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Protein Page:
RPS7 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
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: Ribosomal protein; Translation
Cellular Component: small subunit processome; cytoskeleton; cytoplasm; nucleolus; ribosome; intracellular; nucleus; ribonucleoprotein complex
Molecular Function: structural constituent of ribosome
Biological Process: ribosomal small subunit biogenesis and assembly; translation; neural tube closure; cell differentiation; rRNA processing
Reference #:  P62082 (UniProtKB)
Alt. Names/Synonyms: 40S ribosomal protein S7; ribosomal protein S7; Rps7; Rps7A; RS7; S7
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.


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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


 SS 

SS: 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.


 MS 

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


       mouse

 
0 39 K10-ub SSSAKIVkPNGEkPD
0 4 K15-ac IVkPNGEkPDEFESG
0 40 K15-ub IVkPNGEkPDEFESG
0 1 S24 DEFESGISQALLELE
0 3 K37 LEMNSDLKAQLRELN
0 36 K37-ub LEMNSDLkAQLRELN
0 18 K49-ub ELNITAAkEIEVGGG
0 1 K70 FVPVPQLKSFQkIQV
0 12 K70 FVPVPQLKSFQkIQV
0 2 K74-ac PQLKSFQkIQVRLVR
0 50 K74-ub PQLKSFQkIQVRLVR
0 1 K74-sc PQLKSFQkIQVRLVR
0 1 K85 RLVRELEKKFSGKHV
0 1 K86 LVRELEKKFSGKHVV
0 4 K90 LEKKFSGKHVVFIAQ
0 10 S119-p NKQKRPRsRtLtAVH
0 16 T121-p QKRPRsRtLtAVHDA
0 8 T123-p RPRsRtLtAVHDAIL
0 1 S137 LEDLVFPSEIVGkRI
0 8 K142 FPSEIVGKRIRVKLD
0 29 K142-ub FPSEIVGkRIRVKLD
0 4 K155-ub LDGSRLIkVHLDkAQ
0 4 K160-ub LIkVHLDkAQQNNVE
0 2 K169-ac QQNNVEHkVETFSGV
0 4 K178-ac ETFSGVYkKLTGkDV
0 6 K178-ub ETFSGVYkKLTGkDV
0 1 K178-sc ETFSGVYkKLTGkDV
0 2 K179 TFSGVYkKLTGkDVN
0 1 K183-ac VYkKLTGkDVNFEFP
0 18 K183-ub VYkKLTGkDVNFEFP
  human

 
K10-ub SSSAKIVkPNGEkPD
K15 IVkPNGEKPDEFESG
K15-ub IVkPNGEkPDEFESG
S24-p DEFESGIsQALLELE
K37-ac LEMNSDLkAQLRELN
K37-ub LEMNSDLkAQLRELN
K49-ub ELNITAAkEIEVGGG
K70-ac FVPVPQLkSFQkIQV
K70-ub FVPVPQLkSFQkIQV
K74-ac PQLkSFQkIQVRLVR
K74-ub PQLkSFQkIQVRLVR
K74-sc PQLkSFQkIQVRLVR
K85-ub RLVRELEkkFSGkHV
K86-ub LVRELEkkFSGkHVV
K90-ub LEkkFSGkHVVFIAQ
S119-p NKQKRPRsRtLtAVH
T121-p QKRPRsRtLtAVHDA
T123-p RPRsRtLtAVHDAIL
S137-p LEDLVFPsEIVGkRI
K142-ac FPsEIVGkRIRVKLD
K142-ub FPsEIVGkRIRVKLD
K155-ub LDGSRLIkVHLDkAQ
K160-ub LIkVHLDkAQQNNVE
K169-ac QQNNVEHkVETFSGV
K178-ac ETFSGVYkkLTGkDV
K178-ub ETFSGVYkkLTGkDV
K178-sc ETFSGVYkkLTGkDV
K179-ub TFSGVYkkLTGkDVN
K183 VYkkLTGKDVNFEFP
K183-ub VYkkLTGkDVNFEFP
  rat

 
K10-ub SSSAKIVkPNGEKPD
K15 IVkPNGEKPDEFESG
K15 IVkPNGEKPDEFESG
S24 DEFESGISQALLELE
K37 LEMNSDLKAQLRELN
K37 LEMNSDLKAQLRELN
K49 ELNITAAKEIEVGGG
K70 FVPVPQLKSFQKIQV
K70 FVPVPQLKSFQKIQV
K74 PQLKSFQKIQVRLVR
K74 PQLKSFQKIQVRLVR
K74 PQLKSFQKIQVRLVR
K85 RLVRELEKKFSGKHV
K86 LVRELEKKFSGKHVV
K90 LEKKFSGKHVVFIAQ
S119 NKQKRPRSRTLTAVH
T121 QKRPRSRTLTAVHDA
T123 RPRSRTLTAVHDAIL
S137 LEDLVFPSEIVGKRI
K142 FPSEIVGKRIRVKLD
K142 FPSEIVGKRIRVKLD
K155 LDGSRLIKVHLDKAQ
K160 LIKVHLDKAQQNNVE
K169 QQNNVEHKVETFSGV
K178 ETFSGVYKKLTGKDV
K178 ETFSGVYKKLTGKDV
K178 ETFSGVYKKLTGKDV
K179 TFSGVYKKLTGKDVN
K183 VYKKLTGKDVNFEFP
K183 VYKKLTGKDVNFEFP
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