SIAE_HUMAN - dbPTM
SIAE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIAE_HUMAN
UniProt AC Q9HAT2
Protein Name Sialate O-acetylesterase
Gene Name SIAE
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Lysosome . Secreted.
Protein Description Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid..
Protein Sequence MVAPGLVLGLVLPLILWADRSAGIGFRFASYINNDMVLQKEPAGAVIWGFGTPGATVTVTLRQGQETIMKKVTSVKAHSDTWMVVLDPMKPGGPFEVMAQQTLEKINFTLRVHDVLFGDVWLCSGQSNMQMTVLQIFNATRELSNTAAYQSVRILSVSPIQAEQELEDLVAVDLQWSKPTSENLGHGYFKYMSAVCWLFGRHLYDTLQYPIGLIASSWGGTPIEAWSSGRSLKACGVPKQGSIPYDSVTGPSKHSVLWNAMIHPLCNMTLKGVVWYQGESNINYNTDLYNCTFPALIEDWRETFHRGSQGQTERFFPFGLVQLSSDLSKKSSDDGFPQIRWHQTADFGYVPNPKMPNTFMAVAMDLCDRDSPFGSIHPRDKQTVAYRLHLGARALAYGEKNLTFEGPLPEKIELLAHKGLLNLTYYQQIQVQKKDNKIFEISCCSDHRCKWLPASMNTVSTQSLTLAIDSCHGTVVALRYAWTTWPCEYKQCPLYHPSSALPAPPFIAFITDQGPGHQSNVAK
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
52PhosphorylationAVIWGFGTPGATVTV
EEEEECCCCCCEEEE		19.1127542207
56PhosphorylationGFGTPGATVTVTLRQ
ECCCCCCEEEEEECC		23.7127542207
58PhosphorylationGTPGATVTVTLRQGQ
CCCCCEEEEEECCCC		11.9227542207
60PhosphorylationPGATVTVTLRQGQET
CCCEEEEEECCCCHH		13.5727542207
67PhosphorylationTLRQGQETIMKKVTS
EECCCCHHHHHHEEE		20.6227542207
73PhosphorylationETIMKKVTSVKAHSD
HHHHHHEEEEEECCC		36.3622210691
79PhosphorylationVTSVKAHSDTWMVVL
EEEEEECCCCEEEEE		41.4122210691
81PhosphorylationSVKAHSDTWMVVLDP
EEEECCCCEEEEECC		20.62-
102PhosphorylationFEVMAQQTLEKINFT
HHEEEEHHHHHCCCE		25.4626074081
107N-linked_GlycosylationQQTLEKINFTLRVHD
EHHHHHCCCEEEEEC		34.61UniProtKB CARBOHYD
109PhosphorylationTLEKINFTLRVHDVL
HHHHCCCEEEEECEE		14.7926074081
138N-linked_GlycosylationMTVLQIFNATRELSN
HHHHHHHHHHHHHCC		41.87UniProtKB CARBOHYD
144PhosphorylationFNATRELSNTAAYQS
HHHHHHHCCCHHHCE		27.64-
146PhosphorylationATRELSNTAAYQSVR
HHHHHCCCHHHCEEE		14.86-
231PhosphorylationEAWSSGRSLKACGVP
HHHHCCCCCCCCCCC		37.4325002506
242PhosphorylationCGVPKQGSIPYDSVT
CCCCCCCCCCCCCCC		20.2125002506
245PhosphorylationPKQGSIPYDSVTGPS
CCCCCCCCCCCCCCC		21.1225002506
247PhosphorylationQGSIPYDSVTGPSKH
CCCCCCCCCCCCCHH		18.7425002506
249PhosphorylationSIPYDSVTGPSKHSV
CCCCCCCCCCCHHHH		47.5325002506
252PhosphorylationYDSVTGPSKHSVLWN
CCCCCCCCHHHHHHH		44.3325002506
267N-linked_GlycosylationAMIHPLCNMTLKGVV
HHHHHHHCCEECEEE		33.87UniProtKB CARBOHYD
290N-linked_GlycosylationNYNTDLYNCTFPALI
CCCCCCCCCCHHHHH		26.16UniProtKB CARBOHYD
401N-linked_GlycosylationALAYGEKNLTFEGPL
HHHHCCCCCEEECCC		39.7616399764
401N-linked_GlycosylationALAYGEKNLTFEGPL
HHHHCCCCCEEECCC		39.7616399764
403O-linked_GlycosylationAYGEKNLTFEGPLPE
HHCCCCCEEECCCHH		29.0928657654
422N-linked_GlycosylationLAHKGLLNLTYYQQI
HHHCCHHHEEEEEEE		35.0716399764
422N-linked_GlycosylationLAHKGLLNLTYYQQI
HHHCCHHHEEEEEEE		35.0716399764
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 SIAE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIAE_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 SIAE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBPE_HUMANCPEphysical
26186194
1B07_HUMANHLA-Bphysical
26186194
1B18_HUMANHLA-Bphysical
26186194
ENTP6_HUMANENTPD6physical
26186194
NPTX1_HUMANNPTX1physical
26186194
CNTP3_HUMANCNTNAP3physical
26186194
MANEL_HUMANMANEALphysical
26186194
OAF_HUMANOAFphysical
26186194
CC50A_HUMANTMEM30Aphysical
26186194
HMR1_HUMANMR1physical
26186194
COCH_HUMANCOCHphysical
26186194
F162A_HUMANFAM162Aphysical
26186194
GPR98_HUMANGPR98physical
26186194
GFPT2_HUMANGFPT2physical
26186194
MOXD1_HUMANMOXD1physical
26186194
LCAP_HUMANLNPEPphysical
26186194
PLXB2_HUMANPLXNB2physical
26186194
TECT1_HUMANTCTN1physical
26186194
POC1A_HUMANPOC1Aphysical
26186194
NDST2_HUMANNDST2physical
26186194
SPHM_HUMANSGSHphysical
26186194
TEN3_HUMANTENM3physical
26186194
ERAP1_HUMANERAP1physical
26186194
MANBA_HUMANMANBAphysical
26186194
ITA8_HUMANITGA8physical
26186194
TMEM2_HUMANTMEM2physical
26186194
LAMB2_HUMANLAMB2physical
26186194
FAKD3_HUMANFASTKD3physical
26186194
CHSS3_HUMANCHSY3physical
26186194
GDF11_HUMANGDF11physical
26186194
DDX47_HUMANDDX47physical
26186194
TM131_HUMANTMEM131physical
26186194
ARSK_HUMANARSKphysical
26186194
ARSB_HUMANARSBphysical
26186194
MBTP1_HUMANMBTPS1physical
26186194
COIA1_HUMANCOL18A1physical
26186194
MANEA_HUMANMANEAphysical
26186194
NAAA_HUMANNAAAphysical
26186194
RPP38_HUMANRPP38physical
26186194
NRP2_HUMANNRP2physical
26186194
FPRP_HUMANPTGFRNphysical
26186194
PLTP_HUMANPLTPphysical
26186194
K1161_HUMANKIAA1161physical
26186194
DCBD2_HUMANDCBLD2physical
26186194
SELN_HUMANSEPN1physical
26186194
GALT7_HUMANGALNT7physical
26186194
TGBR3_HUMANTGFBR3physical
26186194
MA2B2_HUMANMAN2B2physical
26186194
T132A_HUMANTMEM132Aphysical
26186194
NAAA_HUMANNAAAphysical
28514442
COIA1_HUMANCOL18A1physical
28514442
CNTP3_HUMANCNTNAP3physical
28514442
PLTP_HUMANPLTPphysical
28514442
GDF11_HUMANGDF11physical
28514442
MANEL_HUMANMANEALphysical
28514442
CBPE_HUMANCPEphysical
28514442
OAF_HUMANOAFphysical
28514442
DCBD2_HUMANDCBLD2physical
28514442
TEN3_HUMANTENM3physical
28514442
NPTX1_HUMANNPTX1physical
28514442
LCAP_HUMANLNPEPphysical
28514442
ARSB_HUMANARSBphysical
28514442
CHSS3_HUMANCHSY3physical
28514442
MA2B2_HUMANMAN2B2physical
28514442
NDST2_HUMANNDST2physical
28514442
TMEM2_HUMANTMEM2physical
28514442
POC1A_HUMANPOC1Aphysical
28514442
LAMB2_HUMANLAMB2physical
28514442
K1161_HUMANKIAA1161physical
28514442
1B07_HUMANHLA-Bphysical
28514442
1B18_HUMANHLA-Bphysical
28514442
COCH_HUMANCOCHphysical
28514442
GALNS_HUMANGALNSphysical
28514442
TGBR3_HUMANTGFBR3physical
28514442
ARSK_HUMANARSKphysical
28514442
ANAG_HUMANNAGLUphysical
28514442
NRP2_HUMANNRP2physical
28514442
TECT1_HUMANTCTN1physical
28514442
CATF_HUMANCTSFphysical
28514442
MBTP1_HUMANMBTPS1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613551Autoimmune disease 6 (AIS6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIAE_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-401 AND ASN-422, AND MASSSPECTROMETRY.

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