GUCY1B1
entrez
2983
canonical
uniprot
Q02153
canonical
ensembl
ENSG00000061918
resolver
ensp
ENSP00000264424
resolver
ensp
ENSP00000420842
resolver
ensp
ENSP00000422313
resolver
ensp
ENSP00000425065
resolver
ensp
ENSP00000426319
resolver
ensp
ENSP00000426786
resolver
ensp
ENSP00000427226
resolver
ensp
ENSP00000673061
resolver
enst
ENST00000502959
resolver
enst
ENST00000505154
resolver
enst
ENST00000507146
resolver
enst
ENST00000513437
resolver
genesymbol
GUCY1B1
resolver
genesymbol
GUCY1B3
resolver
genesymbol_syn
GUC1B3
resolver
genesymbol_syn
GUCSB3
resolver
genesymbol_syn
GUCY1B3
resolver
hgnc
HGNC:4687
resolver
uniprot
B7Z426
resolver
uniprot
B7Z685
resolver
uniprot
B7Z6G8
resolver
uniprot
B7Z9H9
resolver
uniprot
D6RC99
resolver
uniprot
E9PCN2
resolver
uniprot
F6RS12
resolver
uniprot
Q86WY5
resolver
uniprot_entry
B7Z685_HUMAN
resolver
uniprot_entry
B7Z6G8_HUMAN
resolver
uniprot_entry
B7Z9H9_HUMAN
resolver
uniprot_entry
D6RC99_HUMAN
resolver
uniprot_entry
E9PCN2_HUMAN
resolver
uniprot_entry
F6RS12_HUMAN
resolver
uniprot_entry
GCYB1_HUMAN
resolver
uniprot_sec
B7Z426
resolver
uniprot_sec
Q86WY5
resolver
activity_regulation
ACTIVITY REGULATION: Activated by nitric oxide in the presence of magnesium or manganese ions (PubMed:1352257, PubMed:23505436, PubMed:24669844). NO binding to the haem of the beta subunit GUCY1B1 induces a conformational change that allosterically activates the catalytic domain (PubMed:31514202). {ECO:0000269|PubMed:1352257, ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844, ECO:0000269|PubMed:31514202}.
uniprot
proteins
amino_acid_sequence
MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPQFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETKQDDD
uniprot
proteins
ec_number
4.6.1.2
uniprot
proteins
function
FUNCTION: Beta subunit of soluble guanylate cyclase (sGC), a key enzyme in nitric oxide (NO) signaling. sGC functions as a heterodimer consisting of one alpha and one beta subunit. It serves as the primary intracellular receptor for NO, which binds to a heme prosthetic group located on the beta subunit. Upon NO binding, sGC catalyzes the conversion of GTP into cyclic GMP (cGMP), thereby transmitting the NO signal into an ubiquitous intracellular second messenger. {ECO:0000269|PubMed:1352257}.
uniprot
proteins
mass_dalton
70514
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
1352257
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
1680753
uniprot
proteins
pubmed
23505436
uniprot
proteins
pubmed
24669844
uniprot
proteins
pubmed
31514202
uniprot
proteins
pubmed
34535643
uniprot
proteins
pubmed
36972843
uniprot
proteins
sequence_length
619
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}.
uniprot
proteins