Q70E73 · RAPH1_HUMAN
- ProteinRas-associated and pleckstrin homology domains-containing protein 1
- GeneRAPH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1250 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.
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 | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | filopodium | |
Cellular Component | lamellipodium | |
Cellular Component | nuclear body | |
Cellular Component | plasma membrane | |
Biological Process | axon extension | |
Biological Process | signal transduction |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRas-associated and pleckstrin homology domains-containing protein 1
- Short namesRAPH1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ70E73
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Recruited to the membrane, via the PH domain, by the phosphoinositide, PI(3,4)P2. Colocalizes with ENAH/VASP at the tips of lamellipodia and filopodia. Also colocalizes with the pathogens, Vaccinia and Enteropathogenic E.coli (EPEC) at the interface between the pathogen and their actin.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_036009 | 891 | in a breast cancer sample; somatic mutation | |||
Sequence: A → S | ||||||
Natural variant | VAR_036010 | 1228 | in a breast cancer sample; somatic mutation; dbSNP:rs774304253 | |||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,264 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 modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000181352 | 1-1250 | UniProt | Ras-associated and pleckstrin homology domains-containing protein 1 | |||
Sequence: MEQLSDEEIDHGAEEDSDKEDQDLDKMFGAWLGELDKLTQSLDSDKPMEPVKRSPLRQETNMANFSYRFSIYNLNEALNQGETVDLDALMADLCSIEQELSSIGSGNSKRQITETKATQKLPVSRHTLKHGTLKGLSSSSNRIAKPSHASYSLDDVTAQLEQASLSMDEAAQQSVLEDTKPLVTNQHRRTASAGTVSDAEVHSISNSSHSSITSAASSMDSLDIDKVTRPQELDLTHQGQPITEEEQAAKLKAEKIRVALEKIKEAQVKKLVIRVHMSDDSSKTMMVDERQTVRQVLDNLMDKSHCGYSLDWSLVETVSELQMERIFEDHENLVENLLNWTRDSQNKLIFMERIEKYALFKNPQNYLLGKKETAEMADRNKEVLLEECFCGSSVTVPEIEGVLWLKDDGKKSWKKRYFLLRASGIYYVPKGKAKVSRDLVCFLQLDHVNVYYGQDYRNKYKAPTDYCLVLKHPQIQKKSQYIKYLCCDDVRTLHQWVNGIRIAKYGKQLYMNYQEALKRTESAYDWTSLSSSSIKSGSSSSSIPESQSNHSNQSDSGVSDTQPAGHVRSQSIVSSVFSEAWKRGTQLEESSKARMESMNRPYTSLVPPLSPQPKIVTPYTASQPSPPLPPPPPPPPPPPPPPPPPPPPLPSQSAPSAGSAAPMFVKYSTITRLQNASQHSGALFKPPTPPVMQSQSVKPQILVPPNGVVPPPPPPPPPPTPGSAMAQLKPAPCAPSLPQFSAPPPPLKIHQVQHITQVAPPTPPPPPPIPAPLPPQAPPKPLVTIPAPTSTKTVAPVVTQAAPPTPTPPVPPAKKQPAFPASYIPPSPPTPPVPVPPPTLPKQQSFCAKPPPSPLSPVPSVVKQIASQFPPPPTPPAMESQPLKPVPANVAPQSPPAVKAKPKWQPSSIPVPSPDFPPPPPESSLVFPPPPPSPVPAPPPPPPPTASPTPDKSGSPGKKTSKTSSPGGKKPPPTPQRNSSIKSSSGAEHPEPKRPSVDSLVSKFTPPAESGSPSKETLPPPAAPPKPGKLNLSGVNLPGVLQQGCVSAKAPVLSGRGKDSVVEFPSPPSDSDFPPPPPETELPLPPIEIPAVFSGNTSPKVAVVNPQPQQWSKMSVKKAPPPTRPKRNDSTRLTQAEISEQPTMATVVPQVPTSPKSSLSVQPGFLADLNRTLQRKSITRHGSLSSRMSRAEPTATMDDMALPPPPPELLSDQQKAGYGGSHISGYATLRRGPPPAPPKRDQNTKLSRDW | |||||||
Modified residue | 5 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 17 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 150 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 192 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 203 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 205 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 426 | UniProt | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | |||||||
Modified residue | 456 | UniProt | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 610 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 610 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 805 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 807 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 827 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 827 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 830 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 830 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 845 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 845 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 853 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 853 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 856 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 874 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 894 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 894 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 965 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 965 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 974 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 980 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 983 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 996 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 996 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1005 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1010 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1012 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1012 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1060 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1130 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1153 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1154 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1172 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1183 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1183 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1226 | UniProt | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1226 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1228 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform RMO1-RAPH1 is ubiquitously expressed with highest levels in brain, heart, ovary and developing embryo. Isoform RMO1 is widely expressed with highest levels in liver. Low expression in B-cells.
Induction
Reduced expression in metastatic osteosarcomas compared to primary osteosarcoma tumors. Down-regulated in both breast (43% of tissue samples) and ovarian (25% of tissue samples) cancers.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with EVL and VASP and targets them to the leading edge (PubMed:15469845).
Interacts (via Ras associating and PH domains) with RAC1 (PubMed:18499456).
Interacts (via Ras associating and PH domains) with RAC1 (PubMed:18499456).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q70E73 | EGFR P00533 | 2 | EBI-3940924, EBI-297353 | |
XENO | Q70E73 | Sh3gl1 O35964 | 13 | EBI-3940924, EBI-1149235 | |
BINARY | Q70E73 | SH3GL2 Q99962 | 5 | EBI-3940924, EBI-77938 | |
BINARY | Q70E73 | SH3GL3 Q99963 | 4 | EBI-3940924, EBI-473910 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MEQLSDEEIDHGAEEDSDKEDQDLDK | ||||||
Compositional bias | 7-21 | Acidic residues | ||||
Sequence: EEIDHGAEEDSDKED | ||||||
Region | 179-217 | Disordered | ||||
Sequence: TKPLVTNQHRRTASAGTVSDAEVHSISNSSHSSITSAAS | ||||||
Domain | 269-355 | Ras-associating | ||||
Sequence: KKLVIRVHMSDDSSKTMMVDERQTVRQVLDNLMDKSHCGYSLDWSLVETVSELQMERIFEDHENLVENLLNWTRDSQNKLIFMERIE | ||||||
Domain | 396-505 | PH | ||||
Sequence: VPEIEGVLWLKDDGKKSWKKRYFLLRASGIYYVPKGKAKVSRDLVCFLQLDHVNVYYGQDYRNKYKAPTDYCLVLKHPQIQKKSQYIKYLCCDDVRTLHQWVNGIRIAKY | ||||||
Region | 535-570 | Disordered | ||||
Sequence: KSGSSSSSIPESQSNHSNQSDSGVSDTQPAGHVRSQ | ||||||
Region | 588-663 | Disordered | ||||
Sequence: EESSKARMESMNRPYTSLVPPLSPQPKIVTPYTASQPSPPLPPPPPPPPPPPPPPPPPPPPLPSQSAPSAGSAAPM | ||||||
Compositional bias | 606-653 | Pro residues | ||||
Sequence: VPPLSPQPKIVTPYTASQPSPPLPPPPPPPPPPPPPPPPPPPPLPSQS | ||||||
Region | 675-1036 | Disordered | ||||
Sequence: NASQHSGALFKPPTPPVMQSQSVKPQILVPPNGVVPPPPPPPPPPTPGSAMAQLKPAPCAPSLPQFSAPPPPLKIHQVQHITQVAPPTPPPPPPIPAPLPPQAPPKPLVTIPAPTSTKTVAPVVTQAAPPTPTPPVPPAKKQPAFPASYIPPSPPTPPVPVPPPTLPKQQSFCAKPPPSPLSPVPSVVKQIASQFPPPPTPPAMESQPLKPVPANVAPQSPPAVKAKPKWQPSSIPVPSPDFPPPPPESSLVFPPPPPSPVPAPPPPPPPTASPTPDKSGSPGKKTSKTSSPGGKKPPPTPQRNSSIKSSSGAEHPEPKRPSVDSLVSKFTPPAESGSPSKETLPPPAAPPKPGKLNLSGVN | ||||||
Compositional bias | 704-725 | Pro residues | ||||
Sequence: PPNGVVPPPPPPPPPPTPGSAM | ||||||
Compositional bias | 758-785 | Pro residues | ||||
Sequence: VAPPTPPPPPPIPAPLPPQAPPKPLVTI | ||||||
Compositional bias | 786-800 | Polar residues | ||||
Sequence: PAPTSTKTVAPVVTQ | ||||||
Compositional bias | 801-858 | Pro residues | ||||
Sequence: AAPPTPTPPVPPAKKQPAFPASYIPPSPPTPPVPVPPPTLPKQQSFCAKPPPSPLSPV | ||||||
Compositional bias | 866-892 | Pro residues | ||||
Sequence: ASQFPPPPTPPAMESQPLKPVPANVAP | ||||||
Compositional bias | 907-950 | Pro residues | ||||
Sequence: SSIPVPSPDFPPPPPESSLVFPPPPPSPVPAPPPPPPPTASPTP | ||||||
Compositional bias | 951-967 | Polar residues | ||||
Sequence: DKSGSPGKKTSKTSSPG | ||||||
Compositional bias | 1013-1027 | Pro residues | ||||
Sequence: PSKETLPPPAAPPKP | ||||||
Region | 1050-1162 | Disordered | ||||
Sequence: APVLSGRGKDSVVEFPSPPSDSDFPPPPPETELPLPPIEIPAVFSGNTSPKVAVVNPQPQQWSKMSVKKAPPPTRPKRNDSTRLTQAEISEQPTMATVVPQVPTSPKSSLSVQ | ||||||
Compositional bias | 1068-1085 | Pro residues | ||||
Sequence: PSDSDFPPPPPETELPLP | ||||||
Compositional bias | 1098-1116 | Polar residues | ||||
Sequence: SPKVAVVNPQPQQWSKMSV | ||||||
Compositional bias | 1134-1162 | Polar residues | ||||
Sequence: TQAEISEQPTMATVVPQVPTSPKSSLSVQ | ||||||
Compositional bias | 1176-1192 | Polar residues | ||||
Sequence: KSITRHGSLSSRMSRAE | ||||||
Region | 1176-1250 | Disordered | ||||
Sequence: KSITRHGSLSSRMSRAEPTATMDDMALPPPPPELLSDQQKAGYGGSHISGYATLRRGPPPAPPKRDQNTKLSRDW |
Sequence similarities
Belongs to the MRL family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 9 isoforms produced by Alternative splicing.
Q70E73-10
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.
- NameRMO1-RAPH1
- SynonymsLamellipodin, RAPH1
- Length1,250
- Mass (Da)135,256
- Last updated2008-11-25 v3
- Checksum1DFB651F945DA3DC
Q70E73-2
- NameRMO1
Q70E73-3
- NameRMO1a
Q70E73-4
- NameRMO1b
Q70E73-5
- NameRMO1c
- Differences from canonical
- 593-1250: Missing
Q70E73-6
- NameRMO1ab
- SynonymsLamellipodin-S, Lpd-S
Q70E73-7
- NameRMO1ac
Q70E73-8
- NameRMO1bc
Q70E73-9
- NameRMO1abc
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-21 | Acidic residues | ||||
Sequence: EEIDHGAEEDSDKED | ||||||
Alternative sequence | VSP_035784 | 244 | in isoform RMO1a and isoform RMO1ac | |||
Sequence: E → EHAISLRCSSKQAKRHIDFTEEQAELTP | ||||||
Alternative sequence | VSP_035785 | 244 | in isoform RMO1ab and isoform RMO1abc | |||
Sequence: E → EHAISLRCSSKQAKRHIDFTEEQAELTPHSYLDRETSLLLRNIAGKPSHLLTK | ||||||
Alternative sequence | VSP_035786 | 244 | in isoform RMO1b and isoform RMO1bc | |||
Sequence: E → EHSYLDRETSLLLRNIAGKPSHLLTK | ||||||
Alternative sequence | VSP_035788 | 593-597 | in isoform RMO1, isoform RMO1a, isoform RMO1b and isoform RMO1ab | |||
Sequence: ARMES → VTASF | ||||||
Alternative sequence | VSP_035787 | 593-1250 | in isoform RMO1c, isoform RMO1ac, isoform RMO1bc and isoform RMO1abc | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_035789 | 598-1250 | in isoform RMO1, isoform RMO1a, isoform RMO1b and isoform RMO1ab | |||
Sequence: Missing | ||||||
Compositional bias | 606-653 | Pro residues | ||||
Sequence: VPPLSPQPKIVTPYTASQPSPPLPPPPPPPPPPPPPPPPPPPPLPSQS | ||||||
Compositional bias | 704-725 | Pro residues | ||||
Sequence: PPNGVVPPPPPPPPPPTPGSAM | ||||||
Compositional bias | 758-785 | Pro residues | ||||
Sequence: VAPPTPPPPPPIPAPLPPQAPPKPLVTI | ||||||
Compositional bias | 786-800 | Polar residues | ||||
Sequence: PAPTSTKTVAPVVTQ | ||||||
Compositional bias | 801-858 | Pro residues | ||||
Sequence: AAPPTPTPPVPPAKKQPAFPASYIPPSPPTPPVPVPPPTLPKQQSFCAKPPPSPLSPV | ||||||
Compositional bias | 866-892 | Pro residues | ||||
Sequence: ASQFPPPPTPPAMESQPLKPVPANVAP | ||||||
Compositional bias | 907-950 | Pro residues | ||||
Sequence: SSIPVPSPDFPPPPPESSLVFPPPPPSPVPAPPPPPPPTASPTP | ||||||
Compositional bias | 951-967 | Polar residues | ||||
Sequence: DKSGSPGKKTSKTSSPG | ||||||
Compositional bias | 1013-1027 | Pro residues | ||||
Sequence: PSKETLPPPAAPPKP | ||||||
Compositional bias | 1068-1085 | Pro residues | ||||
Sequence: PSDSDFPPPPPETELPLP | ||||||
Sequence conflict | 1081 | in Ref. 2; AAS82582, 4; CAE48361 and 6; BAB21772 | ||||
Sequence: E → D | ||||||
Compositional bias | 1098-1116 | Polar residues | ||||
Sequence: SPKVAVVNPQPQQWSKMSV | ||||||
Compositional bias | 1134-1162 | Polar residues | ||||
Sequence: TQAEISEQPTMATVVPQVPTSPKSSLSVQ | ||||||
Compositional bias | 1176-1192 | Polar residues | ||||
Sequence: KSITRHGSLSSRMSRAE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB053311 EMBL· GenBank· DDBJ | BAB69020.1 EMBL· GenBank· DDBJ | mRNA | ||
AY494951 EMBL· GenBank· DDBJ | AAS82582.1 EMBL· GenBank· DDBJ | mRNA | ||
AY523977 EMBL· GenBank· DDBJ | AAS16935.1 EMBL· GenBank· DDBJ | mRNA | ||
AY523978 EMBL· GenBank· DDBJ | AAS16936.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ584699 EMBL· GenBank· DDBJ | CAE48361.1 EMBL· GenBank· DDBJ | mRNA | ||
AC018891 EMBL· GenBank· DDBJ | AAY14676.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB051468 EMBL· GenBank· DDBJ | BAB21772.1 EMBL· GenBank· DDBJ | mRNA |