SULF1_HUMAN - dbPTM
SULF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SULF1_HUMAN
UniProt AC Q8IWU6
Protein Name Extracellular sulfatase Sulf-1
Gene Name SULF1
Organism Homo sapiens (Human).
Sequence Length 871
Subcellular Localization Endoplasmic reticulum. Golgi apparatus, Golgi stack. Cell surface. Also localized on the cell surface..
Protein Description Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin. Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation..
Protein Sequence MKYSCCALVLAVLGTELLGSLCSTVRSPRFRGRIQQERKNIRPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRTNKKAKIWRDTFLVERGKFLRKKEESSKNIQQSNHLPKYERVKELCQQARYQTACEQPGQKWQCIEDTSGKLRIHKCKGPSDLLTVRQSTRNLYARGFHDKDKECSCRESGYRASRSQRKSQRQFLRNQGTPKYKPRFVHTRQTRSLSVEFEGEIYDINLEEEEELQVLQPRNIAKRHDEGHKGPRDLQASSGGNRGRMLADSSNAVGPPTTVRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSKQSYYNKEKGVKKQEKLKSHLHPFKEAAQEVDSKLQLFKENNRRRKKERKEKRRQRKGEECSLPGLTCFTHDNNHWQTAPFWNLGSFCACTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTVERGILNQLHVQLMELRSCQGYKQCNPRPKNLDVGNKDGGSYDLHRGQLWDGWEG
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
24PhosphorylationLLGSLCSTVRSPRFR
HHHHHHHHHCCHHHH		20.95-
64N-linked_GlycosylationLGSLQVMNKTRKIME
CCCEECHHHHHHHHH		43.63UniProtKB CARBOHYD
76PhosphorylationIMEHGGATFINAFVT
HHHHCCEEEEEECEE		28.46-
83PhosphorylationTFINAFVTTPMCCPS
EEEEECEECCCCCCC		20.8024719451
87OxidationAFVTTPMCCPSRSSM
ECEECCCCCCCCHHH		3.04-
873-oxoalanine (Cys)AFVTTPMCCPSRSSM
ECEECCCCCCCCHHH		3.04-
90PhosphorylationTTPMCCPSRSSMLTG
ECCCCCCCCHHHHCC		30.7724719451
93PhosphorylationMCCPSRSSMLTGKYV
CCCCCCHHHHCCCEE		19.39-
96PhosphorylationPSRSSMLTGKYVHNH
CCCHHHHCCCEEECC		24.00-
111N-linked_GlycosylationNVYTNNENCSSPSWQ
CEECCCCCCCCCCHH		32.85UniProtKB CARBOHYD
131N-linked_GlycosylationRTFAVYLNNTGYRTA
CEEEEEECCCCCCEE		26.74UniProtKB CARBOHYD
148N-linked_GlycosylationGKYLNEYNGSYIPPG
HHHHHHCCCCCCCCC		27.10UniProtKB CARBOHYD
170N-linked_GlycosylationIKNSRFYNYTVCRNG
HHCCCCCCEEEECCC		24.24UniProtKB CARBOHYD
186PhosphorylationKEKHGFDYAKDYFTD
CHHHCCCHHHHHHHH		17.1826074081
190PhosphorylationGFDYAKDYFTDLITN
CCCHHHHHHHHHHCC		13.9926074081
192PhosphorylationDYAKDYFTDLITNES
CHHHHHHHHHHCCCC		24.5426074081
196PhosphorylationDYFTDLITNESINYF
HHHHHHHCCCCCCCH		39.9826074081
197N-linked_GlycosylationYFTDLITNESINYFK
HHHHHHCCCCCCCHH		33.7419159218
199PhosphorylationTDLITNESINYFKMS
HHHHCCCCCCCHHCC		20.4326074081
202PhosphorylationITNESINYFKMSKRM
HCCCCCCCHHCCCCC		11.6926074081
220PhosphorylationRPVMMVISHAAPHGP
CCEEEEEECCCCCCC		8.8227067055
238PhosphorylationAPQFSKLYPNASQHI
CCCHHHHCCCHHHCC		9.7430177828
240N-linked_GlycosylationQFSKLYPNASQHITP
CHHHHCCCHHHCCCC		38.37UniProtKB CARBOHYD
242PhosphorylationSKLYPNASQHITPSY
HHHCCCHHHCCCCCC		29.0030177828
246PhosphorylationPNASQHITPSYNYAP
CCHHHCCCCCCCCCC		12.2130177828
248PhosphorylationASQHITPSYNYAPNM
HHHCCCCCCCCCCCC		19.8430177828
249PhosphorylationSQHITPSYNYAPNMD
HHCCCCCCCCCCCCC		17.2530177828
251PhosphorylationHITPSYNYAPNMDKH
CCCCCCCCCCCCCCC		18.4030177828
285PhosphorylationLQRKRLQTLMSVDDS
HHHHHHHHHCCCCHH		29.0824275569
288PhosphorylationKRLQTLMSVDDSVER
HHHHHHCCCCHHHHH		26.0524275569
367PhosphorylationLNIDLAPTILDIAGL
ECCCCCCCCHHHCCC		28.68-
417AcetylationTFLVERGKFLRKKEE
HHHHHHHHHHHHHHH		47.667296879
432PhosphorylationSSKNIQQSNHLPKYE
HCCCHHHHCCCCHHH		15.1629978859
438PhosphorylationQSNHLPKYERVKELC
HHCCCCHHHHHHHHH		13.66-
480PhosphorylationIHKCKGPSDLLTVRQ
EEECCCHHHHHHHHH		49.9430257219
623N-linked_GlycosylationHKCFILPNDSIHCER
EEEEECCCCCCCCCH		52.82UniProtKB CARBOHYD
648UbiquitinationDHKAYIDKEIEALQD
HHHHHHHHHHHHHHH		51.54-
656UbiquitinationEIEALQDKIKNLREV
HHHHHHHHHHHHHHH		42.49-
678PhosphorylationKPEECSCSKQSYYNK
CCCCCCCCHHHHCCH		19.8930576142
682PhosphorylationCSCSKQSYYNKEKGV
CCCCHHHHCCHHCCC		14.4730576142
683PhosphorylationSCSKQSYYNKEKGVK
CCCHHHHCCHHCCCC		25.6330576142
773N-linked_GlycosylationCACTSSNNNTYWCLR
EEEECCCCCEEEEEE		44.14UniProtKB CARBOHYD
783N-linked_GlycosylationYWCLRTVNETHNFLF
EEEEEECCCCCCCHH		48.08UniProtKB CARBOHYD
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 SULF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SULF1_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 SULF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 SULF1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197, AND MASSSPECTROMETRY.

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