Q9HAU0 · PKHA5_HUMAN
- ProteinPleckstrin homology domain-containing family A member 5
- GenePLEKHA5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1116 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | glutamatergic synapse | |
Cellular Component | membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | postsynaptic density | |
Molecular Function | phosphatidylinositol-3,5-bisphosphate binding | |
Molecular Function | phosphatidylinositol-3-phosphate binding | |
Molecular Function | phosphatidylinositol-4-phosphate binding | |
Molecular Function | phosphatidylinositol-5-phosphate binding | |
Biological Process | reproductive system development |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePleckstrin homology domain-containing family A member 5
- Short namesPH domain-containing family A member 5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9HAU0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,295 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 initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000053883 | 2-1116 | UniProt | Pleckstrin homology domain-containing family A member 5 | |||
Sequence: AADLNLEWISLPRSWTYGITRGGRVFFINEEAKSTTWLHPVTGEAVVTGHRRQSTDLPTGWEEAYTFEGARYYINHNERKVTCKHPVTGQPSQDNCIFVVNEQTVATMTSEEKKERPISMINEASNYNVTSDYAVHPMSPVGRTSRASKKVHNFGKRSNSIKRNPNAPVVRRGWLYKQDSTGMKLWKKRWFVLSDLCLFYYRDEKEEGILGSILLPSFQIALLTSEDHINRKYAFKAAHPNMRTYYFCTDTGKEMELWMKAMLDAALVQTEPVKRVDKITSENAPTKETNNIPNHRVLIKPEIQNNQKNKEMSKIEEKKALEAEKYGFQKDGQDRPLTKINSVKLNSLPSEYESGSACPAQTVHYRPINLSSSENKIVNVSLADLRGGNRPNTGPLYTEADRVIQRTNSMQQLEQWIKIQKGRGHEEETRGVISYQTLPRNMPSHRAQIMARYPEGYRTLPRNSKTRPESICSVTPSTHDKTLGPGAEEKRRSMRDDTMWQLYEWQQRQFYNKQSTLPRHSTLSSPKTMVNISDQTMHSIPTSPSHGSIAAYQGYSPQRTYRSEVSSPIQRGDVTIDRRHRAHHPKHVYVPDRRSVPAGLTLQSVSPQSLQGKTLSQDEGRGTLYKYRPEEVDIDAKLSRLCEQDKVVHALEEKLQQLHKEKYTLEQALLSASQEIEMHADNPAAIQTVVLQRDDLQNGLLSTCRELSRATAELERAWREYDKLEYDVTVTRNQMQEQLDHLGEVQTESAGIQRAQIQKELWRIQDVMEGLSKHKQQRGTTEIGMIGSKPFSTVKYKNEGPDYRLYKSEPELTTVAEVDESNGEEKSEPVSEIETSVVKGSHFPVGVVPPRAKSPTPESSTIASYVTLRKTKKMMDLRTERPRSAVEQLCLAESTRPRMTVEEQMERIRRHQQACLREKKKGLNVIGASDQSPLQSPSNLRDNPFRTTQTRRRDDKELDTAIRENDVKPDHETPATEIVQLKETEPQNVDFSKELKKTENISYEMLFEPEPNGVNSVEMMDKERNKDKMPEDVTFSPQDETQTANHKPEEHPEENTKNSVDEQEETVISYESTPEVSRGNQTMAVKSLSPSPESSASPVPSTQPQLTEGSHFMCV | |||||||
Modified residue | 55 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 126 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 128 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 134 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 301 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 343 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 353 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 382 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 382 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 398 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 399 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 410 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 410 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 436 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 438 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 460 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 476 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 478 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 526 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 543 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 549 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 557 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 568 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 576 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 590 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 607 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 607 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 807 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 809 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 809 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 822 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 837 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 855 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 855 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 857 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 860 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 862 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 865 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 866 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 868 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 885 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 896 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 930 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 933 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 933 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 937 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 937 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 939 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1037 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1070 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1092 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1098 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in heart and kidney.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9HAU0 | ATN1 P54259 | 2 | EBI-945934, EBI-945980 | |
BINARY | Q9HAU0 | ATXN1 P54253 | 2 | EBI-945934, EBI-930964 | |
BINARY | Q9HAU0 | PDZD11 Q5EBL8 | 11 | EBI-945934, EBI-1644207 | |
BINARY | Q9HAU0 | RBFOX1 Q9NWB1 | 2 | EBI-945934, EBI-945906 | |
XENO | Q9HAU0 | rep PRO_0000449629 P0DTD1 | 3 | EBI-945934, EBI-25475885 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-43 | WW 1 | ||||
Sequence: ISLPRSWTYGITRGGRVFFINEEAKSTTWLHPVT | ||||||
Domain | 56-89 | WW 2 | ||||
Sequence: TDLPTGWEEAYTFEGARYYINHNERKVTCKHPVT | ||||||
Region | 140-163 | Disordered | ||||
Sequence: SPVGRTSRASKKVHNFGKRSNSIK | ||||||
Domain | 169-268 | PH | ||||
Sequence: PVVRRGWLYKQDSTGMKLWKKRWFVLSDLCLFYYRDEKEEGILGSILLPSFQIALLTSEDHINRKYAFKAAHPNMRTYYFCTDTGKEMELWMKAMLDAAL | ||||||
Region | 459-495 | Disordered | ||||
Sequence: RTLPRNSKTRPESICSVTPSTHDKTLGPGAEEKRRSM | ||||||
Compositional bias | 464-481 | Polar residues | ||||
Sequence: NSKTRPESICSVTPSTHD | ||||||
Region | 928-978 | Disordered | ||||
Sequence: GASDQSPLQSPSNLRDNPFRTTQTRRRDDKELDTAIRENDVKPDHETPATE | ||||||
Compositional bias | 929-946 | Polar residues | ||||
Sequence: ASDQSPLQSPSNLRDNPF | ||||||
Compositional bias | 947-978 | Basic and acidic residues | ||||
Sequence: RTTQTRRRDDKELDTAIRENDVKPDHETPATE | ||||||
Region | 1025-1116 | Disordered | ||||
Sequence: RNKDKMPEDVTFSPQDETQTANHKPEEHPEENTKNSVDEQEETVISYESTPEVSRGNQTMAVKSLSPSPESSASPVPSTQPQLTEGSHFMCV | ||||||
Compositional bias | 1044-1062 | Basic and acidic residues | ||||
Sequence: TANHKPEEHPEENTKNSVD | ||||||
Compositional bias | 1063-1110 | Polar residues | ||||
Sequence: EQEETVISYESTPEVSRGNQTMAVKSLSPSPESSASPVPSTQPQLTEG |
Domain
Specifically interacts with PI3P, PI4P, PI5P, and PI(3,5)P2.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing.
Q9HAU0-1
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
- SynonymsS
- Length1,116
- Mass (Da)127,464
- Last updated2001-03-01 v1
- Checksum327F792F644B9D48
Q9HAU0-2
- Name2
- Differences from canonical
- 615-615: T → TPEELTLLLIKLRRQQAELSSIREHTLAQLMQLKLEAHSPKNEILSHHLQRNTIYLDHQ
Q9HAU0-3
- Name3
Q9HAU0-4
- Name4
- Differences from canonical
- 800-800: E → EEEEVVPPRPPLPRSYDFTEQPPIIPPLPSDSSSLLCYSRGPVHLPEEKKMYQVQGYPRNGSHC
Q9HAU0-5
- Name5
- Differences from canonical
- 785-840: Missing
Q9HAU0-6
- Name6
- SynonymsL
- NoteSpecifically expressed in brain.
Q9HAU0-7
- Name7
- Differences from canonical
- 77-1116: Missing
Q9HAU0-8
- Name8
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YGJ6 | H0YGJ6_HUMAN | PLEKHA5 | 397 | ||
H0YG48 | H0YG48_HUMAN | PLEKHA5 | 135 | ||
B4DJX4 | B4DJX4_HUMAN | PLEKHA5 | 977 | ||
F6VRM0 | F6VRM0_HUMAN | PLEKHA5 | 196 | ||
A0A9L9PX43 | A0A9L9PX43_HUMAN | PLEKHA5 | 685 | ||
A0A8V8TRE5 | A0A8V8TRE5_HUMAN | PLEKHA5 | 573 | ||
A0A8V8TQJ6 | A0A8V8TQJ6_HUMAN | PLEKHA5 | 799 | ||
A0A8V8TQJ8 | A0A8V8TQJ8_HUMAN | PLEKHA5 | 1156 | ||
A0A8V8TR40 | A0A8V8TR40_HUMAN | PLEKHA5 | 102 | ||
A0A8V8TQ09 | A0A8V8TQ09_HUMAN | PLEKHA5 | 1110 | ||
F5H1X3 | F5H1X3_HUMAN | PLEKHA5 | 118 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047514 | 1-108 | in isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_046861 | 77-1116 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_044678 | 275 | in isoform 6 | |||
Sequence: K → KRITFNF | ||||||
Sequence conflict | 311 | in Ref. 5; BAG57882 | ||||
Sequence: K → R | ||||||
Compositional bias | 464-481 | Polar residues | ||||
Sequence: NSKTRPESICSVTPSTHD | ||||||
Sequence conflict | 534 | in Ref. 5; BAG57882 | ||||
Sequence: S → T | ||||||
Alternative sequence | VSP_009775 | 615 | in isoform 2 and isoform 6 | |||
Sequence: T → TPEELTLLLIKLRRQQAELSSIREHTLAQLMQLKLEAHSPKNEILSHHLQRNTIYLDHQ | ||||||
Alternative sequence | VSP_047515 | 615 | in isoform 8 | |||
Sequence: T → TMKENEPIITMVHTMIENSALRPQLYQQ | ||||||
Alternative sequence | VSP_044679 | 616 | in isoform 6 | |||
Sequence: L → MKENEPIITMVHTMIENSALRPQLYQQFLRQKSKISLYCL | ||||||
Alternative sequence | VSP_009776 | 616-650 | in isoform 3 | |||
Sequence: LSQDEGRGTLYKYRPEEVDIDAKLSRLCEQDKVVH → WGREKVATATGAAEAVASDTHLPRTGSSSPSLLCV | ||||||
Sequence conflict | 627 | in Ref. 5; BAB14419 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_014595 | 651-1116 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 736 | in Ref. 5; BAB14419 | ||||
Sequence: M → T | ||||||
Alternative sequence | VSP_009777 | 785-840 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_009778 | 800 | in isoform 4, isoform 6 and isoform 8 | |||
Sequence: E → EEEEVVPPRPPLPRSYDFTEQPPIIPPLPSDSSSLLCYSRGPVHLPEEKKMYQVQGYPRNGSHC | ||||||
Compositional bias | 929-946 | Polar residues | ||||
Sequence: ASDQSPLQSPSNLRDNPF | ||||||
Compositional bias | 947-978 | Basic and acidic residues | ||||
Sequence: RTTQTRRRDDKELDTAIRENDVKPDHETPATE | ||||||
Sequence conflict | 970 | in Ref. 5; BAA91742 | ||||
Sequence: P → S | ||||||
Compositional bias | 1044-1062 | Basic and acidic residues | ||||
Sequence: TANHKPEEHPEENTKNSVD | ||||||
Compositional bias | 1063-1110 | Polar residues | ||||
Sequence: EQEETVISYESTPEVSRGNQTMAVKSLSPSPESSASPVPSTQPQLTEG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF302150 EMBL· GenBank· DDBJ | AAG22817.1 EMBL· GenBank· DDBJ | mRNA | ||
AB642244 EMBL· GenBank· DDBJ | BAL45489.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051473 EMBL· GenBank· DDBJ | BAB21777.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK001529 EMBL· GenBank· DDBJ | BAA91742.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK023127 EMBL· GenBank· DDBJ | BAB14419.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK294739 EMBL· GenBank· DDBJ | BAG57882.1 EMBL· GenBank· DDBJ | mRNA | ||
AL834259 EMBL· GenBank· DDBJ | CAD38934.1 EMBL· GenBank· DDBJ | mRNA | ||
AC024902 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC087314 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC091805 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092828 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471094 EMBL· GenBank· DDBJ | EAW96393.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000969 EMBL· GenBank· DDBJ | AAH00969.1 EMBL· GenBank· DDBJ | mRNA | ||
BC044245 EMBL· GenBank· DDBJ | AAH44245.1 EMBL· GenBank· DDBJ | mRNA | ||
BC070174 EMBL· GenBank· DDBJ | AAH70174.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC013133 EMBL· GenBank· DDBJ | AAH13133.3 EMBL· GenBank· DDBJ | mRNA | ||
BC127092 EMBL· GenBank· DDBJ | AAI27093.1 EMBL· GenBank· DDBJ | mRNA |