SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 5208607 FitnessBrowser__PV4:5208607 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 2 hits to proteins with known functional sites (download)

Q68CP4 Heparan-alpha-glucosaminide N-acetyltransferase; Transmembrane protein 76; EC 2.3.1.78 from Homo sapiens (Human) (see 10 papers)
26% identity, 97% coverage: 12:387/387 of query aligns to 263:663/663 of Q68CP4

query
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Q68CP4

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P265 (≠ K14) to Q: likely benign variant; does not influence stability; does not influence activity; does not influence cellular localization of the enzyme
G290 (≠ W50) to R: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
H297 (= H59) active site; mutation to A: Loss of enzymatic activity, but correctly targeted and processed.
N301 (≠ H63) to K: in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity
P311 (= P73) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
C333 (≠ W95) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
R372 (= R135) 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 (≠ T157) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
W431 (≠ L170) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
G452 (≠ V186) 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 (≠ I192) mutation to S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.
L473 (≠ K203) to P: in MPS3C; shows practically no enzyme activity
H479 (vs. gap) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
E499 (= E218) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
V509 (= V228) to L: likely benign variant; no loss of enzymatic activity
M510 (≠ N229) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
G514 (= G233) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
A517 (≠ T236) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
S546 (= S267) to F: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
K551 (≠ W272) to Q: no loss of enzymatic activity; dbSNP:rs73569592
S567 (≠ T286) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
S569 (= S288) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
D590 (= D309) to V: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
P599 (≠ G319) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
H633 (≠ E357) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
A643 (≠ M367) to T: in RP73 and MPS3C; unknown pathological 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.

Q3UDW8 Heparan-alpha-glucosaminide N-acetyltransferase; Transmembrane protein 76; EC 2.3.1.78 from Mus musculus (Mouse) (see paper)
27% identity, 84% coverage: 14:338/387 of query aligns to 252:611/656 of Q3UDW8

query
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Q3UDW8

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Sites not aligning to the query:

157 modified: carbohydrate, N-linked (GlcNAc...) asparagine

Query Sequence

>5208607 FitnessBrowser__PV4:5208607
MEPKTDTHPKPAAKPRLMSLDALRGFDMFWILGGEALFAALLVWTGWQGWRIADAQMHHS
QWHGFTFYDLIFPLFIFLSGVALGLSPKRLDSLPWPERLPLYRHAIKRLMLLLLFGVLYN
HGWGTGMPMAADEVRYASVLGRIAFAWFFAALLVWHTDLKTQILVAIGILLGYAAMQLWL
PVPGGVAGDFSISGSINAYVDGKFLPGISYQGRATDPEGILSTLPAIVNALAGVFTGRFI
VKSHPKWGGVKGEWAKVGILLLAGLLSLGLGWLMNPYIPVNKDLWTSSFVMVTLGWSLIL
LAIFYALVDVLKLHRLAFGFVVIGCNAIIIYLASSLVKWDYLASSLFGGAIQALPIEMQP
LASACAMLLVQWLLLYWMYKRGIFIKV

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