O60315 · ZEB2_HUMAN
- ProteinZinc finger E-box-binding homeobox 2
- GeneZEB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1214 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Represses transcription of E-cadherin (PubMed:16061479).
Represses expression of MEOX2 (PubMed:20516212).
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 644-703 | Homeobox; atypical | ||||
Sequence: GMTSPINPYKDHMSVLKAYYAMNMEPNSDELLKISIAVGLPQEFVKEWFEQRKVYQYSNS |
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
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger E-box-binding homeobox 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60315
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Mowat-Wilson syndrome (MOWS)
- Note
- DescriptionA complex developmental disorder characterized by intellectual disability, delayed motor development, epilepsy, microcephaly and a wide spectrum of clinically heterogeneous features suggestive of neurocristopathies at the cephalic, cardiac, and vagal levels. Affected patients show an easily recognizable facial appearance with deep set eyes and hypertelorism, medially divergent, broad eyebrows, prominent columella, pointed chin and uplifted, notched ear lobes. Some patients manifest Hirschsprung disease.
- See alsoMIM:235730
Natural variants in MOWS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_027016 | 99 | missing | in MOWS | |
VAR_027017 | 953 | R>G | in MOWS | |
VAR_027018 | 1119 | Q>R | in MOWS; dbSNP:rs137852983 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_027016 | 99 | in MOWS | |||
Sequence: Missing | ||||||
Natural variant | VAR_027017 | 953 | in MOWS | |||
Sequence: R → G | ||||||
Natural variant | VAR_035563 | 983 | in a colorectal cancer sample; somatic mutation | |||
Sequence: D → N | ||||||
Natural variant | VAR_027018 | 1119 | in MOWS; dbSNP:rs137852983 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,842 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000047236 | 1-1214 | UniProt | Zinc finger E-box-binding homeobox 2 | |||
Sequence: MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREEEEDEIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNEENFSCPLCSYTFAYRTQLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLISVNGRMRNNIKTGSSPNSVSSSPTNSAITQLRNKLENGKPLSMSEQTGLLKIKTEPLDFNDYKVLMATHGFSGTSPFMNGGLGATSPLGVHPSAQSPMQHLGVGMEAPLLGFPTMNSNLSEVQKVLQIVDNTVSRQKMDCKAEEISKLKGYHMKDPCSQPEEQGVTSPNIPPVGLPVVSHNGATKSIIDYTLEKVNEAKACLQSLTTDSRRQISNIKKEKLRTLIDLVTDDKMIENHNISTPFSCQFCKESFPGPIPLHQHERYLCKMNEEIKAVLQPHENIVPNKAGVFVDNKALLLSSVLSEKGMTSPINPYKDHMSVLKAYYAMNMEPNSDELLKISIAVGLPQEFVKEWFEQRKVYQYSNSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVSSSSENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLYTALPPQSAFPPATFMPPVQTSIPGLRPYPGLDQMSFLPHMAYTYPTGAATFADMQQRRKYQRKQGFQGELLDGAQDYMSGLDDMTDSDSCLSRKKIKKTESGMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAYLQSITPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEEFEEEEEESENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 142 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 350 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 356 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 360 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 360 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 364 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 377 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 391 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 391 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 479 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 505 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 555 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 611 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 632 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 647 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 647 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 701 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 703 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 705 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 707 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 713 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 731 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 731 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 741 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 780 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 780 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 782 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 782 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 784 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 853 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 866 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 866 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1050 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1117 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1121 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1122 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1124 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1203 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1203 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CBX4 and CTBP1
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O60315 | EHMT2 Q96KQ7 | 6 | EBI-717614, EBI-744366 | |
BINARY | O60315 | MTA1 Q13330 | 12 | EBI-717614, EBI-714236 | |
BINARY | O60315 | MTA2 O94776 | 4 | EBI-717614, EBI-1783035 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-101 | Disordered | ||||
Sequence: MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREEEEDEIREGGVEHPWHNNE | ||||||
Compositional bias | 37-52 | Basic and acidic residues | ||||
Sequence: ETDEEDKLHIAEDDGI | ||||||
Compositional bias | 57-74 | Polar residues | ||||
Sequence: DQETSPASVPNHESSPHV | ||||||
Compositional bias | 78-96 | Basic and acidic residues | ||||
Sequence: LLPREEEEDEIREGGVEHP | ||||||
Zinc finger | 211-234 | C2H2-type 1 | ||||
Sequence: LTCPYCDRGYKRLTSLKEHIKYRH | ||||||
Zinc finger | 241-263 | C2H2-type 2 | ||||
Sequence: FSCPLCSYTFAYRTQLERHMVTH | ||||||
Zinc finger | 282-304 | C2H2-type 3 | ||||
Sequence: FKCTECGKAFKYKHHLKEHLRIH | ||||||
Zinc finger | 310-334 | C2H2-type 4; atypical | ||||
Sequence: YECPNCKKRFSHSGSYSSHISSKKC | ||||||
Region | 437-487 | SMAD-MH2 binding domain | ||||
Sequence: QHLGVGMEAPLLGFPTMNSNLSEVQKVLQIVDNTVSRQKMDCKAEEISKLK | ||||||
Zinc finger | 581-605 | C2H2-type 5; atypical | ||||
Sequence: FSCQFCKESFPGPIPLHQHERYLCK | ||||||
Compositional bias | 702-726 | Polar residues | ||||
Sequence: NSRSPSLERSSKPLAPNSNPPTKDS | ||||||
Region | 702-740 | Disordered | ||||
Sequence: NSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSIT | ||||||
Region | 771-810 | Disordered | ||||
Sequence: PVEKLDHSRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEE | ||||||
Compositional bias | 778-810 | Polar residues | ||||
Sequence: SRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEE | ||||||
Region | 832-857 | Disordered | ||||
Sequence: ATKNKTKASSISLDHNSVSSSSENSD | ||||||
Compositional bias | 833-857 | Polar residues | ||||
Sequence: TKNKTKASSISLDHNSVSSSSENSD | ||||||
Zinc finger | 999-1021 | C2H2-type 6 | ||||
Sequence: YACDLCDKTFQKSSSLLRHKYEH | ||||||
Zinc finger | 1027-1049 | C2H2-type 7 | ||||
Sequence: HQCQICKKAFKHKHHLIEHSRLH | ||||||
Zinc finger | 1055-1076 | C2H2-type 8; atypical | ||||
Sequence: YQCDKCGKRFSHSGSYSQHMNH | ||||||
Region | 1117-1214 | Disordered | ||||
Sequence: TPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEEFEEEEEESENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM | ||||||
Compositional bias | 1125-1156 | Basic and acidic residues | ||||
Sequence: EERESMPRDGESEKEHEKEGEDGYGKLGRQDG | ||||||
Compositional bias | 1157-1171 | Acidic residues | ||||
Sequence: DEEFEEEEEESENKS | ||||||
Compositional bias | 1172-1214 | Basic and acidic residues | ||||
Sequence: MDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O60315-1
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
- Length1,214
- Mass (Da)136,447
- Last updated1998-08-01 v1
- ChecksumB578FD91339C3FDD
O60315-2
- Name2
- Differences from canonical
- 111-134: Missing
Computationally mapped potential isoform sequences
There are 26 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0JP08 | A0JP08_HUMAN | ZEB2 | 1213 | ||
E7EVG9 | E7EVG9_HUMAN | ZEB2 | 120 | ||
A0A6Q8PH34 | A0A6Q8PH34_HUMAN | ZEB2 | 391 | ||
A0A1X7SC99 | A0A1X7SC99_HUMAN | ZEB2 | 612 | ||
E7EUW9 | E7EUW9_HUMAN | ZEB2 | 731 | ||
E7ESP8 | E7ESP8_HUMAN | ZEB2 | 467 | ||
A0A2R8YDQ8 | A0A2R8YDQ8_HUMAN | ZEB2 | 79 | ||
C9JU62 | C9JU62_HUMAN | ZEB2 | 91 | ||
C9JUQ1 | C9JUQ1_HUMAN | ZEB2 | 63 | ||
A0A1B0GUM8 | A0A1B0GUM8_HUMAN | ZEB2 | 122 | ||
A0A1B0GV02 | A0A1B0GV02_HUMAN | ZEB2 | 1239 | ||
A0A1B0GTH3 | A0A1B0GTH3_HUMAN | ZEB2 | 21 | ||
A0A1B0GWA7 | A0A1B0GWA7_HUMAN | ZEB2 | 36 | ||
A0A1B0GVV8 | A0A1B0GVV8_HUMAN | ZEB2 | 1102 | ||
A0A1B0GW50 | A0A1B0GW50_HUMAN | ZEB2 | 1202 | ||
A0A1W2PS25 | A0A1W2PS25_HUMAN | ZEB2 | 70 | ||
A0A0D9SG93 | A0A0D9SG93_HUMAN | ZEB2 | 41 | ||
A0A0D9SGG5 | A0A0D9SGG5_HUMAN | ZEB2 | 141 | ||
A0A0D9SF71 | A0A0D9SF71_HUMAN | ZEB2 | 41 | ||
A0A0D9SF74 | A0A0D9SF74_HUMAN | ZEB2 | 39 | ||
H7C0G0 | H7C0G0_HUMAN | ZEB2 | 220 | ||
U3KPX6 | U3KPX6_HUMAN | ZEB2 | 87 | ||
U3KPV5 | U3KPV5_HUMAN | ZEB2 | 184 | ||
U3KQ33 | U3KQ33_HUMAN | ZEB2 | 58 | ||
U3KQ51 | U3KQ51_HUMAN | ZEB2 | 955 | ||
A0A8I5KV18 | A0A8I5KV18_HUMAN | ZEB2 | 35 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 37-52 | Basic and acidic residues | ||||
Sequence: ETDEEDKLHIAEDDGI | ||||||
Compositional bias | 57-74 | Polar residues | ||||
Sequence: DQETSPASVPNHESSPHV | ||||||
Compositional bias | 78-96 | Basic and acidic residues | ||||
Sequence: LLPREEEEDEIREGGVEHP | ||||||
Alternative sequence | VSP_044797 | 111-134 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 702-726 | Polar residues | ||||
Sequence: NSRSPSLERSSKPLAPNSNPPTKDS | ||||||
Compositional bias | 778-810 | Polar residues | ||||
Sequence: SRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEE | ||||||
Compositional bias | 833-857 | Polar residues | ||||
Sequence: TKNKTKASSISLDHNSVSSSSENSD | ||||||
Compositional bias | 1125-1156 | Basic and acidic residues | ||||
Sequence: EERESMPRDGESEKEHEKEGEDGYGKLGRQDG | ||||||
Sequence conflict | 1155 | in Ref. 4; BAH11928 | ||||
Sequence: D → G | ||||||
Compositional bias | 1157-1171 | Acidic residues | ||||
Sequence: DEEFEEEEEESENKS | ||||||
Compositional bias | 1172-1214 | Basic and acidic residues | ||||
Sequence: MDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY029472 EMBL· GenBank· DDBJ | AAK52081.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB056507 EMBL· GenBank· DDBJ | BAB40819.1 EMBL· GenBank· DDBJ | mRNA | ||
AB011141 EMBL· GenBank· DDBJ | BAA25495.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK294928 EMBL· GenBank· DDBJ | BAH11928.1 EMBL· GenBank· DDBJ | mRNA | ||
AC009951 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC010130 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC127102 EMBL· GenBank· DDBJ | AAI27103.1 EMBL· GenBank· DDBJ | mRNA | ||
AB015341 EMBL· GenBank· DDBJ | BAA34798.1 EMBL· GenBank· DDBJ | mRNA |