SitesBLAST
Comparing 6936760 FitnessBrowser__SB2B:6936760 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 3 hits to proteins with known functional sites (download)
Q3UDW8 Heparan-alpha-glucosaminide N-acetyltransferase; Transmembrane protein 76; EC 2.3.1.78 from Mus musculus (Mouse) (see paper)
27% identity, 100% coverage: 2:378/378 of query aligns to 250:656/656 of Q3UDW8
Sites not aligning to the query:
- 157 modified: carbohydrate, N-linked (GlcNAc...) asparagine
8tu9A Cryo-em structure of hgsnat-acetyl-coa complex at ph 7.5
26% identity, 97% coverage: 11:378/378 of query aligns to 136:533/533 of 8tu9A
Q68CP4 Heparan-alpha-glucosaminide N-acetyltransferase; Transmembrane protein 76; EC 2.3.1.78 from Homo sapiens (Human) (see 10 papers)
26% identity, 98% coverage: 7:378/378 of query aligns to 262:663/663 of Q68CP4
- P265 (≠ K10) to Q: in MPS3C; likely benign; does not influence stability; does not influence activity; does not influence cellular localization of the enzyme
- G290 (≠ W43) to R: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- H297 (= H55) active site; mutation to A: Loss of enzymatic activity, but correctly targeted and processed.
- N301 (≠ H59) to K: in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity
- P311 (= P69) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- C333 (≠ P91) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
- R372 (= R131) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; to H: in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity
- C402 (≠ I159) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
- W431 (vs. gap) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- G452 (vs. gap) to S: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; to V: in MPS3C; shows practically no enzyme activity
- C462 (vs. gap) mutation to S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.
- L473 (≠ H199) to P: in MPS3C; shows practically no enzyme activity
- H479 (≠ I204) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
- E499 (= E214) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- V509 (= V224) to L: in MPS3C; likely benign; no loss of enzymatic activity
- M510 (≠ N225) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- G514 (= G229) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- A517 (≠ V232) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- S546 (≠ G256) to F: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- K551 (≠ L261) to Q: in MPS3C; likely benign; no loss of enzymatic activity; dbSNP:rs73569592
- S567 (≠ T277) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- S569 (= S279) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
- D590 (= D300) to V: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
- P599 (= P310) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
- H633 (= H343) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
- A643 (= A353) to T: in RP73 and MPS3C; uncertain significance; may act as a modifier of disease severity in patients with retinitis pigmentosa; has a negligible effect on the enzyme expression; moderately reduced enzyme activity; dbSNP:rs112029032
Sites not aligning to the query:
- 82 A → V: in MPS3C; shows practically no enzyme activity
- 104 C → F: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; loss of intralysosomal proteolytic cleavage
- 107 C→S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.
- 141 L → P: in MPS3C; shows practically no enzyme activity
- 142 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 151 C→S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.
- 165 L → P: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- 179 C→S: Loss of intralysosomal proteolytic cleavage and enzymatic activity.
- 236 L→A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209.
- 237 I→A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208.
Query Sequence
>6936760 FitnessBrowser__SB2B:6936760
MQATQTKAAKPRLMSLDALRGFDMFWILGGEKLFIALFALTGWSFWQLADAEMHHSEWHG
FTFYDLIFPLFIFLSGVALGLSPKRLDKLAPAERNPIYRHAVKRLFLLLALGVLYNHGWG
TGIPAHSDEVRYASVLGRIAFAWFFAALLVWHTSLRTQIATALAILFGYAAIQLWLPVPG
GQAGVLTPSGSINAWVDTHFLPGITYQHRPYDPEGILSTLPAIVNALMGVFVGRFIVKPD
ARGDWAKAGILTGAGGLSLVLGWSLDSVLPVNKDLWTSSFVLVTTGWNLLFLALFYVLVD
VLGAKRLAFPFVVIGVNSIIIYLASSLMNWEYLSKSLFGGVIHALPMPAQALAAAIGFLL
VQWALLYWMYRKGIFIRI
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory