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Protein Page:
SAG (human)
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
SAG Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated- phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Retina and pineal gland. Belongs to the arrestin family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; G protein regulator, misc.
Cellular Component: cytosol
Molecular Function: opsin binding; phosphoprotein binding; protein phosphatase inhibitor activity
Biological Process: rhodopsin mediated signaling; phototransduction, visible light; cell surface receptor linked signal transduction; regulation of rhodopsin mediated signaling; visual perception; negative regulation of catalytic activity
Reference #:  P10523 (UniProtKB)
Alt. Names/Synonyms: 48 kDa protein; arrestin 1; ARRS; DKFZp686D1084; DKFZp686I1383; retina and pineal gland (arrestin); Retinal S-antigen; retinal S-antigen (48 KDa protein); Rod photoreceptor arrestin; RP47; S-AG; S-antigen; S-arrestin; SAG
Gene Symbols: SAG
Molecular weight: 45,120 Da
Basal Isoelectric point: 6.14  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SAG

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.


       human

 
0 1 K9-ac AASGKTSkSEPNHVI
0 1 S10 ASGKTSkSEPNHVIF
0 1 Y29-p RDKSVTIyLGNRDYI
0 1 Y62-p LVKGKKVyVtLtCAF
0 1 T64-p KGKKVyVtLtCAFRY
0 1 T66-p KKVyVtLtCAFRYGQ
0 1 Y120-p KKLGSNTyPFLLTFP
0 1 Y129-p FLLTFPDyLPCSVML
0 1 S143-p LQPAPQDsGKSCGVD
0 1 S212 KPLHLAVSLNKEIYF
0 1 N214 LHLAVSLNKEIYFHG
0 1 T227 HGEPIPVTVTVTNNT
0 1 T229 EPIPVTVTVTNNTEK
0 1 T231 IPVTVTVTNNTEKTV
0 1 T234 TVTVTNNTEKTVKKI
0 4 Y254-p QVANVVLySSDyYVK
0 4 Y258-p VVLySSDyYVKPVAM
0 1 S348-p GFLGELTssEVAtEV
0 1 S349-p FLGELTssEVAtEVP
0 1 T353-p LTssEVAtEVPFRLM
  mouse

 
K9 AACGKTNKsHVIFKK
S10-p ACGKTNKsHVIFKKV
Y26 RDKSVTIYLGKRDYV
Y59 LVKGKKVYVTLTCAF
T61 KGKKVYVTLTCAFRY
T63 KKVYVTLTCAFRYGQ
Y117 KKLGDNTYPFLLTFP
Y126 FLLTFPDYLPCSVML
V140 LQPAPQDVGKSCGVD
S209 KPLNLSVSLSKEIYF
S211 LNLSVSLSKEIYFHG
T224 HGEPIPVTVTVTNNT
T226 EPIPVTVTVTNNTDK
T228 IPVTVTVTNNTDKVV
T231 TVTVTNNTDKVVKKI
Y251 QIANVVLYSSDYYVK
Y255 VVLYSSDYYVKPVAS
S345 GFLGELTSSEVATEV
S346 FLGELTSSEVATEVP
T350 LTSSEVATEVPFRLM
  rat

 
K9 AACVKTNKSHVIFKK
S10 ACVKTNKSHVIFKKV
Y26 RDKSVTIYLGKRDYI
Y59 LVKGKKVYVTLTCAF
T61 KGKKVYVTLTCAFRY
T63 KKVYVTLTCAFRYGQ
Y117 KKLGDNTYPFLLTFP
Y126 FLLTFPDYLPCSVML
V140 LQPAPQDVGKSCGVD
S209-p KPLHLSVsLsKEIYF
S211-p LHLSVsLsKEIYFHG
T224-p HGEPIPVtVtVtNNt
T226-p EPIPVtVtVtNNtEK
T228-p IPVtVtVtNNtEKVV
T231-p tVtVtNNtEKVVKKI
Y251 QIANVVLYSSDYYVK
Y255 VVLYSSDYYVKPVAS
S345 GFLGELTSSEVATEV
S346 FLGELTSSEVATEVP
T350 LTSSEVATEVPFRLM
  cow

 
K5 ___MKANKPAPNHVI
P6 __MKANKPAPNHVIF
Y25 RDKSVTIYLGKRDYI
Y58 LVKGKRVYVSLTCAF
S60 KGKRVYVSLTCAFRY
T62 KRVYVSLTCAFRYGQ
Y116 KKLGANTYPFLLTFP
Y125 FLLTFPDYLPCSVML
V139 LQPAPQDVGKSCGVD
S208 KPLRLAVSLSKEIYY
S210 LRLAVSLSKEIYYHG
T223 HGEPIPVTVAVTNST
A225 EPIPVTVAVTNSTEK
T227 IPVTVAVTNSTEKTV
T230 TVAVTNSTEKTVKKI
Y250 QVTNVVLYSSDYYIK
Y254 VVLYSSDYYIKTVAA
S344 GLLGELTSSEVATEV
S345 LLGELTSSEVATEVP
T349 LTSSEVATEVPFRLM
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