O94885 · SASH1_HUMAN
- ProteinSAM and SH3 domain-containing protein 1
- GeneSASH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1247 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Is a positive regulator of NF-kappa-B signaling downstream of TLR4 activation. It acts as a scaffold molecule to assemble a molecular complex that includes TRAF6, MAP3K7, CHUK and IKBKB, thereby facilitating NF-kappa-B signaling activation (PubMed:23776175).
Regulates TRAF6 and MAP3K7 ubiquitination (PubMed:23776175).
Involved in the regulation of cell mobility (PubMed:23333244, PubMed:23776175, PubMed:25315659).
Regulates lipolysaccharide (LPS)-induced endothelial cell migration (PubMed:23776175).
Is involved in the regulation of skin pigmentation through the control of melanocyte migration in the epidermis (PubMed:23333244).
Regulates TRAF6 and MAP3K7 ubiquitination (PubMed:23776175).
Involved in the regulation of cell mobility (PubMed:23333244, PubMed:23776175, PubMed:25315659).
Regulates lipolysaccharide (LPS)-induced endothelial cell migration (PubMed:23776175).
Is involved in the regulation of skin pigmentation through the control of melanocyte migration in the epidermis (PubMed:23333244).
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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | protein-containing complex | |
Molecular Function | G-protein alpha-subunit binding | |
Molecular Function | mitogen-activated protein kinase kinase kinase binding | |
Molecular Function | molecular adaptor activity | |
Molecular Function | protein kinase binding | |
Biological Process | positive regulation of angiogenesis | |
Biological Process | positive regulation of endothelial cell migration | |
Biological Process | positive regulation of JUN kinase activity | |
Biological Process | positive regulation of lipopolysaccharide-mediated signaling pathway | |
Biological Process | positive regulation of non-canonical NF-kappaB signal transduction | |
Biological Process | positive regulation of p38MAPK cascade | |
Biological Process | protein polyubiquitination | |
Biological Process | regulation of epithelial cell migration | |
Biological Process | regulation of protein autoubiquitination | |
Biological Process | regulation of protein K63-linked ubiquitination |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSAM and SH3 domain-containing protein 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 accessionO94885
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Dyschromatosis universalis hereditaria 1 (DUH1)
- Note
- DescriptionA form of dyschromatosis universalis, an autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed randomly over the body, that appear in infancy or early childhood. The trunk and extremities are the dominant sites of abnormal pigmentation. Facial lesions can be seen in 50% of affected individuals, but involvement of palms and soles is unusual. Abnormalities of hair and nails have also been reported. Dyschromatosis universalis hereditaria may be associated with abnormalities of dermal connective tissue, nerve tissue, or other systemic complications.
- See alsoMIM:127500
Natural variants in DUH1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_082102 | 507 | S>A | in DUH1; dbSNP:rs1562489143 | |
VAR_082103 | 509 | E>K | in DUH1; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability; dbSNP:rs1562489156 | |
VAR_082104 | 513 | S>R | in DUH1; uncertain significance; dbSNP:rs1237876014 | |
VAR_082105 | 515 | L>P | in DUH1; affects the regulation of cell mobility resulting in increased melanocyte migration; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability; dbSNP:rs1562489224 | |
VAR_082106 | 519 | S>N | in DUH1; dbSNP:rs1562489240 | |
VAR_082107 | 551 | Y>D | in DUH1; affects the regulation of cell mobility resulting in increased melanocyte migration; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability; dbSNP:rs1562490566 | |
VAR_082108 | 551 | Y>H | in DUH1; dbSNP:rs1562490566 | |
VAR_082109 | 595 | M>T | in DUH1; uncertain significance; dbSNP:rs1562491501 |
Cancer, alopecia, pigment dyscrasia, onychodystrophy, and keratoderma (CAPOK)
- Note
- DescriptionAn autosomal recessive genodermatosis characterized by hypo- and hyperpigmented macular skin lesions, progressive alopecia, palmoplantar keratoderma, dystrophic nails, teeth abnormalities and a predisposition to squamous cell carcinoma.
- See alsoMIM:618373
Natural variants in CAPOK
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_082110 | 617 | E>K | in CAPOK; affects the regulation of cell mobility; patient fibroblasts migrate better than control fibroblasts; dbSNP:rs587781245 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031714 | 298 | in dbSNP:rs35078400 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_082102 | 507 | in DUH1; dbSNP:rs1562489143 | |||
Sequence: S → A | ||||||
Natural variant | VAR_082103 | 509 | in DUH1; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability; dbSNP:rs1562489156 | |||
Sequence: E → K | ||||||
Natural variant | VAR_082104 | 513 | in DUH1; uncertain significance; dbSNP:rs1237876014 | |||
Sequence: S → R | ||||||
Natural variant | VAR_082105 | 515 | in DUH1; affects the regulation of cell mobility resulting in increased melanocyte migration; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability; dbSNP:rs1562489224 | |||
Sequence: L → P | ||||||
Natural variant | VAR_082106 | 519 | in DUH1; dbSNP:rs1562489240 | |||
Sequence: S → N | ||||||
Natural variant | VAR_082107 | 551 | in DUH1; affects the regulation of cell mobility resulting in increased melanocyte migration; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability; dbSNP:rs1562490566 | |||
Sequence: Y → D | ||||||
Natural variant | VAR_082108 | 551 | in DUH1; dbSNP:rs1562490566 | |||
Sequence: Y → H | ||||||
Natural variant | VAR_082109 | 595 | in DUH1; uncertain significance; dbSNP:rs1562491501 | |||
Sequence: M → T | ||||||
Natural variant | VAR_082110 | 617 | in CAPOK; affects the regulation of cell mobility; patient fibroblasts migrate better than control fibroblasts; dbSNP:rs587781245 | |||
Sequence: E → K | ||||||
Mutagenesis | 852-860 | Abolishes interaction with TRAF6. | ||||
Sequence: Missing | ||||||
Natural variant | VAR_031715 | 884 | in dbSNP:rs208696 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,453 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000097597 | 1-1247 | UniProt | SAM and SH3 domain-containing protein 1 | |||
Sequence: MEDAGAAGPGPEPEPEPEPEPEPAPEPEPEPKPGAGTSEAFSRLWTDVMGILDGSLGNIDDLAQQYADYYNTCFSDVCERMEELRKRRVSQDLEVEKPDASPTSLQLRSQIEESLGFCSAVSTPEVERKNPLHKSNSEDSSVGKGDWKKKNKYFWQNFRKNQKGIMRQTSKGEDVGYVASEITMSDEERIQLMMMVKEKMITIEEALARLKEYEAQHRQSAALDPADWPDGSYPTFDGSSNCNSREQSDDETEESVKFKRLHKLVNSTRRVRKKLIRVEEMKKPSTEGGEEHVFENSPVLDERSALYSGVHKKPLFFDGSPEKPPEDDSDSLTTSPSSSSLDTWGAGRKLVKTFSKGESRGLIKPPKKMGTFFSYPEEEKAQKVSRSLTEGEMKKGLGSLSHGRTCSFGGFDLTNRSLHVGSNNSDPMGKEGDFVYKEVIKSPTASRISLGKKVKSVKETMRKRMSKKYSSSVSEQDSGLDGMPGSPPPSQPDPEHLDKPKLKAGGSVESLRSSLSGQSSMSGQTVSTTDSSTSNRESVKSEDGDDEEPPYRGPFCGRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVLSEDEEKPKRPTRRRRKGRPPQPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYDSNSDQSGSQEKLLVDSQGLSGCSPRDSGCYESSENLENGKTRKASLLSAKSSTEPSLKSFSRNQLGNYPTLPLMKSGDALKQGQEEGRLGGGLAPDTSKSCDPPGVTGLNKNRRSLPVSICRSCETLEGPQTVDTWPRSHSLDDLQVEPGAEQDVPTEVTEPPPQIVPEVPQKTTASSTKAQPLEQDSAVDNALLLTQSKRFSEPQKLTTKKLEGSIAASGRGLSPPQCLPRNYDAQPPGAKHGLARTPLEGHRKGHEFEGTHHPLGTKEGVDAEQRMQPKIPSQPPPVPAKKSRERLANGLHPVPMGPSGALPSPDAPCLPVKRGSPASPTSPSDCPPALAPRPLSGQAPGSPPSTRPPPWLSELPENTSLQEHGVKLGPALTRKVSCARGVDLETLTENKLHAEGIDLTEEPYSDKHGRCGIPEALVQRYAEDLDQPERDVAANMDQIRVKQLRKQHRMAIPSGGLTEICRKPVSPGCISSVSDWLISIGLPMYAGTLSTAGFSTLSQVPSLSHTCLQEAGITEERHIRKLLSAARLFKLPPGPEAM | |||||||
Modified residue | 90 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 137 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 244 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 248 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 248 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 297 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 320 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 405 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 407 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 442 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 510 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 541 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 570 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 614 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 706 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 718 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 721 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 730 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 743 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 813 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 817 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 821 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 821 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 837 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 839 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 839 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 858 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 923 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1013 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1025 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1028 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1030 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1031 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1045 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1051 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed ubiquitously, with highest levels in lung, placenta, spleen and thymus. Down-regulated in the majority (74%) of breast tumors in comparison with corresponding normal breast epithelial tissues. Expressed in the epidermis, epidermal keratinocytes, dermal fibroblasts and melanocytes (PubMed:23333244, PubMed:26203640).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with GNAS (PubMed:23333244).
Interacts with IQGAP1 (PubMed:23333244).
Interacts with TRAF6 (via C-terminus); the interaction is LPS-dependent (PubMed:23776175).
Interacts with MAP3K7, CHUK and IKBKB (PubMed:23776175).
Interacts with IQGAP1 (PubMed:23333244).
Interacts with TRAF6 (via C-terminus); the interaction is LPS-dependent (PubMed:23776175).
Interacts with MAP3K7, CHUK and IKBKB (PubMed:23776175).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O94885 | SFN P31947 | 4 | EBI-1761310, EBI-476295 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-39 | Disordered | ||||
Sequence: MEDAGAAGPGPEPEPEPEPEPEPAPEPEPEPKPGAGTSE | ||||||
Region | 126-145 | Disordered | ||||
Sequence: VERKNPLHKSNSEDSSVGKG | ||||||
Compositional bias | 127-145 | Basic and acidic residues | ||||
Sequence: ERKNPLHKSNSEDSSVGKG | ||||||
Region | 221-257 | Disordered | ||||
Sequence: AALDPADWPDGSYPTFDGSSNCNSREQSDDETEESVK | ||||||
Region | 316-344 | Disordered | ||||
Sequence: FFDGSPEKPPEDDSDSLTTSPSSSSLDTW | ||||||
Compositional bias | 330-344 | Polar residues | ||||
Sequence: DSLTTSPSSSSLDTW | ||||||
Region | 449-573 | Disordered | ||||
Sequence: SLGKKVKSVKETMRKRMSKKYSSSVSEQDSGLDGMPGSPPPSQPDPEHLDKPKLKAGGSVESLRSSLSGQSSMSGQTVSTTDSSTSNRESVKSEDGDDEEPPYRGPFCGRARVHTDFTPSPYDTD | ||||||
Compositional bias | 509-535 | Polar residues | ||||
Sequence: ESLRSSLSGQSSMSGQTVSTTDSSTSN | ||||||
Compositional bias | 536-553 | Basic and acidic residues | ||||
Sequence: RESVKSEDGDDEEPPYRG | ||||||
Domain | 554-615 | SH3 | ||||
Sequence: PFCGRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVLSE | ||||||
Region | 616-639 | Disordered | ||||
Sequence: DEEKPKRPTRRRRKGRPPQPKSVE | ||||||
Domain | 633-697 | SAM 1 | ||||
Sequence: PQPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEY | ||||||
Compositional bias | 713-768 | Polar residues | ||||
Sequence: DSQGLSGCSPRDSGCYESSENLENGKTRKASLLSAKSSTEPSLKSFSRNQLGNYPT | ||||||
Region | 713-810 | Disordered | ||||
Sequence: DSQGLSGCSPRDSGCYESSENLENGKTRKASLLSAKSSTEPSLKSFSRNQLGNYPTLPLMKSGDALKQGQEEGRLGGGLAPDTSKSCDPPGVTGLNKN | ||||||
Region | 846-884 | Disordered | ||||
Sequence: EPGAEQDVPTEVTEPPPQIVPEVPQKTTASSTKAQPLEQ | ||||||
Region | 852-860 | Required for interaction with TRAF6 | ||||
Sequence: DVPTEVTEP | ||||||
Compositional bias | 868-884 | Polar residues | ||||
Sequence: VPQKTTASSTKAQPLEQ | ||||||
Region | 903-946 | Disordered | ||||
Sequence: PQKLTTKKLEGSIAASGRGLSPPQCLPRNYDAQPPGAKHGLART | ||||||
Region | 971-1065 | Disordered | ||||
Sequence: DAEQRMQPKIPSQPPPVPAKKSRERLANGLHPVPMGPSGALPSPDAPCLPVKRGSPASPTSPSDCPPALAPRPLSGQAPGSPPSTRPPPWLSELP | ||||||
Compositional bias | 1030-1060 | Pro residues | ||||
Sequence: TSPSDCPPALAPRPLSGQAPGSPPSTRPPPW | ||||||
Domain | 1177-1241 | SAM 2 | ||||
Sequence: GCISSVSDWLISIGLPMYAGTLSTAGFSTLSQVPSLSHTCLQEAGITEERHIRKLLSAARLFKLP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,247
- Mass (Da)136,653
- Last updated2007-04-17 v3
- Checksum48A806B3AE32E563
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1B0GWB9 | A0A1B0GWB9_HUMAN | SASH1 | 359 | ||
A0A1B0GVF9 | A0A1B0GVF9_HUMAN | SASH1 | 41 | ||
A0A1B0GVI0 | A0A1B0GVI0_HUMAN | SASH1 | 161 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 127-145 | Basic and acidic residues | ||||
Sequence: ERKNPLHKSNSEDSSVGKG | ||||||
Compositional bias | 330-344 | Polar residues | ||||
Sequence: DSLTTSPSSSSLDTW | ||||||
Compositional bias | 509-535 | Polar residues | ||||
Sequence: ESLRSSLSGQSSMSGQTVSTTDSSTSN | ||||||
Compositional bias | 536-553 | Basic and acidic residues | ||||
Sequence: RESVKSEDGDDEEPPYRG | ||||||
Compositional bias | 713-768 | Polar residues | ||||
Sequence: DSQGLSGCSPRDSGCYESSENLENGKTRKASLLSAKSSTEPSLKSFSRNQLGNYPT | ||||||
Sequence conflict | 751 | in Ref. 6; BAB14909 | ||||
Sequence: T → A | ||||||
Compositional bias | 868-884 | Polar residues | ||||
Sequence: VPQKTTASSTKAQPLEQ | ||||||
Compositional bias | 1030-1060 | Pro residues | ||||
Sequence: TSPSDCPPALAPRPLSGQAPGSPPSTRPPPW | ||||||
Sequence conflict | 1157 | in Ref. 6; BAB14909 | ||||
Sequence: H → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ507735 EMBL· GenBank· DDBJ | CAD47811.1 EMBL· GenBank· DDBJ | mRNA | ||
BN000088 EMBL· GenBank· DDBJ | CAD92036.1 EMBL· GenBank· DDBJ | mRNA | ||
AY351979 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351960 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351961 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351962 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351963 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351964 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351965 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351966 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351967 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351968 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351969 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351970 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351971 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351972 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351973 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351974 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351975 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351976 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351977 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY351978 EMBL· GenBank· DDBJ | AAQ55463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB018333 EMBL· GenBank· DDBJ | BAA34510.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL513164 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL033378 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK024403 EMBL· GenBank· DDBJ | BAB14909.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CH471051 EMBL· GenBank· DDBJ | EAW47815.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC028303 EMBL· GenBank· DDBJ | AAH28303.1 EMBL· GenBank· DDBJ | mRNA |