Q9Z0R4 · ITSN1_MOUSE
- ProteinIntersectin-1
- GeneItsn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1714 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:10064583).
Acts as a guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (By similarity).
Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity).
Recruits FCHSD2 to clathrin-coated pits (By similarity).
Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (PubMed:16914641).
Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (By similarity).
Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways (PubMed:16914641).
In chromaffin cells, required for normal exocytosis of catecholamines (PubMed:18676989).
Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (PubMed:23633571).
Inhibits ARHGAP31 activity toward RAC1 (By similarity).
Acts as a guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (By similarity).
Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity).
Recruits FCHSD2 to clathrin-coated pits (By similarity).
Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (PubMed:16914641).
Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (By similarity).
Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways (PubMed:16914641).
In chromaffin cells, required for normal exocytosis of catecholamines (PubMed:18676989).
Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (PubMed:23633571).
Inhibits ARHGAP31 activity toward RAC1 (By similarity).
Isoform 1
Plays a role in synaptic vesicle endocytosis in brain neurons.
Miscellaneous
Overexpression results in the inhibition of the transferrin uptake and the blockage of the clathrin-mediated endocytosis.
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 68 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 70 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 72 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 77 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 267 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 269 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 271 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 273 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 278 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1660 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1663 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 1666 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIntersectin-1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9Z0R4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with SGIP1 at the plasma membrane in structures corresponding most probably to clathrin-coated pits. Colocalizes with RAB13 on cytoplasmic vesicles that are most likely recycling endosomes.
Isoform 2
Note: Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype, except that about 13% of the pups do not thrive. Mice are born at the expected Mendelian rate (PubMed:18676989).
Mutant mice display no obvious defects in synaptic responses to single stimuli at the calyx of Held. Repetitive stimulation gives rise to decreased synaptic responses, due to perturbation of the replenishment of release-ready synaptic vesicles (PubMed:23633571).
Mutant mice display no obvious defects in synaptic responses to single stimuli at the calyx of Held. Repetitive stimulation gives rise to decreased synaptic responses, due to perturbation of the replenishment of release-ready synaptic vesicles (PubMed:23633571).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 91 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080958 | 1-1714 | Intersectin-1 | |||
Sequence: MAQFPTPFGGSLDVWAITVEERAKHDQQFLSLKPIAGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQLPSTLPPVMKQQPVAISSAPAFGIGGIASMPPLTAVAPVPMGSIPVVGMSPPLVSSVPPAAVPPLANGAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASAPPAAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGMSVISSSSVDQRLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNNQLKELREIHSKQQLQKQRSLEAARLKQKEQERKSLELEKQKEDAQRRVQERDKQWLEHVQQEEQPRPRKPHEEDRLKREDSVRKKEAEERAKPEMQDKQSRLFHPHQEPAKLATQAPWSTTEKGPLTISAQESVKVVYYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEKIPENEVPTPAKPVTDLTSAPAPKLALRETPAPLPVTSSEPSTTPNNWADFSSTWPSSSNEKPETDNWDTWAAQPSLTVPSAGQLRQRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKSDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISGPVRKSTSIDTGPTESPASLKRVASPAAKPAIPGEEFIAMYTYESSEQGDLTFQQGDVIVVTKKDGDWWTGTVGDKSGVFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYAATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSPGTSKITPTELPKTAVQPAVCQVIGMYDYTAQNDDELAFSKGQIINVLNKEDPDWWKGEVSGQVGLFPSNYVKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLTESELLTEKEVAMIFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSCQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLSEQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEIRVADIKKDQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP | ||||||
Modified residue | 203 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 318 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 334 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 335 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 685 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 890 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 894 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 895 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 897 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 971 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 977 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 979 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 988 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1130 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1137 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1638 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in brain, adrenal gland and heart (PubMed:16914641, PubMed:18676989).
Detected in neurons at the calyx of Held (at protein level) (PubMed:23633571).
Isoform 1: Primarily detected in brain neurons. Isoform 2: Primarily detected in glia (at protein level) (PubMed:18676989).
Widely expressed. Expressed at high levels in brain, heart and skeletal muscle (PubMed:10064583).
Detected in neurons at the calyx of Held (at protein level) (PubMed:23633571).
Isoform 1: Primarily detected in brain neurons. Isoform 2: Primarily detected in glia (at protein level) (PubMed:18676989).
Widely expressed. Expressed at high levels in brain, heart and skeletal muscle (PubMed:10064583).
Gene expression databases
Interaction
Subunit
Interacts (via DH domain) with CDC42. Interacts (via SH3 domain 1) with WASL (By similarity).
Interacts with dynamin, SNAP25 and SNAP23 (By similarity).
Interacts with clathrin-associated proteins and other components of the endocytic machinery, such as SPIN90, EPS15, EPN1, EPN2, STON2, FCHO1, FCHO2 and DAB2 (PubMed:10064583, PubMed:20448150).
Interacts (via SH3 domains) with REPS1 and SGIP1. Interacts with ARHGAP31 (PubMed:11744688).
Interacts with ADAM15 (By similarity).
Interacts with PRRT2 (PubMed:26797119).
Interacts (via SH3 domain 4) with FCHSD2 (via SH3 domain 2). Interacts (via SH3 domain 1) with DENND2B (By similarity).
Interacts (via SH3 domains) with CBL (PubMed:16914641).
Isoform 2: Interacts with CBL and DNM1. Isoform 2: Interacts with LMNA (By similarity).
Isoform 2: Interacts with importin subunit KPNA1; this is likely to mediate its import into the nucleus (PubMed:29599122).
Interacts with DNM2 (By similarity).
Interacts with dynamin, SNAP25 and SNAP23 (By similarity).
Interacts with clathrin-associated proteins and other components of the endocytic machinery, such as SPIN90, EPS15, EPN1, EPN2, STON2, FCHO1, FCHO2 and DAB2 (PubMed:10064583, PubMed:20448150).
Interacts (via SH3 domains) with REPS1 and SGIP1. Interacts with ARHGAP31 (PubMed:11744688).
Interacts with ADAM15 (By similarity).
Interacts with PRRT2 (PubMed:26797119).
Interacts (via SH3 domain 4) with FCHSD2 (via SH3 domain 2). Interacts (via SH3 domain 1) with DENND2B (By similarity).
Interacts (via SH3 domains) with CBL (PubMed:16914641).
Isoform 2: Interacts with CBL and DNM1. Isoform 2: Interacts with LMNA (By similarity).
Isoform 2: Interacts with importin subunit KPNA1; this is likely to mediate its import into the nucleus (PubMed:29599122).
Interacts with DNM2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Z0R4 | Arhgap31 A6X8Z5 | 3 | EBI-645386, EBI-4325995 | |
BINARY | Q9Z0R4 | Dennd1a Q8K382 | 3 | EBI-645386, EBI-7186684 | |
BINARY | Q9Z0R4-2 | Inppl1 Q6P549 | 2 | EBI-8052786, EBI-2642932 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-109 | EH 1 | ||||
Sequence: ERAKHDQQFLSLKPIAGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQLPSTLPPVMKQQPVAI | ||||||
Domain | 53-88 | EF-hand 1 | ||||
Sequence: LPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLK | ||||||
Domain | 221-310 | EH 2 | ||||
Sequence: SRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRR | ||||||
Domain | 254-289 | EF-hand 2 | ||||
Sequence: LPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVA | ||||||
Region | 310-356 | Disordered | ||||
Sequence: RVRSGSGMSVISSSSVDQRLPEEPSSEDEQQPEKKLPVTFEDKKREN | ||||||
Compositional bias | 314-329 | Polar residues | ||||
Sequence: GSGMSVISSSSVDQRL | ||||||
Region | 326-702 | KLERQ | ||||
Sequence: DQRLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNNQLKELREIHSKQQLQKQRSLEAARLKQKEQERKSLELEKQKEDAQRRVQERDKQWLEHVQQEEQPRPRKPHEEDRLKREDSVRKKEAEERAKPEMQDK | ||||||
Compositional bias | 330-356 | Basic and acidic residues | ||||
Sequence: PEEPSSEDEQQPEKKLPVTFEDKKREN | ||||||
Coiled coil | 354-658 | |||||
Sequence: RENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNNQLKELREIHSKQQLQKQRSLEAARLKQKEQERKSLELEKQKEDAQRRVQERDKQ | ||||||
Region | 614-706 | Disordered | ||||
Sequence: SKQQLQKQRSLEAARLKQKEQERKSLELEKQKEDAQRRVQERDKQWLEHVQQEEQPRPRKPHEEDRLKREDSVRKKEAEERAKPEMQDKQSRL | ||||||
Compositional bias | 625-706 | Basic and acidic residues | ||||
Sequence: EAARLKQKEQERKSLELEKQKEDAQRRVQERDKQWLEHVQQEEQPRPRKPHEEDRLKREDSVRKKEAEERAKPEMQDKQSRL | ||||||
Domain | 738-799 | SH3 1 | ||||
Sequence: VKVVYYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEKIPE | ||||||
Region | 827-863 | Disordered | ||||
Sequence: APLPVTSSEPSTTPNNWADFSSTWPSSSNEKPETDNW | ||||||
Compositional bias | 830-863 | Polar residues | ||||
Sequence: PVTSSEPSTTPNNWADFSSTWPSSSNEKPETDNW | ||||||
Domain | 906-964 | SH3 2 | ||||
Sequence: VEGLQAQALYPWRAKKDNHLNFNKSDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISG | ||||||
Domain | 995-1053 | SH3 3 | ||||
Sequence: IPGEEFIAMYTYESSEQGDLTFQQGDVIVVTKKDGDWWTGTVGDKSGVFPSNYVRLKDS | ||||||
Domain | 1067-1131 | SH3 4 | ||||
Sequence: KKPEIAQVIASYAATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSP | ||||||
Region | 1067-1131 | Required for interaction with FCHSD2 | ||||
Sequence: KKPEIAQVIASYAATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSP | ||||||
Motif | 1097-1120 | Bipartite nuclear localization signal; in isoform 2 | ||||
Sequence: RKKNPGGWWEGELQARGKKRQIGW | ||||||
Domain | 1148-1207 | SH3 5 | ||||
Sequence: PAVCQVIGMYDYTAQNDDELAFSKGQIINVLNKEDPDWWKGEVSGQVGLFPSNYVKLTTD | ||||||
Domain | 1230-1416 | DH | ||||
Sequence: KRQGYIHELIVTEENYVNDLQLVTEIFQKPLTESELLTEKEVAMIFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSCQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEG | ||||||
Domain | 1455-1564 | PH | ||||
Sequence: KFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASE | ||||||
Domain | 1572-1688 | C2 | ||||
Sequence: KKREKAYLVRSQRATGIGRLMVNVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEIRVADIKKDQGSKGPV |
Domain
SH3-3, SH3-4 and SH3-5, but not SH3-1 and SH3-2 domains, bind to dynamin (By similarity).
SH3-1 and SH3-4 bind to ARHGAP31
SH3-1 and SH3-4 bind to ARHGAP31
The KLERQ domain binds to SNAP-25 and SNAP-23.
In an autoinhibited form the SH3 domain 5 may bind intramolecularly to the DH domain, thus blocking the CDC42-binding site.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q9Z0R4-1
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
- SynonymsEse1L
- Length1,714
- Mass (Da)194,297
- Last updated2012-10-03 v2
- ChecksumBCF5038160E8208E
Q9Z0R4-2
- Name2
- SynonymsITSN-s
- Differences from canonical
- 1214-1714: Missing
Computationally mapped potential isoform sequences
There are 17 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6ZX53 | F6ZX53_MOUSE | Itsn1 | 66 | ||
F6TCC6 | F6TCC6_MOUSE | Itsn1 | 173 | ||
A0A338P7I4 | A0A338P7I4_MOUSE | Itsn1 | 279 | ||
A0A338P6K7 | A0A338P6K7_MOUSE | Itsn1 | 187 | ||
A0A338P6L8 | A0A338P6L8_MOUSE | Itsn1 | 131 | ||
F6R6C8 | F6R6C8_MOUSE | Itsn1 | 256 | ||
F6ZLP6 | F6ZLP6_MOUSE | Itsn1 | 73 | ||
E9Q3I4 | E9Q3I4_MOUSE | Itsn1 | 1176 | ||
E9Q3I5 | E9Q3I5_MOUSE | Itsn1 | 1218 | ||
E9Q3I8 | E9Q3I8_MOUSE | Itsn1 | 1142 | ||
E9Q3I9 | E9Q3I9_MOUSE | Itsn1 | 1147 | ||
E9Q0N0 | E9Q0N0_MOUSE | Itsn1 | 1719 | ||
Q6J1S9 | Q6J1S9_MOUSE | Itsn1 | 77 | ||
Q6J1F0 | Q6J1F0_MOUSE | Itsn1 | 16 | ||
D3Z6P4 | D3Z6P4_MOUSE | Itsn1 | 359 | ||
Q6NZJ5 | Q6NZJ5_MOUSE | Itsn1 | 621 | ||
F6U8U1 | F6U8U1_MOUSE | Itsn1 | 346 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 179 | in Ref. 1; AAD19749/AAD19746 | ||||
Sequence: L → W | ||||||
Compositional bias | 314-329 | Polar residues | ||||
Sequence: GSGMSVISSSSVDQRL | ||||||
Compositional bias | 330-356 | Basic and acidic residues | ||||
Sequence: PEEPSSEDEQQPEKKLPVTFEDKKREN | ||||||
Sequence conflict | 402 | in Ref. 1; AAD19749/AAD19746 | ||||
Sequence: R → A | ||||||
Compositional bias | 625-706 | Basic and acidic residues | ||||
Sequence: EAARLKQKEQERKSLELEKQKEDAQRRVQERDKQWLEHVQQEEQPRPRKPHEEDRLKREDSVRKKEAEERAKPEMQDKQSRL | ||||||
Compositional bias | 830-863 | Polar residues | ||||
Sequence: PVTSSEPSTTPNNWADFSSTWPSSSNEKPETDNW | ||||||
Alternative sequence | VSP_004296 | 1214-1714 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF132481 EMBL· GenBank· DDBJ | AAD19749.1 EMBL· GenBank· DDBJ | mRNA | ||
AF132478 EMBL· GenBank· DDBJ | AAD19746.1 EMBL· GenBank· DDBJ | mRNA | ||
AC126053 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC131691 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC134837 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF169621 EMBL· GenBank· DDBJ | AAD48848.1 EMBL· GenBank· DDBJ | mRNA | ||
AF356517 EMBL· GenBank· DDBJ | AAK40228.1 EMBL· GenBank· DDBJ | Genomic DNA |