SPTC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SPTC1_HUMAN
• UniProt AC: O15269
• Protein Name: Serine palmitoyltransferase 1
• Gene Name: SPTLC1
• Organism: Homo sapiens (Human).
• Sequence Length: 473
• Subcellular Localization: Endoplasmic reticulum membrane; Single-pass membrane protein.
• Protein Description: Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 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-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference..
• Protein Sequence: MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEELIEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCMNRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL

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
3	Phosphorylation	-----MATATEQWVL -----CCCHHHHHHH	32.58	24043423
5	Phosphorylation	---MATATEQWVLVE ---CCCHHHHHHHHH	25.10	24043423
18	Phosphorylation	VEMVQALYEAPAYHL HHHHHHHHHCCHHHH	17.04	24043423
23	Phosphorylation	ALYEAPAYHLILEGI HHHHCCHHHHHHHHH	8.97	24043423
41	Phosphorylation	WIIRLLFSKTYKLQE HHHHHHHCCCCCCHH	24.85	24719451
44	Phosphorylation	RLLFSKTYKLQERSD HHHHCCCCCCHHCCC	17.28	22817900
45	Ubiquitination	LLFSKTYKLQERSDL HHHCCCCCCHHCCCC	49.26	21890473
45	Ubiquitination	LLFSKTYKLQERSDL HHHCCCCCCHHCCCC	49.26	21890473
50	Phosphorylation	TYKLQERSDLTVKEK CCCCHHCCCCCHHHH	35.90	22167270
53	Phosphorylation	LQERSDLTVKEKEEL CHHCCCCCHHHHHHH	34.23	22167270
55	Ubiquitination	ERSDLTVKEKEELIE HCCCCCHHHHHHHHH	58.81	21906983
57	Ubiquitination	SDLTVKEKEELIEEW CCCCHHHHHHHHHHH	51.26	21906983
75	Ubiquitination	PLVPPVPKDHPALNY CCCCCCCCCCCCCCC	69.75	-
82	Phosphorylation	KDHPALNYNIVSGPP CCCCCCCCEECCCCC	13.71	21945579
86	Phosphorylation	ALNYNIVSGPPSHKT CCCCEECCCCCCCCE	41.61	21945579
90	Phosphorylation	NIVSGPPSHKTVVNG EECCCCCCCCEEECC	40.52	21945579
92	Ubiquitination	VSGPPSHKTVVNGKE CCCCCCCCEEECCHH	47.56	21890473
118	Ubiquitination	LLDNPRVKAAALASL CCCCHHHHHHHHHHH	33.32	-
126	Acetylation	AAALASLKKYGVGTC HHHHHHHHHHCCCCC	41.26	25953088
126	Ubiquitination	AAALASLKKYGVGTC HHHHHHHHHHCCCCC	41.26	-
127	Ubiquitination	AALASLKKYGVGTCG HHHHHHHHHCCCCCC	53.16	-
127	2-Hydroxyisobutyrylation	AALASLKKYGVGTCG HHHHHHHHHCCCCCC	53.16	-
164	Phosphorylation	KTEEAIIYSYGFATI CCHHHHHHHHHHHHH	6.96	23454272
197	Ubiquitination	AACFAIQKGLQASRS HHHHHHHHHHHCCHH	56.31	-
202	Phosphorylation	IQKGLQASRSDIKLF HHHHHHCCHHHHHHH	21.25	25159151
204	Phosphorylation	KGLQASRSDIKLFKH HHHHCCHHHHHHHHC	40.99	28348404
207	Ubiquitination	QASRSDIKLFKHNDM HCCHHHHHHHHCCCH	53.51	21890473
210	2-Hydroxyisobutyrylation	RSDIKLFKHNDMADL HHHHHHHHCCCHHHH	52.51	-
210	Malonylation	RSDIKLFKHNDMADL HHHHHHHHCCCHHHH	52.51	26320211
210	Acetylation	RSDIKLFKHNDMADL HHHHHHHHCCCHHHH	52.51	25953088
210	Methylation	RSDIKLFKHNDMADL HHHHHHHHCCCHHHH	52.51	42371369
210	Ubiquitination	RSDIKLFKHNDMADL HHHHHHHHCCCHHHH	52.51	-
222	Ubiquitination	ADLERLLKEQEIEDQ HHHHHHHHHHHHHHC	63.04	21890473
230	Ubiquitination	EQEIEDQKNPRKARV HHHHHHCCCHHHHHH	79.73	21890473
369	Ubiquitination	IFAVLKEKCGQIHKA HHHHHHHHHCHHHHH	41.92	-
375	Ubiquitination	EKCGQIHKALQGISG HHHCHHHHHHHHCCC	53.04	-
384	Ubiquitination	LQGISGLKVVGESLS HHHCCCCEEECCCCC	38.10	21890473
389	Phosphorylation	GLKVVGESLSPAFHL CCEEECCCCCCCEEE	28.37	-
391	Phosphorylation	KVVGESLSPAFHLQL EEECCCCCCCEEEEH	24.38	-
420	Sulfoxidation	QEIVDQCMNRSIALT HHHHHHHHHHHHHHH	3.77	21406390
434	Ubiquitination	TQARYLEKEEKCLPP HHHHHHHHHHHCCCC	69.45	-
434	Acetylation	TQARYLEKEEKCLPP HHHHHHHHHHHCCCC	69.45	25953088
443	Phosphorylation	EKCLPPPSIRVVVTV HHCCCCCCEEEEEEE	28.88	18491316
453	Phosphorylation	VVVTVEQTEEELERA EEEEEECCHHHHHHH	31.68	-
465	Ubiquitination	ERAASTIKEVAQAVL HHHHHHHHHHHHHHH	46.34	21890473

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
164	Y	Phosphorylation	Kinase	ABL1	P00519	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SPTC1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SPTC1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SPTC1_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 162400: Neuropathy, hereditary sensory and autonomic, 1A (HSAN1A)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00133: L-Serine