SAHH_HUMAN - dbPTM
SAHH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAHH_HUMAN
UniProt AC P23526
Protein Name Adenosylhomocysteinase
Gene Name AHCY
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Cytoplasm . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine..
Protein Sequence MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY
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------MSDKLPYKV
------CCCCCCCCH		43.3727499020
4Acetylation----MSDKLPYKVAD
----CCCCCCCCHHH		44.0223749302
4Ubiquitination----MSDKLPYKVAD
----CCCCCCCCHHH		44.02-
8UbiquitinationMSDKLPYKVADIGLA
CCCCCCCCHHHHHHH		29.0721890473
8UbiquitinationMSDKLPYKVADIGLA
CCCCCCCCHHHHHHH		29.0721890473
8MethylationMSDKLPYKVADIGLA
CCCCCCCCHHHHHHH		29.0766698133
20UbiquitinationGLAAWGRKALDIAEN
HHHHCHHHHHHHHHC		49.73-
29SulfoxidationLDIAENEMPGLMRMR
HHHHHCCCCCHHHHH		4.8721406390
33SulfoxidationENEMPGLMRMRERYS
HCCCCCHHHHHHHHC		3.8130846556
34MethylationNEMPGLMRMRERYSA
CCCCCHHHHHHHHCC		26.50115493191
39PhosphorylationLMRMRERYSASKPLK
HHHHHHHHCCCCCCC		12.1128152594
40PhosphorylationMRMRERYSASKPLKG
HHHHHHHCCCCCCCC		32.0828152594
42PhosphorylationMRERYSASKPLKGAR
HHHHHCCCCCCCCCC		28.9424719451
43UbiquitinationRERYSASKPLKGARI
HHHHCCCCCCCCCCC		54.83-
46UbiquitinationYSASKPLKGARIAGC
HCCCCCCCCCCCHHH		60.08-
100PhosphorylationAKAGIPVYAWKGETD
HHCCCCEEEECCCCC		11.0328152594
127SulfoxidationFKDGPLNMILDDGGD
CCCCCCEEEECCCCC		4.1930846556
136PhosphorylationLDDGGDLTNLIHTKY
ECCCCCHHHHHHHCC		32.49-
142UbiquitinationLTNLIHTKYPQLLPG
HHHHHHHCCCHHCCC		40.55-
143PhosphorylationTNLIHTKYPQLLPGI
HHHHHHCCCHHCCCC		9.4328152594
151MethylationPQLLPGIRGISEETT
CHHCCCCCCCCCCCC		42.16115493215
154PhosphorylationLPGIRGISEETTTGV
CCCCCCCCCCCCCHH		32.0030624053
157PhosphorylationIRGISEETTTGVHNL
CCCCCCCCCCHHHHH		26.1323312004
158PhosphorylationRGISEETTTGVHNLY
CCCCCCCCCHHHHHH		25.4923312004
159PhosphorylationGISEETTTGVHNLYK
CCCCCCCCHHHHHHH		44.6323312004
166UbiquitinationTGVHNLYKMMANGIL
CHHHHHHHHHHCCCE		25.9321890473
166AcetylationTGVHNLYKMMANGIL
CHHHHHHHHHHCCCE		25.9323236377
166UbiquitinationTGVHNLYKMMANGIL
CHHHHHHHHHHCCCE		25.9321890473
174UbiquitinationMMANGILKVPAINVN
HHHCCCEEECEEECC		44.2321906983
183PhosphorylationPAINVNDSVTKSKFD
CEEECCCCCCHHHCC		26.8720873877
185PhosphorylationINVNDSVTKSKFDNL
EECCCCCCHHHCCCC		33.2925159151
186AcetylationNVNDSVTKSKFDNLY
ECCCCCCHHHCCCCC		49.8725953088
186UbiquitinationNVNDSVTKSKFDNLY
ECCCCCCHHHCCCCC		49.8721906983
187PhosphorylationVNDSVTKSKFDNLYG
CCCCCCHHHCCCCCC		29.2328348404
188AcetylationNDSVTKSKFDNLYGC
CCCCCHHHCCCCCCH		59.2925953088
188UbiquitinationNDSVTKSKFDNLYGC
CCCCCHHHCCCCCCH		59.2921890473
188UbiquitinationNDSVTKSKFDNLYGC
CCCCCHHHCCCCCCH		59.2921890473
193PhosphorylationKSKFDNLYGCRESLI
HHHCCCCCCHHHHHH		22.0427273156
195S-nitrosylationKFDNLYGCRESLIDG
HCCCCCCHHHHHHHH		2.4924105792
198PhosphorylationNLYGCRESLIDGIKR
CCCCHHHHHHHHHHH		15.9830576142
204SuccinylationESLIDGIKRATDVMI
HHHHHHHHHHHHCEE		41.3223954790
204AcetylationESLIDGIKRATDVMI
HHHHHHHHHHHHCEE		41.3225953088
204UbiquitinationESLIDGIKRATDVMI
HHHHHHHHHHHHCEE		41.32-
210SulfoxidationIKRATDVMIAGKVAV
HHHHHHCEECCEEEE		1.6130846556
221PhosphorylationKVAVVAGYGDVGKGC
EEEEEECCCHHHHHH		10.6228152594
226AcetylationAGYGDVGKGCAQALR
ECCCHHHHHHHHHHH		51.1426051181
226UbiquitinationAGYGDVGKGCAQALR
ECCCHHHHHHHHHHH		51.1421890473
226UbiquitinationAGYGDVGKGCAQALR
ECCCHHHHHHHHHHH		51.1421890473
233MethylationKGCAQALRGFGARVI
HHHHHHHHHCCCEEE		41.22115493199
291MethylationGRHFEQMKDDAIVCN
CCCHHHCCCCEEEEC		52.75-
291"N6,N6-dimethyllysine"GRHFEQMKDDAIVCN
CCCHHHCCCCEEEEC		52.75-
318UbiquitinationLNENAVEKVNIKPQV
CCCCCEEECCCCCCC		33.70-
318AcetylationLNENAVEKVNIKPQV
CCCCCEEECCCCCCC		33.7025953088
322SumoylationAVEKVNIKPQVDRYR
CEEECCCCCCCEEEE		24.97-
322UbiquitinationAVEKVNIKPQVDRYR
CEEECCCCCCCEEEE		24.97-
322AcetylationAVEKVNIKPQVDRYR
CEEECCCCCCCEEEE		24.9726822725
373AcetylationVMAQIELWTHPDKYP
HHHHEEEECCCCCCC		4.6619608861
379PhosphorylationLWTHPDKYPVGVHFL
EECCCCCCCCCEEEC		15.5528152594
380AcetylationWTHPDKYPVGVHFLP
ECCCCCCCCCEEECC		23.3319608861
389UbiquitinationGVHFLPKKLDEAVAE
CEEECCHHHHHHHHH		60.27-
401AcetylationVAEAHLGKLNVKLTK
HHHHHHCHHHHHHEE		43.1623954790
401UbiquitinationVAEAHLGKLNVKLTK
HHHHHHCHHHHHHEE		43.1619608861
405SuccinylationHLGKLNVKLTKLTEK
HHCHHHHHHEECCHH		49.7323954790
405UbiquitinationHLGKLNVKLTKLTEK
HHCHHHHHHEECCHH		49.73-
405AcetylationHLGKLNVKLTKLTEK
HHCHHHHHHEECCHH		49.7325953088
407PhosphorylationGKLNVKLTKLTEKQA
CHHHHHHEECCHHHH		20.4925056879
408AcetylationKLNVKLTKLTEKQAQ
HHHHHHEECCHHHHH		64.9423954790
408UbiquitinationKLNVKLTKLTEKQAQ
HHHHHHEECCHHHHH		64.9419608861
410PhosphorylationNVKLTKLTEKQAQYL
HHHHEECCHHHHHHH		42.57-
412AcetylationKLTKLTEKQAQYLGM
HHEECCHHHHHHHCC		45.7825953088
412UbiquitinationKLTKLTEKQAQYLGM
HHEECCHHHHHHHCC		45.7821890473
412UbiquitinationKLTKLTEKQAQYLGM
HHEECCHHHHHHHCC		45.7821890473
416PhosphorylationLTEKQAQYLGMSCDG
CCHHHHHHHCCCCCC		14.2921406692
420PhosphorylationQAQYLGMSCDGPFKP
HHHHHCCCCCCCCCC		13.7821406692
426AcetylationMSCDGPFKPDHYRY-
CCCCCCCCCCCCCC-		53.3125953088
430PhosphorylationGPFKPDHYRY-----
CCCCCCCCCC-----		20.9821406692
431MethylationPFKPDHYRY------
CCCCCCCCC------		27.54115493207
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 SAHH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAHH_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 SAHH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XIAP_HUMANXIAPphysical
22939629
SDC1_HUMANSDC1physical
22939629
SPB6_HUMANSERPINB6physical
22939629
SIR1_HUMANSIRT1physical
22939629
VATA_HUMANATP6V1Aphysical
22939629
PAXI_HUMANPXNphysical
21988832
PUR9_HUMANATICphysical
22863883
CAPZB_HUMANCAPZBphysical
22863883
DHX15_HUMANDHX15physical
22863883
EF1A2_HUMANEEF1A2physical
22863883
H2AV_HUMANH2AFVphysical
22863883
HDGF_HUMANHDGFphysical
22863883
MSHR_HUMANMC1Rphysical
22863883
MOES_HUMANMSNphysical
22863883
NSF1C_HUMANNSFL1Cphysical
22863883
PAPS1_HUMANPAPSS1physical
22863883
PYGL_HUMANPYGLphysical
22863883
TBCE_HUMANTBCEphysical
22863883
SAHH_HUMANAHCYphysical
25416956
APBP2_HUMANAPPBP2physical
25416956
CA050_HUMANC1orf50physical
25416956
ANR40_HUMANANKRD40physical
25416956
SAHH2_HUMANAHCYL1physical
26186194
CA050_HUMANC1orf50physical
26186194
ANR40_HUMANANKRD40physical
26186194
CA050_HUMANC1orf50physical
21516116
CA050_HUMANC1orf50physical
28514442
ANR40_HUMANANKRD40physical
28514442
SAHH2_HUMANAHCYL1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613752Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAHH_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-408, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory