SPEE_HUMAN - dbPTM
SPEE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPEE_HUMAN
UniProt AC P19623
Protein Name Spermidine synthase
Gene Name SRM
Organism Homo sapiens (Human).
Sequence Length 302
Subcellular Localization
Protein Description Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine..
Protein Sequence MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPTYPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALNDVS
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
1Acetylation-------MEPGPDGP
-------CCCCCCCC		14.6622223895
11PhosphorylationGPDGPAASGPAAIRE
CCCCCCCCCCCHHCC		47.6324850871
17DimethylationASGPAAIREGWFRET
CCCCCHHCCCCEECC		31.48-
17MethylationASGPAAIREGWFRET
CCCCCHHCCCCEECC		31.48115384391
22DimethylationAIREGWFRETCSLWP
HHCCCCEECCCCCCC		31.63-
22MethylationAIREGWFRETCSLWP
HHCCCCEECCCCCCC		31.63115390147
46PhosphorylationQLLHHRRSRYQDILV
HHHHHCHHHCCCEEE		34.9828152594
48PhosphorylationLHHRRSRYQDILVFR
HHHCHHHCCCEEEEE		16.2828152594
56PhosphorylationQDILVFRSKTYGNVL
CCEEEEECCCCCCEE		20.2024719451
57UbiquitinationDILVFRSKTYGNVLV
CEEEEECCCCCCEEE		41.3221890473
72PhosphorylationLDGVIQCTERDEFSY
ECCEEEECCCCCCCH		20.0624719451
96MalonylationCSHPNPRKVLIIGGG
CCCCCCCEEEEECCC		42.5226320211
96UbiquitinationCSHPNPRKVLIIGGG
CCCCCCCEEEEECCC		42.5223000965
113UbiquitinationGVLREVVKHPSVESV
HHHHHHHCCCCCCCE		55.7821963094
116PhosphorylationREVVKHPSVESVVQC
HHHHCCCCCCCEEEC		37.93-
123GlutathionylationSVESVVQCEIDEDVI
CCCCEEECCCCHHHH		3.1522555962
134UbiquitinationEDVIQVSKKFLPGMA
HHHHHHCHHHCCCCE		49.0023000965
134AcetylationEDVIQVSKKFLPGMA
HHHHHHCHHHCCCCE		49.0025953088
135AcetylationDVIQVSKKFLPGMAI
HHHHHCHHHCCCCEE		44.6325953088
135UbiquitinationDVIQVSKKFLPGMAI
HHHHHCHHHCCCCEE		44.6323000965
144PhosphorylationLPGMAIGYSSSKLTL
CCCCEEEECCCEEEE		10.1621406692
145PhosphorylationPGMAIGYSSSKLTLH
CCCEEEECCCEEEEE		23.9525159151
146PhosphorylationGMAIGYSSSKLTLHV
CCEEEECCCEEEEEE		24.0225159151
147PhosphorylationMAIGYSSSKLTLHVG
CEEEECCCEEEEEEC		26.2425159151
178SulfoxidationITDSSDPMGPAESLF
EECCCCCCCCHHHHH		13.9130846556
183PhosphorylationDPMGPAESLFKESYY
CCCCCHHHHHHHHHH		41.0124719451
193SulfoxidationKESYYQLMKTALKED
HHHHHHHHHHHHHHC		1.8230846556
194UbiquitinationESYYQLMKTALKEDG
HHHHHHHHHHHHHCC		38.9621906983
198AcetylationQLMKTALKEDGVLCC
HHHHHHHHHCCEEEE		51.8226051181
198UbiquitinationQLMKTALKEDGVLCC
HHHHHHHHHCCEEEE		51.8221963094
253SumoylationIGFMLCSKNPSTNFQ
EEEEEEECCCCCCCC		72.40-
253UbiquitinationIGFMLCSKNPSTNFQ
EEEEEEECCCCCCCC		72.40-
274SulfoxidationTQQQVAQMQLKYYNS
CHHHHHHHHHHHCCC		3.4830846556
277SumoylationQVAQMQLKYYNSDVH
HHHHHHHHHCCCHHH		28.88-
277UbiquitinationQVAQMQLKYYNSDVH
HHHHHHHHHCCCHHH		28.8821963094
277AcetylationQVAQMQLKYYNSDVH
HHHHHHHHHCCCHHH		28.8826051181
278PhosphorylationVAQMQLKYYNSDVHR
HHHHHHHHCCCHHHH		19.2428152594
279PhosphorylationAQMQLKYYNSDVHRA
HHHHHHHCCCHHHHH		13.4528152594
296SumoylationVLPEFARKALNDVS-
HCHHHHHHHHHCCC-		54.52-
296UbiquitinationVLPEFARKALNDVS-
HCHHHHHHHHHCCC-		54.5229967540
296SumoylationVLPEFARKALNDVS-
HCHHHHHHHHHCCC-		54.52-
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 SPEE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPEE_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 SPEE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRK_HUMANCRKphysical
26344197
HXK2_HUMANHK2physical
26344197
TIPRL_HUMANTIPRLphysical
26344197
EFHC1_HUMANEFHC1physical
27173435
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
DB00118S-Adenosylmethionine
Regulatory Network of SPEE_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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