SPTC2_HUMAN - dbPTM
SPTC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPTC2_HUMAN
UniProt AC O15270
Protein Name Serine palmitoyltransferase 2
Gene Name SPTLC2
Organism Homo sapiens (Human).
Sequence Length 562
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein.
Protein Description Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate..
Protein Sequence MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFNEAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRHRLVPLLDRPFDETTYEETED
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
32PhosphorylationVRNGYVRSSAAAAAA
EECCCCCHHHHHHHH		17.8128857561
33PhosphorylationRNGYVRSSAAAAAAA
ECCCCCHHHHHHHHH		16.0328857561
127PhosphorylationNFYTRNLYMRIRDNW
HHHHCCHHHHHHCCC		6.4624043423
161UbiquitinationHDYNWSFKYTGNIIK
CCCCCCEEECCCEEE		36.0721890473
176PhosphorylationGVINMGSYNYLGFAR
EEEECCCCEEEECCC		11.33-
178PhosphorylationINMGSYNYLGFARNT
EECCCCEEEECCCCC		10.4421552520
194UbiquitinationSCQEAAAKVLEEYGA
CHHHHHHHHHHHHCC		42.50-
215UbiquitinationQEIGNLDKHEELEEL
HHHCCCCHHHHHHHH		56.96-
281MalonylationGATIRIFKHNNMQSL
CCEEEEEECCCHHHH		42.9526320211
281MethylationGATIRIFKHNNMQSL
CCEEEEEECCCHHHH		42.95115980573
293MalonylationQSLEKLLKDAIVYGQ
HHHHHHHHHHHHHCC		56.3930639696
293UbiquitinationQSLEKLLKDAIVYGQ
HHHHHHHHHHHHHCC		56.39-
298PhosphorylationLLKDAIVYGQPRTRR
HHHHHHHHCCCCCCC		12.1624719451
303PhosphorylationIVYGQPRTRRPWKKI
HHHCCCCCCCCHHHH		37.4024719451
362PhosphorylationTGRGVVEYFGLDPED
CCCCCHHHCCCCHHH		7.4323401153
376PhosphorylationDVDVMMGTFTKSFGA
HCCEEEEECCCCCCC		15.3823401153
378PhosphorylationDVMMGTFTKSFGASG
CEEEEECCCCCCCCC		26.1423401153
379OtherVMMGTFTKSFGASGG
EEEEECCCCCCCCCC		39.33-
379N6-(pyridoxal phosphate)lysineVMMGTFTKSFGASGG
EEEEECCCCCCCCCC		39.33-
384PhosphorylationFTKSFGASGGYIGGK
CCCCCCCCCCCCCCC		32.8822817900
387PhosphorylationSFGASGGYIGGKKEL
CCCCCCCCCCCCHHH		10.4222817900
391UbiquitinationSGGYIGGKKELIDYL
CCCCCCCCHHHHHHH		37.55-
392UbiquitinationGGYIGGKKELIDYLR
CCCCCCCHHHHHHHH		62.11-
402PhosphorylationIDYLRTHSHSAVYAT
HHHHHHCCCCCEEEC		20.65-
409PhosphorylationSHSAVYATSLSPPVV
CCCCEEECCCCHHHH		16.71-
412PhosphorylationAVYATSLSPPVVEQI
CEEECCCCHHHHHHH		27.25-
432PhosphorylationCIMGQDGTSLGKECV
HHHCCCCCHHHHHHH		29.12-
433PhosphorylationIMGQDGTSLGKECVQ
HHCCCCCHHHHHHHH		40.43-
436UbiquitinationQDGTSLGKECVQQLA
CCCCHHHHHHHHHHH		53.91-
474PhosphorylationPVVPLMLYMPAKIGA
CCEEEEEEEEHHHCH		6.2622817900
501PhosphorylationVVVGFPATPIIESRA
EEEECCCCHHHHHHH		18.4328348404
513PhosphorylationSRARFCLSAAHTKEI
HHHHHHHHHHCHHHH		25.2929414761
538UbiquitinationVGDLLQLKYSRHRLV
HHHHHHHHHCCCCCH		28.3721890473
550MethylationRLVPLLDRPFDETTY
CCHHCCCCCCCCCCC		33.48115917673
555PhosphorylationLDRPFDETTYEETED
CCCCCCCCCCCCCCC		36.2026552605
556PhosphorylationDRPFDETTYEETED-
CCCCCCCCCCCCCC-		27.2127251275
557PhosphorylationRPFDETTYEETED--
CCCCCCCCCCCCC--		21.1328796482
560PhosphorylationDETTYEETED-----
CCCCCCCCCC-----		33.2526552605
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 SPTC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPTC2_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 SPTC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPTC2_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613640Neuropathy, hereditary sensory and autonomic, 1C (HSAN1C)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00133L-Serine
Regulatory Network of SPTC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND TYR-387, ANDMASS SPECTROMETRY.

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