SRP9

Signal recognition particle 9 kDa protein

103 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity).

Belongs to the SRP9 family.

12.023 kDa

MVYIASWDEFVDRSVQLFRADPESTRYVMKYRHCDGKLVLKVTDNKECLKFKTDQAQEAKKMEKLNNIFFTLMARGPDVDLSEVTGKEQMETQPAKKGRGRKQ

SRP9

Signal recognition particle 9 kDa protein

103 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity).

Belongs to the SRP9 family.

12.077 kDa

MVYVDSWEEFVERSVQLFRGDPNATRYVMKYRHCEGKLVLKVTDDRECLKFKTDQAQDAKKMEKLNNIFFALMTRGPDVDISEVSGKEQAEQQQAKKGRGRRQ

SRP9

Signal recognition particle 9 kDa protein

86 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.

Belongs to the SRP9 family.

10.046 kDa

MAQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGSLCIKVTDDLVCLVYRTDQAQDVKKIEKFHSQLMRLMVAKESRSVAMETD

SRP9

Signal recognition particle 9 kDa protein

86 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.

Belongs to the SRP9 family.

10.112 kDa

MPQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGNLCVKVTDDLVCLVYKTDQAQDVKKIEKFHSQLMRLMVAKEARNVTMETE

SRP9

Signal recognition particle 9 kDa protein

86 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity).

Belongs to the SRP9 family.

10.142 kDa

MPQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGNLCVKVTDDLVCLVYKTEQAQDVKKIEKFHSQLMRLMVAKESRNVTMETE

Srp9

Signal recognition particle 9 kDa protein

86 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.

Belongs to the SRP9 family.

10.194 kDa

MPQFQTWEEFSRAAEKLYLADPMKVRVVLKYRHVDGNLCIKVTDDLVCLVYRTDQAQDVKKIEKFHSQLMRLMVAKESRNVTMETE

Srp9

Signal recognition particle 9 kDa protein

77 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Srp9 together with Srp14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of Srp9 and Srp14 is required for SRP RNA binding (By similarity).

Belongs to the SRP9 family.

8.974 kDa

MVFVKNWDDFEIAVENMYLANPQNCRLTMKYAHSKGHILLKMTDNVKCVQYKAENMPDLRKIEKITSNLVGHMASKE

srp9

Signal recognition particle 9 kDa protein

75 amino acids

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity).

Belongs to the SRP9 family.

9.29 kDa

MYIEDWDEFYDKSEQLYRTDPKRTRFSFKFRHVEGKVVLKVTNDTVNLKFQTDKENDFKRIDQINSLFFRLTTEQ