GCYA2_HUMAN - dbPTM
GCYA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCYA2_HUMAN
UniProt AC P33402
Protein Name Guanylate cyclase soluble subunit alpha-2
Gene Name GUCY1A2
Organism Homo sapiens (Human).
Sequence Length 732
Subcellular Localization Cytoplasm.
Protein Description Has guanylyl cyclase on binding to the beta-1 subunit.; Isoform 2 acts as a negative regulator of guanylyl cyclase activity as it forms non-functional heterodimers with the beta subunits..
Protein Sequence MSRRKISSESFSSLGSDYLETSPEEEGECPLSRLCWNGSRSPPGPLEPSPAAAAAAAAPAPTPAASAAAAAATAGARRVQRRRRVNLDSLGESISRLTAPSPQTIQQTLKRTLQYYEHQVIGYRDAEKNFHNISNRCSYADHSNKEEIEDVSGILQCTANILGLKFEEIQKRFGEEFFNICFHENERVLRAVGGTLQDFFNGFDALLEHIRTSFGKQATLESPSFLCKELPEGTLMLHYFHPHHIVGFAMLGMIKAAGKKIYRLDVEVEQVANEKLCSDVSNPGNCSCLTFLIKECENTNIMKNLPQGTSQVPADLRISINTFCRAFPFHLMFDPSMSVLQLGEGLRKQLRCDTHKVLKFEDCFEIVSPKVNATFERVLLRLSTPFVIRTKPEASGSENKDKVMEVKGQMIHVPESNSILFLGSPCVDKLDELMGRGLHLSDIPIHDATRDVILVGEQAKAQDGLKKRMDKLKATLERTHQALEEEKKKTVDLLYSIFPGDVAQQLWQGQQVQARKFDDVTMLFSDIVGFTAICAQCTPMQVISMLNELYTRFDHQCGFLDIYKVETIGDAYCVAAGLHRKSLCHAKPIALMALKMMELSEEVLTPDGRPIQMRIGIHSGSVLAGVVGVRMPRYCLFGNNVTLASKFESGSHPRRINVSPTTYQLLKREESFTFIPRSREELPDNFPKEIPGICYFLEVRTGPKPPKPSLSSSRIKKVSYNIGTMFLRETSL
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
7Phosphorylation-MSRRKISSESFSSL
-CCCCCCCHHHHHHC		30.9628857561
8PhosphorylationMSRRKISSESFSSLG
CCCCCCCHHHHHHCC		40.5128857561
10PhosphorylationRRKISSESFSSLGSD
CCCCCHHHHHHCCCC		32.1728857561
12PhosphorylationKISSESFSSLGSDYL
CCCHHHHHHCCCCCC		33.6528857561
13PhosphorylationISSESFSSLGSDYLE
CCHHHHHHCCCCCCC		34.4428857561
16PhosphorylationESFSSLGSDYLETSP
HHHHHCCCCCCCCCC		28.5128857561
18PhosphorylationFSSLGSDYLETSPEE
HHHCCCCCCCCCCCC		14.2422798277
21PhosphorylationLGSDYLETSPEEEGE
CCCCCCCCCCCCCCC		47.1628857561
22PhosphorylationGSDYLETSPEEEGEC
CCCCCCCCCCCCCCC		22.4224076635
41PhosphorylationLCWNGSRSPPGPLEP
HCCCCCCCCCCCCCC		36.8224076635
49PhosphorylationPPGPLEPSPAAAAAA
CCCCCCCCHHHHHHH		20.1429255136
89PhosphorylationRRRVNLDSLGESISR
HHCCCHHHHCHHHHH		41.2530576142
93PhosphorylationNLDSLGESISRLTAP
CHHHHCHHHHHHCCC		24.86-
98PhosphorylationGESISRLTAPSPQTI
CHHHHHHCCCCHHHH		35.1030576142
101PhosphorylationISRLTAPSPQTIQQT
HHHHCCCCHHHHHHH		27.4630576142
108PhosphorylationSPQTIQQTLKRTLQY
CHHHHHHHHHHHHHH		20.19-
368PhosphorylationEDCFEIVSPKVNATF
HHHHHHCCCCCCCCH		25.3524719451
460UbiquitinationILVGEQAKAQDGLKK
EEECCHHHHHHHHHH		46.4029967540
466AcetylationAKAQDGLKKRMDKLK
HHHHHHHHHHHHHHH		43.817676373
479PhosphorylationLKATLERTHQALEEE
HHHHHHHHHHHHHHH		14.6829514088
600PhosphorylationALKMMELSEEVLTPD
HHHHHHHCCCCCCCC		20.5723403867
605PhosphorylationELSEEVLTPDGRPIQ
HHCCCCCCCCCCEEE		25.2223403867
619PhosphorylationQMRIGIHSGSVLAGV
EEEEEECCCCCEEEE		30.7323403867
621PhosphorylationRIGIHSGSVLAGVVG
EEEECCCCCEEEEEC		19.5723403867
662PhosphorylationRINVSPTTYQLLKRE
EEEECHHHHHHHHHH		16.8024076635
663PhosphorylationINVSPTTYQLLKREE
EEECHHHHHHHHHHH		10.3124076635
671PhosphorylationQLLKREESFTFIPRS
HHHHHHHCCCCCCCC		25.4924076635
673PhosphorylationLKREESFTFIPRSRE
HHHHHCCCCCCCCHH		29.90-
701PhosphorylationCYFLEVRTGPKPPKP
EEEEEECCCCCCCCC		64.11-
702PhosphorylationYFLEVRTGPKPPKPS
EEEEECCCCCCCCCC		20.0527251275
709PhosphorylationGPKPPKPSLSSSRIK
CCCCCCCCCCHHHCE		47.1925002506
711PhosphorylationKPPKPSLSSSRIKKV
CCCCCCCCHHHCEEE		30.5225002506
712PhosphorylationPPKPSLSSSRIKKVS
CCCCCCCHHHCEEEE		29.0025002506
713PhosphorylationPKPSLSSSRIKKVSY
CCCCCCHHHCEEEEE		34.3525002506
719PhosphorylationSSRIKKVSYNIGTMF
HHHCEEEEEECCCHH		22.7228857561
740Phosphorylation---------------
---------------		32142685
750Phosphorylation-------------------------
-------------------------		27251275
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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:17873020
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCYA2_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 GCYA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCYB1_HUMANGUCY1B3physical
11572861
DLG1_HUMANDLG1physical
11572861
DLG2_HUMANDLG2physical
11572861
DLG3_HUMANDLG3physical
11572861
DLG4_HUMANDLG4physical
11572861
CHIP_HUMANSTUB1physical
17873020
HSP74_HUMANHSPA4physical
17873020
HS90A_HUMANHSP90AA1physical
17873020
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GCYA2_HUMAN

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Related Literatures of Post-Translational Modification

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