SUFU_HUMAN - dbPTM
SUFU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUFU_HUMAN
UniProt AC Q9UMX1
Protein Name Suppressor of fused homolog
Gene Name SUFU
Organism Homo sapiens (Human).
Sequence Length 484
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Negative regulator in the hedgehog/smoothened signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. [PubMed: 15367681]
Protein Sequence MAELRPSGAPGPTAPPAPGPTAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWLGGPDPLDYVSMYRNVGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICIGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINPQRQNGLAHDRAPSRKDSLESDSSTAIIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH
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
13PhosphorylationPSGAPGPTAPPAPGP
CCCCCCCCCCCCCCC		58.68-
21PhosphorylationAPPAPGPTAPPAFAS
CCCCCCCCCCCHHHH		58.68-
257 (in isoform 1)Ubiquitination-59.9521890473
257UbiquitinationHLQERVDKGIETDGS
HHHHHHHHCCCCCCC		59.9518997815
257 (in isoform 2)Ubiquitination-59.9521890473
257 (in isoform 3)Ubiquitination-59.9521890473
267PhosphorylationETDGSNLSGVSAKCA
CCCCCCCCCCCCCCC		41.2025627689
290PhosphorylationEDDEDSRSICIGTQP
CCCCCCCCEEEECCC		26.2623403867
295PhosphorylationSRSICIGTQPRRLSG
CCCEEEECCCCCCCC		18.5823403867
301PhosphorylationGTQPRRLSGKDTEQI
ECCCCCCCCCCHHHH		41.8223927012
303UbiquitinationQPRRLSGKDTEQIRE
CCCCCCCCCHHHHHH		59.0919608861
303AcetylationQPRRLSGKDTEQIRE
CCCCCCCCCHHHHHH		59.0919608861
305PhosphorylationRRLSGKDTEQIRETL
CCCCCCCHHHHHHHH		33.0223403867
311PhosphorylationDTEQIRETLRRGLEI
CHHHHHHHHHHHCCC		18.7328555341
321 (in isoform 2)Ubiquitination-34.3621890473
321 (in isoform 1)Ubiquitination-34.3621890473
321 (in isoform 3)Ubiquitination-34.3621890473
321UbiquitinationRGLEINSKPVLPPIN
HHCCCCCCCCCCCCC		34.3621890473
321SumoylationRGLEINSKPVLPPIN
HHCCCCCCCCCCCCC		34.3628112733
342PhosphorylationLAHDRAPSRKDSLES
CCCCCCCCCHHCCCC		51.4826055452
344UbiquitinationHDRAPSRKDSLESDS
CCCCCCCHHCCCCCC		56.88-
346PhosphorylationRAPSRKDSLESDSST
CCCCCHHCCCCCCCC		36.7529255136
349PhosphorylationSRKDSLESDSSTAII
CCHHCCCCCCCCEEC		48.3530266825
351PhosphorylationKDSLESDSSTAIIPH
HHCCCCCCCCEECCH		38.5830278072
352PhosphorylationDSLESDSSTAIIPHE
HCCCCCCCCEECCHH		27.1830278072
353PhosphorylationSLESDSSTAIIPHEL
CCCCCCCCEECCHHH		26.3123927012
368PhosphorylationIRTRQLESVHLKFNQ
HHCCCCEEEEEEEEC		24.3529083192
399 (in isoform 2)Phosphorylation-18.2424043423
401 (in isoform 2)Phosphorylation-33.9324043423
407 (in isoform 2)Phosphorylation-14.4024043423
410 (in isoform 2)Phosphorylation-18.4324043423
411 (in isoform 2)Phosphorylation-39.6924043423
419 (in isoform 2)Phosphorylation-35.1424043423
424 (in isoform 2)Phosphorylation-20.5124043423
457 (in isoform 1)Ubiquitination-68.1321890473
457UbiquitinationLTSPEEFKLPKEYSW
CCCHHHHCCCCCCCC		68.132190698
470UbiquitinationSWPEKKLKVSILPDV
CCCCHHCCEEECCCC		42.70-
481PhosphorylationLPDVVFDSPLH----
CCCCCCCCCCC----		20.2130266825
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
342SPhosphorylationKinaseGSK3BP49841
PSP
346SPhosphorylationKinasePRKACAP17612
GPS
346SPhosphorylationKinasePKA-FAMILY-GPS
-KUbiquitinationE3 ubiquitin ligaseFBXL17Q9UF56
PMID:27234298
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:29515120
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
257Kubiquitylation

27234298
342SPhosphorylation

23186163
342SPhosphorylation

23186163
342Subiquitylation

23186163
342Subiquitylation

23186163
346Subiquitylation

23186163
346Subiquitylation

23186163
346SPhosphorylation

23186163
346SPhosphorylation

23186163
352SPhosphorylation

27234298
352SPhosphorylation

27234298
352Subiquitylation

27234298
352Subiquitylation

27234298
353TPhosphorylation

27234298
353TPhosphorylation

27234298
353Tubiquitylation

27234298
353Tubiquitylation

27234298
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 SUFU_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLIS3_HUMANGLIS3physical
16189514
RCN3_HUMANRCN3physical
16189514
ZN446_HUMANZNF446physical
16189514
ZN764_HUMANZNF764physical
16189514
M1IP1_HUMANMID1IP1physical
16189514
PEX26_HUMANPEX26physical
16189514
SUFU_HUMANSUFUphysical
10564661
GLI2_HUMANGLI2physical
10564661
GLI3_HUMANGLI3physical
10564661
GLI1_HUMANGLI1physical
10559945
GLI1_HUMANGLI1physical
12426310
ZN747_HUMANZNF747physical
20211142
HDX_HUMANHDXphysical
20211142
SAP18_HUMANSAP18physical
17002296
GLIS3_HUMANGLIS3physical
21543335
GLI1_HUMANGLI1physical
21543335
GLIS3_MOUSEGlis3physical
21543335
ZN747_HUMANZNF747physical
25416956
GLI1_HUMANGLI1physical
25241761
FXL17_HUMANFBXL17physical
27234298
GLI1_HUMANGLI1physical
27234298
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
155255Medulloblastoma (MDB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUFU_HUMAN

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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-303, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASSSPECTROMETRY.

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