Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
SAG (human)

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: G protein regulator, misc.; Motility/polarity/chemotaxis
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
Select Structure to View Below

SAG

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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 S10 ASGKTSKSEPNHVIF
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
  mouse

 
S10-p ACGKTNKsHVIFKKV
S209 KPLNLSVSLSKEIYF
S211 LNLSVSLSKEIYFHG
T224 HGEPIPVTVTVTNNT
T226 EPIPVTVTVTNNTDK
T228 IPVTVTVTNNTDKVV
T231 TVTVTNNTDKVVKKI
Y251 QIANVVLYSSDYYVK
Y255 VVLYSSDYYVKPVAS
  rat

 
S10 ACVKTNKSHVIFKKV
S209-p KPLHLSVsLsKEIYF
S211-p LHLSVsLsKEIYFHG
T224-p HGEPIPVtVtVtNNt
T226-p EPIPVtVtVtNNtEK
T228-p IPVtVtVtNNtEKVV
T231-p tVtVtNNtEKVVKKI
Y251 QIANVVLYSSDYYVK
Y255 VVLYSSDYYVKPVAS
  cow

 
P6 __MKANKPAPNHVIF
S208 KPLRLAVSLSKEIYY
S210 LRLAVSLSKEIYYHG
T223 HGEPIPVTVAVTNST
A225 EPIPVTVAVTNSTEK
T227 IPVTVAVTNSTEKTV
T230 TVAVTNSTEKTVKKI
Y250 QVTNVVLYSSDYYIK
Y254 VVLYSSDYYIKTVAA
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.