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Protein Page:
GUCY1B3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
GUCY1B3 Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Heterodimer of an alpha and a beta chain. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Nucleotide Metabolism - purine; EC 4.6.1.2; Lyase; Guanylyl cyclase; Receptor, misc.
Cellular Component: guanylate cyclase complex, soluble; intracellular membrane-bound organelle; cytoplasm
Molecular Function: guanylate cyclase activity; GTP binding; protein heterodimerization activity; metal ion binding; heme binding; Hsp90 protein binding; receptor activity
Biological Process: blood circulation; blood coagulation; nitric oxide mediated signal transduction
Reference #:  Q02153 (UniProtKB)
Alt. Names/Synonyms: GC-S-beta-1; GC-SB3; GCS-beta-1; GCS-beta-3; GCYB1; guanylate cyclase 1, soluble, beta 3; Guanylate cyclase soluble subunit beta-1; Guanylate cyclase soluble subunit beta-3; GUC1B3; GUCB3; GUCSB3; GUCY1B1; GUCY1B3; Soluble guanylate cyclase small subunit
Gene Symbols: GUCY1B3
Molecular weight: 70,514 Da
Basal Isoelectric point: 5.2  Predict pI for various phosphorylation states
Select Structure to View Below

GUCY1B3
Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: Y192‑p

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 K47 RIIYDDSKTYDLVAA
2 0 Y192-p ESKEEDFyEDLDRFE
0 1 Y540-p IGQRMPRyCLFGNTV
0 1 Y567-p GKINVSEyTYRCLMS
  mouse

 
K47-u RIIYDDSkTYDLVAA
Y192 ESKEEDFYEDLDRFE
Y540 IGQRMPRYCLFGNTV
Y567 GKINVSEYTYRCLMS
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