O94913 · PCF11_HUMAN
- ProteinPre-mRNA cleavage complex 2 protein Pcf11
- GenePCF11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1555 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of pre-mRNA cleavage complex II, which promotes transcription termination by RNA polymerase II.
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 | cytoplasm | |
Cellular Component | mitochondrion | |
Cellular Component | mRNA cleavage factor complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | mRNA binding | |
Molecular Function | RNA polymerase II complex binding | |
Biological Process | co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway | |
Biological Process | termination of RNA polymerase II transcription |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePre-mRNA cleavage complex 2 protein Pcf11
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94913
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 120-121 | Abolished phosphorylation by WNK1, leading to mRNA retention in the nucleus and in prolonged association with polyadenylated mRNAs at transcription loci. | ||||
Sequence: ST → AA | ||||||
Natural variant | VAR_036878 | 651 | in dbSNP:rs7935175 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_036879 | 1119 | in dbSNP:rs17513642 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_036880 | 1402 | in dbSNP:rs11233510 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,412 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 initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000058246 | 2-1555 | UniProt | Pre-mRNA cleavage complex 2 protein Pcf11 | |||
Sequence: SEQTPAEAGAAGAREDACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYLMDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKKLYALDVRVNSLDPAWPIKPLPPNVNTSSIHVNPKFLNKSPEEPSTPGTVVSSPSISTPPIVPDIQKNLTQEQLIRQQLLAKQKQLLELQQKKLELELEQAKAQLAVSLSVQQETSNLGPGSAPSKLHVSQIPPMAVKAPHQVPVQSEKSRPGPSLQIQDLKGTNRDPRLNRISQHSHGKDQSHRKEFLMNTLNQSDTKTSKTIPSEKLNSSKQEKSKSGEKITKKELDQLDSKSKSKSKSPSPLKNKLSHTKDLKNQESESMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLAGSRNKIINGIVQKQDTITEESEKQGTKPGRSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQRSMSPTSTPKAGKIRQSGAKQSHMEEFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETTNQHSTKSGTEPKENVENWQSSKSAKRWKSGWEENKSLQQVDEHSKPPHLRHRESWSSTKGILSPRAPKQQQHRLSVDANLQIPKELTLASKRELLQKTSERLASGEITQDDFLVVVHQIRQLFQYQEGVREEQRSPFNDRFPLKRPRYEDSDKPFVDSPASRFAGLDTNQRLTALAEDRPLFDGPSRPSVARDGPTKMIFEGPNKLSPRIDGPPTPASLRFDGSPGQMGGGGPLRFEGPQGQLGGGCPLRFEGPPGPVGTPLRFEGPIGQAGGGGFRFEGSPGLRFEGSPGGLRFEGPGGQPVGGLRFEGHRGQPVGGLRFEGPHGQPVGGLRFDNPRGQPVGGLRFEGGHGPSGAAIRFDGPHGQPGGGIRFEGPLLQQGVGMRFEGPHGQSVAGLRFEGQHNQLGGNLRFEGPHGQPGVGIRFEGPLVQQGGGMRFEGPSVPGGGLRIEGPLGQGGPRFEGCHALRFDGQPGQPSLLPRFDGLHGQPGPRFERTPGQPGPQRFDGPPGQQVQPRFDGVPQRFDGPQHQQASRFDIPLGLQGTRFDNHPSQRLESVSFNQTGPYNDPPGNAFNAPSQGLQFQRHEQIFDSPQGPNFNGPHGPGNQSFSNPLNRASGHYFDEKNLQSSQFGNFGNIPAPMTVGNIQASQQVLSGVAQPVAFGQGQQFLPVHPQNPGFVQNPSGALPKAYPDNHLSQVDVNELFSKLLKTGILKLSQTDSATTQVSEVTAQPPPEEEEDQNEDQDVPDLTNFTVEELKQRYDSVINRLYTGIQCYSCGMRFTTSQTDVYADHLDWHYRQNRTEKDVSRKVTHRRWYYSLTDWIEFEEIADLEERAKSQFFEKVHEEVVLKTQEAAKEKEFQSVPAGPAGAVESCEICQEQFEQYWDEEEEEWHLKNAIRVDGKIYHPSCYEDYQNTSSFDCTPSPSKTPVENPLNIMLNIVKNELQEPCDSPKVKEERIDTPPACTEESIATPSEIKTENDTVESV | |||||||
Modified residue | 120 | UniProt | Phosphoserine; by WNK1 | ||||
Sequence: S | |||||||
Modified residue | 121 | UniProt | Phosphothreonine; by WNK1 | ||||
Sequence: T | |||||||
Modified residue | 169 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 182 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 187 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 291 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 328 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 372 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 456 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 459 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 487 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 489 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 494 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 509 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 509 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 511 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 511 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 513 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 535 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 645 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 645 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 654 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 705 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 705 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 723 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 728 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 759 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 777 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 777 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 785 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 785 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 794 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 794 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 805 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 820 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 833 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 851 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 851 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 929 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 942 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 955 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 981 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 994 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 1007 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 1093 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 1104 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 1161 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1278 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 1419 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1493 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1497 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1511 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1524 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 1530 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1530 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1541 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1546 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1554 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-120 and/or Thr-121 by WNK1 weakens its association with POLR2A/RNA polymerase II, promoting transcript release from the chromatin template and mRNA export to the cytoplasm.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Associates with the phosphorylated CTD domain of POLR2A /RNA polymerase II.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O94913 | CLP1 Q92989 | 3 | EBI-2559809, EBI-2559831 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-142 | CID | ||||
Sequence: AREDACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYLMDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKKLYALDVRVNSLD | ||||||
Region | 167-186 | Disordered | ||||
Sequence: NKSPEEPSTPGTVVSSPSIS | ||||||
Coiled coil | 202-239 | |||||
Sequence: QLIRQQLLAKQKQLLELQQKKLELELEQAKAQLAVSLS | ||||||
Region | 266-648 | Disordered | ||||
Sequence: VKAPHQVPVQSEKSRPGPSLQIQDLKGTNRDPRLNRISQHSHGKDQSHRKEFLMNTLNQSDTKTSKTIPSEKLNSSKQEKSKSGEKITKKELDQLDSKSKSKSKSPSPLKNKLSHTKDLKNQESESMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLAGSRNKIINGIVQKQDTITEESEKQGTKPGRSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQRSMSPTSTPKAGKIRQSGAKQSHMEEFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETTNQHSTKSGTEPKENVENWQSSKSAKRWKSGWEENKSLQQVDEHSKPPHLRHRESWSSTKGILSPRAPKQQQHRLSVDA | ||||||
Compositional bias | 277-293 | Polar residues | ||||
Sequence: EKSRPGPSLQIQDLKGT | ||||||
Compositional bias | 294-316 | Basic and acidic residues | ||||
Sequence: NRDPRLNRISQHSHGKDQSHRKE | ||||||
Compositional bias | 317-337 | Polar residues | ||||
Sequence: FLMNTLNQSDTKTSKTIPSEK | ||||||
Compositional bias | 338-365 | Basic and acidic residues | ||||
Sequence: LNSSKQEKSKSGEKITKKELDQLDSKSK | ||||||
Compositional bias | 376-443 | Basic and acidic residues | ||||
Sequence: NKLSHTKDLKNQESESMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLA | ||||||
Compositional bias | 473-507 | Basic residues | ||||
Sequence: RSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQ | ||||||
Compositional bias | 508-522 | Polar residues | ||||
Sequence: RSMSPTSTPKAGKIR | ||||||
Compositional bias | 533-570 | Basic and acidic residues | ||||
Sequence: EFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETT | ||||||
Compositional bias | 571-595 | Polar residues | ||||
Sequence: NQHSTKSGTEPKENVENWQSSKSAK | ||||||
Compositional bias | 596-625 | Basic and acidic residues | ||||
Sequence: RWKSGWEENKSLQQVDEHSKPPHLRHRESW | ||||||
Compositional bias | 626-647 | Polar residues | ||||
Sequence: SSTKGILSPRAPKQQQHRLSVD | ||||||
Compositional bias | 707-726 | Basic and acidic residues | ||||
Sequence: FNDRFPLKRPRYEDSDKPFV | ||||||
Region | 707-732 | Disordered | ||||
Sequence: FNDRFPLKRPRYEDSDKPFVDSPASR | ||||||
Region | 749-781 | Disordered | ||||
Sequence: RPLFDGPSRPSVARDGPTKMIFEGPNKLSPRID | ||||||
Region | 1056-1081 | Disordered | ||||
Sequence: HGQPGPRFERTPGQPGPQRFDGPPGQ | ||||||
Region | 1127-1147 | Disordered | ||||
Sequence: VSFNQTGPYNDPPGNAFNAPS | ||||||
Region | 1159-1187 | Disordered | ||||
Sequence: FDSPQGPNFNGPHGPGNQSFSNPLNRASG | ||||||
Region | 1289-1315 | Disordered | ||||
Sequence: SATTQVSEVTAQPPPEEEEDQNEDQDV | ||||||
Region | 1516-1555 | Disordered | ||||
Sequence: EPCDSPKVKEERIDTPPACTEESIATPSEIKTENDTVESV | ||||||
Compositional bias | 1517-1532 | Basic and acidic residues | ||||
Sequence: PCDSPKVKEERIDTPP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,555
- Mass (Da)173,050
- Last updated2007-10-23 v3
- Checksum0AEAE04D7CB4A34F
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PQ01 | E9PQ01_HUMAN | PCF11 | 998 | ||
E9PQF9 | E9PQF9_HUMAN | PCF11 | 99 | ||
E9PNY7 | E9PNY7_HUMAN | PCF11 | 198 | ||
E9PKN0 | E9PKN0_HUMAN | PCF11 | 784 | ||
A0A8I5KX04 | A0A8I5KX04_HUMAN | PCF11 | 1686 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 277-293 | Polar residues | ||||
Sequence: EKSRPGPSLQIQDLKGT | ||||||
Compositional bias | 294-316 | Basic and acidic residues | ||||
Sequence: NRDPRLNRISQHSHGKDQSHRKE | ||||||
Compositional bias | 317-337 | Polar residues | ||||
Sequence: FLMNTLNQSDTKTSKTIPSEK | ||||||
Compositional bias | 338-365 | Basic and acidic residues | ||||
Sequence: LNSSKQEKSKSGEKITKKELDQLDSKSK | ||||||
Compositional bias | 376-443 | Basic and acidic residues | ||||
Sequence: NKLSHTKDLKNQESESMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLA | ||||||
Compositional bias | 473-507 | Basic residues | ||||
Sequence: RSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQ | ||||||
Compositional bias | 508-522 | Polar residues | ||||
Sequence: RSMSPTSTPKAGKIR | ||||||
Compositional bias | 533-570 | Basic and acidic residues | ||||
Sequence: EFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETT | ||||||
Compositional bias | 571-595 | Polar residues | ||||
Sequence: NQHSTKSGTEPKENVENWQSSKSAK | ||||||
Compositional bias | 596-625 | Basic and acidic residues | ||||
Sequence: RWKSGWEENKSLQQVDEHSKPPHLRHRESW | ||||||
Compositional bias | 626-647 | Polar residues | ||||
Sequence: SSTKGILSPRAPKQQQHRLSVD | ||||||
Compositional bias | 707-726 | Basic and acidic residues | ||||
Sequence: FNDRFPLKRPRYEDSDKPFV | ||||||
Sequence conflict | 783 | in Ref. 4; AAC03107 | ||||
Sequence: P → L | ||||||
Sequence conflict | 784 | in Ref. 4; AAC03107 | ||||
Sequence: P → R | ||||||
Compositional bias | 1517-1532 | Basic and acidic residues | ||||
Sequence: PCDSPKVKEERIDTPP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB020631 EMBL· GenBank· DDBJ | BAA74847.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CH471076 EMBL· GenBank· DDBJ | EAW75083.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC065384 EMBL· GenBank· DDBJ | AAH65384.2 EMBL· GenBank· DDBJ | mRNA | ||
BC146778 EMBL· GenBank· DDBJ | AAI46779.1 EMBL· GenBank· DDBJ | mRNA | ||
AF046935 EMBL· GenBank· DDBJ | AAC03107.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |