Q9BZ29 · DOCK9_HUMAN
- ProteinDedicator of cytokinesis protein 9
- GeneDOCK9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2069 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation.
Miscellaneous
'Zizim' means 'spike' in Hebrew.
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 | cytosol | |
Cellular Component | endomembrane system | |
Cellular Component | membrane | |
Molecular Function | cadherin binding | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Biological Process | positive regulation of GTPase activity | |
Biological Process | small GTPase-mediated signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDedicator of cytokinesis protein 9
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BZ29
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with membranes.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_062000 | 455 | in dbSNP:rs56010605 | |||
Sequence: A → T | ||||||
Natural variant | VAR_053067 | 1416 | in dbSNP:rs16955934 | |||
Sequence: K → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,659 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_0000189999 | 1-2069 | UniProt | Dedicator of cytokinesis protein 9 | |||
Sequence: MSQPPLLPASAETRKFTRALSKPGTAAELRQSVSEVVRGSVLLAKPKLIEPLDYENVIVQKKTQILNDCLREMLLFPYDDFQTAILRRQGRYICSTVPAKAEEEAQSLFVTECIKTYNSDWHLVNYKYEDYSGEFRQLPNKVVKLDKLPVHVYEVDEEVDKDEDAASLGSQKGGITKHGWLYKGNMNSAISVTMRSFKRRFFHLIQLGDGSYNLNFYKDEKISKEPKGSIFLDSCMGVVQNNKVRRFAFELKMQDKSSYLLAADSEVEMEEWITILNKILQLNFEAAMQEKRNGDSHEDDEQSKLEGSGSGLDSYLPELAKSAREAEIKLKSESRVKLFYLDPDAQKLDFSSAEPEVKSFEEKFGKRILVKCNDLSFNLQCCVAENEEGPTTNVEPFFVTLSLFDIKYNRKISADFHVDLNHFSVRQMLATTSPALMNGSGQSPSVLKGILHEAAMQYPKQGIFSVTCPHPDIFLVARIEKVLQGSITHCAEPYMKSSDSSKVAQKVLKNAKQACQRLGQYRMPFAWAARTLFKDASGNLDKNARFSAIYRQDSNKLSNDDMLKLLADFRKPEKMAKLPVILGNLDITIDNVSSDFPNYVNSSYIPTKQFETCSKTPITFEVEEFVPCIPKHTQPYTIYTNHLYVYPKYLKYDSQKSFAKARNIAICIEFKDSDEEDSQPLKCIYGRPGGPVFTRSAFAAVLHHHQNPEFYDEIKIELPTQLHEKHHLLLTFFHVSCDNSSKGSTKKRDVVETQVGYSWLPLLKDGRVVTSEQHIPVSANLPSGYLGYQELGMGRHYGPEIKWVDGGKPLLKISTHLVSTVYTQDQHLHNFFQYCQKTESGAQALGNELVKYLKSLHAMEGHVMIAFLPTILNQLFRVLTRATQEEVAVNVTRVIIHVVAQCHEEGLESHLRSYVKYAYKAEPYVASEYKTVHEELTKSMTTILKPSADFLTSNKLLKYSWFFFDVLIKSMAQHLIENSKVKLLRNQRFPASYHHAVETVVNMLMPHITQKFRDNPEASKNANHSLAVFIKRCFTFMDRGFVFKQINNYISCFAPGDPKTLFEYKFEFLRVVCNHEHYIPLNLPMPFGKGRIQRYQDLQLDYSLTDEFCRNHFLVGLLLREVGTALQEFREVRLIAISVLKNLLIKHSFDDRYASRSHQARIATLYLPLFGLLIENVQRINVRDVSPFPVNAGMTVKDESLALPAVNPLVTPQKGSTLDNSLHKDLLGAISGIASPYTTSTPNINSVRNADSRGSLISTDSGNSLPERNSEKSNSLDKHQQSSTLGNSVVRCDKLDQSEIKSLLMCFLYILKSMSDDALFTYWNKASTSELMDFFTISEVCLHQFQYMGKRYIARTGMMHARLQQLGSLDNSLTFNHSYGHSDADVLHQSLLEANIATEVCLTALDTLSLFTLAFKNQLLADHGHNPLMKKVFDVYLCFLQKHQSETALKNVFTALRSLIYKFPSTFYEGRADMCAALCYEILKCCNSKLSSIRTEASQLLYFLMRNNFDYTGKKSFVRTHLQVIISVSQLIADVVGIGGTRFQQSLSIINNCANSDRLIKHTSFSSDVKDLTKRIRTVLMATAQMKEHENDPEMLVDLQYSLAKSYASTPELRKTWLDSMARIHVKNGDLSEAAMCYVHVTALVAEYLTRKEAVQWEPPLLPHSHSACLRRSRGGVFRQGCTAFRVITPNIDEEASMMEDVGMQDVHFNEDVLMELLEQCADGLWKAERYELIADIYKLIIPIYEKRRDFERLAHLYDTLHRAYSKVTEVMHSGRRLLGTYFRVAFFGQAAQYQFTDSETDVEGFFEDEDGKEYIYKEPKLTPLSEISQRLLKLYSDKFGSENVKMIQDSGKVNPKDLDSKYAYIQVTHVIPFFDEKELQERKTEFERSHNIRRFMFEMPFTQTGKRQGGVEEQCKRRTILTAIHCFPYVKKRIPVMYQHHTDLNPIEVAIDEMSKKVAELRQLCSSAEVDMIKLQLKLQGSVSVQVNAGPLAYARAFLDDTNTKRYPDNKVKLLKEVFRQFVEACGQALAVNERLIKEDQLEYQEEMKANYREMAKELSEIMHEQLG | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 21 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 32 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 40 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 167 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 170 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 340 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 433 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 443 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 443 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 927 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 927 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1211 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1217 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1235 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1237 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1240 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1241 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1241 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1259 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1261 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1264 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1264 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1282 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1288 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, with highest expression in heart and placenta. Expressed at intermediate level in kidney, brain, lung and skeletal muscle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer (Probable). Interacts preferentially with nucleotide-depleted CDC42.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BZ29 | SMAD2 Q15796 | 3 | EBI-2695893, EBI-1040141 | |
BINARY | Q9BZ29 | SMAD3 P84022 | 3 | EBI-2695893, EBI-347161 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 174-281 | PH | ||||
Sequence: GITKHGWLYKGNMNSAISVTMRSFKRRFFHLIQLGDGSYNLNFYKDEKISKEPKGSIFLDSCMGVVQNNKVRRFAFELKMQDKSSYLLAADSEVEMEEWITILNKILQ | ||||||
Compositional bias | 290-306 | Basic and acidic residues | ||||
Sequence: EKRNGDSHEDDEQSKLE | ||||||
Region | 290-313 | Disordered | ||||
Sequence: EKRNGDSHEDDEQSKLEGSGSGLD | ||||||
Domain | 640-818 | C2 DOCK-type | ||||
Sequence: TNHLYVYPKYLKYDSQKSFAKARNIAICIEFKDSDEEDSQPLKCIYGRPGGPVFTRSAFAAVLHHHQNPEFYDEIKIELPTQLHEKHHLLLTFFHVSCDNSSKGSTKKRDVVETQVGYSWLPLLKDGRVVTSEQHIPVSANLPSGYLGYQELGMGRHYGPEIKWVDGGKPLLKISTHLV | ||||||
Region | 1241-1282 | Disordered | ||||
Sequence: TPNINSVRNADSRGSLISTDSGNSLPERNSEKSNSLDKHQQS | ||||||
Domain | 1605-2069 | DOCKER | ||||
Sequence: KSYASTPELRKTWLDSMARIHVKNGDLSEAAMCYVHVTALVAEYLTRKEAVQWEPPLLPHSHSACLRRSRGGVFRQGCTAFRVITPNIDEEASMMEDVGMQDVHFNEDVLMELLEQCADGLWKAERYELIADIYKLIIPIYEKRRDFERLAHLYDTLHRAYSKVTEVMHSGRRLLGTYFRVAFFGQAAQYQFTDSETDVEGFFEDEDGKEYIYKEPKLTPLSEISQRLLKLYSDKFGSENVKMIQDSGKVNPKDLDSKYAYIQVTHVIPFFDEKELQERKTEFERSHNIRRFMFEMPFTQTGKRQGGVEEQCKRRTILTAIHCFPYVKKRIPVMYQHHTDLNPIEVAIDEMSKKVAELRQLCSSAEVDMIKLQLKLQGSVSVQVNAGPLAYARAFLDDTNTKRYPDNKVKLLKEVFRQFVEACGQALAVNERLIKEDQLEYQEEMKANYREMAKELSEIMHEQLG | ||||||
Region | 1693-2069 | Interaction with CDC42 | ||||
Sequence: DEEASMMEDVGMQDVHFNEDVLMELLEQCADGLWKAERYELIADIYKLIIPIYEKRRDFERLAHLYDTLHRAYSKVTEVMHSGRRLLGTYFRVAFFGQAAQYQFTDSETDVEGFFEDEDGKEYIYKEPKLTPLSEISQRLLKLYSDKFGSENVKMIQDSGKVNPKDLDSKYAYIQVTHVIPFFDEKELQERKTEFERSHNIRRFMFEMPFTQTGKRQGGVEEQCKRRTILTAIHCFPYVKKRIPVMYQHHTDLNPIEVAIDEMSKKVAELRQLCSSAEVDMIKLQLKLQGSVSVQVNAGPLAYARAFLDDTNTKRYPDNKVKLLKEVFRQFVEACGQALAVNERLIKEDQLEYQEEMKANYREMAKELSEIMHEQLG | ||||||
Coiled coil | 1948-1982 | |||||
Sequence: IEVAIDEMSKKVAELRQLCSSAEVDMIKLQLKLQG | ||||||
Coiled coil | 2034-2067 | |||||
Sequence: NERLIKEDQLEYQEEMKANYREMAKELSEIMHEQ |
Domain
The DOCKER domain is necessary and sufficient for the GEF activity.
Sequence similarities
Belongs to the DOCK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q9BZ29-1
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
- Length2,069
- Mass (Da)236,446
- Last updated2002-10-19 v2
- Checksum95073CD751745AAE
Q9BZ29-5
- Name2
- Differences from canonical
- 1-43: MSQPPLLPASAETRKFTRALSKPGTAAELRQSVSEVVRGSVLL → MQADKCRTSSRSVKKELVIESPLQYKDAAQGEVEAESPGPVP
Q9BZ29-3
- Name3
- Differences from canonical
- 1355-1378: RTGMMHARLQQLGSLDNSLTFNHS → SVRKISSVLGISVDNG
Q9BZ29-4
- Name4
- NoteProduced by exon skipping that results in a frameshift.
- Differences from canonical
- 1791-1804: Missing
- 2068-2069: LG → ICPLEEKTSVLPNSLHIFNAISGTPTSTMVHGMTSSSSVV
Q9BZ29-6
- Name5
- Differences from canonical
- 1-43: MSQPPLLPASAETRKFTRALSKPGTAAELRQSVSEVVRGSVLL → MQADKCRTSSRSVKKELVIESPLQYKDAAQGEVEAESPGPVP
- 1234-1254: ASPYTTSTPNINSVRNADSRG → GNAPCSCGLLSTITLKVSWSQ
- 1255-2069: Missing
Computationally mapped potential isoform sequences
There are 15 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5JUD8 | Q5JUD8_HUMAN | DOCK9 | 424 | ||
A0A1B0GVL8 | A0A1B0GVL8_HUMAN | DOCK9 | 152 | ||
H0Y572 | H0Y572_HUMAN | DOCK9 | 116 | ||
H0Y3S1 | H0Y3S1_HUMAN | DOCK9 | 669 | ||
A0A0D9SF41 | A0A0D9SF41_HUMAN | DOCK9 | 69 | ||
A0A804HIE8 | A0A804HIE8_HUMAN | DOCK9 | 2092 | ||
A0A0D9SFH5 | A0A0D9SFH5_HUMAN | DOCK9 | 705 | ||
A0A0A0MT38 | A0A0A0MT38_HUMAN | DOCK9 | 1254 | ||
Q6ZSL5 | Q6ZSL5_HUMAN | DOCK9 | 1393 | ||
H7BZ79 | H7BZ79_HUMAN | DOCK9 | 390 | ||
X6RGR3 | X6RGR3_HUMAN | DOCK9 | 2061 | ||
A0A8V8TRI9 | A0A8V8TRI9_HUMAN | DOCK9 | 2010 | ||
A0A8V8TQS9 | A0A8V8TQS9_HUMAN | DOCK9 | 2055 | ||
A0A8V8TR95 | A0A8V8TR95_HUMAN | DOCK9 | 2078 | ||
A0A088AWN3 | A0A088AWN3_HUMAN | DOCK9 | 2081 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_017128 | 1-43 | in isoform 2 and isoform 5 | |||
Sequence: MSQPPLLPASAETRKFTRALSKPGTAAELRQSVSEVVRGSVLL → MQADKCRTSSRSVKKELVIESPLQYKDAAQGEVEAESPGPVP | ||||||
Sequence conflict | 170 | in Ref. 4; BAG54337 | ||||
Sequence: S → P | ||||||
Compositional bias | 290-306 | Basic and acidic residues | ||||
Sequence: EKRNGDSHEDDEQSKLE | ||||||
Sequence conflict | 296 | in Ref. 4; BAG54337 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_045683 | 1234-1254 | in isoform 5 | |||
Sequence: ASPYTTSTPNINSVRNADSRG → GNAPCSCGLLSTITLKVSWSQ | ||||||
Alternative sequence | VSP_045684 | 1255-2069 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_004024 | 1355-1378 | in isoform 3 | |||
Sequence: RTGMMHARLQQLGSLDNSLTFNHS → SVRKISSVLGISVDNG | ||||||
Alternative sequence | VSP_007709 | 1791-1804 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_007710 | 2068-2069 | in isoform 4 | |||
Sequence: LG → ICPLEEKTSVLPNSLHIFNAISGTPTSTMVHGMTSSSSVV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF527605 EMBL· GenBank· DDBJ | AAM90306.1 EMBL· GenBank· DDBJ | mRNA | ||
AB028981 EMBL· GenBank· DDBJ | BAA83010.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK126492 EMBL· GenBank· DDBJ | BAG54337.1 EMBL· GenBank· DDBJ | mRNA | ||
AL139084 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL161420 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL391122 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC043506 EMBL· GenBank· DDBJ | AAH43506.1 EMBL· GenBank· DDBJ | mRNA |