHKCQVVAREQYEQMARSRKCQDRQDLYYLAGTYDPTTGRLVTAD |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,639
- Mass (Da)280,016
- Last updated2018-03-28 v4
- Checksum3A21114C7ACF1D9D
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAG2UUZ7 | A0AAG2UUZ7_HUMAN | BAHCC1 | 2639 | ||
A0AAG2UUQ8 | A0AAG2UUQ8_HUMAN | BAHCC1 | 2608 | ||
F8WBW8 | F8WBW8_HUMAN | BAHCC1 | 2608 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 195-249 | Basic and acidic residues | ||||
Sequence: SCSRDRDRGEAGSLQKGPKDFDRFLVGKELGREKAGKAAEGKERPAAEEDGGKER | ||||||
Compositional bias | 680-696 | Basic and acidic residues | ||||
Sequence: RPDCARSREHDTTHGDG | ||||||
Compositional bias | 945-964 | Basic and acidic residues | ||||
Sequence: QRKPEDQHLDLEEPAQEKAP | ||||||
Compositional bias | 976-1016 | Pro residues | ||||
Sequence: TAPGAPSPAAGPTKLPPCCHPPDPKPPASSPTPPPRPSAPC | ||||||
Compositional bias | 1104-1126 | Polar residues | ||||
Sequence: SDVHSSNLEDPETMQTTAPGAQP | ||||||
Compositional bias | 1223-1237 | Polar residues | ||||
Sequence: QGPSSGASSQVLEQR | ||||||
Compositional bias | 1248-1275 | Acidic residues | ||||
Sequence: GEQPAPEEDELEEDELGQQSMEDSEEDC | ||||||
Compositional bias | 1307-1322 | Pro residues | ||||
Sequence: DSPPDPQPPAASGPPS | ||||||
Compositional bias | 1457-1480 | Basic and acidic residues | ||||
Sequence: QRELARLQRKHDHERDESSRSPAR | ||||||
Compositional bias | 1868-1890 | Acidic residues | ||||
Sequence: FDDNSSFSEEEEDEEEEEEDSGP | ||||||
Compositional bias | 2348-2375 | Polar residues | ||||
Sequence: SSSSSGSSTSSSSGSVSTSSLCSSDNED | ||||||
Compositional bias | 2442-2468 | Basic and acidic residues | ||||
Sequence: KSKLKRKEALSFSKAKELSRRQRPPSV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC110285 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC139149 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC213194 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AADB02019016 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AB040880 EMBL· GenBank· DDBJ | BAA95971.1 EMBL· GenBank· DDBJ | mRNA | ||
BC033222 EMBL· GenBank· DDBJ | AAH33222.1 EMBL· GenBank· DDBJ | mRNA |