Q9Y4G8 · RPGF2_HUMAN
- ProteinRap guanine nucleotide exchange factor 2
- GeneRAPGEF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1499 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10548487, PubMed:10608844, PubMed:11359771).
Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions
Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRap guanine nucleotide exchange factor 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y4G8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with the synaptic plasma membrane. Colocalizes with ADRB1 at the plasma membrane. Synaptosome. Enriched in synaptic plasma membrane and neuronal cell body. Colocalized with CTNNB1 at cell-cell contacts (By similarity).
Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane
Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Epilepsy, familial adult myoclonic, 7 (FAME7)
- Note
- DescriptionA form of familial myoclonic epilepsy, a neurologic disorder characterized by cortical hand tremors, myoclonic jerks and occasional generalized or focal seizures with a non-progressive or very slowly progressive disease course. Usually, myoclonic tremor is the presenting symptom, characterized by tremulous finger movements and myoclonic jerks of the limbs increased by action and posture. In a minority of patients, seizures are the presenting symptom. Some patients exhibit mild cognitive impairment. FAME7 inheritance is autosomal dominant.
- See alsoMIM:618075
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 211 | Abolishes cAMP-binding. | ||||
Sequence: K → R | ||||||
Mutagenesis | 215 | Does not abolish cAMP-binding. | ||||
Sequence: R → D | ||||||
Mutagenesis | 396-399 | Loss of cell membrane targeting. | ||||
Sequence: PLPF → AAA | ||||||
Mutagenesis | 606-626 | Abolishes interaction with RAP1AGTP-bound form and translocation from the cytoplasm to the perinuclear region. Does not abolish GEF activity on RAP1A. | ||||
Sequence: Missing | ||||||
Mutagenesis | 898 | Does not inhibit interaction with NEDD4. Does not interact with HRAS. Reduces ubiquitination. | ||||
Sequence: R → D | ||||||
Mutagenesis | 1406 | Abolishes interaction with NEDD4 and NEDD4-induced ubiquitination and degradation; when associated with A-1428. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 1428 | Abolishes interaction with NEDD4 and NEDD4-induced ubiquitination and degradation; when associated with A-1406. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 1497-1499 | No loss of cell membrane targeting. | ||||
Sequence: SAV → AAA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,275 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).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000068865 | 1-1499 | UniProt | Rap guanine nucleotide exchange factor 2 | |||
Sequence: MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEKNMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEEKRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVEVATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSSFLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQYSLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAVASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVARSSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV | |||||||
Modified residue | 501 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 585 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 602 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 644 | UniProt | Phosphothreonine; by PLK2 | ||||
Sequence: T | |||||||
Modified residue | 806 | UniProt | Phosphoserine; by PLK2 | ||||
Sequence: S | |||||||
Modified residue | 930 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 930 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 933 | UniProt | Phosphoserine; by PLK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 933 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 935 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 938 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 942 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 959 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 960 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1021 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1022 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1022 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1080 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1080 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1089 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1089 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1095 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1095 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1116 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1119 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1120 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1159 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1159 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1176 | UniProt | Phosphoserine; by PLK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1256 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1313 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1316 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1325 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated by NEDD4, leading to proteasomal degradation.
Phosphorylation by PLK2 promotes its activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in primary neuronal and endocrine cells (at protein level). Highest expression levels in brain. Lower expression levels in heart, kidney, lung, placenta and blood leukocytes.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CDH1, CTNNB1 and TJP1 (By similarity).
Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW domains); the interaction occurs before or after NGF stimulation. Interacts with KIDINS220 and NTRK1; the interactions occur after NGF stimulation (By similarity).
Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a neuronal growth factor (NGF)-dependent manner. Interacts (via C-terminal domain) with NEDD4 (via WW domains); this interaction leads to ubiquitination and degradation via the proteasome pathway in a cAMP-independent manner. Interacts with MAGI1 isoform 3 (via PDZ domain). Interacts with ADRB1 (via C-terminal PDZ motif); the interaction is direct. Interacts (via Ras-associating domain) with RAP1A (via GTP-bound active form). Interacts weakly with HRAS (via GDP- and GTP-bound forms). Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW domains).
Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW domains); the interaction occurs before or after NGF stimulation. Interacts with KIDINS220 and NTRK1; the interactions occur after NGF stimulation (By similarity).
Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a neuronal growth factor (NGF)-dependent manner. Interacts (via C-terminal domain) with NEDD4 (via WW domains); this interaction leads to ubiquitination and degradation via the proteasome pathway in a cAMP-independent manner. Interacts with MAGI1 isoform 3 (via PDZ domain). Interacts with ADRB1 (via C-terminal PDZ motif); the interaction is direct. Interacts (via Ras-associating domain) with RAP1A (via GTP-bound active form). Interacts weakly with HRAS (via GDP- and GTP-bound forms). Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW domains).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y4G8 | MAGI1 Q96QZ7-3 | 2 | EBI-307079, EBI-8769674 | |
BINARY | Q9Y4G8 | YWHAZ P63104 | 2 | EBI-307079, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 40-59 | Disordered | ||||
Sequence: HVSSSHSGCSITSDSGSSSL | ||||||
Region | 68-101 | Disordered | ||||
Sequence: SEAGDMDLSGLPETAVDSEDDDDEEDIERASDPL | ||||||
Compositional bias | 81-96 | Acidic residues | ||||
Sequence: TAVDSEDDDDEEDIER | ||||||
Domain | 267-380 | N-terminal Ras-GEF | ||||
Sequence: KGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAK | ||||||
Domain | 385-470 | PDZ | ||||
Sequence: LMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVF | ||||||
Domain | 606-692 | Ras-associating | ||||
Sequence: PDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNME | ||||||
Domain | 717-944 | Ras-GEF | ||||
Sequence: STVEVATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVL | ||||||
Region | 1002-1050 | Disordered | ||||
Sequence: PATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQSLPQPQQQPPPAHKI | ||||||
Compositional bias | 1024-1038 | Polar residues | ||||
Sequence: VAPRAGSQQKAQSLP | ||||||
Region | 1095-1160 | Disordered | ||||
Sequence: SLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSF | ||||||
Compositional bias | 1106-1160 | Polar residues | ||||
Sequence: TISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSF | ||||||
Region | 1224-1256 | Disordered | ||||
Sequence: PSTEELSQDQGDRASLDAADSGRGSWTSCSSGS | ||||||
Compositional bias | 1305-1336 | Polar residues | ||||
Sequence: TKYNRQNQSRESLEQAQSRASWASSTGYWGED | ||||||
Region | 1305-1499 | Disordered | ||||
Sequence: TKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAVASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVARSSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV | ||||||
Compositional bias | 1339-1353 | Basic and acidic residues | ||||
Sequence: GDTGTIKRRGGKDVS | ||||||
Compositional bias | 1355-1369 | Polar residues | ||||
Sequence: EAESSSLTSVTTEET | ||||||
Compositional bias | 1435-1467 | Polar residues | ||||
Sequence: SRMVARSSDTAGPSSVQQPHGHPTSSRPVNKPQ |
Domain
The Ras-associating domain is necessary for the Rap guanine nucleotide exchange activity. The N-terminal regionis necessary for cAMP-binding. The PDZ domain is necessary for its targeting to the cell membrane.
Sequence similarities
Belongs to the RAPGEF2 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,499
- Mass (Da)167,417
- Last updated1999-11-01 v1
- Checksum1909E8A12637E001
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y661 | A0A2R8Y661_HUMAN | RAPGEF2 | 1559 | ||
A0A2R8YGD3 | A0A2R8YGD3_HUMAN | RAPGEF2 | 1679 | ||
D6RAK0 | D6RAK0_HUMAN | RAPGEF2 | 155 | ||
D6RC78 | D6RC78_HUMAN | RAPGEF2 | 154 | ||
A0A8I5KZ40 | A0A8I5KZ40_HUMAN | RAPGEF2 | 1660 | ||
A0A994J7S7 | A0A994J7S7_HUMAN | RAPGEF2 | 1540 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 81-96 | Acidic residues | ||||
Sequence: TAVDSEDDDDEEDIER | ||||||
Compositional bias | 1024-1038 | Polar residues | ||||
Sequence: VAPRAGSQQKAQSLP | ||||||
Compositional bias | 1106-1160 | Polar residues | ||||
Sequence: TISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSF | ||||||
Compositional bias | 1305-1336 | Polar residues | ||||
Sequence: TKYNRQNQSRESLEQAQSRASWASSTGYWGED | ||||||
Compositional bias | 1339-1353 | Basic and acidic residues | ||||
Sequence: GDTGTIKRRGGKDVS | ||||||
Compositional bias | 1355-1369 | Polar residues | ||||
Sequence: EAESSSLTSVTTEET | ||||||
Compositional bias | 1435-1467 | Polar residues | ||||
Sequence: SRMVARSSDTAGPSSVQQPHGHPTSSRPVNKPQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB002311 EMBL· GenBank· DDBJ | BAA20772.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CH471056 EMBL· GenBank· DDBJ | EAX04847.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471056 EMBL· GenBank· DDBJ | EAX04848.1 EMBL· GenBank· DDBJ | Genomic DNA |