SIA4A_HUMAN - dbPTM
SIA4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIA4A_HUMAN
UniProt AC Q11201
Protein Name CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
Gene Name ST3GAL1
Organism Homo sapiens (Human).
Sequence Length 340
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein. Secreted. Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Protein Description Responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O-linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values..
Protein Sequence MVTLRKRTLKVLTFLVLFIFLTSFFLNYSHTMVATTWFPKQMVLELSENLKRLIKHRPCTCTHCIGQRKLSAWFDERFNQTMQPLLTAQNALLEDDTYRWWLRLQREKKPNNLNDTIKELFRVVPGNVDPMLEKRSVGCRRCAVVGNSGNLRESSYGPEIDSHDFVLRMNKAPTAGFEADVGTKTTHHLVYPESFRELGDNVSMILVPFKTIDLEWVVSAITTGTISHTYIPVPAKIRVKQDKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSMHVCDEVDLYGFGADSKGNWHHYWENNPSAGAFRKTGVHDADFESNVTATLASINKIRIFKGR
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
27N-linked_GlycosylationFLTSFFLNYSHTMVA
HHHHHHHCCCCCCHH
30.98-
27N-linked_GlycosylationFLTSFFLNYSHTMVA
HHHHHHHCCCCCCHH
30.9811690653
79N-linked_GlycosylationAWFDERFNQTMQPLL
HHHHHHHHHHHHHHH
42.51UniProtKB CARBOHYD
79N-linked_GlycosylationAWFDERFNQTMQPLL
HHHHHHHHHHHHHHH
42.5111690653
81O-linked_GlycosylationFDERFNQTMQPLLTA
HHHHHHHHHHHHHHH
20.91OGP
87O-linked_GlycosylationQTMQPLLTAQNALLE
HHHHHHHHHHHHHHC
33.60OGP
114N-linked_GlycosylationEKKPNNLNDTIKELF
CCCCCCCHHHHHHHH
46.64UniProtKB CARBOHYD
114N-linked_GlycosylationEKKPNNLNDTIKELF
CCCCCCCHHHHHHHH
46.6411690653
148PhosphorylationRCAVVGNSGNLRESS
EEEEECCCCCCCCCC
24.1123879269
201N-linked_GlycosylationSFRELGDNVSMILVP
HHHHHCCCEEEEEEE
26.43UniProtKB CARBOHYD
201N-linked_GlycosylationSFRELGDNVSMILVP
HHHHHCCCEEEEEEE
26.4311690653
225O-linked_GlycosylationVSAITTGTISHTYIP
HHHHHCCCCCCEEEC
19.74OGP
323N-linked_GlycosylationHDADFESNVTATLAS
CCCCCCCCCEEEEHH
28.14UniProtKB CARBOHYD
323N-linked_GlycosylationHDADFESNVTATLAS
CCCCCCCCCEEEEHH
28.1411690653

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 SIA4A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIA4A_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 SIA4A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOLP3_HUMANGOLPH3physical
28514442
ASPH2_HUMANASPHD2physical
28514442
ZNT7_HUMANSLC30A7physical
28514442
AT2B2_HUMANATP2B2physical
28514442
ITAV_HUMANITGAVphysical
28514442
RMND1_HUMANRMND1physical
28514442
ANR46_HUMANANKRD46physical
28514442
CF120_HUMANC6orf120physical
28514442
S39AB_HUMANSLC39A11physical
28514442
UB2J1_HUMANUBE2J1physical
28514442
GPHRA_HUMANGPR89Bphysical
28514442
GPHRB_HUMANGPR89Bphysical
28514442
LMBR1_HUMANLMBR1physical
28514442
METL9_HUMANMETTL9physical
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 SIA4A_HUMAN

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Related Literatures of Post-Translational Modification

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