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protein HEG homolog 1 (HEG1, KIAA1237)
Structure: contains 2 EGF-like domains
Compartment:
- isoform 1: membrane
- isoform 2: secreted
General
glycoprotein
membrane protein
secreted protein
Properties
SIZE: MW = 147 kD
entity length = 1381 aa
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-29}
N-glycosylation site {N123}
N-glycosylation site {N159}
N-glycosylation site {N180}
N-glycosylation site {N314}
N-glycosylation site {N462}
serine-rich region {463-743}
MOTIF: serine residue (SEVERAL)
N-glycosylation site {N520}
N-glycosylation site {N610}
EGF domain {985-1023}
MOTIF: cysteine residue {C989}
MODIFICATION: cysteine residue {C1000}
cysteine residue {C994}
MODIFICATION: cysteine residue {C1011}
cysteine residue {C1000}
MODIFICATION: cysteine residue {C989}
cysteine residue {C1011}
MODIFICATION: cysteine residue {C994}
cysteine residue {C1013}
MODIFICATION: cysteine residue {C1022}
cysteine residue {C1022}
MODIFICATION: cysteine residue {C1013}
EGF domain {1025-1063}
MOTIF: cysteine residue {C1029}
MODIFICATION: cysteine residue {C1040}
cysteine residue {C1034}
MODIFICATION: cysteine residue {C1049}
cysteine residue {C1040}
MODIFICATION: cysteine residue {C1029}
cysteine residue {C1049}
MODIFICATION: cysteine residue {C1034}
cysteine residue {C1051}
MODIFICATION: cysteine residue {C1062}
cysteine residue {C1062}
MODIFICATION: cysteine residue {C1051}
N-glycosylation site {N1137}
transmembrane domain {1249-1269}
Database Correlations
UniProt Q9ULI3
PFAM correlations
References
UniProt :accession Q9ULI3