SPP2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SPP2A_HUMAN
• UniProt AC: Q8TCT8
• Protein Name: Signal peptide peptidase-like 2A {ECO:0000303|PubMed:15385547, ECO:0000312|HGNC:HGNC:30227}
• Gene Name: SPPL2A {ECO:0000303|PubMed:15385547, ECO:0000312|HGNC:HGNC:30227}
• Organism: Homo sapiens (Human).
• Sequence Length: 520
• Subcellular Localization: Late endosome membrane ; Multi-pass membrane protein . Lysosome membrane ; Multi-pass membrane protein . Membrane ; Multi-pass membrane protein ; Lumenal side . Colocalizes with palmitoylated and myristoylated proteins at the plasma membrane.
• Protein Description: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing. [PubMed: 16829952]
• Protein Sequence: MGPQRRLSPAGAALLWGFLLQLTAAQEAILHASGNGTTKDYCMLYNPYWTALPSTLENATSISLMNLTSTPLCNLSDIPPVGIKSKAVVVPWGSCHFLEKARIAQKGGAEAMLVVNNSVLFPPSGNRSEFPDVKILIAFISYKDFRDMNQTLGDNITVKMYSPSWPNFDYTMVVIFVIAVFTVALGGYWSGLVELENLKAVTTEDREMRKKKEEYLTFSPLTVVIFVVICCVMMVLLYFFYKWLVYVMIAIFCIASAMSLYNCLAALIHKIPYGQCTIACRGKNMEVRLIFLSGLCIAVAVVWAVFRNEDRWAWILQDILGIAFCLNLIKTLKLPNFKSCVILLGLLLLYDVFFVFITPFITKNGESIMVELAAGPFGNNEKLPVVIRVPKLIYFSVMSVCLMPVSILGFGDIIVPGLLIAYCRRFDVQTGSSYIYYVSSTVAYAIGMILTFVVLVLMKKGQPALLYLVPCTLITASVVAWRRKEMKKFWKGNSYQMMDHLDCATNEENPVISGEQIVQQ

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
58	N-linked_Glycosylation	ALPSTLENATSISLM CCCHHHCCCCCCEEE	52.19	UniProtKB CARBOHYD
66	N-linked_Glycosylation	ATSISLMNLTSTPLC CCCCEEECCCCCCCC	45.52	UniProtKB CARBOHYD
74	N-linked_Glycosylation	LTSTPLCNLSDIPPV CCCCCCCCHHHCCCC	50.71	UniProtKB CARBOHYD
85	Phosphorylation	IPPVGIKSKAVVVPW CCCCCCCCCEEEECC	24.75	20068231
94	Phosphorylation	AVVVPWGSCHFLEKA EEEECCCHHHHHHHH	10.68	20068231
95	S-palmitoylation	VVVPWGSCHFLEKAR EEECCCHHHHHHHHH	2.01	29575903
100	Ubiquitination	GSCHFLEKARIAQKG CHHHHHHHHHHHHCC	45.15	-
100	2-Hydroxyisobutyrylation	GSCHFLEKARIAQKG CHHHHHHHHHHHHCC	45.15	-
116	N-linked_Glycosylation	AEAMLVVNNSVLFPP CCEEEEEECCEECCC	27.81	UniProtKB CARBOHYD
126	N-linked_Glycosylation	VLFPPSGNRSEFPDV EECCCCCCCCCCCCC	48.95	UniProtKB CARBOHYD
149	N-linked_Glycosylation	YKDFRDMNQTLGDNI HHHHHHHHHHCCCCE	35.65	17660510
155	N-linked_Glycosylation	MNQTLGDNITVKMYS HHHHCCCCEEEEEEC	29.99	17660510
215	Phosphorylation	MRKKKEEYLTFSPLT HHHHHHHHCCCCHHH	16.48	23607784
217	Phosphorylation	KKKEEYLTFSPLTVV HHHHHHCCCCHHHHH	22.59	23607784
219	Phosphorylation	KEEYLTFSPLTVVIF HHHHCCCCHHHHHHH	17.48	23607784
222	Phosphorylation	YLTFSPLTVVIFVVI HCCCCHHHHHHHHHH	18.99	23607784
238	Phosphorylation	CVMMVLLYFFYKWLV HHHHHHHHHHHHHHH	6.36	23607784
241	Phosphorylation	MVLLYFFYKWLVYVM HHHHHHHHHHHHHHH	7.43	23607784
382	Acetylation	GPFGNNEKLPVVIRV CCCCCCCCCCEEEEC	61.28	12437937

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SPP2A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SPP2A_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 SPP2A_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SPP2A_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.