SAE1_HUMAN - dbPTM
SAE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAE1_HUMAN
UniProt AC Q9UBE0
Protein Name SUMO-activating enzyme subunit 1
Gene Name SAE1
Organism Homo sapiens (Human).
Sequence Length 346
Subcellular Localization Nucleus .
Protein Description The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2..
Protein Sequence MVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTKVAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCPVKEALEVDWSSEKAKAALKRTTSDYFLLQVLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCFSEMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKGNGIVECLGPK
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-------MVEKEEAG
-------CCCHHCCC		8.7322814378
2Acetylation------MVEKEEAGG
------CCCHHCCCC		16.8819413330
12PhosphorylationEEAGGGISEEEAAQY
HCCCCCCCHHHHHHH		42.0819664994
19PhosphorylationSEEEAAQYDRQIRLW
CHHHHHHHHHHHHHH		14.3628985074
24MethylationAQYDRQIRLWGLEAQ
HHHHHHHHHHCHHHH		18.95115919413
322-HydroxyisobutyrylationLWGLEAQKRLRASRV
HHCHHHHHHHHHHHH		61.52-
32UbiquitinationLWGLEAQKRLRASRV
HHCHHHHHHHHHHHH		61.5221890473
32UbiquitinationLWGLEAQKRLRASRV
HHCHHHHHHHHHHHH		61.5221890473
32AcetylationLWGLEAQKRLRASRV
HHCHHHHHHHHHHHH		61.5225953088
37PhosphorylationAQKRLRASRVLLVGL
HHHHHHHHHHHHHCC		19.25-
45UbiquitinationRVLLVGLKGLGAEIA
HHHHHCCHHHHHHHH		46.2721890473
452-HydroxyisobutyrylationRVLLVGLKGLGAEIA
HHHHHCCHHHHHHHH		46.27-
53UbiquitinationGLGAEIAKNLILAGV
HHHHHHHHHHHHHCC		58.9321890473
53UbiquitinationGLGAEIAKNLILAGV
HHHHHHHHHHHHHCC		58.9321890473
61UbiquitinationNLILAGVKGLTMLDH
HHHHHCCCCEEECCC		47.4921890473
65SulfoxidationAGVKGLTMLDHEQVT
HCCCCEEECCCCCCC		5.0730846556
86PhosphorylationQFLIRTGSVGRNRAE
CEEEECCCCCCCHHH		22.3027067055
95PhosphorylationGRNRAEASLERAQNL
CCCHHHHHHHHHHHC		23.4422210691
105SulfoxidationRAQNLNPMVDVKVDT
HHHHCCCCCEEEECH		3.8021406390
109SumoylationLNPMVDVKVDTEDIE
CCCCCEEEECHHHHH		29.90-
109UbiquitinationLNPMVDVKVDTEDIE
CCCCCEEEECHHHHH		29.9021906983
109SumoylationLNPMVDVKVDTEDIE
CCCCCEEEECHHHHH		29.90-
141UbiquitinationCSRDVIVKVDQICHK
CCCCEEEEHHHHHHC		29.04-
141AcetylationCSRDVIVKVDQICHK
CCCCEEEEHHHHHHC		29.0425953088
148UbiquitinationKVDQICHKNSIKFFT
EHHHHHHCCCCEEEE		48.23-
150PhosphorylationDQICHKNSIKFFTGD
HHHHHCCCCEEEECC		31.77-
152UbiquitinationICHKNSIKFFTGDVF
HHHCCCCEEEECCCC		33.96-
178UbiquitinationEHEFVEEKTKVAKVS
CCHHHHCHHHEEEHH		39.89-
180UbiquitinationEFVEEKTKVAKVSQG
HHHHCHHHEEEHHHC		51.79-
183UbiquitinationEEKTKVAKVSQGVED
HCHHHEEEHHHCCCC		45.4621890473
185PhosphorylationKTKVAKVSQGVEDGP
HHHEEEHHHCCCCCC		22.1017525332
194PhosphorylationGVEDGPDTKRAKLDS
CCCCCCCCCCCCCCC		26.0920068231
195UbiquitinationVEDGPDTKRAKLDSS
CCCCCCCCCCCCCCC		58.7121890473
195AcetylationVEDGPDTKRAKLDSS
CCCCCCCCCCCCCCC		58.7125953088
195SumoylationVEDGPDTKRAKLDSS
CCCCCCCCCCCCCCC		58.71-
198UbiquitinationGPDTKRAKLDSSETT
CCCCCCCCCCCCCCC		57.78-
198AcetylationGPDTKRAKLDSSETT
CCCCCCCCCCCCCCC		57.7823749302
201PhosphorylationTKRAKLDSSETTMVK
CCCCCCCCCCCCEEE		40.2829255136
202PhosphorylationKRAKLDSSETTMVKK
CCCCCCCCCCCEEEE		38.3329255136
204PhosphorylationAKLDSSETTMVKKKV
CCCCCCCCCEEEEEE		23.3429255136
205PhosphorylationKLDSSETTMVKKKVV
CCCCCCCCEEEEEEE		18.8629255136
206SulfoxidationLDSSETTMVKKKVVF
CCCCCCCEEEEEEEE		5.6221406390
208UbiquitinationSSETTMVKKKVVFCP
CCCCCEEEEEEEEEE		35.7321906983
2082-HydroxyisobutyrylationSSETTMVKKKVVFCP
CCCCCEEEEEEEEEE		35.73-
209UbiquitinationSETTMVKKKVVFCPV
CCCCEEEEEEEEEEH		39.11-
210UbiquitinationETTMVKKKVVFCPVK
CCCEEEEEEEEEEHH		37.60-
217UbiquitinationKVVFCPVKEALEVDW
EEEEEEHHHHHCCCC		23.55-
228UbiquitinationEVDWSSEKAKAALKR
CCCCCHHHHHHHHHH		58.0721890473
2282-HydroxyisobutyrylationEVDWSSEKAKAALKR
CCCCCHHHHHHHHHH		58.07-
228AcetylationEVDWSSEKAKAALKR
CCCCCHHHHHHHHHH		58.0723236377
230UbiquitinationDWSSEKAKAALKRTT
CCCHHHHHHHHHHHC		45.30-
236PhosphorylationAKAALKRTTSDYFLL
HHHHHHHHCCHHHHH		29.1224719451
236 (in isoform 2)Phosphorylation-29.1223663014
237 (in isoform 2)Phosphorylation-24.5123663014
238PhosphorylationAALKRTTSDYFLLQV
HHHHHHCCHHHHHHH		29.6923403867
238 (in isoform 2)Phosphorylation-29.6923663014
240PhosphorylationLKRTTSDYFLLQVLL
HHHHCCHHHHHHHHH		8.9023403867
240 (in isoform 2)Phosphorylation-8.9023663014
246 (in isoform 2)Phosphorylation-2.5123663014
248 (in isoform 2)Phosphorylation-28.7423663014
262PhosphorylationRDPSSDTYEEDSELL
CCCCCCCCHHHHHHH		23.47-
266PhosphorylationSDTYEEDSELLLQIR
CCCCHHHHHHHHHHH		33.16-
283PhosphorylationVLDSLGISPDLLPED
HHHHCCCCCCCCCHH		15.5728348404
288 (in isoform 3)Phosphorylation-46.54-
291 (in isoform 3)Phosphorylation-3.00-
294PhosphorylationLPEDFVRYCFSEMAP
CCHHHHHHHHHHHHH		7.7923532336
299 (in isoform 3)Phosphorylation-5.04-
335UbiquitinationFFFFDGMKGNGIVEC
EEECCCCCCCCCEEC		55.54-
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 SAE1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAE1_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 SAE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAE2_HUMANUBA2physical
17353931
SUMO3_HUMANSUMO3physical
17353931
UNC79_HUMANUNC79physical
17353931
CP1B1_HUMANCYP1B1physical
17353931
SAE2_HUMANUBA2physical
10217437
SAE2_HUMANUBA2physical
10187858
ETV4_HUMANETV4physical
19307308
SAE2_HUMANUBA2physical
9920803
A4_HUMANAPPphysical
21832049
SAE2_HUMANUBA2physical
22939629
UBC9_HUMANUBE2Iphysical
12641448
SYAC_HUMANAARSphysical
22863883
PUR8_HUMANADSLphysical
22863883
DHYS_HUMANDHPSphysical
22863883
LPP_HUMANLPPphysical
22863883
PDE12_HUMANPDE12physical
22863883
RAGP1_HUMANRANGAP1physical
22863883
TPD54_HUMANTPD52L2physical
22863883
WDR4_HUMANWDR4physical
22863883
SNUT2_HUMANUSP39physical
25027693
HSP72_HUMANHSPA2physical
25027693
UBC9_HUMANUBE2Iphysical
19250909
SUMO3_HUMANSUMO3physical
26344197
TYSY_HUMANTYMSphysical
26344197
CATC_HUMANCTSCphysical
26496610
SUMO2_HUMANSUMO2physical
26496610
GDF15_HUMANGDF15physical
26496610
SAE2_HUMANUBA2physical
26496610
PQBP1_HUMANPQBP1physical
26496610
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 SAE1_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.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASSSPECTROMETRY.

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