SULF2_HUMAN - dbPTM
SULF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SULF2_HUMAN
UniProt AC Q8IWU5
Protein Name Extracellular sulfatase Sulf-2
Gene Name SULF2
Organism Homo sapiens (Human).
Sequence Length 870
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..
Protein Sequence MGPPSLVLCLLSATVFSLLGGSSAFLSHHRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHGSDYSKDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNRFHLKKKMRVWRDSFLVERGKLLHKRDNDKVDAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDATGKLKLHKCKGPMRLGGSRALSNLVPKYYGQGSEACTCDSGDYKLSLAGRRKKLFKKKYKASYVRSRSIRSVAIEVDGRVYHVGLGDAAQPRNLTKRHWPGAPEDQDDKDGGDFSGTGGLPDYSAANPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHKISYHTQHKGRLKHRGSSLHPFRKGLQEKDKVWLLREQKRKKKLRKLLKRLQNNDTCSMPGLTCFTHDNQHWQTAPFWTLGPFCACTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNAVNTLDRDVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLKDGGSYEQYRQFQRRKWPEMKRPSSKSLGQLWEGWEG
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
5Phosphorylation---MGPPSLVLCLLS
---CCCHHHHHHHHH		33.9524505115
14PhosphorylationVLCLLSATVFSLLGG
HHHHHHHHHHHHHCC		20.7824505115
22PhosphorylationVFSLLGGSSAFLSHH
HHHHHCCCHHHHCHH		19.3924719451
27PhosphorylationGGSSAFLSHHRLKGR
CCCHHHHCHHHHCCC		15.7024505115
65N-linked_GlycosylationLGSMQVMNKTRRIME
HHHHHHHHHHHHHHH		43.63UniProtKB CARBOHYD
883-oxoalanine (Cys)AFVTTPMCCPSRSSI
EEEECCCCCCCCCHH		3.04-
88OxidationAFVTTPMCCPSRSSI
EEEECCCCCCCCCHH		3.04-
112N-linked_GlycosylationNTYTNNENCSSPSWQ
CCCCCCCCCCCCCHH		32.85UniProtKB CARBOHYD
130PhosphorylationESRTFAVYLNSTGYR
CCCEEEEEECCCCCC		9.20-
132N-linked_GlycosylationRTFAVYLNSTGYRTA
CEEEEEECCCCCCCH		21.60UniProtKB CARBOHYD
148PhosphorylationFGKYLNEYNGSYVPP
HHHHHHHCCCCCCCC		24.61-
149N-linked_GlycosylationGKYLNEYNGSYVPPG
HHHHHHCCCCCCCCC		27.10UniProtKB CARBOHYD
152PhosphorylationLNEYNGSYVPPGWKE
HHHCCCCCCCCCHHH		20.55-
171N-linked_GlycosylationLKNSRFYNYTLCRNG
HHCCCCCCEEEECCC		22.17UniProtKB CARBOHYD
198N-linked_GlycosylationYLTDLITNDSVSFFR
HHHHHHCCCCCCCCC		32.3419159218
202PhosphorylationLITNDSVSFFRTSKK
HHCCCCCCCCCCCCC		23.7124719451
241N-linked_GlycosylationQYSRLFPNASQHITP
CHHHHCCCHHHCCCC		44.91UniProtKB CARBOHYD
269AcetylationMRYTGPMKPIHMEFT
HHHCCCCCCCCHHHH		43.9119821039
282AcetylationFTNMLQRKRLQTLMS
HHHHHHHHHHHHHHC		44.4919821045
286PhosphorylationLQRKRLQTLMSVDDS
HHHHHHHHHHCCCHH		29.0824275569
289PhosphorylationKRLQTLMSVDDSMET
HHHHHHHCCCHHHHH		26.05-
368PhosphorylationLNIDLAPTILDIAGL
EEEECCCCHHHHCCC		28.68-
385PhosphorylationPADMDGKSILKLLDT
CCCCCCHHHHHHHCC		38.3924719451
497PhosphorylationSNLVPKYYGQGSEAC
HHCCCCCCCCCCCCE		14.75-
514PhosphorylationDSGDYKLSLAGRRKK
CCCCEEEEECHHHHH		16.4224719451
561N-linked_GlycosylationGDAAQPRNLTKRHWP
CCCCCCCCCCCCCCC		59.76UniProtKB CARBOHYD
608N-linked_GlycosylationHRCYILENDTVQCDL
EEEEEECCCEEEECH		46.97UniProtKB CARBOHYD
692UbiquitinationFRKGLQEKDKVWLLR
CHHHCCHHHHHHHHH		50.3022817900
693UbiquitinationRKGLQEKDKVWLLRE
HHHCCHHHHHHHHHH		50.4122817900
694 (in isoform 1)Ubiquitination-46.5121890473
694 (in isoform 2)Ubiquitination-46.5121890473
694UbiquitinationKGLQEKDKVWLLREQ
HHCCHHHHHHHHHHH		46.5121890473
695UbiquitinationGLQEKDKVWLLREQK
HCCHHHHHHHHHHHH		6.6321890473
717N-linked_GlycosylationLLKRLQNNDTCSMPG
HHHHHHCCCCCCCCC		32.76UniProtKB CARBOHYD
754N-linked_GlycosylationCACTSANNNTYWCMR
EEEECCCCCEEEEEE		41.77UniProtKB CARBOHYD
764N-linked_GlycosylationYWCMRTINETHNFLF
EEEEEECCCCCCCHH		47.72UniProtKB CARBOHYD
834 (in isoform 1)Ubiquitination-53.1521890473
834UbiquitinationRNMDLGLKDGGSYEQ
CCCCCCCCCCCCHHH		53.1522817900
835UbiquitinationNMDLGLKDGGSYEQY
CCCCCCCCCCCHHHH		72.2621890473
838PhosphorylationLGLKDGGSYEQYRQF
CCCCCCCCHHHHHHH		30.9029691806
839PhosphorylationGLKDGGSYEQYRQFQ
CCCCCCCHHHHHHHH		15.4427794612
842PhosphorylationDGGSYEQYRQFQRRK
CCCCHHHHHHHHHCC		8.4027794612
851UbiquitinationQFQRRKWPEMKRPSS
HHHHCCCHHHCCCCC		34.5322817900
854UbiquitinationRRKWPEMKRPSSKSL
HCCCHHHCCCCCCCH		60.5422817900
855UbiquitinationRKWPEMKRPSSKSLG
CCCHHHCCCCCCCHH		34.7122817900
856 (in isoform 2)Ubiquitination-37.1221890473
856UbiquitinationKWPEMKRPSSKSLGQ
CCHHHCCCCCCCHHH		37.1221890473
859 (in isoform 1)Ubiquitination-54.7821890473
859UbiquitinationEMKRPSSKSLGQLWE
HHCCCCCCCHHHHHC		54.7822817900
860UbiquitinationMKRPSSKSLGQLWEG
HCCCCCCCHHHHHCC		39.4121890473
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 SULF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SULF2_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 SULF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SULF2_HUMAN !!
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 SULF2_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-198, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14, AND MASSSPECTROMETRY.

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