GCYB1_HUMAN - dbPTM
GCYB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCYB1_HUMAN
UniProt AC Q02153
Protein Name Guanylate cyclase soluble subunit beta-1 {ECO:0000305}
Gene Name GUCY1B1 {ECO:0000312|HGNC:HGNC:4687}
Organism Homo sapiens (Human).
Sequence Length 619
Subcellular Localization Cytoplasm .
Protein Description Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP..
Protein Sequence MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPQFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETKQDDD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
26UbiquitinationPEVWEDIKKEAQLDE
HHHHHHHHHHHCCCC
57.81-
145UbiquitinationEREGLQDIVIGIIKT
CCCCCHHHHHHHHHH
1.24-
165UbiquitinationHGTEIDMKVIQQRNE
HCCCCCHHHHHHHHH
32.22-
192PhosphorylationESKEEDFYEDLDRFE
HHCCCCHHHCHHHHH
22.3628796482
395PhosphorylationKKTDTLLYSVLPPSV
HCCCEEEECCCCHHH
10.3927067055
396PhosphorylationKTDTLLYSVLPPSVA
CCCEEEECCCCHHHH
19.6927067055
401PhosphorylationLYSVLPPSVANELRH
EECCCCHHHHHHHHC
31.7427067055
471UbiquitinationRKNPFVYKVETVGDK
CCCCCEEEEEEECCC
28.44-
540PhosphorylationIGQRMPRYCLFGNTV
CCCCCCEEEEECCEE
6.40-
541UbiquitinationGQRMPRYCLFGNTVN
CCCCCEEEEECCEEE
2.40-
561UbiquitinationETTGEKGKINVSEYT
EECCCCCEEEEHHEE
42.02-
567PhosphorylationGKINVSEYTYRCLMS
CEEEEHHEEEEEECC
11.10-
574PhosphorylationYTYRCLMSPENSDPQ
EEEEEECCCCCCCCC
19.0029978859
578PhosphorylationCLMSPENSDPQFHLE
EECCCCCCCCCCCCC
49.3529978859
591PhosphorylationLEHRGPVSMKGKKEP
CCCCCCCCCCCCCCC
20.2229978859
609PhosphorylationWFLSRKNTGTEETKQ
EEEEECCCCCCCCCC
48.8228152594
611PhosphorylationLSRKNTGTEETKQDD
EEECCCCCCCCCCCC
28.7128152594
614PhosphorylationKNTGTEETKQDDD--
CCCCCCCCCCCCC--
27.9828152594

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
192YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCYB1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GCYB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOS3_HUMANNOS3physical
12676772
HS90A_HUMANHSP90AA1physical
12676772
A4_HUMANAPPphysical
21832049
GCYA2_HUMANGUCY1A2physical
28514442
GCYA3_HUMANGUCY1A3physical
28514442
MXRA7_HUMANMXRA7physical
28514442
UACA_HUMANUACAphysical
28514442
MTFR2_HUMANMTFR2physical
28514442
MYCB2_HUMANMYCBP2physical
28514442
BBS2_HUMANBBS2physical
28514442
MUL1_HUMANMUL1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GCYB1_HUMAN

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Related Literatures of Post-Translational Modification

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