Q13428 · TCOF_HUMAN
- ProteinTreacle protein
- GeneTCOF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1488 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832).
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 | cytosol | |
Cellular Component | fibrillar center | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | protein-macromolecule adaptor activity | |
Molecular Function | RNA binding | |
Molecular Function | scaffold protein binding | |
Biological Process | neural crest cell development | |
Biological Process | neural crest formation | |
Biological Process | nucleolar large rRNA transcription by RNA polymerase I | |
Biological Process | regulation of translation | |
Biological Process | skeletal system development |
Enzyme and pathway databases
Serves as a scaffold protein necessary for the formation of the fibrillar center of the nucleolus through self-assembly.
Names & Taxonomy
Protein names
- Recommended nameTreacle protein
- Alternative names
Gene names
- Community suggested namesTCOF1;Treacle
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13428
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Treacher Collins syndrome 1 (TCS1)
- Note
- DescriptionA form of Treacher Collins syndrome, a disorder of craniofacial development. Treacher Collins syndrome is characterized by a combination of bilateral downward slanting of the palpebral fissures, colobomas of the lower eyelids with a paucity of eyelashes medial to the defect, hypoplasia of the facial bones, cleft palate, malformation of the external ears, atresia of the external auditory canals, and bilateral conductive hearing loss.
- See alsoMIM:154500
Natural variants in TCS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_005630 | 53 | W>R | in TCS1 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_005630 | 53 | in TCS1 | |||
Sequence: W → R | ||||||
Natural variant | VAR_057002 | 221 | in dbSNP:rs11541811 | |||
Sequence: A → P | ||||||
Natural variant | VAR_005631 | 516 | in dbSNP:rs138645438 | |||
Sequence: P → L | ||||||
Natural variant | VAR_029869 | 665 | in dbSNP:rs2071240 | |||
Sequence: A → P | ||||||
Natural variant | VAR_005632 | 887 | in dbSNP:rs7713638 | |||
Sequence: V → A | ||||||
Natural variant | VAR_035666 | 1030 | in a colorectal cancer sample; somatic mutation; dbSNP:rs1206146416 | |||
Sequence: R → K | ||||||
Natural variant | VAR_059729 | 1176 | in dbSNP:rs1136103 | |||
Sequence: P → R | ||||||
Natural variant | VAR_059730 | 1280 | in dbSNP:rs11541812 | |||
Sequence: G → R | ||||||
Natural variant | VAR_005633 | 1390 | in dbSNP:rs15251 | |||
Sequence: A → V | ||||||
Natural variant | VAR_061709 | 1431 | in dbSNP:rs45491898 | |||
Sequence: G → A | ||||||
Natural variant | VAR_005634 | 1432 | in dbSNP:rs151344580 | |||
Sequence: D → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,961 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, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000072459 | 1-1488 | UniProt | Treacle protein | |||
Sequence: MAEARKRRELLPLIYHHLLRAGYVRAAREVKEQSGQKCFLAQPVTLLDIYTHWQQTSELGRKRKAEEDAALQAKKTRVSDPISTSESSEEEEEAEAETAKATPRLASTNSSVLGADLPSSMKEKAKAETEKAGKTGNSMPHPATGKTVANLLSGKSPRKSAEPSANTTLVSETEEEGSVPAFGAAAKPGMVSAGQADSSSEDTSSSSDETDVEGKPSVKPAQVKASSVSTKESPARKAAPAPGKVGDVTPQVKGGALPPAKRAKKPEEESESSEEGSESEEEAPAGTRSQVKASEKILQVRAASAPAKGTPGKGATPAPPGKAGAVASQTKAGKPEEDSESSSEESSDSEEETPAAKALLQAKASGKTSQVGAASAPAKESPRKGAAPAPPGKTGPAVAKAQAGKREEDSQSSSEESDSEEEAPAQAKPSGKAPQVRAASAPAKESPRKGAAPAPPRKTGPAAAQVQVGKQEEDSRSSSEESDSDREALAAMNAAQVKPLGKSPQVKPASTMGMGPLGKGAGPVPPGKVGPATPSAQVGKWEEDSESSSEESSDSSDGEVPTAVAPAQEKSLGNILQAKPTSSPAKGPPQKAGPVAVQVKAEKPMDNSESSEESSDSADSEEAPAAMTAAQAKPALKIPQTKACPKKTNTTASAKVAPVRVGTQAPRKAGTATSPAGSSPAVAGGTQRPAEDSSSSEESDSEEEKTGLAVTVGQAKSVGKGLQVKAASVPVKGSLGQGTAPVLPGKTGPTVTQVKAEKQEDSESSEEESDSEEAAASPAQVKTSVKKTQAKANPAAARAPSAKGTISAPGKVVTAAAQAKQRSPSKVKPPVRNPQNSTVLARGPASVPSVGKAVATAAQAQTGPEEDSGSSEEESDSEEEAETLAQVKPSGKTHQIRAALAPAKESPRKGAAPTPPGKTGPSAAQAGKQDDSGSSSEESDSDGEAPAAVTSAQVIKPPLIFVDPNRSPAGPAATPAQAQAASTPRKARASESTARSSSSESEDEDVIPATQCLTPGIRTNVVTMPTAHPRIAPKASMAGASSSKESSRISDGKKQEGPATQVSKKNPASLPLTQAALKVLAQKASEAQPPVARTQPSSGVDSAVGTLPATSPQSTSVQAKGTNKLRKPKLPEVQQATKAPESSDDSEDSSDSSSGSEEDGEGPQGAKSAHTLGPTPSRTETLVEETAAESSEDDVVAPSQSLLSGYMTPGLTPANSQASKATPKLDSSPSVSSTLAAKDDPDGKQEAKPQQAAGMLSPKTGGKEAASGTTPQKSRKPKKGAGNPQASTLALQSNITQCLLGQPWPLNEAQVQASVVKVLTELLEQERKKVVDTTKESSRKGWESRKRKLSGDQPAARTPRSKKKKKLGAGEGGEASVSPEKTSTTSKGKAKRDKASGDVKEKKGKGSLGSQGAKDEPEEELQKGMGTVEGGDQSNPKSKKEKKKSDKRKKDKEKKEKKKKAKKASTKDSESPSQKKKKKKKKTAEQTV | |||||||
Modified residue | 83 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 83 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 84 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 85 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 87 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 102 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 107 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 111 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 119 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 126 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 134 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 153 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 153 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 155 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 156 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 171 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 171 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 173 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 173 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 233 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 233 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 249 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 272 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 273 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 296 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 310 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 310 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 313 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 316 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 316 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 322 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 349 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 368 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 381 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 413 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 414 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 419 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 440 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 446 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 482 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 484 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 484 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 503 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 503 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 507 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 533 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 581 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 581 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 582 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 583 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 600 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 600 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 620 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 637 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 673 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 674 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 679 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 679 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 699 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 701 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 716 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 720 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 725 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 732 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 734 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 755 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 755 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 755 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 762 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 764 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 764 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 765 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 765 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 769 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 769 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 771 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 777 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 777 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 801 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 823 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 846 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 868 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 870 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 871 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 875 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 877 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 877 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 906 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 906 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 914 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 914 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 967 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 967 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 974 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 974 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 982 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 983 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 983 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 998 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1036 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1050 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1069 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1110 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1111 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1111 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1175 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1175 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1186 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1190 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1222 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1222 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1224 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1228 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1228 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1230 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1233 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1234 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1234 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1238 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1248 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1257 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1257 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1260 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1269 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1270 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1350 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1350 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1358 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1358 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1376 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1376 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1378 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1382 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1384 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1407 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1410 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1410 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1414 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 1414 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1434 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1469 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1471 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1471 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA species. Within this complex directly interacts with NOP56 in an RNA-independent manner (PubMed:12777385).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13428 | ARRB1 P49407 | 3 | EBI-396105, EBI-743313 | |
BINARY | Q13428 | ARRB2 P32121 | 3 | EBI-396105, EBI-714559 | |
BINARY | Q13428 | FGF12 P61328-2 | 9 | EBI-396105, EBI-10699759 | |
BINARY | Q13428 | NBN O60934 | 10 | EBI-396105, EBI-494844 | |
BINARY | Q13428 | SRPK2 P78362 | 2 | EBI-396105, EBI-593303 | |
BINARY | Q13428-5 | APLP2 Q06481-5 | 3 | EBI-25832010, EBI-25646567 | |
BINARY | Q13428-5 | NEK7 Q8TDX7 | 3 | EBI-25832010, EBI-1055945 | |
BINARY | Q13428-5 | PECAM1 P16284 | 3 | EBI-25832010, EBI-716404 | |
BINARY | Q13428-5 | TGFBR2 P37173 | 3 | EBI-25832010, EBI-296151 | |
BINARY | Q13428-5 | VIM P08670 | 3 | EBI-25832010, EBI-353844 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-38 | LisH | ||||
Sequence: KRRELLPLIYHHLLRAGYVRAAREVKEQSGQKC | ||||||
Compositional bias | 57-74 | Basic and acidic residues | ||||
Sequence: SELGRKRKAEEDAALQAK | ||||||
Region | 57-1288 | Disordered | ||||
Sequence: SELGRKRKAEEDAALQAKKTRVSDPISTSESSEEEEEAEAETAKATPRLASTNSSVLGADLPSSMKEKAKAETEKAGKTGNSMPHPATGKTVANLLSGKSPRKSAEPSANTTLVSETEEEGSVPAFGAAAKPGMVSAGQADSSSEDTSSSSDETDVEGKPSVKPAQVKASSVSTKESPARKAAPAPGKVGDVTPQVKGGALPPAKRAKKPEEESESSEEGSESEEEAPAGTRSQVKASEKILQVRAASAPAKGTPGKGATPAPPGKAGAVASQTKAGKPEEDSESSSEESSDSEEETPAAKALLQAKASGKTSQVGAASAPAKESPRKGAAPAPPGKTGPAVAKAQAGKREEDSQSSSEESDSEEEAPAQAKPSGKAPQVRAASAPAKESPRKGAAPAPPRKTGPAAAQVQVGKQEEDSRSSSEESDSDREALAAMNAAQVKPLGKSPQVKPASTMGMGPLGKGAGPVPPGKVGPATPSAQVGKWEEDSESSSEESSDSSDGEVPTAVAPAQEKSLGNILQAKPTSSPAKGPPQKAGPVAVQVKAEKPMDNSESSEESSDSADSEEAPAAMTAAQAKPALKIPQTKACPKKTNTTASAKVAPVRVGTQAPRKAGTATSPAGSSPAVAGGTQRPAEDSSSSEESDSEEEKTGLAVTVGQAKSVGKGLQVKAASVPVKGSLGQGTAPVLPGKTGPTVTQVKAEKQEDSESSEEESDSEEAAASPAQVKTSVKKTQAKANPAAARAPSAKGTISAPGKVVTAAAQAKQRSPSKVKPPVRNPQNSTVLARGPASVPSVGKAVATAAQAQTGPEEDSGSSEEESDSEEEAETLAQVKPSGKTHQIRAALAPAKESPRKGAAPTPPGKTGPSAAQAGKQDDSGSSSEESDSDGEAPAAVTSAQVIKPPLIFVDPNRSPAGPAATPAQAQAASTPRKARASESTARSSSSESEDEDVIPATQCLTPGIRTNVVTMPTAHPRIAPKASMAGASSSKESSRISDGKKQEGPATQVSKKNPASLPLTQAALKVLAQKASEAQPPVARTQPSSGVDSAVGTLPATSPQSTSVQAKGTNKLRKPKLPEVQQATKAPESSDDSEDSSDSSSGSEEDGEGPQGAKSAHTLGPTPSRTETLVEETAAESSEDDVVAPSQSLLSGYMTPGLTPANSQASKATPKLDSSPSVSSTLAAKDDPDGKQEAKPQQAAGMLSPKTGGKEAASGTTPQKSRKPKKGAGNPQAST | ||||||
Compositional bias | 102-116 | Polar residues | ||||
Sequence: TPRLASTNSSVLGAD | ||||||
Compositional bias | 140-174 | Polar residues | ||||
Sequence: PHPATGKTVANLLSGKSPRKSAEPSANTTLVSETE | ||||||
Compositional bias | 473-487 | Basic and acidic residues | ||||
Sequence: EDSRSSSEESDSDRE | ||||||
Compositional bias | 643-657 | Polar residues | ||||
Sequence: ACPKKTNTTASAKVA | ||||||
Compositional bias | 667-681 | Polar residues | ||||
Sequence: RKAGTATSPAGSSPA | ||||||
Compositional bias | 776-790 | Polar residues | ||||
Sequence: ASPAQVKTSVKKTQA | ||||||
Compositional bias | 828-843 | Polar residues | ||||
Sequence: KPPVRNPQNSTVLARG | ||||||
Compositional bias | 976-996 | Polar residues | ||||
Sequence: AQAQAASTPRKARASESTARS | ||||||
Compositional bias | 1053-1070 | Polar residues | ||||
Sequence: KKQEGPATQVSKKNPASL | ||||||
Compositional bias | 1088-1122 | Polar residues | ||||
Sequence: QPPVARTQPSSGVDSAVGTLPATSPQSTSVQAKGT | ||||||
Compositional bias | 1170-1184 | Polar residues | ||||
Sequence: HTLGPTPSRTETLVE | ||||||
Compositional bias | 1193-1235 | Polar residues | ||||
Sequence: DDVVAPSQSLLSGYMTPGLTPANSQASKATPKLDSSPSVSSTL | ||||||
Compositional bias | 1322-1353 | Basic and acidic residues | ||||
Sequence: LLEQERKKVVDTTKESSRKGWESRKRKLSGDQ | ||||||
Region | 1322-1488 | Disordered | ||||
Sequence: LLEQERKKVVDTTKESSRKGWESRKRKLSGDQPAARTPRSKKKKKLGAGEGGEASVSPEKTSTTSKGKAKRDKASGDVKEKKGKGSLGSQGAKDEPEEELQKGMGTVEGGDQSNPKSKKEKKKSDKRKKDKEKKEKKKKAKKASTKDSESPSQKKKKKKKKTAEQTV | ||||||
Compositional bias | 1385-1425 | Basic and acidic residues | ||||
Sequence: TSKGKAKRDKASGDVKEKKGKGSLGSQGAKDEPEEELQKGM | ||||||
Compositional bias | 1441-1462 | Basic residues | ||||
Sequence: EKKKSDKRKKDKEKKEKKKKAK | ||||||
Compositional bias | 1474-1488 | Basic residues | ||||
Sequence: QKKKKKKKKTAEQTV |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing.
Q13428-1
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
- NoteMajor.
- Length1,488
- Mass (Da)152,106
- Last updated2010-08-10 v3
- Checksum6348306D0479790B
Q13428-2
- Name2
- Differences from canonical
- 214-290: Missing
Q13428-3
- Name3
- Differences from canonical
- 1172-1172: L → LV
Q13428-4
- Name4
- NoteMinor.
- Differences from canonical
- 953-953: Q → QDSNSKPARSKTLAPAPPERNTEGSSESSEEELPLTQ
Q13428-5
- Name5
Q13428-6
- Name6
- Differences from canonical
- 1062-1099: Missing
Q13428-7
- Name7
- Differences from canonical
- 1062-1099: Missing
- 1172-1172: L → LV
Q13428-8
- Name8
- Differences from canonical
- 214-290: Missing
- 1172-1172: L → LV
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y857 | A0A2R8Y857_HUMAN | TCOF1 | 297 | ||
A0A2R8Y4M7 | A0A2R8Y4M7_HUMAN | TCOF1 | 108 | ||
E7ETY2 | E7ETY2_HUMAN | TCOF1 | 1488 | ||
H0YA99 | H0YA99_HUMAN | TCOF1 | 188 | ||
H0YAB7 | H0YAB7_HUMAN | TCOF1 | 148 | ||
H0Y8Y7 | H0Y8Y7_HUMAN | TCOF1 | 994 | ||
A0A6I8PRA0 | A0A6I8PRA0_HUMAN | TCOF1 | 1240 | ||
A0A3B3IS06 | A0A3B3IS06_HUMAN | TCOF1 | 1358 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 57-74 | Basic and acidic residues | ||||
Sequence: SELGRKRKAEEDAALQAK | ||||||
Compositional bias | 102-116 | Polar residues | ||||
Sequence: TPRLASTNSSVLGAD | ||||||
Compositional bias | 140-174 | Polar residues | ||||
Sequence: PHPATGKTVANLLSGKSPRKSAEPSANTTLVSETE | ||||||
Alternative sequence | VSP_022295 | 214-290 | in isoform 2 and isoform 8 | |||
Sequence: Missing | ||||||
Compositional bias | 473-487 | Basic and acidic residues | ||||
Sequence: EDSRSSSEESDSDRE | ||||||
Compositional bias | 643-657 | Polar residues | ||||
Sequence: ACPKKTNTTASAKVA | ||||||
Compositional bias | 667-681 | Polar residues | ||||
Sequence: RKAGTATSPAGSSPA | ||||||
Compositional bias | 776-790 | Polar residues | ||||
Sequence: ASPAQVKTSVKKTQA | ||||||
Compositional bias | 828-843 | Polar residues | ||||
Sequence: KPPVRNPQNSTVLARG | ||||||
Alternative sequence | VSP_022296 | 953 | in isoform 4 | |||
Sequence: Q → QDSNSKPARSKTLAPAPPERNTEGSSESSEEELPLTQ | ||||||
Alternative sequence | VSP_023133 | 954-958 | in isoform 5 | |||
Sequence: VIKPP → DQESS | ||||||
Alternative sequence | VSP_023134 | 959-1488 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 976-996 | Polar residues | ||||
Sequence: AQAQAASTPRKARASESTARS | ||||||
Compositional bias | 1053-1070 | Polar residues | ||||
Sequence: KKQEGPATQVSKKNPASL | ||||||
Alternative sequence | VSP_040382 | 1062-1099 | in isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Compositional bias | 1088-1122 | Polar residues | ||||
Sequence: QPPVARTQPSSGVDSAVGTLPATSPQSTSVQAKGT | ||||||
Compositional bias | 1170-1184 | Polar residues | ||||
Sequence: HTLGPTPSRTETLVE | ||||||
Alternative sequence | VSP_022297 | 1172 | in isoform 3, isoform 7 and isoform 8 | |||
Sequence: L → LV | ||||||
Compositional bias | 1193-1235 | Polar residues | ||||
Sequence: DDVVAPSQSLLSGYMTPGLTPANSQASKATPKLDSSPSVSSTL | ||||||
Sequence conflict | 1271 | in Ref. 7; BAG64623 | ||||
Sequence: P → L | ||||||
Compositional bias | 1322-1353 | Basic and acidic residues | ||||
Sequence: LLEQERKKVVDTTKESSRKGWESRKRKLSGDQ | ||||||
Compositional bias | 1385-1425 | Basic and acidic residues | ||||
Sequence: TSKGKAKRDKASGDVKEKKGKGSLGSQGAKDEPEEELQKGM | ||||||
Sequence conflict | 1389 | in Ref. 2; AAB40722 | ||||
Sequence: K → Q | ||||||
Compositional bias | 1441-1462 | Basic residues | ||||
Sequence: EKKKSDKRKKDKEKKEKKKKAK | ||||||
Compositional bias | 1474-1488 | Basic residues | ||||
Sequence: QKKKKKKKKTAEQTV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U40847 EMBL· GenBank· DDBJ | AAC50903.1 EMBL· GenBank· DDBJ | mRNA | ||
U76366 EMBL· GenBank· DDBJ | AAC51181.1 EMBL· GenBank· DDBJ | mRNA | ||
U84664 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84640 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84641 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84642 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84643 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84644 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84645 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84646 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84647 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84648 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84649 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84650 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84651 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84652 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84653 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84654 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84655 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84656 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84657 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84658 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84659 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84660 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84661 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84662 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84663 EMBL· GenBank· DDBJ | AAC51185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79659 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79645 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79646 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79647 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79648 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79649 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79650 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79651 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79652 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79653 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79654 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79655 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79656 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79657 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U79658 EMBL· GenBank· DDBJ | AAB40722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY460334 EMBL· GenBank· DDBJ | AAR87774.1 EMBL· GenBank· DDBJ | mRNA | ||
AC011372 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC011764 EMBL· GenBank· DDBJ | AAH11764.1 EMBL· GenBank· DDBJ | mRNA | ||
BC014559 EMBL· GenBank· DDBJ | AAH14559.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016144 EMBL· GenBank· DDBJ | AAH16144.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC027252 EMBL· GenBank· DDBJ | AAH27252.1 EMBL· GenBank· DDBJ | mRNA | ||
BC033093 EMBL· GenBank· DDBJ | AAH33093.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303611 EMBL· GenBank· DDBJ | BAG64623.1 EMBL· GenBank· DDBJ | mRNA |