dbPTM

SC24B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SC24B_HUMAN
UniProt AC	O95487
Protein Name	Protein transport protein Sec24B {ECO:0000305}
Gene Name	SEC24B {ECO:0000312\|HGNC:HGNC:10704}
Organism	Homo sapiens (Human).
Sequence Length	1268
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: 17499046]
Protein Sequence	MSAPAGSSHPAASARIPPKFGGAAVSGAAAPAGPGAGPAPHQQNGPAQNQMQVPSGYGLHHQNYIAPSGHYSQGPGKMTSLPLDTQCGDYYSALYTVPTQNVTPNTVNQQPGAQQLYSRGPPAPHIVGSTLGSFQGAASSASHLHTSASQPYSSFVNHYNSPAMYSASSSVASQGFPSTCGHYAMSTVSNAAYPSVSYPSLPAGDTYGQMFTSQNAPTVRPVKDNSFSGQNTAISHPSPLPPLPSQQHHQQQSLSGYSTLTWSSPGLPSTQDNLIRNHTGSLAVANNNPTITVADSLSCPVMQNVQPPKSSPVVSTVLSGSSGSSSTRTPPTANHPVEPVTSVTQPSELLQQKGVQYGEYVNNQASSAPTPLSSTSDDEEEEEEDEEAGVDSSSTTSSASPMPNSYDALEGGSYPDMLSSSASSPAPDPAPEPDPASAPAPASAPAPVVPQPSKMAKPFGYGYPTLQPGYQNATAPLISGVQPSNPVYSGFQQYPQQYPGVNQLSSSIGGLSLQSSPQPESLRPVNLTQERNILPMTPVWAPVPNLNADLKKLNCSPDSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIVRCRSCRTYINPFVSFIDQRRWKCNLCYRVNDVPEEFMYNPLTRSYGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPTPDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYTHNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVRSTDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAICLLANMAVDRSVSSSLSDARDALVNAVVDSLSAYGSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGTSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLYRIDRLTDEGAVHVNDRIVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGCDNNFIEDVLGYTNFASIPQKMTHLPELDTLSSERARSFITWLRDSRPLSPILHIVKDESPAKAEFFQHLIEDRTEAAFSYYEFLLHVQQQICK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSAPAGSSH ------CCCCCCCCC	55.02	19413330
2	Phosphorylation	------MSAPAGSSH ------CCCCCCCCC	55.02	29255136
7	Phosphorylation	-MSAPAGSSHPAASA -CCCCCCCCCCCHHC	27.81	23898821
8	Phosphorylation	MSAPAGSSHPAASAR CCCCCCCCCCCHHCC	32.35	23898821
13	Phosphorylation	GSSHPAASARIPPKF CCCCCCHHCCCCCCC	21.86	24043423
55	Phosphorylation	QNQMQVPSGYGLHHQ CCCCCCCCCCCCCCC	45.87	-
55 (in isoform 3)	Phosphorylation	-	45.87	24275569
64	Phosphorylation	YGLHHQNYIAPSGHY CCCCCCCEECCCCCC	7.59	-
68	Phosphorylation	HQNYIAPSGHYSQGP CCCEECCCCCCCCCC	29.22	-
71	Phosphorylation	YIAPSGHYSQGPGKM EECCCCCCCCCCCCC	13.25	-
72	Phosphorylation	IAPSGHYSQGPGKMT ECCCCCCCCCCCCCC	24.00	-
90	Phosphorylation	LDTQCGDYYSALYTV CCCCCCCCEEEEEEE	5.65	-
95	Phosphorylation	GDYYSALYTVPTQNV CCCEEEEEEECCCCC	12.86	-
117	Phosphorylation	QPGAQQLYSRGPPAP CCCHHHHHCCCCCCC	7.62	16094384
118	Phosphorylation	PGAQQLYSRGPPAPH CCHHHHHCCCCCCCC	39.08	24719451
139	O-linked_Glycosylation	GSFQGAASSASHLHT HHCCCHHHHCHHCCC	26.38	30059200
142	O-linked_Glycosylation	QGAASSASHLHTSAS CCHHHHCHHCCCCCC	28.64	30059200
147	O-linked_Glycosylation	SASHLHTSASQPYSS HCHHCCCCCCCCCHH	18.38	30059200
149	O-linked_Glycosylation	SHLHTSASQPYSSFV HHCCCCCCCCCHHHC	31.30	30059200
197	O-linked_Glycosylation	NAAYPSVSYPSLPAG CCCCCCCCCCCCCCC	35.35	30059200
207	Phosphorylation	SLPAGDTYGQMFTSQ CCCCCCCHHHCCCCC	15.31	-
212	O-linked_Glycosylation	DTYGQMFTSQNAPTV CCHHHCCCCCCCCCE	24.86	30059200
226	O-linked_Glycosylation	VRPVKDNSFSGQNTA EEECCCCCCCCCCCC	30.81	30059200
228	O-linked_Glycosylation	PVKDNSFSGQNTAIS ECCCCCCCCCCCCCC	39.01	30059200
232	O-linked_Glycosylation	NSFSGQNTAISHPSP CCCCCCCCCCCCCCC	19.92	30059200
235	O-linked_Glycosylation	SGQNTAISHPSPLPP CCCCCCCCCCCCCCC	27.21	30059200
238	O-linked_Glycosylation	NTAISHPSPLPPLPS CCCCCCCCCCCCCCC	33.38	30059200
245	O-linked_Glycosylation	SPLPPLPSQQHHQQQ CCCCCCCCCCCCCCC	50.59	30059200
253	O-linked_Glycosylation	QQHHQQQSLSGYSTL CCCCCCCCCCCCCEE	21.84	30059200
255	O-linked_Glycosylation	HHQQQSLSGYSTLTW CCCCCCCCCCCEEEE	40.72	30059200
258	O-linked_Glycosylation	QQSLSGYSTLTWSSP CCCCCCCCEEEECCC	22.07	30059200
259	O-linked_Glycosylation	QSLSGYSTLTWSSPG CCCCCCCEEEECCCC	21.52	30059200
261	O-linked_Glycosylation	LSGYSTLTWSSPGLP CCCCCEEEECCCCCC	24.32	30059200
269	O-linked_Glycosylation	WSSPGLPSTQDNLIR ECCCCCCCCCCCHHH	43.68	30059200
270	O-linked_Glycosylation	SSPGLPSTQDNLIRN CCCCCCCCCCCHHHH	37.69	30059200
310	O-linked_Glycosylation	QNVQPPKSSPVVSTV CCCCCCCCCCCEEEE	45.72	30059200
310	Phosphorylation	QNVQPPKSSPVVSTV CCCCCCCCCCCEEEE	45.72	22199227
311	O-linked_Glycosylation	NVQPPKSSPVVSTVL CCCCCCCCCCEEEEE	28.04	30059200
311	Phosphorylation	NVQPPKSSPVVSTVL CCCCCCCCCCEEEEE	28.04	21815630
315	O-linked_Glycosylation	PKSSPVVSTVLSGSS CCCCCCEEEEEECCC	17.03	30059200
315	Phosphorylation	PKSSPVVSTVLSGSS CCCCCCEEEEEECCC	17.03	26074081
316	O-linked_Glycosylation	KSSPVVSTVLSGSSG CCCCCEEEEEECCCC	17.54	30059200
316	Phosphorylation	KSSPVVSTVLSGSSG CCCCCEEEEEECCCC	17.54	21815630
319	Phosphorylation	PVVSTVLSGSSGSSS CCEEEEEECCCCCCC	32.09	25159151
321	Phosphorylation	VSTVLSGSSGSSSTR EEEEEECCCCCCCCC	28.31	26074081
322	Phosphorylation	STVLSGSSGSSSTRT EEEEECCCCCCCCCC	46.34	26074081
324	Phosphorylation	VLSGSSGSSSTRTPP EEECCCCCCCCCCCC	24.06	25159151
325	Phosphorylation	LSGSSGSSSTRTPPT EECCCCCCCCCCCCC	38.97	30576142
326	Phosphorylation	SGSSGSSSTRTPPTA ECCCCCCCCCCCCCC	24.49	25159151
327	O-linked_Glycosylation	GSSGSSSTRTPPTAN CCCCCCCCCCCCCCC	40.27	30059200
327	Phosphorylation	GSSGSSSTRTPPTAN CCCCCCCCCCCCCCC	40.27	25159151
329	O-linked_Glycosylation	SGSSSTRTPPTANHP CCCCCCCCCCCCCCC	33.44	30059200
329	Phosphorylation	SGSSSTRTPPTANHP CCCCCCCCCCCCCCC	33.44	23401153
332	O-linked_Glycosylation	SSTRTPPTANHPVEP CCCCCCCCCCCCCCC	41.10	30059200
332	Phosphorylation	SSTRTPPTANHPVEP CCCCCCCCCCCCCCC	41.10	29255136
341	O-linked_Glycosylation	NHPVEPVTSVTQPSE CCCCCCCCCCCCHHH	28.35	30059200
341	Phosphorylation	NHPVEPVTSVTQPSE CCCCCCCCCCCCHHH	28.35	29255136
342	O-linked_Glycosylation	HPVEPVTSVTQPSEL CCCCCCCCCCCHHHH	24.33	30059200
342	Phosphorylation	HPVEPVTSVTQPSEL CCCCCCCCCCCHHHH	24.33	23663014
344	O-linked_Glycosylation	VEPVTSVTQPSELLQ CCCCCCCCCHHHHHH	34.23	30059200
344	Phosphorylation	VEPVTSVTQPSELLQ CCCCCCCCCHHHHHH	34.23	28450419
347	O-linked_Glycosylation	VTSVTQPSELLQQKG CCCCCCHHHHHHHCC	30.93	30059200
347	Phosphorylation	VTSVTQPSELLQQKG CCCCCCHHHHHHHCC	30.93	28450419
413	Phosphorylation	YDALEGGSYPDMLSS CCCCCCCCCCHHHCC	44.33	24275569
421	Phosphorylation	YPDMLSSSASSPAPD CCHHHCCCCCCCCCC	28.88	24275569
423	Phosphorylation	DMLSSSASSPAPDPA HHHCCCCCCCCCCCC	38.51	24275569
537	Phosphorylation	ERNILPMTPVWAPVP CCCCCCCCCCEECCC	16.86	27273156
551	Acetylation	PNLNADLKKLNCSPD CCCCCCHHHCCCCCC	56.62	24471065
552	Ubiquitination	NLNADLKKLNCSPDS CCCCCHHHCCCCCCC	52.83	-
556	Phosphorylation	DLKKLNCSPDSFRCT CHHHCCCCCCCCEEE	30.57	21815630
559	Phosphorylation	KLNCSPDSFRCTLTN HCCCCCCCCEEECCC	20.27	23312004
576	Ubiquitination	QTQALLNKAKLPLGL HHHHHHHHCCCCHHH	47.03	-
578	Ubiquitination	QALLNKAKLPLGLLL HHHHHHCCCCHHHHH	52.85	-
581	Ubiquitination	LNKAKLPLGLLLHPF HHHCCCCHHHHHCCC	12.52	-
582	Ubiquitination	NKAKLPLGLLLHPFR HHCCCCHHHHHCCCC	16.61	-
598	Phosphorylation	LTQLPVITSNTIVRC CCCCCEECCCCEEEE	19.03	27732954
599	Phosphorylation	TQLPVITSNTIVRCR CCCCEECCCCEEEEC	22.35	27732954
601	Phosphorylation	LPVITSNTIVRCRSC CCEECCCCEEEECCC	22.18	27732954
606	Ubiquitination	SNTIVRCRSCRTYIN CCCEEEECCCCCCCC	28.38	-
608	Ubiquitination	TIVRCRSCRTYINPF CEEEECCCCCCCCCC	1.63	-
625	Ubiquitination	FIDQRRWKCNLCYRV HHHHCCEECCEEEEE	16.07	-
655	Ubiquitination	YGEPHKRPEVQNSTV CCCCCCCCCCCCCCE	51.41	-
660	O-linked_Glycosylation	KRPEVQNSTVEFIAS CCCCCCCCCEEEEEC	19.42	30059200
668	Phosphorylation	TVEFIASSDYMLRPP CEEEEECCCCCCCCC	24.60	22210691
670	Phosphorylation	EFIASSDYMLRPPQP EEEECCCCCCCCCCC	10.45	-
781	Phosphorylation	NALPNMFTNTRETHS HHCCCCCCCCHHHHH	25.55	29978859
783	Phosphorylation	LPNMFTNTRETHSAL CCCCCCCCHHHHHHH	27.16	29978859
804	Phosphorylation	AFKLMSPTGGRVSVF HHHHHCCCCCCEEEE	44.98	-
817	Phosphorylation	VFQTQLPSLGAGLLQ EEEECCCCCCCCCCC	48.29	-
834	Phosphorylation	EDPNQRSSTKVVQHL CCCCCCCCCHHHHHH	34.14	-
836	Ubiquitination	PNQRSSTKVVQHLGP CCCCCCCHHHHHHCC	42.21	-
849	2-Hydroxyisobutyrylation	GPATDFYKKLALDCS CCCCHHHHHHCHHCC	41.10	-
849	Acetylation	GPATDFYKKLALDCS CCCCHHHHHHCHHCC	41.10	23236377
849	Ubiquitination	GPATDFYKKLALDCS CCCCHHHHHHCHHCC	41.10	-
879	Acetylation	SDLASLACMSKYSAG HHHHHHHHHHHCCCC	3.72	-
880	Ubiquitination	DLASLACMSKYSAGC HHHHHHHHHHCCCCE	3.01	-
883	Phosphorylation	SLACMSKYSAGCIYY HHHHHHHCCCCEEEE	9.10	20090780
890	Phosphorylation	YSAGCIYYYPSFHYT CCCCEEEEECCHHCC	6.76	20090780
947	Ubiquitination	NFFVRSTDLLSLANI CEEEECCCHHHHCCC	47.03	-
988	Acetylation	ALLYTSSKGERRIRV EEHHCCCCCCCEEEE	65.64	30592285
1089	Phosphorylation	LKQKAFRTGTSTRLD HHHHHHHCCCCCCCH	38.06	20068231
1091	Phosphorylation	QKAFRTGTSTRLDDR HHHHHCCCCCCCHHH	26.72	20068231
1092	Phosphorylation	KAFRTGTSTRLDDRV HHHHCCCCCCCHHHH	16.93	20068231
1093	Phosphorylation	AFRTGTSTRLDDRVY HHHCCCCCCCHHHHH	34.78	20068231
1100	Phosphorylation	TRLDDRVYAMCQIKS CCCHHHHHEEEEECC	6.90	20090780
1147	Ubiquitination	VPQPPLQKLSAEKLT CCCCCHHHCCHHHCC	52.68	-
1149	Phosphorylation	QPPLQKLSAEKLTRE CCCHHHCCHHHCCCC	41.22	26091039
1152	Ubiquitination	LQKLSAEKLTREGAF HHHCCHHHCCCCCCE	55.67	-
1154	Phosphorylation	KLSAEKLTREGAFLM HCCHHHCCCCCCEEE	37.43	22964224
1177	Ubiquitination	WVGKGCDNNFIEDVL EECCCCCCCHHHHHH	49.76	-
1182	Ubiquitination	CDNNFIEDVLGYTNF CCCCHHHHHHCCCCC	35.80	-
1197	Phosphorylation	ASIPQKMTHLPELDT CCCCHHHCCCCCHHH	27.57	22210691
1207	Phosphorylation	PELDTLSSERARSFI CCHHHCCHHHHHHHH	33.93	22210691
1212	Phosphorylation	LSSERARSFITWLRD CCHHHHHHHHHHHHC	21.73	22210691
1220	Phosphorylation	FITWLRDSRPLSPIL HHHHHHCCCCCCCCE	29.39	23401153
1224	Phosphorylation	LRDSRPLSPILHIVK HHCCCCCCCCEEEEC	16.75	29255136
1234	Phosphorylation	LHIVKDESPAKAEFF EEEECCCCHHHHHHH	40.05	23403867

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 SC24B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SC24B_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 SC24B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SC23A_HUMAN	SEC23A	physical	10075675
RN139_HUMAN	RNF139	physical	19706601
PFD3_HUMAN	VBP1	physical	26344197
PLEC_HUMAN	PLEC	physical	27173435
VIP2_HUMAN	PPIP5K2	physical	27173435
LUZP1_HUMAN	LUZP1	physical	27173435
DVL3_HUMAN	DVL3	physical	27173435
URGCP_HUMAN	URGCP	physical	27173435
QSER1_HUMAN	QSER1	physical	27173435

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 SC24B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-1224, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117 AND SER-1224, ANDMASS SPECTROMETRY.	16094384 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1100, AND MASSSPECTROMETRY.	18083107 [Abstract]