SUMF2_HUMAN - dbPTM
SUMF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUMF2_HUMAN
UniProt AC Q8NBJ7
Protein Name Inactive C-alpha-formylglycine-generating enzyme 2 {ECO:0000305}
Gene Name SUMF2 {ECO:0000303|PubMed:15962010, ECO:0000312|HGNC:HGNC:20415}
Organism Homo sapiens (Human).
Sequence Length 301
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Lacks formylglycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1..
Protein Sequence MARHGLPLLPLLSLLVGAWLKLGNGQATSMVQLQGGRFLMGTNSPDSRDGDGPVREATVKPFAIDIFPVTNKDFRDFVREKKYRTEAEMFGWSFVFEDFVSDELRNKATQPMKSVLWWLPVEKAFWRQPAGPGSGIRERLEHPVLHVSWNDARAYCAWRGKRLPTEEEWEFAARGGLKGQVYPWGNWFQPNRTNLWQGKFPKGDKAEDGFHGVSPVNAFPAQNNYGLYDLLGNVWEWTASPYQAAEQDMRVLRGASWIDTADGSANHRARVTTRMGNTPDSASDNLGFRCAADAGRPPGEL
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
40SulfoxidationLQGGRFLMGTNSPDS
EECCEEEECCCCCCC
5.9828465586
42O-linked_GlycosylationGGRFLMGTNSPDSRD
CCEEEECCCCCCCCC
20.68OGP
47O-linked_GlycosylationMGTNSPDSRDGDGPV
ECCCCCCCCCCCCCC
35.3428510447
60UbiquitinationPVREATVKPFAIDIF
CCCCCEECCCEEEEE
30.0221906983
60 (in isoform 4)Ubiquitination-30.0221906983
70PhosphorylationAIDIFPVTNKDFRDF
EEEEEECCCCHHHHH
36.47-
79 (in isoform 3)Ubiquitination-50.4321890473
79UbiquitinationKDFRDFVREKKYRTE
CHHHHHHHHHHHCHH
50.43-
111 (in isoform 2)Ubiquitination-28.0221890473
124 (in isoform 4)Phosphorylation-8.8420068231
132UbiquitinationFWRQPAGPGSGIRER
HHCCCCCCCCCHHHH
35.56-
153MethylationHVSWNDARAYCAWRG
EEEHHHHHHHHHHCC
29.02115918001
162MethylationYCAWRGKRLPTEEEW
HHHHCCCCCCCHHHH
49.04115918005
165PhosphorylationWRGKRLPTEEEWEFA
HCCCCCCCHHHHHHH
61.70-
167 (in isoform 4)Phosphorylation-71.5322210691
170 (in isoform 4)Phosphorylation-28.7822210691
172MethylationTEEEWEFAARGGLKG
CHHHHHHHHHCCCCC
5.68-
174MethylationEEWEFAARGGLKGQV
HHHHHHHHCCCCCEE
35.96115918009
176 (in isoform 4)Phosphorylation-20.7522210691
181MethylationRGGLKGQVYPWGNWF
HCCCCCEEECCCCCC
9.39-
184PhosphorylationLKGQVYPWGNWFQPN
CCCEEECCCCCCCCC
8.61-
191N-linked_GlycosylationWGNWFQPNRTNLWQG
CCCCCCCCCCCCCCC
53.2615687489
193MethylationNWFQPNRTNLWQGKF
CCCCCCCCCCCCCCC
41.10-
197UbiquitinationPNRTNLWQGKFPKGD
CCCCCCCCCCCCCCC
48.65-
199 (in isoform 1)Ubiquitination-43.3121890473
199UbiquitinationRTNLWQGKFPKGDKA
CCCCCCCCCCCCCCC
43.3121906983
199 (in isoform 3)Ubiquitination-43.3121890473
210N-linked_GlycosylationGDKAEDGFHGVSPVN
CCCCCCCCCCCCCCC
7.5815687489
218UbiquitinationHGVSPVNAFPAQNNY
CCCCCCCCCCCCCCC
16.42-
218 (in isoform 3)Ubiquitination-16.4221890473
253MethylationEQDMRVLRGASWIDT
HHHHHHHHCCCEEEC
35.46115918013
272MethylationANHRARVTTRMGNTP
CCHHEEEEEECCCCC
11.79-
275SulfoxidationRARVTTRMGNTPDSA
HEEEEEECCCCCCCH
4.5721406390
278 (in isoform 4)Phosphorylation-23.8122210691
286 (in isoform 4)Phosphorylation-9.1222210691
296 (in isoform 3)Phosphorylation-35.6422210691
304 (in isoform 3)Phosphorylation-22210691

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 SUMF2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUMF2_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 SUMF2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBXW7_HUMANFBXW7physical
16169070
ANR40_HUMANANKRD40physical
26186194
APOD_HUMANAPODphysical
26186194
CLUS_HUMANCLUphysical
26186194
WDR34_HUMANWDR34physical
26186194
APOD_HUMANAPODphysical
28514442
ANR40_HUMANANKRD40physical
28514442

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 SUMF2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme.";
Dickmanns A., Schmidt B., Rudolph M.G., Mariappan M., Dierks T.,von Figura K., Ficner R.;
J. Biol. Chem. 280:15180-15187(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 27-301 IN COMPLEX WITHCALCIUM IONS, GLYCOSYLATION AT ASN-191, AND DISULFIDE BONDS.

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