SPCS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SPCS2_HUMAN
• UniProt AC: Q15005
• Protein Name: Signal peptidase complex subunit 2
• Gene Name: SPCS2
• Organism: Homo sapiens (Human).
• Sequence Length: 226
• Subcellular Localization: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
• Protein Description: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum..
• Protein Sequence: MAAAAVQGGRSGGSGGCSGAGGASNCGTGSGRSGLLDKWKIDDKPVKIDKWDGSAVKNSLDDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIFLVAHRKDPTGMDPDDIWQLSSSLKRFDDKYTLKLTFISGRTKQQREAEFTKSIAKFFDHSGTLVMDAYEPEISRLHDSLAIERKIK

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
2	Acetylation	------MAAAAVQGG ------CCCCCCCCC	13.05	25944712
11	Phosphorylation	AAVQGGRSGGSGGCS CCCCCCCCCCCCCCC	51.27	25159151
14	Phosphorylation	QGGRSGGSGGCSGAG CCCCCCCCCCCCCCC	35.22	25159151
18	Phosphorylation	SGGSGGCSGAGGASN CCCCCCCCCCCCCCC	34.65	28450419
24	Phosphorylation	CSGAGGASNCGTGSG CCCCCCCCCCCCCCC	35.61	28450419
28	Phosphorylation	GGASNCGTGSGRSGL CCCCCCCCCCCCCCC	30.30	28450419
30	Phosphorylation	ASNCGTGSGRSGLLD CCCCCCCCCCCCCCC	30.76	26074081
33	Phosphorylation	CGTGSGRSGLLDKWK CCCCCCCCCCCCCCC	37.00	26074081
38	Ubiquitination	GRSGLLDKWKIDDKP CCCCCCCCCCCCCCC	50.81	33845483
38	Acetylation	GRSGLLDKWKIDDKP CCCCCCCCCCCCCCC	50.81	25953088
40	Ubiquitination	SGLLDKWKIDDKPVK CCCCCCCCCCCCCEE	41.83	29967540
44	2-Hydroxyisobutyrylation	DKWKIDDKPVKIDKW CCCCCCCCCEEEEEC	48.22	-
47	Ubiquitination	KIDDKPVKIDKWDGS CCCCCCEEEEECCCH	54.43	29967540
50	2-Hydroxyisobutyrylation	DKPVKIDKWDGSAVK CCCEEEEECCCHHHH	51.13	-
50	Ubiquitination	DKPVKIDKWDGSAVK CCCEEEEECCCHHHH	51.13	29967540
54	Phosphorylation	KIDKWDGSAVKNSLD EEEECCCHHHHHHCC	27.67	21815630
57	Ubiquitination	KWDGSAVKNSLDDSA ECCCHHHHHHCCHHH	40.30	21906983
66	Ubiquitination	SLDDSAKKVLLEKYK HCCHHHHHHHHHHHH	37.52	-
71	2-Hydroxyisobutyrylation	AKKVLLEKYKYVENF HHHHHHHHHHHHHHC	47.19	-
71	Acetylation	AKKVLLEKYKYVENF HHHHHHHHHHHHHHC	47.19	25825284
71	Ubiquitination	AKKVLLEKYKYVENF HHHHHHHHHHHHHHC	47.19	29967540
71	Malonylation	AKKVLLEKYKYVENF HHHHHHHHHHHHHHC	47.19	26320211
73	Acetylation	KVLLEKYKYVENFGL HHHHHHHHHHHHCCC	54.62	26051181
137	Ubiquitination	IYTSYKEKSIFLVAH HHHHCCCCEEEEEEE	44.70	33845483
138	Phosphorylation	YTSYKEKSIFLVAHR HHHCCCCEEEEEEEC	21.47	21406692
146	Ubiquitination	IFLVAHRKDPTGMDP EEEEEECCCCCCCCH	59.18	29967540
149	Phosphorylation	VAHRKDPTGMDPDDI EEECCCCCCCCHHHH	56.10	20068231
160	Phosphorylation	PDDIWQLSSSLKRFD HHHHHHHHHHHCCCC	11.63	30108239
161	Phosphorylation	DDIWQLSSSLKRFDD HHHHHHHHHHCCCCC	48.56	30108239
162	Phosphorylation	DIWQLSSSLKRFDDK HHHHHHHHHCCCCCC	34.24	30108239
164	2-Hydroxyisobutyrylation	WQLSSSLKRFDDKYT HHHHHHHCCCCCCEE	53.63	-
164	Ubiquitination	WQLSSSLKRFDDKYT HHHHHHHCCCCCCEE	53.63	21906983
169	2-Hydroxyisobutyrylation	SLKRFDDKYTLKLTF HHCCCCCCEEEEEEE	41.81	-
169	Ubiquitination	SLKRFDDKYTLKLTF HHCCCCCCEEEEEEE	41.81	22817900
169	Acetylation	SLKRFDDKYTLKLTF HHCCCCCCEEEEEEE	41.81	19608861
169	Malonylation	SLKRFDDKYTLKLTF HHCCCCCCEEEEEEE	41.81	26320211
175	Phosphorylation	DKYTLKLTFISGRTK CCEEEEEEEEECCCH	19.82	23312004
178	Phosphorylation	TLKLTFISGRTKQQR EEEEEEEECCCHHHH	20.31	24719451
191	2-Hydroxyisobutyrylation	QREAEFTKSIAKFFD HHHHHHHHHHHHHHC	45.23	-
191	Malonylation	QREAEFTKSIAKFFD HHHHHHHHHHHHHHC	45.23	26320211
191	Ubiquitination	QREAEFTKSIAKFFD HHHHHHHHHHHHHHC	45.23	27667366
191	Acetylation	QREAEFTKSIAKFFD HHHHHHHHHHHHHHC	45.23	19608861
192	Phosphorylation	REAEFTKSIAKFFDH HHHHHHHHHHHHHCC	25.40	24719451
195	Ubiquitination	EFTKSIAKFFDHSGT HHHHHHHHHHCCCCC	44.91	21963094
195	Acetylation	EFTKSIAKFFDHSGT HHHHHHHHHHCCCCC	44.91	25953088
200	Phosphorylation	IAKFFDHSGTLVMDA HHHHHCCCCCEEEEC	35.00	28348404
202	Phosphorylation	KFFDHSGTLVMDAYE HHHCCCCCEEEECCC	21.13	28348404
208	Phosphorylation	GTLVMDAYEPEISRL CCEEEECCCHHHHHH	27.96	-
218	Phosphorylation	EISRLHDSLAIERKI HHHHHHHHHHHHHCC	14.67	29214152
224	Ubiquitination	DSLAIERKIK----- HHHHHHHCCC-----	41.90	29967540

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

Oops, there are no upstream regulatory protein records of SPCS2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SPCS2_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 SPCS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TM14C_HUMAN	TMEM14C	physical	22939629
TM9S4_HUMAN	TM9SF4	physical	22939629
TGO1_HUMAN	MIA3	physical	26186194
SPCS1_HUMAN	SPCS1	physical	26186194
SC11C_HUMAN	SEC11C	physical	26186194
TM87A_HUMAN	TMEM87A	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169 AND LYS-191, AND MASSSPECTROMETRY.
PubMed: 19608861