O00267 · SPT5H_HUMAN
- ProteinTranscription elongation factor SPT5
- GeneSUPT5H
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1087 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | DSIF complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | enzyme binding | |
Molecular Function | mRNA binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | RNA binding | |
Biological Process | negative regulation of DNA-templated transcription, elongation | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of DNA-templated transcription, elongation | |
Biological Process | positive regulation of macroautophagy | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of transcription elongation by RNA polymerase II | |
Biological Process | transcription elongation by RNA polymerase II | |
Biological Process | transcription elongation-coupled chromatin remodeling |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription elongation factor SPT5
- Short nameshSPT5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00267
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 246 | Reduces the affinity for Pol II elongation complex; when associated with A-247, A-249, A-250 and A-251. | ||||
Sequence: R → A | ||||||
Mutagenesis | 247 | Reduces the affinity for Pol II elongation complex; when associated with A-246, A-249, A-250 and A-251. | ||||
Sequence: L → A | ||||||
Mutagenesis | 249 | Reduces the affinity for Pol II elongation complex; when associated with A-246, A-247, A-250 and A-251. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 250 | Reduces the affinity for Pol II elongation complex; when associated with A-246, A-247, A-249 and A-251. | ||||
Sequence: W → A | ||||||
Mutagenesis | 251 | Reduces the affinity for Pol II elongation complex; when associated with A-246, A-247, A-249 and A-250. | ||||
Sequence: N → A | ||||||
Mutagenesis | 577 | Reduces the affinity for Pol II elongation complex; when associated with A-578, A-579 and A-582. | ||||
Sequence: R → A | ||||||
Mutagenesis | 577 | Reduces the affinity for Pol II elongation complex; when associated with E-578, E-579 and E-582. | ||||
Sequence: R → E | ||||||
Mutagenesis | 578 | Reduces the affinity for Pol II elongation complex; when associated with A-577, A-579 and A-582. | ||||
Sequence: K → A | ||||||
Mutagenesis | 578 | Reduces the affinity for Pol II elongation complex; when associated with E-577, E-579 and E-582. | ||||
Sequence: K → E | ||||||
Mutagenesis | 579 | Reduces the affinity for Pol II elongation complex; when associated with A-577, A-578 and A-582. | ||||
Sequence: K → A | ||||||
Mutagenesis | 579 | Reduces the affinity for Pol II elongation complex; when associated with E-577, E-578 and E-582. | ||||
Sequence: K → E | ||||||
Mutagenesis | 582 | Reduces the affinity for Pol II elongation complex; when associated with A-577, A-578 and A-579. | ||||
Sequence: R → A | ||||||
Mutagenesis | 582 | Reduces the affinity for Pol II elongation complex; when associated with E-577, E-578 and E-579. | ||||
Sequence: R → E | ||||||
Mutagenesis | 681 | Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698. | ||||
Sequence: R → A | ||||||
Mutagenesis | 681 | Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698. | ||||
Sequence: R → K | ||||||
Mutagenesis | 696 | Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698. | ||||
Sequence: R → A | ||||||
Mutagenesis | 696 | Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698. | ||||
Sequence: R → K | ||||||
Mutagenesis | 698 | Enhances transcriptional elongation. Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-696. | ||||
Sequence: R → A | ||||||
Mutagenesis | 698 | Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696. | ||||
Sequence: R → K | ||||||
Mutagenesis | 1002 | Defective in regulation of transcriptional elongation. | ||||
Sequence: G → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,009 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, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000208468 | 1-1087 | UniProt | Transcription elongation factor SPT5 | |||
Sequence: MSDSEDSNFSEEEDSERSSDGEEAEVDEERRSAAGSEKEEEPEDEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKILSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPQTVGVIVRLERETFQVLNMYGKVVTVRHQAVTRKKDNRFAVALDSEQNNIHVKDIVKVIDGPHSGREGEIRHLFRSFAFLHCKKLVENGGMFVCKTRHLVLAGGSKPRDVTNFTVGGFAPMSPRISSPMHPSAGGQRGGFGSPGGGSGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVGSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQVVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIVRMDLDEQLKILNLRFLGKLLEA | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 32 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 36 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 108 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 143 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 655 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 658 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 666 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 666 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 670 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 671 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 681 | UniProt | Asymmetric dimethylarginine; by PRMT1; alternate | ||||
Sequence: R | |||||||
Modified residue | 681 | UniProt | Omega-N-methylarginine; by PRMT1; alternate | ||||
Sequence: R | |||||||
Modified residue | 686 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 686 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 696 | UniProt | Asymmetric dimethylarginine; by PRMT1; alternate | ||||
Sequence: R | |||||||
Modified residue | 696 | UniProt | Omega-N-methylarginine; by PRMT1; alternate | ||||
Sequence: R | |||||||
Modified residue | 698 | UniProt | Asymmetric dimethylarginine; by PRMT1; alternate | ||||
Sequence: R | |||||||
Modified residue | 698 | UniProt | Omega-N-methylarginine; by PRMT1 and PRMT5; alternate | ||||
Sequence: R | |||||||
Modified residue | 698 | UniProt | Symmetric dimethylarginine; by PRMT5; alternate | ||||
Sequence: R | |||||||
Modified residue | 718 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 744 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 755 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 763 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 768 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 775 | UniProt | Phosphothreonine; by CDK9 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 775 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 780 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 784 | UniProt | Phosphothreonine; by CDK9 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 789 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 789 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 791 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 791 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 797 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 799 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 804 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 804 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 806 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 806 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 812 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 814 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 828 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 959 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1034 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1034 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1036 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 1037 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00267 | CDK7 P50613 | 3 | EBI-710464, EBI-1245958 | |
XENO | O00267 | PA Q5EP34 | 3 | EBI-710464, EBI-25772799 | |
BINARY | O00267 | PIN1 Q13526 | 4 | EBI-710464, EBI-714158 | |
BINARY | O00267 | POLR2A P24928 | 6 | EBI-710464, EBI-295301 | |
XENO | O00267 | POLR2A G3MZY8 | 2 | EBI-710464, EBI-6551200 | |
XENO | O00267 | POLR2B A5PJW8 | 5 | EBI-710464, EBI-15586776 | |
BINARY | O00267 | PPIA P62937 | 2 | EBI-710464, EBI-437708 | |
BINARY | O00267 | SUPT4H1 P63272 | 16 | EBI-710464, EBI-727250 | |
BINARY | O00267 | TERF1 P54274 | 2 | EBI-710464, EBI-710997 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Acidic residues | ||||
Sequence: MSDSEDSNFSEEEDSERSSDGEE | ||||||
Region | 1-92 | Disordered | ||||
Sequence: MSDSEDSNFSEEEDSERSSDGEEAEVDEERRSAAGSEKEEEPEDEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQW | ||||||
Compositional bias | 24-38 | Basic and acidic residues | ||||
Sequence: AEVDEERRSAAGSEK | ||||||
Compositional bias | 39-63 | Acidic residues | ||||
Sequence: EEEPEDEEEEEEEEEYDEEEEEEDD | ||||||
Compositional bias | 64-79 | Basic and acidic residues | ||||
Sequence: DRPPKKPRHGGFILDE | ||||||
Region | 176-270 | Interaction with SUPT4H1 | ||||
Sequence: DPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEV | ||||||
Domain | 273-306 | KOW 1 | ||||
Sequence: LKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLK | ||||||
Region | 313-420 | Interaction with RNA polymerase II | ||||
Sequence: YDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNF | ||||||
Motif | 328-334 | UBR5-degron | ||||
Sequence: KRKKFKR | ||||||
Domain | 420-451 | KOW 2 | ||||
Sequence: FQPGDNVEVCEGELINLQGKILSVDGNKITIM | ||||||
Domain | 472-503 | KOW 3 | ||||
Sequence: FKMGDHVKVIAGRFEGDTGLIVRVEENFVILF | ||||||
Domain | 594-627 | KOW 4 | ||||
Sequence: IHVKDIVKVIDGPHSGREGEIRHLFRSFAFLHCK | ||||||
Region | 670-700 | Disordered | ||||
Sequence: SSPMHPSAGGQRGGFGSPGGGSGGMSRGRGR | ||||||
Domain | 704-737 | KOW 5 | ||||
Sequence: ELIGQTVRISQGPYKGYIGVVKDATESTARVELH | ||||||
Compositional bias | 747-831 | Polar residues | ||||
Sequence: RQRLTTVGSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSR | ||||||
Region | 747-978 | Disordered | ||||
Sequence: RQRLTTVGSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSD | ||||||
Repeat | 754-759 | CTR1-1; approximate | ||||
Sequence: GSRRPG | ||||||
Region | 754-817 | 9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1 | ||||
Sequence: GSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQ | ||||||
Repeat | 760-765 | CTR1-2 | ||||
Sequence: GMTSTY | ||||||
Repeat | 766-771 | CTR1-3 | ||||
Sequence: GRTPMY | ||||||
Repeat | 772-778 | CTR1-4 | ||||
Sequence: GSQTPMY | ||||||
Repeat | 781-787 | CTR1-5 | ||||
Sequence: GSRTPMY | ||||||
Repeat | 788-794 | CTR1-6 | ||||
Sequence: GSQTPLQ | ||||||
Repeat | 796-802 | CTR1-7 | ||||
Sequence: GSRTPHY | ||||||
Repeat | 803-809 | CTR1-8 | ||||
Sequence: GSQTPLH | ||||||
Repeat | 811-817 | CTR1-9 | ||||
Sequence: GSRTPAQ | ||||||
Repeat | 844-851 | CTR2-1 | ||||
Sequence: PTPSPQAY | ||||||
Region | 844-950 | 10 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2 | ||||
Sequence: PTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGY | ||||||
Compositional bias | 850-872 | Pro residues | ||||
Sequence: AYGGTPNPQTPGYPDPSSPQVNP | ||||||
Repeat | 854-862 | CTR2-2; approximate | ||||
Sequence: TPNPQTPGY | ||||||
Repeat | 863-869 | CTR2-3; approximate | ||||
Sequence: PDPSSPQ | ||||||
Compositional bias | 873-947 | Polar residues | ||||
Sequence: QYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSP | ||||||
Repeat | 881-885 | CTR2-4; half-length | ||||
Sequence: TPAMY | ||||||
Repeat | 896-902 | CTR2-5; approximate | ||||
Sequence: PSPQGSY | ||||||
Repeat | 904-911 | CTR2-6 | ||||
Sequence: PSPSPQSY | ||||||
Repeat | 916-921 | CTR2-7; approximate | ||||
Sequence: PSPAGY | ||||||
Repeat | 924-930 | CTR2-8 | ||||
Sequence: THSPASY | ||||||
Repeat | 932-939 | CTR2-9 | ||||
Sequence: PTPSPMAY | ||||||
Repeat | 943-950 | CTR2-10 | ||||
Sequence: PSPSPVGY | ||||||
Compositional bias | 948-962 | Pro residues | ||||
Sequence: VGYSPMTPGAPSPGG |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O00267-1
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
- Length1,087
- Mass (Da)121,000
- Last updated1997-07-01 v1
- ChecksumEC3F402A670A5B7D
O00267-2
- Name2
- Differences from canonical
- 103-106: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Acidic residues | ||||
Sequence: MSDSEDSNFSEEEDSERSSDGEE | ||||||
Compositional bias | 24-38 | Basic and acidic residues | ||||
Sequence: AEVDEERRSAAGSEK | ||||||
Compositional bias | 39-63 | Acidic residues | ||||
Sequence: EEEPEDEEEEEEEEEYDEEEEEEDD | ||||||
Compositional bias | 64-79 | Basic and acidic residues | ||||
Sequence: DRPPKKPRHGGFILDE | ||||||
Alternative sequence | VSP_016282 | 103-106 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 181 | in Ref. 1; AAC51102 | ||||
Sequence: T → I | ||||||
Sequence conflict | 483 | in Ref. 1; AAC51102 | ||||
Sequence: G → A | ||||||
Compositional bias | 747-831 | Polar residues | ||||
Sequence: RQRLTTVGSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSR | ||||||
Sequence conflict | 820 | in Ref. 1; AAC51102 | ||||
Sequence: A → G | ||||||
Sequence conflict | 846 | in Ref. 3; BAA24075 | ||||
Sequence: P → R | ||||||
Compositional bias | 850-872 | Pro residues | ||||
Sequence: AYGGTPNPQTPGYPDPSSPQVNP | ||||||
Compositional bias | 873-947 | Polar residues | ||||
Sequence: QYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSP | ||||||
Compositional bias | 948-962 | Pro residues | ||||
Sequence: VGYSPMTPGAPSPGG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U56402 EMBL· GenBank· DDBJ | AAC51102.1 EMBL· GenBank· DDBJ | mRNA | ||
Y12790 EMBL· GenBank· DDBJ | CAA73326.1 EMBL· GenBank· DDBJ | mRNA | ||
AB000516 EMBL· GenBank· DDBJ | BAA24075.1 EMBL· GenBank· DDBJ | mRNA | ||
AF040253 EMBL· GenBank· DDBJ | AAD02179.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209257 EMBL· GenBank· DDBJ | BAD92494.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC024203 EMBL· GenBank· DDBJ | AAH24203.1 EMBL· GenBank· DDBJ | mRNA |