dbPTM

SC24C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SC24C_HUMAN
UniProt AC	P53992
Protein Name	Protein transport protein Sec24C {ECO:0000305}
Gene Name	SEC24C {ECO:0000312\|HGNC:HGNC:10705}
Organism	Homo sapiens (Human).
Sequence Length	1094
Subcellular Localization	Cytoplasmic vesicle, COPII-coated vesicle membrane Peripheral membrane protein Cytoplasmic side . Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side . Cytoplasm, cytosol .
Protein Description	Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. [PubMed: 10214955]
Protein Sequence	MNVNQSVPPVPPFGQPQPIYPGYHQSSYGGQSGSTAPAIPYGAYNGPVPGYQQTPPQGMSRAPPSSGAPPASTAQAPCGQAAYGQFGQGDVQNGPSSTVQMQRLPGSQPFGSPLAPVGNQPPVLQPYGPPPTSAQVATQLSGMQISGAVAPAPPSSGLGFGPPTSLASASGSFPNSGLYGSYPQGQAPPLSQAQGHPGIQTPQRSAPSQASSFTPPASGGPRLPSMTGPLLPGQSFGGPSVSQPNHVSSPPQALPPGTQMTGPLGPLPPMHSPQQPGYQPQQNGSFGPARGPQSNYGGPYPAAPTFGSQPGPPQPLPPKRLDPDAIPSPIQVIEDDRNNRGTEPFVTGVRGQVPPLVTTNFLVKDQGNASPRYIRCTSYNIPCTSDMAKQAQVPLAAVIKPLARLPPEEASPYVVDHGESGPLRCNRCKAYMCPFMQFIEGGRRFQCCFCSCINDVPPQYFQHLDHTGKRVDAYDRPELSLGSYEFLATVDYCKNNKFPSPPAFIFMIDVSYNAIRTGLVRLLCEELKSLLDFLPREGGAEESAIRVGFVTYNKVLHFYNVKSSLAQPQMMVVSDVADMFVPLLDGFLVNVNESRAVITSLLDQIPEMFADTRETETVFVPVIQAGMEALKAAECAGKLFLFHTSLPIAEAPGKLKNRDDRKLINTDKEKTLFQPQTGAYQTLAKECVAQGCCVDLFLFPNQYVDVATLSVVPQLTGGSVYKYASFQVENDQERFLSDLRRDVQKVVGFDAVMRVRTSTGIRAVDFFGAFYMSNTTDVELAGLDGDKTVTVEFKHDDRLNEESGALLQCALLYTSCAGQRRLRIHNLALNCCTQLADLYRNCETDTLINYMAKFAYRGVLNSPVKAVRDTLITQCAQILACYRKNCASPSSAGQLILPECMKLLPVYLNCVLKSDVLQPGAEVTTDDRAYVRQLVTSMDVTETNVFFYPRLLPLTKSPVESTTEPPAVRASEERLSNGDIYLLENGLNLFLWVGASVQQGVVQSLFSVSSFSQITSGLSVLPVLDNPLSKKVRGLIDSLRAQRSRYMKLTVVKQEDKMEMLFKHFLVEDKSLSGGASYVDFLCHMHKEIRQLLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
65	Phosphorylation	GMSRAPPSSGAPPAS CCCCCCCCCCCCCCC	40.10	26552605
66	Phosphorylation	MSRAPPSSGAPPAST CCCCCCCCCCCCCCC	44.76	26552605
72	Phosphorylation	SSGAPPASTAQAPCG CCCCCCCCCCCCCCC	30.01	26552605
73	Phosphorylation	SGAPPASTAQAPCGQ CCCCCCCCCCCCCCC	25.54	26552605
83	Phosphorylation	APCGQAAYGQFGQGD CCCCCCCCCCCCCCC	17.93	26552605
96	Phosphorylation	GDVQNGPSSTVQMQR CCCCCCCCCCEEEEE	39.79	26552605
97	Phosphorylation	DVQNGPSSTVQMQRL CCCCCCCCCEEEEEC	35.41	26552605
98	Phosphorylation	VQNGPSSTVQMQRLP CCCCCCCCEEEEECC	21.06	26552605
101	Ubiquitination	GPSSTVQMQRLPGSQ CCCCCEEEEECCCCC	1.86	-
113	Ubiquitination	GSQPFGSPLAPVGNQ CCCCCCCCCCCCCCC	32.68	-
132	Ubiquitination	QPYGPPPTSAQVATQ CCCCCCCCHHHHHHH	42.33	-
161	Ubiquitination	PSSGLGFGPPTSLAS CCCCCCCCCCCHHHH	26.02	-
168	O-linked_Glycosylation	GPPTSLASASGSFPN CCCCHHHHCCCCCCC	28.41	20305658
170	O-linked_Glycosylation	PTSLASASGSFPNSG CCHHHHCCCCCCCCC	32.26	20305658
176	Phosphorylation	ASGSFPNSGLYGSYP CCCCCCCCCCCCCCC	30.34	-
179	Phosphorylation	SFPNSGLYGSYPQGQ CCCCCCCCCCCCCCC	13.93	-
204	Ubiquitination	PGIQTPQRSAPSQAS CCCCCCCCCCCCCCC	35.67	-
211	Phosphorylation	RSAPSQASSFTPPAS CCCCCCCCCCCCCCC	20.53	26270265
212	Phosphorylation	SAPSQASSFTPPASG CCCCCCCCCCCCCCC	35.83	21601212
214	Phosphorylation	PSQASSFTPPASGGP CCCCCCCCCCCCCCC	30.25	25159151
218	Phosphorylation	SSFTPPASGGPRLPS CCCCCCCCCCCCCCC	50.48	23312004
222	Dimethylation	PPASGGPRLPSMTGP CCCCCCCCCCCCCCC	63.61	-
222	Methylation	PPASGGPRLPSMTGP CCCCCCCCCCCCCCC	63.61	52717277
294	Phosphorylation	GPARGPQSNYGGPYP CCCCCCCCCCCCCCC	34.84	21945579
296	Phosphorylation	ARGPQSNYGGPYPAA CCCCCCCCCCCCCCC	28.80	21945579
296	Ubiquitination	ARGPQSNYGGPYPAA CCCCCCCCCCCCCCC	28.80	-
300	Phosphorylation	QSNYGGPYPAAPTFG CCCCCCCCCCCCCCC	14.58	21945579
305	Ubiquitination	GPYPAAPTFGSQPGP CCCCCCCCCCCCCCC	35.58	-
305	Phosphorylation	GPYPAAPTFGSQPGP CCCCCCCCCCCCCCC	35.58	21945579
308	Phosphorylation	PAAPTFGSQPGPPQP CCCCCCCCCCCCCCC	29.07	21945579
319	Acetylation	PPQPLPPKRLDPDAI CCCCCCCCCCCCCCC	64.75	26051181
319	Ubiquitination	PPQPLPPKRLDPDAI CCCCCCCCCCCCCCC	64.75	-
328	Phosphorylation	LDPDAIPSPIQVIED CCCCCCCCCEEEEEC	28.64	29496963
335	Ubiquitination	SPIQVIEDDRNNRGT CCEEEEECCCCCCCC	49.39	-
335	Acetylation	SPIQVIEDDRNNRGT CCEEEEECCCCCCCC	49.39	-
350	Methylation	EPFVTGVRGQVPPLV CCCCCCCCCCCCCCE	31.04	115493551
364	Ubiquitination	VTTNFLVKDQGNASP EEECEEECCCCCCCC	46.62	-
379	Phosphorylation	RYIRCTSYNIPCTSD CEEEEEECCCCCCHH	10.04	29759185
389	Ubiquitination	PCTSDMAKQAQVPLA CCCHHHHHHCCCCHH	39.26	-
400	Ubiquitination	VPLAAVIKPLARLPP CCHHHHHHHHHCCCH	27.64	-
483	Phosphorylation	RPELSLGSYEFLATV CCCCCCCCEEEEEEH	27.12	29038488
492	Phosphorylation	EFLATVDYCKNNKFP EEEEEHHHHHCCCCC	10.86	29038488
529	Phosphorylation	LLCEELKSLLDFLPR HHHHHHHHHHHHCCC	46.95	21712546
608	Sulfoxidation	LLDQIPEMFADTRET HHHHHHHHHCCCCCC	2.55	21406390
615	Phosphorylation	MFADTRETETVFVPV HHCCCCCCCEEEHHH	33.40	20068231
617	Phosphorylation	ADTRETETVFVPVIQ CCCCCCCEEEHHHHH	27.02	20068231
638	Ubiquitination	KAAECAGKLFLFHTS HHHHHCCCHHEEECC	19.96	-
638	Acetylation	KAAECAGKLFLFHTS HHHHHCCCHHEEECC	19.96	26051181
654	Ubiquitination	PIAEAPGKLKNRDDR CHHCCCCCCCCCCCC	56.05	-
656	Ubiquitination	AEAPGKLKNRDDRKL HCCCCCCCCCCCCCC	54.12	-
662	Ubiquitination	LKNRDDRKLINTDKE CCCCCCCCCCCCCHH	61.79	-
666	Phosphorylation	DDRKLINTDKEKTLF CCCCCCCCCHHHCCC	41.26	-
668	Acetylation	RKLINTDKEKTLFQP CCCCCCCHHHCCCCC	60.10	25953088
668	2-Hydroxyisobutyrylation	RKLINTDKEKTLFQP CCCCCCCHHHCCCCC	60.10	-
670	Ubiquitination	LINTDKEKTLFQPQT CCCCCHHHCCCCCCC	57.16	21890473
677	Phosphorylation	KTLFQPQTGAYQTLA HCCCCCCCCHHHHHH	30.38	28152594
680	Phosphorylation	FQPQTGAYQTLAKEC CCCCCCHHHHHHHHH	11.90	28152594
682	Phosphorylation	PQTGAYQTLAKECVA CCCCHHHHHHHHHHH	18.92	28152594
737	Phosphorylation	NDQERFLSDLRRDVQ CHHHHHHHHHHHHHH	31.70	24719451
745	Ubiquitination	DLRRDVQKVVGFDAV HHHHHHHHHHCCCEE	38.44	-
773	Phosphorylation	FFGAFYMSNTTDVEL EEEEEEECCCCCEEE	21.46	21712546
773	O-linked_Glycosylation	FFGAFYMSNTTDVEL EEEEEEECCCCCEEE	21.46	20305658
775	O-linked_Glycosylation	GAFYMSNTTDVELAG EEEEECCCCCEEEEC	19.64	20305658
776	O-linked_Glycosylation	AFYMSNTTDVELAGL EEEECCCCCEEEECC	42.15	20305658
776	Phosphorylation	AFYMSNTTDVELAGL EEEECCCCCEEEECC	42.15	21712546
833	Phosphorylation	NLALNCCTQLADLYR HHHHHHHHHHHHHHH	28.90	-
853	Ubiquitination	TLINYMAKFAYRGVL HHHHHHHHHHHHHHH	17.63	-
856	Phosphorylation	NYMAKFAYRGVLNSP HHHHHHHHHHHHCCH	15.84	30576142
862	Phosphorylation	AYRGVLNSPVKAVRD HHHHHHCCHHHHHHH	27.23	25159151
865	Ubiquitination	GVLNSPVKAVRDTLI HHHCCHHHHHHHHHH	44.54	-
884	Ubiquitination	QILACYRKNCASPSS HHHHHHHHCCCCCCH	29.88	-
888	Phosphorylation	CYRKNCASPSSAGQL HHHHCCCCCCHHHCC	27.75	30278072
890	Phosphorylation	RKNCASPSSAGQLIL HHCCCCCCHHHCCHH	30.26	23663014
891	Phosphorylation	KNCASPSSAGQLILP HCCCCCCHHHCCHHH	39.54	25159151
913	Acetylation	VYLNCVLKSDVLQPG HHHHHEECCCCCCCC	24.98	26051181
913	Ubiquitination	VYLNCVLKSDVLQPG HHHHHEECCCCCCCC	24.98	-
928	Methylation	AEVTTDDRAYVRQLV CEEECCCHHHHHHHH	30.54	115493557
955	Phosphorylation	YPRLLPLTKSPVEST ECCCCCCCCCCCCCC	27.77	28348404
956	Ubiquitination	PRLLPLTKSPVESTT CCCCCCCCCCCCCCC	61.52	21890473
957	Phosphorylation	RLLPLTKSPVESTTE CCCCCCCCCCCCCCC	29.01	27251275
1044	Phosphorylation	DSLRAQRSRYMKLTV HHHHHHHHHHCEEEE	18.71	22617229
1046	Phosphorylation	LRAQRSRYMKLTVVK HHHHHHHHCEEEEEC	10.39	22617229
1048	Ubiquitination	AQRSRYMKLTVVKQE HHHHHHCEEEEECHH	31.88	21890473
1048	Ubiquitination	AQRSRYMKLTVVKQE HHHHHHCEEEEECHH	31.88	21890473
1057	Ubiquitination	TVVKQEDKMEMLFKH EEECHHHHHHHHHHH	35.69	-
1071	Phosphorylation	HFLVEDKSLSGGASY HHHCCCCCCCCCHHH	39.84	28348404
1073	Phosphorylation	LVEDKSLSGGASYVD HCCCCCCCCCHHHHH	42.12	28348404
1087	Ubiquitination	DFLCHMHKEIRQLLS HHHHHHHHHHHHHHC	47.46	19608861
1087	Acetylation	DFLCHMHKEIRQLLS HHHHHHHHHHHHHHC	47.46	23749302
1094	Phosphorylation	KEIRQLLS------- HHHHHHHC-------	46.93	29514088

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 SC24C_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SC24C_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 SC24C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SC23B_HUMAN	SEC23B	physical	16189514
SC23A_HUMAN	SEC23A	physical	10075675
A4_HUMAN	APP	physical	21832049
SC24D_HUMAN	SEC24D	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
SERPH_HUMAN	SERPINH1	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22863883
CSDE1_HUMAN	CSDE1	physical	22863883
OTU6B_HUMAN	OTUD6B	physical	22863883
SBNO1_HUMAN	SBNO1	physical	22863883
SSRP1_HUMAN	SSRP1	physical	22863883
CD2AP_HUMAN	CD2AP	physical	26344197
SC23A_HUMAN	SEC23A	physical	26344197
SC23B_HUMAN	SEC23B	physical	26344197
SC24A_HUMAN	SEC24A	physical	26344197
SH3K1_HUMAN	SH3KBP1	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.

Regulatory Network of SC24C_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-1087, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND MASSSPECTROMETRY.	15302935 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND MASSSPECTROMETRY.	18669648 [Abstract]