Q13136 · LIPA1_HUMAN
- ProteinLiprin-alpha-1
- GenePPFIA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1202 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.
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 | axon | |
Cellular Component | cell cortex | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | presynaptic active zone | |
Cellular Component | protein-containing complex | |
Cellular Component | Schaffer collateral - CA1 synapse | |
Cellular Component | spine apparatus | |
Biological Process | cell-matrix adhesion | |
Biological Process | cortical microtubule organization | |
Biological Process | negative regulation of protein localization to plasma membrane | |
Biological Process | negative regulation of stress fiber assembly | |
Biological Process | regulation of postsynaptic membrane neurotransmitter receptor levels | |
Biological Process | signal transduction | |
Biological Process | synapse organization |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLiprin-alpha-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13136
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with PTPRF near focal adhesions.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_017756 | 71 | in dbSNP:rs546502 | |||
Sequence: V → I | ||||||
Natural variant | VAR_049998 | 1072 | in dbSNP:rs11236045 | |||
Sequence: L → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,302 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_0000191026 | 1-1202 | UniProt | Liprin-alpha-1 | |||
Sequence: MMCEVMPTISEAEGPPGGGGGHGSGSPSQPDADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDADVSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRVGSGSLDNLGRFRSMSSIPPYPASSLASSSPPGSGRSTPRRIPHSPAREVDRLGVMTLLPPSREEVRDDKTTIKCETSPPSSPRALRLDRLHKGALHTVSHEDIRDIRNSTGSQDGPVSNPSSSNSSQDSLHKAPKKKGIKSSIGRLFGKKEKGRPGQTGKEALGQAGVSETDNSSQDALGLSKLGGQAEKNRKLQKKHELLEEARRQGLPFAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLTSPSAPPTSRTTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRLNYDRKELERKREESQSEIKDVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLLVMGTDRRFDEDDDKSFRRAPSWRKKFRPKDIRGLAAGSAETLPANFRVTSSMSSPSMQPKKMQMDGNVSGTQRLDSATVRTYSC | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 150 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 230 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 239 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 242 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 242 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 244 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 244 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 448 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 448 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 530 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 546 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 572 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 666 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 666 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 668 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 668 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 680 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 692 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 693 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 693 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 697 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 700 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 708 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 740 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 741 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 744 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 745 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 761 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 761 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 763 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 763 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 774 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 776 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 789 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 790 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 793 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1133 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1159 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1159 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1171 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1174 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer. Interacts with PTPRF (via D2 domain) (PubMed:7796809).
Part of a cortical microtubule stabilization complex (CMSC) composed of KANK1, PPFIA1, PPFIBP1, ERC1/ELKS, PHLDB2/LL5beta, CLASPs, KIF21A and possibly additional interactors; within CMSCs KANK1 and PHLDB2/LL5beta seem to be the core components for recruiting microtubule-binding proteins KIF21A and CLASPs, whereas PPFIA1, PPFIBP1 and ERC1/ELKS serve as scaffolds for protein clustering (PubMed:24120883, PubMed:27410476).
Part of a cortical microtubule stabilization complex (CMSC) composed of KANK1, PPFIA1, PPFIBP1, ERC1/ELKS, PHLDB2/LL5beta, CLASPs, KIF21A and possibly additional interactors; within CMSCs KANK1 and PHLDB2/LL5beta seem to be the core components for recruiting microtubule-binding proteins KIF21A and CLASPs, whereas PPFIA1, PPFIBP1 and ERC1/ELKS serve as scaffolds for protein clustering (PubMed:24120883, PubMed:27410476).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13136 | CCNH P51946 | 6 | EBI-745426, EBI-741406 | |
BINARY | Q13136 | CDK18 Q07002 | 3 | EBI-745426, EBI-746238 | |
BINARY | Q13136 | DTNB O60941 | 7 | EBI-745426, EBI-740402 | |
BINARY | Q13136 | DYNC1I2 Q13409-3 | 3 | EBI-745426, EBI-12094038 | |
BINARY | Q13136 | ELOA Q14241 | 3 | EBI-745426, EBI-742350 | |
BINARY | Q13136 | FAM161A Q3B820 | 5 | EBI-745426, EBI-719941 | |
BINARY | Q13136 | GAS8 O95995 | 3 | EBI-745426, EBI-1052570 | |
XENO | Q13136 | Gria2 P19491 | 2 | EBI-745426, EBI-77718 | |
XENO | Q13136 | Grip1 P97879 | 4 | EBI-745426, EBI-936113 | |
BINARY | Q13136 | MBIP Q9NS73 | 3 | EBI-745426, EBI-741953 | |
BINARY | Q13136 | PPP2R5A Q15172 | 3 | EBI-745426, EBI-641666 | |
BINARY | Q13136 | PPP2R5D Q14738 | 5 | EBI-745426, EBI-396563 | |
BINARY | Q13136 | TXLNA P40222 | 5 | EBI-745426, EBI-359793 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: MMCEVMPTISEAEGPPGGGGGHGSGSPSQPDAD | ||||||
Coiled coil | 34-141 | |||||
Sequence: SHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRM | ||||||
Coiled coil | 176-214 | |||||
Sequence: EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKK | ||||||
Compositional bias | 224-239 | Polar residues | ||||
Sequence: NHEQENTPSTSGKRSS | ||||||
Region | 224-245 | Disordered | ||||
Sequence: NHEQENTPSTSGKRSSDGSLSH | ||||||
Coiled coil | 249-521 | |||||
Sequence: LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL | ||||||
Region | 426-446 | Disordered | ||||
Sequence: KNQELQRARQREKMNEEHNKR | ||||||
Coiled coil | 623-669 | |||||
Sequence: ADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRVGSGSL | ||||||
Region | 651-855 | Disordered | ||||
Sequence: ENTEQRAEEIESRVGSGSLDNLGRFRSMSSIPPYPASSLASSSPPGSGRSTPRRIPHSPAREVDRLGVMTLLPPSREEVRDDKTTIKCETSPPSSPRALRLDRLHKGALHTVSHEDIRDIRNSTGSQDGPVSNPSSSNSSQDSLHKAPKKKGIKSSIGRLFGKKEKGRPGQTGKEALGQAGVSETDNSSQDALGLSKLGGQAEKN | ||||||
Compositional bias | 681-699 | Polar residues | ||||
Sequence: IPPYPASSLASSSPPGSGR | ||||||
Compositional bias | 749-772 | Basic and acidic residues | ||||
Sequence: LRLDRLHKGALHTVSHEDIRDIRN | ||||||
Compositional bias | 773-793 | Polar residues | ||||
Sequence: STGSQDGPVSNPSSSNSSQDS | ||||||
Compositional bias | 831-845 | Polar residues | ||||
Sequence: GVSETDNSSQDALGL | ||||||
Coiled coil | 847-871 | |||||
Sequence: KLGGQAEKNRKLQKKHELLEEARRQ | ||||||
Domain | 878-944 | SAM 1 | ||||
Sequence: WDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSL | ||||||
Domain | 963-1027 | SAM 2 | ||||
Sequence: NHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL | ||||||
Coiled coil | 1021-1050 | |||||
Sequence: IMCLRRLNYDRKELERKREESQSEIKDVLV | ||||||
Domain | 1051-1120 | SAM 3 | ||||
Sequence: WSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLLVM | ||||||
Region | 1163-1202 | Disordered | ||||
Sequence: NFRVTSSMSSPSMQPKKMQMDGNVSGTQRLDSATVRTYSC |
Domain
The N-terminal coiled coil regions mediate homodimerization preferentially and heterodimerization type alpha/alpha. The C-terminal, non-coiled coil regions mediate heterodimerization type alpha/beta and interaction with PTPRD, PTPRF and PTPRS.
Sequence similarities
Belongs to the liprin family. Liprin-alpha subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q13136-1
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
- SynonymsLAR-interacting protein 1b, LIP.1b, b
- Length1,202
- Mass (Da)135,779
- Last updated1996-11-01 v1
- ChecksumC8CF7C20B298BFB1
Q13136-2
- Name2
- SynonymsLAR-interacting protein 1a, LIP.1a, a
- NoteDue to intron retention.
- Differences from canonical
- 1185-1202: NVSGTQRLDSATVRTYSC → M
Computationally mapped potential isoform sequences
There are 20 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y7R9 | A0A2R8Y7R9_HUMAN | PPFIA1 | 1224 | ||
A0AAG2UY63 | A0AAG2UY63_HUMAN | PPFIA1 | 99 | ||
A0AAG2UWS2 | A0AAG2UWS2_HUMAN | PPFIA1 | 237 | ||
A0AAG2UWZ2 | A0AAG2UWZ2_HUMAN | PPFIA1 | 1242 | ||
A0AAG2UWZ6 | A0AAG2UWZ6_HUMAN | PPFIA1 | 253 | ||
A0AAG2UWH4 | A0AAG2UWH4_HUMAN | PPFIA1 | 158 | ||
A0AAG2UWI0 | A0AAG2UWI0_HUMAN | PPFIA1 | 389 | ||
A0AAG2UWJ5 | A0AAG2UWJ5_HUMAN | PPFIA1 | 386 | ||
H0YEF9 | H0YEF9_HUMAN | PPFIA1 | 387 | ||
H0YDZ8 | H0YDZ8_HUMAN | PPFIA1 | 253 | ||
H0YF15 | H0YF15_HUMAN | PPFIA1 | 97 | ||
H0YEK0 | H0YEK0_HUMAN | PPFIA1 | 46 | ||
H0YD72 | H0YD72_HUMAN | PPFIA1 | 237 | ||
H0YDW2 | H0YDW2_HUMAN | PPFIA1 | 389 | ||
H0YD39 | H0YD39_HUMAN | PPFIA1 | 33 | ||
A0A1B0GVT3 | A0A1B0GVT3_HUMAN | PPFIA1 | 271 | ||
E9PPF6 | E9PPF6_HUMAN | PPFIA1 | 158 | ||
E9PJZ7 | E9PJZ7_HUMAN | PPFIA1 | 583 | ||
E9PID5 | E9PID5_HUMAN | PPFIA1 | 99 | ||
A0A3B3ITS2 | A0A3B3ITS2_HUMAN | PPFIA1 | 166 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 224-239 | Polar residues | ||||
Sequence: NHEQENTPSTSGKRSS | ||||||
Sequence conflict | 492 | in Ref. 3; AAH34046 | ||||
Sequence: E → G | ||||||
Sequence conflict | 555 | in Ref. 3; AAH34046 | ||||
Sequence: P → T | ||||||
Sequence conflict | 672-674 | in Ref. 4; BAA08353 | ||||
Sequence: LGR → EFG | ||||||
Compositional bias | 681-699 | Polar residues | ||||
Sequence: IPPYPASSLASSSPPGSGR | ||||||
Compositional bias | 749-772 | Basic and acidic residues | ||||
Sequence: LRLDRLHKGALHTVSHEDIRDIRN | ||||||
Compositional bias | 773-793 | Polar residues | ||||
Sequence: STGSQDGPVSNPSSSNSSQDS | ||||||
Sequence conflict | 800-801 | in Ref. 4; BAA08353 | ||||
Sequence: KK → EE | ||||||
Compositional bias | 831-845 | Polar residues | ||||
Sequence: GVSETDNSSQDALGL | ||||||
Sequence conflict | 866 | in Ref. 3; AAH34046 | ||||
Sequence: E → G | ||||||
Sequence conflict | 994 | in Ref. 4; BAA08353 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 1023 | in Ref. 4; BAA08353 | ||||
Sequence: C → S | ||||||
Sequence conflict | 1044 | in Ref. 4; BAA08353 | ||||
Sequence: E → EVRV | ||||||
Sequence conflict | 1121-1123 | in Ref. 4; BAA08353 | ||||
Sequence: GTD → PEF | ||||||
Alternative sequence | VSP_009391 | 1185-1202 | in isoform 2 | |||
Sequence: NVSGTQRLDSATVRTYSC → M |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U22815 EMBL· GenBank· DDBJ | AAC50172.1 EMBL· GenBank· DDBJ | mRNA | ||
U22816 EMBL· GenBank· DDBJ | AAC50173.1 EMBL· GenBank· DDBJ | mRNA | ||
AP002336 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC034046 EMBL· GenBank· DDBJ | AAH34046.1 EMBL· GenBank· DDBJ | mRNA | ||
D49354 EMBL· GenBank· DDBJ | BAA08353.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |