HEM3_HUMAN - dbPTM
HEM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEM3_HUMAN
UniProt AC P08397
Protein Name Porphobilinogen deaminase
Gene Name HMBS
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization Cytoplasm .
Protein Description Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps..
Protein Sequence MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDAH
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
2Phosphorylation------MSGNGNAAA
------CCCCCCCCC		40.7525159151
2Acetylation------MSGNGNAAA
------CCCCCCCCC		40.7519413330
10PhosphorylationGNGNAAATAEENSPK
CCCCCCCCCCCCCCC		29.8528450419
15PhosphorylationAATAEENSPKMRVIR
CCCCCCCCCCEEEEE		29.2229255136
17AcetylationTAEENSPKMRVIRVG
CCCCCCCCEEEEEEE		38.8820167786
53UbiquitinationYPGLQFEIIAMSTTG
CCCCEEEEEEEECCC		2.2832015554
57UbiquitinationQFEIIAMSTTGDKIL
EEEEEEEECCCHHHH		17.5029967540
62UbiquitinationAMSTTGDKILDTALS
EEECCCHHHHHHHHH		46.6532015554
66PhosphorylationTGDKILDTALSKIGE
CCHHHHHHHHHHHCH		26.5030576142
69PhosphorylationKILDTALSKIGEKSL
HHHHHHHHHHCHHHH		21.5523917254
70AcetylationILDTALSKIGEKSLF
HHHHHHHHHCHHHHH		56.4325953088
70UbiquitinationILDTALSKIGEKSLF
HHHHHHHHHCHHHHH		56.4332015554
70 (in isoform 2)Acetylation-56.43-
74UbiquitinationALSKIGEKSLFTKEL
HHHHHCHHHHHHHHH		47.4429967540
74AcetylationALSKIGEKSLFTKEL
HHHHHCHHHHHHHHH		47.4423954790
79UbiquitinationGEKSLFTKELEHALE
CHHHHHHHHHHHHHH		53.6332015554
87AcetylationELEHALEKNEVDLVV
HHHHHHHHCCCCEEE		60.2923749302
98UbiquitinationDLVVHSLKDLPTVLP
CEEEECCCCCCCCCC		61.3032015554
102PhosphorylationHSLKDLPTVLPPGFT
ECCCCCCCCCCCCCE		41.8127461979
109PhosphorylationTVLPPGFTIGAICKR
CCCCCCCEEECCCCC		25.1527461979
111UbiquitinationLPPGFTIGAICKREN
CCCCCEEECCCCCCC		13.0629967540
114S-nitrosylationGFTIGAICKRENPHD
CCEEECCCCCCCCCC		3.1819483679
114S-nitrosocysteineGFTIGAICKRENPHD
CCEEECCCCCCCCCC		3.18-
115UbiquitinationFTIGAICKRENPHDA
CEEECCCCCCCCCCE		57.5432015554
123UbiquitinationRENPHDAVVFHPKFV
CCCCCCEEEECHHHC		6.1829967540
128UbiquitinationDAVVFHPKFVGKTLE
CEEEECHHHCCCCHH		44.0829967540
132AcetylationFHPKFVGKTLETLPE
ECHHHCCCCHHCCCC		44.6425953088
132UbiquitinationFHPKFVGKTLETLPE
ECHHHCCCCHHCCCC		44.64-
140UbiquitinationTLETLPEKSVVGTSS
CHHCCCCCCCCCHHH		46.7629967540
145PhosphorylationPEKSVVGTSSLRRAA
CCCCCCCHHHHHHHH		11.9726546556
146PhosphorylationEKSVVGTSSLRRAAQ
CCCCCCHHHHHHHHH		22.8026546556
147PhosphorylationKSVVGTSSLRRAAQL
CCCCCHHHHHHHHHH		26.2328857561
157UbiquitinationRAAQLQRKFPHLEFR
HHHHHHHHCCCCHHH		50.73-
210UbiquitinationGQILHPEECMYAVGQ
CCCCCHHHHHHHCCC		29.0933845483
227UbiquitinationLGVEVRAKDQDILDL
CCCEEEECCCCHHHH		45.4133845483
261S-nitrosylationLRHLEGGCSVPVAVH
HHHHCCCCCCCEEEE		5.652212679
261S-(dipyrrolylmethanemethyl)cysteineLRHLEGGCSVPVAVH
HHHHCCCCCCCEEEE		5.65-
261PyrrolylationLRHLEGGCSVPVAVH
HHHHCCCCCCCEEEE		5.65-
262PhosphorylationRHLEGGCSVPVAVHT
HHHCCCCCCCEEEEE		32.50-
269PhosphorylationSVPVAVHTAMKDGQL
CCCEEEEEEECCCEE		23.11-
288UbiquitinationGVWSLDGSDSIQETM
CEEECCCCCHHHHHH		28.0532015554
291UbiquitinationSLDGSDSIQETMQAT
ECCCCCHHHHHHHEE		5.2829967540
305UbiquitinationTIHVPAQHEDGPEDD
EEECCCCCCCCCCCC		36.9032015554
308UbiquitinationVPAQHEDGPEDDPQL
CCCCCCCCCCCCCCC		25.2229967540
319PhosphorylationDPQLVGITARNIPRG
CCCCEEEEECCCCCC		17.4020068231
328UbiquitinationRNIPRGPQLAAQNLG
CCCCCCHHHHHHHHC		46.7032015554
331UbiquitinationPRGPQLAAQNLGISL
CCCHHHHHHHHCHHH		13.8529967540
337PhosphorylationAAQNLGISLANLLLS
HHHHHCHHHHHHHHC		21.4529083192
344PhosphorylationSLANLLLSKGAKNIL
HHHHHHHCCCHHHHH		29.0729083192
345UbiquitinationLANLLLSKGAKNILD
HHHHHHCCCHHHHHH		63.9632015554
348UbiquitinationLLLSKGAKNILDVAR
HHHCCCHHHHHHHHH		53.8729967540
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

Oops, there are no upstream regulatory protein records of HEM3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEM3_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 HEM3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RANB9_HUMANRANBP9physical
12917623
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
176000Acute intermittent porphyria (AIP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HEM3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.

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