SCLY_HUMAN - dbPTM
SCLY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCLY_HUMAN
UniProt AC Q96I15
Protein Name Selenocysteine lyase
Gene Name SCLY
Organism Homo sapiens (Human).
Sequence Length 445
Subcellular Localization Cytoplasm, cytosol.
Protein Description Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium..
Protein Sequence MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGNPSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTSKGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDILAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCNFSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGRSTTRAEVDLVVQDLKQAVAQLEDQA
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-------MEAAVAPG
-------CCCCCCCC
7.7422814378
17PhosphorylationDAPAPAASQPSGCGK
CCCCCCCCCCCCCCC
44.7423312004
20PhosphorylationAPAASQPSGCGKHNS
CCCCCCCCCCCCCCC
38.7923312004
24UbiquitinationSQPSGCGKHNSPERK
CCCCCCCCCCCCCCC
43.63-
27PhosphorylationSGCGKHNSPERKVYM
CCCCCCCCCCCCEEE
28.0530624053
31UbiquitinationKHNSPERKVYMDYNA
CCCCCCCCEEECCCC
35.73-
32UbiquitinationHNSPERKVYMDYNAT
CCCCCCCEEECCCCC
6.32-
33PhosphorylationNSPERKVYMDYNATT
CCCCCCEEECCCCCC
6.31-
36PhosphorylationERKVYMDYNATTPLE
CCCEEECCCCCCCCC
7.08-
39UbiquitinationVYMDYNATTPLEPEV
EEECCCCCCCCCHHH
25.88-
63PhosphorylationEAWGNPSSPYSAGRK
HHHCCCCCCCCCCHH
29.16-
70AcetylationSPYSAGRKAKDIINA
CCCCCCHHHHHHHHH
59.8925953088
80UbiquitinationDIINAARESLAKMIG
HHHHHHHHHHHHHHC
45.43-
81PhosphorylationIINAARESLAKMIGG
HHHHHHHHHHHHHCC
28.2423911959
89PhosphorylationLAKMIGGKPQDIIFT
HHHHHCCCCCEEEEE
34.00-
89MethylationLAKMIGGKPQDIIFT
HHHHHCCCCCEEEEE
34.00-
89UbiquitinationLAKMIGGKPQDIIFT
HHHHHCCCCCEEEEE
34.00-
97UbiquitinationPQDIIFTSGGTESNN
CCEEEEECCCCCCCC
25.20-
124PhosphorylationNQTSKGHTGGHHSPV
CCCCCCCCCCCCCCC
54.2320068231
129PhosphorylationGHTGGHHSPVKGAKP
CCCCCCCCCCCCCCC
26.2230631047
132PhosphorylationGGHHSPVKGAKPHFI
CCCCCCCCCCCCCEE
57.4420068231
137PhosphorylationPVKGAKPHFITSSVE
CCCCCCCCEECCCCC
26.4919651622
140UbiquitinationGAKPHFITSSVEHDS
CCCCCEECCCCCCCC
17.63-
140PhosphorylationGAKPHFITSSVEHDS
CCCCCEECCCCCCCC
17.6323312004
141PhosphorylationAKPHFITSSVEHDSI
CCCCEECCCCCCCCC
27.8023312004
142PhosphorylationKPHFITSSVEHDSIR
CCCEECCCCCCCCCC
23.9120068231
143UbiquitinationPHFITSSVEHDSIRL
CCEECCCCCCCCCCC
8.30-
147PhosphorylationTSSVEHDSIRLPLEH
CCCCCCCCCCCCHHH
16.1220068231
150PhosphorylationVEHDSIRLPLEHLVE
CCCCCCCCCHHHHHH
5.6020068231
222UbiquitinationALNQERVAAGLPPIL
HHHHHHHHCCCCCEE
11.31-
240UbiquitinationDAAQALGKQRVDVED
HHHHHHCCCCCCHHH
35.46-
248UbiquitinationQRVDVEDLGVDFLTI
CCCCHHHHCCCEEEE
4.57-
259OtherFLTIVGHKFYGPRIG
EEEECCCCCCCCCCE
34.06-
259N6-(pyridoxal phosphate)lysineFLTIVGHKFYGPRIG
EEEECCCCCCCCCCE
34.06-
280PhosphorylationLGEFTPLYPMLFGGG
CCCCCCCCCCCCCCC
6.4418180459
288PhosphorylationPMLFGGGQERNFRPG
CCCCCCCCCCCCCCC
50.15-
307UbiquitinationPMIAGLGKAAELVTQ
CCCCCCHHHHHHHHH
49.84-
315UbiquitinationAAELVTQNCEAYEAH
HHHHHHHHHHHHHHH
19.07-
341UbiquitinationLEAEFGQKRIHLNSQ
HHHHHCCCCEECCCC
54.41-
341AcetylationLEAEFGQKRIHLNSQ
HHHHHCCCCEECCCC
54.4125953088
349UbiquitinationRIHLNSQFPGTQRLP
CEECCCCCCCCCCCC
6.38-
352PhosphorylationLNSQFPGTQRLPNTC
CCCCCCCCCCCCCCC
15.6822210691
362PhosphorylationLPNTCNFSIRGPRLQ
CCCCCCEEEECCCCC
9.4428857561

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 SCLY_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCLY_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 SCLY_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAK2_HUMANPAK2physical
22863883
UBFD1_HUMANUBFD1physical
22863883
ZN622_HUMANZNF622physical
22863883
KAT1_HUMANCCBL1physical
26344197
HYI_HUMANHYIphysical
26344197
IDE_HUMANIDEphysical
26344197
NTF2_HUMANNUTF2physical
26344197
WDR1_HUMANWDR1physical
26344197

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 SCLY_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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