Q62417 · SRBS1_MOUSE
- ProteinSorbin and SH3 domain-containing protein 1
- GeneSorbs1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1290 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions.
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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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSorbin and SH3 domain-containing protein 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 accessionQ62417
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalized with PXN at focal adhesions during myogenic differentiation (By similarity).
Colocalizes with actin stress fibers. Also detected at the plasma membrane and in neuronal intranuclear inclusions. Colocalizes with the Ten-1 ICD form of TENM1 in the nucleus
Colocalizes with actin stress fibers. Also detected at the plasma membrane and in neuronal intranuclear inclusions. Colocalizes with the Ten-1 ICD form of TENM1 in the nucleus
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000072186 | 1-1290 | Sorbin and SH3 domain-containing protein 1 | |||
Sequence: MSSECDVGSSKAVVNGLASGNHGPDKDMDPTKICTGKGTVTLRASSSYRGTPSSSPVSPQESPKHESKSGLEPEDPSADEWKLSSSADTNGNAQPSPLAAKGYRSVHPSLSADKPQGSPLLNEVSSSHIETDSQDFPPTSRPSSAYPSTTIVNPTIVLLQHNRDPASERRAGEQDPVPTPAELTSPGRASERRAKDASRRVVRSAQDLSDVSTDEVGIPLRNTERSKDWYKTMFKQIHKLNRDDDSDVHSPRYSFSDDTKSPLSVPRSKSEMNYIEGEKVVKRSATLPLPARSSSLKSSPERNDWEPLDKKVDTRKYRAEPKSIYEYQPGKSSVLTNEKMSRDISPEEIDLKNEPWYKFFSELEFGRPTNLEKDLSFCQAELEADLEKVETVNKSPSANSPQSSAVSPTPDITSEPPGYIYSSNFHAVKRESDGTPGGLASLENERQIYKSVLEGGDIPLQGLSGLKRPSSSASTKVDRKGGNAHMISSSSVHSRTFHTSNALGPGCKHKKPLSAAKACISEILPSKFKPRLSAPSALLQEQKSVLLPSEKAQSCENLCVSLNDSKRGLPLRVGGSIENLLMRSRRDYDSKSSSTMSLQEYGTSSRRPCPLSRKAGLHFSMFYRDMHQINRAGLSLGSISSSSVRDLASHFERSSLTLARGELGASQEGSEHIPKHTVSSRITAFEQLIQRSRSMPSLDFSGRLSKSPTPVLSRSGLTSARSAESLLESTKLRPREMDGMDSGGVYASPTCSNMADHALSFRSLVPSEPLSICSDELDHCSNVSNDSREGSGGSVHGDFPKHRLNKCKGTCPASYTRFTTIRKHEQQSSRQSDWRSDSRGDKNSLLRNIHLMSPLPFRLKKPLQQHPRQPPPSDSSESPAGQKADLPCHDPQDQPHSAGKPQVPTRLSSRHTMARLSHNSEPPLDRPAGLEDCTRAINNGNPVPYSDHGLDRNNNPQSELAAAHGDSESPRHFIPADYLESTEEFIRRRHDDKEKLLADQRRLKREQEEADIAARRHTGVIPTHHQFITNERFGDLLNIDDTAKRKSGLEMRPARAKFDFKAQTLKELPLQKGDVVYIYRQIDQNWYEGEHHGRVGIFPRTYIELLPPAEKAQPRKLAPVQVLEYGEAIAKFNFNGDTQVEMSFRKGERITLLRQVDENWYEGRIPGTSRQGIFPITYVDVLKRPLVKTPVDYIDLPYSSSPSRSATVSPQQPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL | ||||||
Modified residue | 51 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 55 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 62 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 164 | In isoform Q62417-2; Phosphoserine | ||||
Sequence: D | ||||||
Modified residue | 164 | In isoform Q62417-5; Phosphoserine | ||||
Sequence: D | ||||||
Modified residue | 175 | In isoform Q62417-6; Phosphoserine | ||||
Sequence: D | ||||||
Modified residue | 179 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 185 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 194 | In isoform Q62417-4; Phosphoserine | ||||
Sequence: A | ||||||
Modified residue | 204 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 209 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 254 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 261 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 270 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 288 | In isoform Q62417-7; Phosphoserine | ||||
Sequence: P | ||||||
Modified residue | 325 | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | ||||||
Modified residue | 345 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 346 | In isoform Q62417-2; Phosphoserine | ||||
Sequence: P | ||||||
Modified residue | 346 | In isoform Q62417-5; Phosphoserine | ||||
Sequence: P | ||||||
Modified residue | 357 | In isoform Q62417-6; Phosphoserine | ||||
Sequence: Y | ||||||
Modified residue | 376 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 376 | In isoform Q62417-4; Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 407 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 421 | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | ||||||
Modified residue | 432 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 470 | In isoform Q62417-7; Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 475 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 969 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1189 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1193 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1198 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1201 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1209 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1238 | Phosphotyrosine; by ABL1 | ||||
Sequence: Y |
Post-translational modification
O-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues tested: heart, brain, spleen, lung, liver, muscle, kidney and testis. Expressed in 3T3-L1 adipocytes but not in 3T3-L1 fibroblasts.
Interaction
Subunit
Interacts (via SH3 domain 2) with PXN (By similarity).
Interacts with the long isoform of AFDN and with VCL. AFDN and VCL bind to SORBS1 in a competitive manner and do not form a ternary complex. Interacts with ABL1, CBL, CBLB and INPPL1/SHIP2 through the third SH3 domain. Interaction with ABL1 occurs only after insulin stimulation while this has no effect on the interaction with INPPL1. Interacts with the insulin receptor but dissociates from it following insulin stimulation. Also interacts with SCA7, PTK2/FAK1 and flotillin. Interacts (via third SH3 domain) with the Ten-1 ICD form of TENM1; the interaction induces the translocation of SORBS1 to the nucleus. Interacts with INSM1.
Interacts with the long isoform of AFDN and with VCL. AFDN and VCL bind to SORBS1 in a competitive manner and do not form a ternary complex. Interacts with ABL1, CBL, CBLB and INPPL1/SHIP2 through the third SH3 domain. Interaction with ABL1 occurs only after insulin stimulation while this has no effect on the interaction with INPPL1. Interacts with the insulin receptor but dissociates from it following insulin stimulation. Also interacts with SCA7, PTK2/FAK1 and flotillin. Interacts (via third SH3 domain) with the Ten-1 ICD form of TENM1; the interaction induces the translocation of SORBS1 to the nucleus. Interacts with INSM1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q62417-2 | PXN P49023 | 8 | EBI-7072893, EBI-702209 | |
XENO | Q62417-2 | VCL P18206 | 3 | EBI-7072893, EBI-716775 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-211 | Disordered | ||||
Sequence: MSSECDVGSSKAVVNGLASGNHGPDKDMDPTKICTGKGTVTLRASSSYRGTPSSSPVSPQESPKHESKSGLEPEDPSADEWKLSSSADTNGNAQPSPLAAKGYRSVHPSLSADKPQGSPLLNEVSSSHIETDSQDFPPTSRPSSAYPSTTIVNPTIVLLQHNRDPASERRAGEQDPVPTPAELTSPGRASERRAKDASRRVVRSAQDLSDV | ||||||
Compositional bias | 38-64 | Polar residues | ||||
Sequence: GTVTLRASSSYRGTPSSSPVSPQESPK | ||||||
Compositional bias | 65-81 | Basic and acidic residues | ||||
Sequence: HESKSGLEPEDPSADEW | ||||||
Compositional bias | 82-96 | Polar residues | ||||
Sequence: KLSSSADTNGNAQPS | ||||||
Compositional bias | 111-157 | Polar residues | ||||
Sequence: SADKPQGSPLLNEVSSSHIETDSQDFPPTSRPSSAYPSTTIVNPTIV | ||||||
Compositional bias | 188-203 | Basic and acidic residues | ||||
Sequence: RASERRAKDASRRVVR | ||||||
Domain | 202-247 | SoHo | ||||
Sequence: VRSAQDLSDVSTDEVGIPLRNTERSKDWYKTMFKQIHKLNRDDDSD | ||||||
Compositional bias | 238-254 | Basic and acidic residues | ||||
Sequence: HKLNRDDDSDVHSPRYS | ||||||
Region | 238-271 | Disordered | ||||
Sequence: HKLNRDDDSDVHSPRYSFSDDTKSPLSVPRSKSE | ||||||
Region | 286-313 | Disordered | ||||
Sequence: TLPLPARSSSLKSSPERNDWEPLDKKVD | ||||||
Region | 389-416 | Disordered | ||||
Sequence: VETVNKSPSANSPQSSAVSPTPDITSEP | ||||||
Compositional bias | 392-416 | Polar residues | ||||
Sequence: VNKSPSANSPQSSAVSPTPDITSEP | ||||||
Region | 463-482 | Disordered | ||||
Sequence: LSGLKRPSSSASTKVDRKGG | ||||||
Compositional bias | 465-482 | Polar residues | ||||
Sequence: GLKRPSSSASTKVDRKGG | ||||||
Region | 588-607 | Disordered | ||||
Sequence: YDSKSSSTMSLQEYGTSSRR | ||||||
Compositional bias | 591-606 | Polar residues | ||||
Sequence: KSSSTMSLQEYGTSSR | ||||||
Compositional bias | 697-726 | Polar residues | ||||
Sequence: SLDFSGRLSKSPTPVLSRSGLTSARSAESL | ||||||
Region | 697-739 | Disordered | ||||
Sequence: SLDFSGRLSKSPTPVLSRSGLTSARSAESLLESTKLRPREMDG | ||||||
Region | 783-803 | Disordered | ||||
Sequence: VSNDSREGSGGSVHGDFPKHR | ||||||
Region | 822-841 | Disordered | ||||
Sequence: RKHEQQSSRQSDWRSDSRGD | ||||||
Compositional bias | 823-841 | Basic and acidic residues | ||||
Sequence: KHEQQSSRQSDWRSDSRGD | ||||||
Region | 862-972 | Disordered | ||||
Sequence: PLQQHPRQPPPSDSSESPAGQKADLPCHDPQDQPHSAGKPQVPTRLSSRHTMARLSHNSEPPLDRPAGLEDCTRAINNGNPVPYSDHGLDRNNNPQSELAAAHGDSESPRH | ||||||
Compositional bias | 898-916 | Polar residues | ||||
Sequence: AGKPQVPTRLSSRHTMARL | ||||||
Compositional bias | 948-962 | Polar residues | ||||
Sequence: HGLDRNNNPQSELAA | ||||||
Domain | 1049-1108 | SH3 1 | ||||
Sequence: LEMRPARAKFDFKAQTLKELPLQKGDVVYIYRQIDQNWYEGEHHGRVGIFPRTYIELLPP | ||||||
Domain | 1123-1184 | SH3 2 | ||||
Sequence: LEYGEAIAKFNFNGDTQVEMSFRKGERITLLRQVDENWYEGRIPGTSRQGIFPITYVDVLKR | ||||||
Region | 1198-1227 | Disordered | ||||
Sequence: YSSSPSRSATVSPQQPQAQQRRVTPDRSQP | ||||||
Domain | 1229-1290 | SH3 3 | ||||
Sequence: LDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
Q62417-1
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
- Length1,290
- Mass (Da)143,070
- Last updated2004-08-16 v2
- Checksum07C9A74BD794E390
Q62417-2
- Name2
- SynonymsCAPsm
Q62417-3
- Name3
- SynonymsPonsin-2
Q62417-4
- Name4
- SynonymsPonsin-1
Q62417-5
- Name5
Q62417-6
- Name6
Q62417-7
- Name7
- Differences from canonical
- 70-78: Missing
- 117-117: G → GATSSSSAPSEVIVVPLYLVNTDRGQGQEGTARTPASLGPLGCVHTVPATTPAASPLTFPTLDDFIPPHLQRRPHHSQPASACGSLSPASQTSPPSPPPPLVPPVPEDLHRGLEPDLPGAVSSTG
- 163-163: R → REQQKRLSSLS
- 341-402: Missing
- 477-965: Missing
- 1212-1290: QPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL → VSKLSNSACSFHPQLCQRHTALLGLLFHALIKSYLEQAGWEFFSYMSVAFS
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PYX6 | E9PYX6_MOUSE | Sorbs1 | 724 | ||
A0A668KLG2 | A0A668KLG2_MOUSE | Sorbs1 | 352 | ||
E9Q6A3 | E9Q6A3_MOUSE | Sorbs1 | 714 | ||
A0A5F8MPJ2 | A0A5F8MPJ2_MOUSE | Sorbs1 | 1189 | ||
D3Z5J3 | D3Z5J3_MOUSE | Sorbs1 | 938 | ||
A0A286YD34 | A0A286YD34_MOUSE | Sorbs1 | 126 | ||
A0A286YCQ0 | A0A286YCQ0_MOUSE | Sorbs1 | 684 | ||
A0A286YCN8 | A0A286YCN8_MOUSE | Sorbs1 | 170 | ||
A0A286YCI8 | A0A286YCI8_MOUSE | Sorbs1 | 1290 | ||
A0A286YDN0 | A0A286YDN0_MOUSE | Sorbs1 | 695 | ||
A0A286YDJ3 | A0A286YDJ3_MOUSE | Sorbs1 | 28 | ||
A0A668KL65 | A0A668KL65_MOUSE | Sorbs1 | 1005 | ||
E9QNA7 | E9QNA7_MOUSE | Sorbs1 | 740 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_050885 | 26 | in isoform 4 | |||
Sequence: K → KADPFRARSISAVKIIPVKTVKSPSGLVLPP | ||||||
Compositional bias | 38-64 | Polar residues | ||||
Sequence: GTVTLRASSSYRGTPSSSPVSPQESPK | ||||||
Compositional bias | 65-81 | Basic and acidic residues | ||||
Sequence: HESKSGLEPEDPSADEW | ||||||
Alternative sequence | VSP_050886 | 70-78 | in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Compositional bias | 82-96 | Polar residues | ||||
Sequence: KLSSSADTNGNAQPS | ||||||
Compositional bias | 111-157 | Polar residues | ||||
Sequence: SADKPQGSPLLNEVSSSHIETDSQDFPPTSRPSSAYPSTTIVNPTIV | ||||||
Alternative sequence | VSP_050887 | 117 | in isoform 6 | |||
Sequence: G → GATSSSSAPSEG | ||||||
Alternative sequence | VSP_050888 | 117 | in isoform 7 | |||
Sequence: G → GATSSSSAPSEVIVVPLYLVNTDRGQGQEGTARTPASLGPLGCVHTVPATTPAASPLTFPTLDDFIPPHLQRRPHHSQPASACGSLSPASQTSPPSPPPPLVPPVPEDLHRGLEPDLPGAVSSTG | ||||||
Alternative sequence | VSP_050889 | 163 | in isoform 2, isoform 4, isoform 5, isoform 6 and isoform 7 | |||
Sequence: R → REQQKRLSSLS | ||||||
Compositional bias | 188-203 | Basic and acidic residues | ||||
Sequence: RASERRAKDASRRVVR | ||||||
Sequence conflict | 205 | in Ref. 7; BAC28980 | ||||
Sequence: A → T | ||||||
Compositional bias | 238-254 | Basic and acidic residues | ||||
Sequence: HKLNRDDDSDVHSPRYS | ||||||
Sequence conflict | 308 | in Ref. 7; BAC28980 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_050890 | 341-402 | in isoform 2, isoform 4, isoform 5, isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_050891 | 369-402 | in isoform 3 | |||
Sequence: TNLEKDLSFCQAELEADLEKVETVNKSPSANSPQ → PPKKIWDYTPGDCSILPREDRK | ||||||
Compositional bias | 392-416 | Polar residues | ||||
Sequence: VNKSPSANSPQSSAVSPTPDITSEP | ||||||
Compositional bias | 465-482 | Polar residues | ||||
Sequence: GLKRPSSSASTKVDRKGG | ||||||
Alternative sequence | VSP_050892 | 477-965 | in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7 | |||
Sequence: Missing | ||||||
Compositional bias | 591-606 | Polar residues | ||||
Sequence: KSSSTMSLQEYGTSSR | ||||||
Compositional bias | 697-726 | Polar residues | ||||
Sequence: SLDFSGRLSKSPTPVLSRSGLTSARSAESL | ||||||
Compositional bias | 823-841 | Basic and acidic residues | ||||
Sequence: KHEQQSSRQSDWRSDSRGD | ||||||
Compositional bias | 898-916 | Polar residues | ||||
Sequence: AGKPQVPTRLSSRHTMARL | ||||||
Compositional bias | 948-962 | Polar residues | ||||
Sequence: HGLDRNNNPQSELAA | ||||||
Alternative sequence | VSP_050893 | 994-1049 | in isoform 3, isoform 4, isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 1004 | in Ref. 4; AAM77354 | ||||
Sequence: K → M | ||||||
Alternative sequence | VSP_050894 | 1212-1290 | in isoform 7 | |||
Sequence: QPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL → VSKLSNSACSFHPQLCQRHTALLGLLFHALIKSYLEQAGWEFFSYMSVAFS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U58883 EMBL· GenBank· DDBJ | AAC71776.1 EMBL· GenBank· DDBJ | mRNA | ||
AF078666 EMBL· GenBank· DDBJ | AAD16007.1 EMBL· GenBank· DDBJ | mRNA | ||
AF078667 EMBL· GenBank· DDBJ | AAD16008.1 EMBL· GenBank· DDBJ | mRNA | ||
AF521593 EMBL· GenBank· DDBJ | AAM77354.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122487 EMBL· GenBank· DDBJ | BAC65769.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK035212 EMBL· GenBank· DDBJ | BAC28980.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012703 EMBL· GenBank· DDBJ | AAH12703.1 EMBL· GenBank· DDBJ | mRNA |