SPSY_HUMAN - dbPTM
SPSY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPSY_HUMAN
UniProt AC P52788
Protein Name Spermine synthase
Gene Name SMS
Organism Homo sapiens (Human).
Sequence Length 366
Subcellular Localization
Protein Description Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM)..
Protein Sequence MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFANLRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVLDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDLSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAKP
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
2Acetylation------MAAARHSTL
------CCCCCCCCH		15.1619413330
7Phosphorylation-MAAARHSTLDFMLG
-CCCCCCCCHHHHHC		25.7220068231
8PhosphorylationMAAARHSTLDFMLGA
CCCCCCCCHHHHHCC		24.9928857561
16UbiquitinationLDFMLGAKADGETIL
HHHHHCCCCCHHHHH		45.2521963094
162-HydroxyisobutyrylationLDFMLGAKADGETIL
HHHHHCCCCCHHHHH		45.25-
21PhosphorylationGAKADGETILKGLQS
CCCCCHHHHHHHHHH		36.8220068231
49UbiquitinationWQDHGYLATYTNKNG
CCCCCEEEEEECCCC		7.0621963094
57PhosphorylationTYTNKNGSFANLRIY
EEECCCCCEEEEEEE		30.4923897707
64UbiquitinationSFANLRIYPHGLVLL
CEEEEEEECCCEEEE		5.2424816145
83UbiquitinationYDGDAQGKEEIDSIL
CCCCCCCHHHHHHHH		39.8421963094
88PhosphorylationQGKEEIDSILNKVEE
CCHHHHHHHHHHHHH		34.3425159151
92UbiquitinationEIDSILNKVEERMKE
HHHHHHHHHHHHHHH		47.8029967540
98UbiquitinationNKVEERMKELSQDST
HHHHHHHHHHHCCCC		62.8221963094
98 (in isoform 2)Ubiquitination-62.8221890473
101PhosphorylationEERMKELSQDSTGRV
HHHHHHHHCCCCCCC		32.7928857561
103UbiquitinationRMKELSQDSTGRVKR
HHHHHHCCCCCCCCC		44.8023503661
104PhosphorylationMKELSQDSTGRVKRL
HHHHHCCCCCCCCCC		25.7320068231
105PhosphorylationKELSQDSTGRVKRLP
HHHHCCCCCCCCCCC		36.9820068231
117UbiquitinationRLPPIVRGGAIDRYW
CCCCEECCCCCCCCC		20.9921890473
122MethylationVRGGAIDRYWPTADG
ECCCCCCCCCCCCCC		29.33115917321
122UbiquitinationVRGGAIDRYWPTADG
ECCCCCCCCCCCCCC		29.3323503661
133 (in isoform 2)Ubiquitination-41.9221890473
133UbiquitinationTADGRLVEYDIDEVV
CCCCCEEEEECCEEE		41.9227667366
134PhosphorylationADGRLVEYDIDEVVY
CCCCEEEEECCEEEE		15.66-
139UbiquitinationVEYDIDEVVYDEDSP
EEEECCEEEECCCCC		4.2529967540
141PhosphorylationYDIDEVVYDEDSPYQ
EECCEEEECCCCCCC		20.84-
147PhosphorylationVYDEDSPYQNIKILH
EECCCCCCCCEEEEE		20.3825147952
151 (in isoform 1)Ubiquitination-46.9221890473
151UbiquitinationDSPYQNIKILHSKQF
CCCCCCEEEEEECEE		46.9221963094
152UbiquitinationSPYQNIKILHSKQFG
CCCCCEEEEEECEEC		3.5627667366
156UbiquitinationNIKILHSKQFGNILI
CEEEEEECEECCEEE		38.6123503661
177 (in isoform 2)Ubiquitination-12.2121890473
177UbiquitinationLAESDLAYTRAIMGS
HHHCHHHHHHHHHCC		12.2123000965
178UbiquitinationAESDLAYTRAIMGSG
HHCHHHHHHHHHCCC		14.1723000965
182SulfoxidationLAYTRAIMGSGKEDY
HHHHHHHHCCCCCCC		3.2230846556
182UbiquitinationLAYTRAIMGSGKEDY
HHHHHHHHCCCCCCC		3.2223000965
184PhosphorylationYTRAIMGSGKEDYTG
HHHHHHCCCCCCCCC		29.34-
186 (in isoform 1)Ubiquitination-49.4621890473
186UbiquitinationRAIMGSGKEDYTGKD
HHHHCCCCCCCCCCE		49.4621906983
1862-HydroxyisobutyrylationRAIMGSGKEDYTGKD
HHHHCCCCCCCCCCE		49.46-
189PhosphorylationMGSGKEDYTGKDVLI
HCCCCCCCCCCEEEE		20.62-
190PhosphorylationGSGKEDYTGKDVLIL
CCCCCCCCCCEEEEE		50.51-
192UbiquitinationGKEDYTGKDVLILGG
CCCCCCCCEEEEECC		36.5421963094
196UbiquitinationYTGKDVLILGGGDGG
CCCCEEEEECCCCCC		3.1823000965
197UbiquitinationTGKDVLILGGGDGGI
CCCEEEEECCCCCCC		4.5723000965
201UbiquitinationVLILGGGDGGILCEI
EEEECCCCCCCEEEE		56.2623000965
208UbiquitinationDGGILCEIVKLKPKM
CCCCEEEEEECCCCE		3.0232015554
211UbiquitinationILCEIVKLKPKMVTM
CEEEEEECCCCEEEE		8.7621963094
217PhosphorylationKLKPKMVTMVEIDQM
ECCCCEEEEEEEEHH		16.4125002506
230UbiquitinationQMVIDGCKKYMRKTC
HHHHHHHHHHHHHHH		53.0923000965
230 (in isoform 1)Ubiquitination-53.0921890473
231UbiquitinationMVIDGCKKYMRKTCG
HHHHHHHHHHHHHHH		48.6423000965
235UbiquitinationGCKKYMRKTCGDVLD
HHHHHHHHHHHHHHH		31.4723000965
2352-HydroxyisobutyrylationGCKKYMRKTCGDVLD
HHHHHHHHHHHHHHH		31.47-
236PhosphorylationCKKYMRKTCGDVLDN
HHHHHHHHHHHHHHH		16.03-
245AcetylationGDVLDNLKGDCYQVL
HHHHHHCCCCHHHHH		59.9826051181
245UbiquitinationGDVLDNLKGDCYQVL
HHHHHHCCCCHHHHH		59.9821963094
258UbiquitinationVLIEDCIPVLKRYAK
HHHHHHHHHHHHHHH		31.5529967540
2612-HydroxyisobutyrylationEDCIPVLKRYAKEGR
HHHHHHHHHHHHCCC		43.53-
261AcetylationEDCIPVLKRYAKEGR
HHHHHHHHHHHHCCC		43.5326051181
261UbiquitinationEDCIPVLKRYAKEGR
HHHHHHHHHHHHCCC		43.5332015554
291PhosphorylationTSPEEDSTWEFLRLI
CCCCCCCHHHHHHHH		41.14-
311UbiquitinationKVLKQDGKYFTQGNC
HHHHHCCCEECCCCE		45.5429967540
337S-palmitoylationEQLGRLYCPVEFSKE
HHHCCCCCCCCCCCC		3.4429575903
342PhosphorylationLYCPVEFSKEIVCVP
CCCCCCCCCCEEEEC		18.8421712546
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 SPSY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPSY_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 SPSY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHRD1_HUMANCHORDC1physical
22863883
DX39A_HUMANDDX39Aphysical
22863883
CH60_HUMANHSPD1physical
22863883
KYNU_HUMANKYNUphysical
22863883
LDHA_HUMANLDHAphysical
22863883
NHRF1_HUMANSLC9A3R1physical
22863883
SMAP_HUMANC11orf58physical
22863883
DHSO_HUMANSORDphysical
22863883
ENOPH_HUMANENOPH1physical
26344197
VIGLN_HUMANHDLBPphysical
26344197
MTRR_HUMANMTRRphysical
26344197
UCHL3_HUMANUCHL3physical
26344197
XIAP_HUMANXIAPphysical
26496610
VATC1_HUMANATP6V1C1physical
26496610
ETFA_HUMANETFAphysical
26496610
STXB2_HUMANSTXBP2physical
26496610
BAP1_HUMANBAP1physical
26496610
IASPP_HUMANPPP1R13Lphysical
26496610
HEAT3_HUMANHEATR3physical
26496610
PDRG1_HUMANPDRG1physical
26496610
PRC2B_HUMANPRRC2Bphysical
26496610
CMBL_HUMANCMBLphysical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
309583X-linked syndromic mental retardation Snyder-Robinson type (MRXSSR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00127Spermine
Regulatory Network of SPSY_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 ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, AND MASSSPECTROMETRY.

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