Q86YV5 · PRAG1_HUMAN
- ProteinInactive tyrosine-protein kinase PRAG1
- GenePRAG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1406 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytically inactive protein kinase that acts as a scaffold protein. Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By similarity).
Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity).
Acts as a critical coactivator of Notch signaling (By similarity).
Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity).
Acts as a critical coactivator of Notch signaling (By similarity).
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 | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | protein kinase activity | |
Biological Process | cell migration | |
Biological Process | negative regulation of neuron projection development | |
Biological Process | positive regulation of Rho protein signal transduction | |
Biological Process | regulation of cell motility | |
Biological Process | regulation of cell shape | |
Biological Process | regulation of Notch signaling pathway |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInactive tyrosine-protein kinase PRAG1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86YV5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalized with NOTCH1 in the nucleus.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_041803 | 122 | in dbSNP:rs55764617 | |||
Sequence: L → I | ||||||
Natural variant | VAR_041804 | 137 | in dbSNP:rs56290960 | |||
Sequence: R → G | ||||||
Natural variant | VAR_041805 | 139 | in dbSNP:rs34346032 | |||
Sequence: V → I | ||||||
Natural variant | VAR_041806 | 404 | in dbSNP:rs3896980 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_041807 | 569 | in dbSNP:rs4840955 | |||
Sequence: P → L | ||||||
Natural variant | VAR_041808 | 578 | in dbSNP:rs4840953 | |||
Sequence: S → C | ||||||
Natural variant | VAR_041809 | 595 | in dbSNP:rs55994745 | |||
Sequence: P → A | ||||||
Natural variant | VAR_041810 | 662 | in dbSNP:rs56351643 | |||
Sequence: P → T | ||||||
Natural variant | VAR_041811 | 814 | in dbSNP:rs56207906 | |||
Sequence: P → L | ||||||
Natural variant | VAR_041812 | 851 | in dbSNP:rs56215812 | |||
Sequence: H → R | ||||||
Mutagenesis | 955 | Decreases homodimerization. Abolished interaction with PEAK1. No effect on cell migration. | ||||
Sequence: L → A | ||||||
Mutagenesis | 966 | Decreases homodimerization. Abolished interaction with PEAK1. Decreases cell migration. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_041813 | 1003 | in dbSNP:rs56289289 | |||
Sequence: S → L | ||||||
Natural variant | VAR_041814 | 1041 | in dbSNP:rs28533138 | |||
Sequence: V → M | ||||||
Natural variant | VAR_041815 | 1113 | in dbSNP:rs12549973 | |||
Sequence: A → T | ||||||
Mutagenesis | 1243 | No effect on homodimerization. Decreases oligomerization. Decreases interaction with PEAK1. | ||||
Sequence: I → A | ||||||
Mutagenesis | 1271 | Decreases homodimerization. Decreases interaction with PEAK1. | ||||
Sequence: F → A | ||||||
Mutagenesis | 1278 | Decreases homodimerization. | ||||
Sequence: R → A | ||||||
Mutagenesis | 1282 | No effect on homodimerization. Decreases oligomerization. Decreases interaction with PEAK1. No effect on cell migration. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_041816 | 1315 | in dbSNP:rs1314830862 | |||
Sequence: R → H | ||||||
Mutagenesis | 1366 | Decreases homodimerization. Abolished interaction with PEAK1. Decreases cell migration. | ||||
Sequence: F → A | ||||||
Mutagenesis | 1382 | Decreases homodimerization. Abolished interaction with PEAK1. Decreases cell migration. | ||||
Sequence: W → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,227 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000263008 | 1-1406 | UniProt | Inactive tyrosine-protein kinase PRAG1 | |||
Sequence: MHQTLCLNPESLKMSACSDFVEHIWKPGSCKNCFCLRSDHQLVAGPPQPRAGSLPPPPRLPPRPENCRLEDEGVNSSPYSKPTIAVKPTMMSSEASDVWTEANLSAEVSQVIWRRAPGKLPLPKQEDAPVVYLGSFRGVQKPAGPSTSPDGNSRCPPAYTMVGLHNLEPRGERNIAFHPVSFPEEKAVHKEKPSFPYQDRPSTQESFRQKLAAFAGTTSGCHQGPGPLRESLPSEDDSDQRCSPSGDSEGGEYCSILDCCPGSPVAKAASQTAGSRGRHGGRDCSPTCWEQGKCSGPAEQEKRGPSFPKECCSQGPTAHPSCLGPKKLSLTSEAAISSDGLSCGSGSGSGSGASSPFVPHLESDYCSLMKEPAPEKQQDPGCPGVTPSRCLGLTGEPQPPAHPREATQPEPIYAESTKRKKAAPVPSKSQAKIEHAAAAQGQGQVCTGNAWAQKAASGWGRDSPDPTPQVSATITVMAAHPEEDHRTIYLSSPDSAVGVQWPRGPVSQNSEVGEEETSAGQGLSSRESHAHSASESKPKERPAIPPKLSKSSPVGSPVSPSAGGPPVSPLADLSDGSSGGSSIGPQPPSQGPADPAPSCRTNGVAISDPSRCPQPAASSASEQRRPRFQAGTWSRQCRIEEEEEVEQELLSHSWGRETKNGPTDHSNSTTWHRLHPTDGSSGQNSKVGTGMSKSASFAFEFPKDRSGIETFSPPPPPPKSRHLLKMNKSSSDLEKVSQGSAESLSPSFRGVHVSFTTGSTDSLASDSRTCSDGGPSSELAHSPTNSGKKLFAPVPFPSGSTEDVSPSGPQQPPPLPQKKIVSRAASSPDGFFWTQGSPKPGTASPKLNLSHSETNVHDESHFSYSLSPGNRHHPVFSSSDPLEKAFKGSGHWLPAAGLAGNRGGCGSPGLQCKGAPSASSSQLSVSSQASTGSTQLQLHGLLSNISSKEGTYAKLGGLYTQSLARLVAKCEDLFMGGQKKELHFNENNWSLFKLTCNKPCCDSGDAIYYCATCSEDPGSTYAVKICKAPEPKTVSYCSPSVPVHFNIQQDCGHFVASVPSSMLSSPDAPKDPVPALPTHPPAQEQDCVVVITREVPHQTASDFVRDSAASHQAEPEAYERRVCFLLLQLCNGLEHLKEHGIIHRDLCLENLLLVHCTLQAGPGPAPAPAPAPAPAAAAPPCSSAAPPAGGTLSPAAGPASPEGPREKQLPRLIISNFLKAKQKPGGTPNLQQKKSQARLAPEIVSASQYRKFDEFQTGILIYELLHQPNPFEVRAQLRERDYRQEDLPPLPALSLYSPGLQQLAHLLLEADPIKRIRIGEAKRVLQCLLWGPRRELVQQPGTSEEALCGTLHNWIDMKRALMMMKFAEKAVDRRRGVELEDWLCCQYLASAEPGALLQSLKLLQLL | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 135 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 148 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 148 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 253 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 365 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 386 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 413 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 413 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 416 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 492 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 510 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 632 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 694 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 696 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 696 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 712 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 729 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 737 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 740 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 743 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 745 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 745 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 747 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 754 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 759 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 760 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 782 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 782 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 786 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 798 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 801 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 805 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 826 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 826 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 827 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 834 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 837 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 842 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 844 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 852 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 854 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 864 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 867 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 878 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 889 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 907 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1227 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated by CSK on Tyr-253, Tyr-365, and Tyr-413; Tyr-413 is a primary site of phosphorylation.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer (PubMed:29079850).
Dimerization leads to the catalytic activation of CSK (By similarity).
Interacts (via C-terminus) with RND2 (By similarity).
Interacts with CSK (via SH2 domain) in a Tyr-413 phosphorylation-dependent manner; this interaction potentiates kinase activity of CSK (By similarity).
Interacts with PEAK1 (PubMed:29079850).
Interacts with NOTCH1 intracellular domain (N1ICD) (By similarity).
Forms a complex with N1ICD and MAML1, in a MAML1-dependent manner (By similarity).
Dimerization leads to the catalytic activation of CSK (By similarity).
Interacts (via C-terminus) with RND2 (By similarity).
Interacts with CSK (via SH2 domain) in a Tyr-413 phosphorylation-dependent manner; this interaction potentiates kinase activity of CSK (By similarity).
Interacts with PEAK1 (PubMed:29079850).
Interacts with NOTCH1 intracellular domain (N1ICD) (By similarity).
Forms a complex with N1ICD and MAML1, in a MAML1-dependent manner (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86YV5 | SFN P31947 | 2 | EBI-719420, EBI-476295 | |
BINARY | Q86YV5 | YWHAE P62258 | 2 | EBI-719420, EBI-356498 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 184-205 | Disordered | ||||
Sequence: EEKAVHKEKPSFPYQDRPSTQE | ||||||
Region | 217-248 | Disordered | ||||
Sequence: TTSGCHQGPGPLRESLPSEDDSDQRCSPSGDS | ||||||
Region | 372-470 | Disordered | ||||
Sequence: PAPEKQQDPGCPGVTPSRCLGLTGEPQPPAHPREATQPEPIYAESTKRKKAAPVPSKSQAKIEHAAAAQGQGQVCTGNAWAQKAASGWGRDSPDPTPQV | ||||||
Region | 484-854 | Disordered | ||||
Sequence: DHRTIYLSSPDSAVGVQWPRGPVSQNSEVGEEETSAGQGLSSRESHAHSASESKPKERPAIPPKLSKSSPVGSPVSPSAGGPPVSPLADLSDGSSGGSSIGPQPPSQGPADPAPSCRTNGVAISDPSRCPQPAASSASEQRRPRFQAGTWSRQCRIEEEEEVEQELLSHSWGRETKNGPTDHSNSTTWHRLHPTDGSSGQNSKVGTGMSKSASFAFEFPKDRSGIETFSPPPPPPKSRHLLKMNKSSSDLEKVSQGSAESLSPSFRGVHVSFTTGSTDSLASDSRTCSDGGPSSELAHSPTNSGKKLFAPVPFPSGSTEDVSPSGPQQPPPLPQKKIVSRAASSPDGFFWTQGSPKPGTASPKLNLSHSET | ||||||
Compositional bias | 502-529 | Polar residues | ||||
Sequence: PRGPVSQNSEVGEEETSAGQGLSSRESH | ||||||
Compositional bias | 530-544 | Basic and acidic residues | ||||
Sequence: AHSASESKPKERPAI | ||||||
Compositional bias | 603-630 | Polar residues | ||||
Sequence: GVAISDPSRCPQPAASSASEQRRPRFQA | ||||||
Compositional bias | 654-692 | Polar residues | ||||
Sequence: WGRETKNGPTDHSNSTTWHRLHPTDGSSGQNSKVGTGMS | ||||||
Compositional bias | 730-784 | Polar residues | ||||
Sequence: SSDLEKVSQGSAESLSPSFRGVHVSFTTGSTDSLASDSRTCSDGGPSSELAHSPT | ||||||
Compositional bias | 828-851 | Polar residues | ||||
Sequence: PDGFFWTQGSPKPGTASPKLNLSH | ||||||
Region | 933-976 | Required for homodimerization | ||||
Sequence: STQLQLHGLLSNISSKEGTYAKLGGLYTQSLARLVAKCEDLFMG | ||||||
Domain | 978-1329 | Protein kinase | ||||
Sequence: QKKELHFNENNWSLFKLTCNKPCCDSGDAIYYCATCSEDPGSTYAVKICKAPEPKTVSYCSPSVPVHFNIQQDCGHFVASVPSSMLSSPDAPKDPVPALPTHPPAQEQDCVVVITREVPHQTASDFVRDSAASHQAEPEAYERRVCFLLLQLCNGLEHLKEHGIIHRDLCLENLLLVHCTLQAGPGPAPAPAPAPAPAAAAPPCSSAAPPAGGTLSPAAGPASPEGPREKQLPRLIISNFLKAKQKPGGTPNLQQKKSQARLAPEIVSASQYRKFDEFQTGILIYELLHQPNPFEVRAQLRERDYRQEDLPPLPALSLYSPGLQQLAHLLLEADPIKRIRIGEAKRVLQCLL | ||||||
Compositional bias | 1163-1181 | Pro residues | ||||
Sequence: GPAPAPAPAPAPAAAAPPC | ||||||
Region | 1163-1206 | Disordered | ||||
Sequence: GPAPAPAPAPAPAAAAPPCSSAAPPAGGTLSPAAGPASPEGPRE | ||||||
Region | 1331-1406 | Required for homodimerization | ||||
Sequence: GPRRELVQQPGTSEEALCGTLHNWIDMKRALMMMKFAEKAVDRRRGVELEDWLCCQYLASAEPGALLQSLKLLQLL |
Domain
The dimerization region encompasses helices both from the N- and C-terminal of the protein kinase domain.
Sequence similarities
Belongs to the protein kinase superfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,406
- Mass (Da)149,624
- Last updated2014-10-01 v4
- Checksum941BCF315B826148
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAG2UYF2 | A0AAG2UYF2_HUMAN | PRAG1 | 1404 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 502-529 | Polar residues | ||||
Sequence: PRGPVSQNSEVGEEETSAGQGLSSRESH | ||||||
Compositional bias | 530-544 | Basic and acidic residues | ||||
Sequence: AHSASESKPKERPAI | ||||||
Compositional bias | 603-630 | Polar residues | ||||
Sequence: GVAISDPSRCPQPAASSASEQRRPRFQA | ||||||
Compositional bias | 654-692 | Polar residues | ||||
Sequence: WGRETKNGPTDHSNSTTWHRLHPTDGSSGQNSKVGTGMS | ||||||
Compositional bias | 730-784 | Polar residues | ||||
Sequence: SSDLEKVSQGSAESLSPSFRGVHVSFTTGSTDSLASDSRTCSDGGPSSELAHSPT | ||||||
Compositional bias | 828-851 | Polar residues | ||||
Sequence: PDGFFWTQGSPKPGTASPKLNLSH | ||||||
Compositional bias | 1163-1181 | Pro residues | ||||
Sequence: GPAPAPAPAPAPAAAAPPC | ||||||
Sequence conflict | 1226 | in Ref. 2; BAC56923 and 3; CAD38729 | ||||
Sequence: G → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC068353 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC103957 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK122582 EMBL· GenBank· DDBJ | BAC56923.1 EMBL· GenBank· DDBJ | mRNA | ||
AL833872 EMBL· GenBank· DDBJ | CAD38729.1 EMBL· GenBank· DDBJ | mRNA |