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Protein Page:
RPS7 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RPS7 Required for rRNA maturation. Defects in RPS7 are the cause of Diamond-Blackfan anemia type 8 (DBA8). DBA8 is a form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Belongs to the ribosomal protein S7e family. Note: This description may include information from UniProtKB.
Protein type: Translation; Ribosomal
Cellular Component: cytoplasm; cytoskeleton; focal adhesion; intracellular; membrane; nucleolus; nucleus; ribonucleoprotein complex; ribosome; small subunit processome
Molecular Function: poly(U) binding; structural constituent of ribosome
Biological Process: cell differentiation; neural tube closure; ribosomal small subunit biogenesis and assembly; rRNA processing; translation
Reference #:  P62082 (UniProtKB)
Gene Symbols: Rps7
Molecular weight: 22,127 Da
Basal Isoelectric point: 10.09  Predict pI for various phosphorylation states
Select Structure to View Below

RPS7

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 1 S3‑p _____MFsSSAKIVk
0 38 K10‑ub sSSAKIVkPNGEkPD
0 4 K15‑ac IVkPNGEkPDEFESG
0 39 K15‑ub IVkPNGEkPDEFESG
0 1 S24 DEFESGISQALLELE
0 3 K37 LEMNSDLKAQLRELN
0 35 K37‑ub LEMNSDLkAQLRELN
0 18 K49‑ub ELNITAAkEIEVGGG
0 1 K58 IEVGGGRKAIIIFVP
0 1 K70 FVPVPQLKSFQkIQV
0 11 K70 FVPVPQLKSFQkIQV
0 4 K74‑ac PQLKSFQkIQVRLVR
0 51 K74‑ub PQLKSFQkIQVRLVR
0 1 K74‑sc PQLKSFQkIQVRLVR
0 1 K85 RLVRELEKKFSGKHV
0 1 K85 RLVRELEKKFSGKHV
0 1 K86 LVRELEKKFSGKHVV
0 1 S88 RELEKKFSGKHVVFI
0 1 K90 LEKKFSGKHVVFIAQ
0 4 K90 LEKKFSGKHVVFIAQ
0 13 S119 NKQKRPRSRtLtAVH
0 18 T121‑p QKRPRSRtLtAVHDA
0 9 T123‑p RPRSRtLtAVHDAIL
0 1 S137 LEDLVFPSEIVGkRI
0 8 K142 FPSEIVGKRIRVKLD
0 29 K142‑ub FPSEIVGkRIRVKLD
0 3 K155 LDGSRLIKVHLDkAQ
0 5 K155‑ub LDGSRLIkVHLDkAQ
0 5 K160‑ub LIkVHLDkAQQNNVE
0 3 K169‑ac QQNNVEHkVETFSGV
0 1 K169 QQNNVEHKVETFSGV
0 1 S174 EHkVETFSGVYkKLT
0 1 Y177 VETFSGVYkKLTGkD
0 4 K178‑ac ETFSGVYkKLTGkDV
0 6 K178‑ub ETFSGVYkKLTGkDV
0 1 K178‑sc ETFSGVYkKLTGkDV
0 2 K179 TFSGVYkKLTGkDVN
0 2 K183‑ac VYkKLTGkDVNFEFP
0 18 K183‑ub VYkKLTGkDVNFEFP
  human

 
S3‑p _____MFsSSAKIVk
K10‑ub sSSAKIVkPNGEkPD
K15 IVkPNGEKPDEFESG
K15‑ub IVkPNGEkPDEFESG
S24‑p DEFESGIsQALLELE
K37‑ac LEMNSDLkAQLRELN
K37‑ub LEMNSDLkAQLRELN
K49‑ub ELNITAAkEIEVGGG
K58‑ub IEVGGGRkAIIIFVP
K70‑ac FVPVPQLkSFQkIQV
K70‑ub FVPVPQLkSFQkIQV
K74‑ac PQLkSFQkIQVRLVR
K74‑ub PQLkSFQkIQVRLVR
K74‑sc PQLkSFQkIQVRLVR
K85 RLVRELEKkFsGkHV
K85‑ub RLVRELEkkFsGkHV
K86‑ub LVRELEkkFsGkHVV
S88‑p RELEkkFsGkHVVFI
K90 LEkkFsGKHVVFIAQ
K90‑ub LEkkFsGkHVVFIAQ
S119‑p NKQKRPRsRtLtAVH
T121‑p QKRPRsRtLtAVHDA
T123‑p RPRsRtLtAVHDAIL
S137‑p LEDLVFPsEIVGkRI
K142‑ac FPsEIVGkRIRVKLD
K142‑ub FPsEIVGkRIRVKLD
K155‑ac LDGSRLIkVHLDkAQ
K155‑ub LDGSRLIkVHLDkAQ
K160‑ub LIkVHLDkAQQNNVE
K169‑ac QQNNVEHkVETFsGV
K169‑ub QQNNVEHkVETFsGV
S174‑p EHkVETFsGVykkLT
Y177‑p VETFsGVykkLTGkD
K178‑ac ETFsGVykkLTGkDV
K178‑ub ETFsGVykkLTGkDV
K178‑sc ETFsGVykkLTGkDV
K179‑ub TFsGVykkLTGkDVN
K183 VykkLTGKDVNFEFP
K183‑ub VykkLTGkDVNFEFP
  rat

 
S3 _____MFSSSAKIVk
K10‑ub SSSAKIVkPNGEKPD
K15 IVkPNGEKPDEFESG
K15 IVkPNGEKPDEFESG
S24 DEFESGISQALLELE
K37 LEMNSDLKAQLRELN
K37 LEMNSDLKAQLRELN
K49 ELNITAAKEIEVGGG
K58 IEVGGGRKAIIIFVP
K70 FVPVPQLKSFQkIQV
K70 FVPVPQLKSFQkIQV
K74‑ac PQLKSFQkIQVRLVR
K74 PQLKSFQKIQVRLVR
K74 PQLKSFQKIQVRLVR
K85‑ac RLVRELEkKFSGkHV
K85 RLVRELEKKFSGkHV
K86 LVRELEkKFSGkHVV
S88 RELEkKFSGkHVVFI
K90‑ac LEkKFSGkHVVFIAQ
K90 LEkKFSGKHVVFIAQ
S119 NKQKRPRSRTLTAVH
T121 QKRPRSRTLTAVHDA
T123 RPRSRTLTAVHDAIL
S137 LEDLVFPSEIVGKRI
K142 FPSEIVGKRIRVKLD
K142 FPSEIVGKRIRVKLD
K155‑ac LDGSRLIkVHLDKAQ
K155 LDGSRLIKVHLDKAQ
K160 LIkVHLDKAQQNNVE
K169‑ac QQNNVEHkVETFSGV
K169 QQNNVEHKVETFSGV
S174 EHkVETFSGVYKKLT
Y177 VETFSGVYKKLTGkD
K178 ETFSGVYKKLTGkDV
K178 ETFSGVYKKLTGkDV
K178 ETFSGVYKKLTGkDV
K179 TFSGVYKKLTGkDVN
K183‑ac VYKKLTGkDVNFEFP
K183 VYKKLTGKDVNFEFP
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