dbPTM

GORS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GORS2_HUMAN
UniProt AC	Q9H8Y8
Protein Name	Golgi reassembly-stacking protein 2
Gene Name	GORASP2
Organism	Homo sapiens (Human).
Sequence Length	452
Subcellular Localization	Golgi apparatus membrane Lipid-anchor. Membrane Peripheral membrane protein. Membrane Lipid-anchor .
Protein Description	Plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after mitotic breakdown. May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA..
Protein Sequence	MGSSQSVEIPGGGTEGYHVLRVQENSPGHRAGLEPFFDFIVSINGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKTLELRETSVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPTRPFEEGKKISLPGQMAGTPITPLKDGFTEVQLSSVNPPSLSPPGTTGIEQSLTGLSISSTPPAVSSVLSTGVPTVPLLPPQVNQSLTSVPPMNPATTLPGLMPLPAGLPNLPNLNLNLPAPHIMPGVGLPELVNPGLPPLPSMPPRNLPGIAPLPLPSEFLPSFPLVPESSSAASSGELLSSLPPTSNAPSDPATTTAKADAASSLTVDVTPPTAKAPTTVEDRVGDSTPVSEKPVSAAVDANASESP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGSSQSVEI ------CCCCCEEEE	35.68	25807930
2	N-myristoyl glycine	------MGSSQSVEI ------CCCCCEEEE	35.68	-
4	Phosphorylation	----MGSSQSVEIPG ----CCCCCEEEECC	22.27	19562805
4 (in isoform 2)	Phosphorylation	-	22.27	24719451
7	Ubiquitination	-MGSSQSVEIPGGGT -CCCCCEEEECCCCC	6.32	30230243
8 (in isoform 2)	Phosphorylation	-	49.03	24719451
26	Phosphorylation	VLRVQENSPGHRAGL EEEEEECCCCCCCCC	31.35	-
30	Methylation	QENSPGHRAGLEPFF EECCCCCCCCCCHHC	35.94	-
47	Methylation	IVSINGSRLNKDNDT EEEECCCCCCCCCHH	43.61	-
50	Ubiquitination	INGSRLNKDNDTLKD ECCCCCCCCCHHHHH	63.60	30230243
54	Phosphorylation	RLNKDNDTLKDLLKA CCCCCCHHHHHHHHH	41.80	20873877
56	Acetylation	NKDNDTLKDLLKANV CCCCHHHHHHHHHCC	48.71	23236377
56	Ubiquitination	NKDNDTLKDLLKANV CCCCHHHHHHHHHCC	48.71	32142685
60	Ubiquitination	DTLKDLLKANVEKPV HHHHHHHHHCCCCCE	45.25	33845483
62	Ubiquitination	LKDLLKANVEKPVKM HHHHHHHCCCCCEEE	40.67	-
65	Ubiquitination	LLKANVEKPVKMLIY HHHHCCCCCEEEEEE	51.32	29967540
68	Acetylation	ANVEKPVKMLIYSSK HCCCCCEEEEEEECC	36.19	-
72	Phosphorylation	KPVKMLIYSSKTLEL CCEEEEEEECCCEEE	11.70	24719451
73	Phosphorylation	PVKMLIYSSKTLELR CEEEEEEECCCEEEE	20.54	30206219
74	Phosphorylation	VKMLIYSSKTLELRE EEEEEEECCCEEEEC	16.82	30206219
75	Ubiquitination	KMLIYSSKTLELRET EEEEEECCCEEEECC	51.71	30230243
76	Phosphorylation	MLIYSSKTLELRETS EEEEECCCEEEECCC	27.67	24719451
87	Ubiquitination	RETSVTPSNLWGGQG ECCCCCHHHHCCCCC	34.88	-
143 (in isoform 2)	Ubiquitination	-	5.10	-
143	Ubiquitination	IIGADTVMNESEDLF EECCCCCCCCCHHHH	5.10	32015554
144 (in isoform 2)	Ubiquitination	-	45.35	-
144	Ubiquitination	IGADTVMNESEDLFS ECCCCCCCCCHHHHH	45.35	23503661
154	Phosphorylation	EDLFSLIETHEAKPL HHHHHHHHHHCCCCE	49.78	32142685
154 (in isoform 2)	Phosphorylation	-	49.78	24719451
157	Phosphorylation	FSLIETHEAKPLKLY HHHHHHHCCCCEEEE	66.85	32142685
157 (in isoform 2)	Phosphorylation	-	66.85	24719451
166	Phosphorylation	KPLKLYVYNTDTDNC CCEEEEEEECCCCCE	9.97	28152594
168	Phosphorylation	LKLYVYNTDTDNCRE EEEEEEECCCCCEEE	23.69	28152594
189	Phosphorylation	SAWGGEGSLGCGIGY CCCCCCCCCCCCCCC	19.79	-
204	Phosphorylation	GYLHRIPTRPFEEGK CCCCCCCCCCCCCCC	48.91	22985185
211	Ubiquitination	TRPFEEGKKISLPGQ CCCCCCCCCCCCCCC	50.65	32015554
211	2-Hydroxyisobutyrylation	TRPFEEGKKISLPGQ CCCCCCCCCCCCCCC	50.65	-
212	Ubiquitination	RPFEEGKKISLPGQM CCCCCCCCCCCCCCC	48.67	23503661
214	Phosphorylation	FEEGKKISLPGQMAG CCCCCCCCCCCCCCC	37.07	29255136
219	Sulfoxidation	KISLPGQMAGTPITP CCCCCCCCCCCCCCC	4.62	21406390
222	Phosphorylation	LPGQMAGTPITPLKD CCCCCCCCCCCCCCC	11.28	29255136
222	O-linked_Glycosylation	LPGQMAGTPITPLKD CCCCCCCCCCCCCCC	11.28	OGP
223	Ubiquitination	PGQMAGTPITPLKDG CCCCCCCCCCCCCCC	27.77	-
224	Ubiquitination	GQMAGTPITPLKDGF CCCCCCCCCCCCCCC	6.60	-
225	Phosphorylation	QMAGTPITPLKDGFT CCCCCCCCCCCCCCE	24.62	29255136
232	Phosphorylation	TPLKDGFTEVQLSSV CCCCCCCEEEEECCC	40.55	26074081
243	Phosphorylation	LSSVNPPSLSPPGTT ECCCCCCCCCCCCCC	42.61	26074081
245	Phosphorylation	SVNPPSLSPPGTTGI CCCCCCCCCCCCCCC	33.13	26074081
249	Phosphorylation	PSLSPPGTTGIEQSL CCCCCCCCCCCCHHC	27.85	26074081
250	Phosphorylation	SLSPPGTTGIEQSLT CCCCCCCCCCCHHCC	41.92	26074081
260	O-linked_Glycosylation	EQSLTGLSISSTPPA CHHCCCCCCCCCCCC	23.05	23301498
260	Phosphorylation	EQSLTGLSISSTPPA CHHCCCCCCCCCCCC	23.05	26074081
262	O-linked_Glycosylation	SLTGLSISSTPPAVS HCCCCCCCCCCCCHH	25.45	23301498
262	Phosphorylation	SLTGLSISSTPPAVS HCCCCCCCCCCCCHH	25.45	26074081
263	Phosphorylation	LTGLSISSTPPAVSS CCCCCCCCCCCCHHH	43.17	26074081
263	O-linked_Glycosylation	LTGLSISSTPPAVSS CCCCCCCCCCCCHHH	43.17	23301498
264	Phosphorylation	TGLSISSTPPAVSSV CCCCCCCCCCCHHHH	26.88	26074081
269	O-linked_Glycosylation	SSTPPAVSSVLSTGV CCCCCCHHHHHCCCC	19.48	23301498
274	O-linked_Glycosylation	AVSSVLSTGVPTVPL CHHHHHCCCCCCCCC	37.73	23301498
301	O-linked_Glycosylation	PPMNPATTLPGLMPL CCCCCCCCCCCCCCC	32.82	23301498
347 (in isoform 2)	Phosphorylation	-	5.10	24719451
347	Phosphorylation	GLPPLPSMPPRNLPG CCCCCCCCCCCCCCC	5.10	32142685
352 (in isoform 2)	Ubiquitination	-	4.31	-
352	Ubiquitination	PSMPPRNLPGIAPLP CCCCCCCCCCCCCCC	4.31	23503661
362	Phosphorylation	IAPLPLPSEFLPSFP CCCCCCCCCCCCCCC	48.98	28348404
365	Phosphorylation	LPLPSEFLPSFPLVP CCCCCCCCCCCCCCC	2.81	33259812
365 (in isoform 2)	Phosphorylation	-	2.81	24719451
367	Phosphorylation	LPSEFLPSFPLVPES CCCCCCCCCCCCCCC	41.46	28348404
374	Phosphorylation	SFPLVPESSSAASSG CCCCCCCCCCCCCCC	24.43	28348404
375	Phosphorylation	FPLVPESSSAASSGE CCCCCCCCCCCCCCC	23.49	28348404
376	Phosphorylation	PLVPESSSAASSGEL CCCCCCCCCCCCCCH	36.81	28348404
379	Phosphorylation	PESSSAASSGELLSS CCCCCCCCCCCHHHC	38.30	28348404
380	Phosphorylation	ESSSAASSGELLSSL CCCCCCCCCCHHHCC	31.40	28348404
381 (in isoform 2)	Phosphorylation	-	27.38	24719451
383 (in isoform 2)	Phosphorylation	-	6.84	24719451
385	Phosphorylation	ASSGELLSSLPPTSN CCCCCHHHCCCCCCC	42.31	28348404
386	Phosphorylation	SSGELLSSLPPTSNA CCCCHHHCCCCCCCC	44.88	29496963
390	Phosphorylation	LLSSLPPTSNAPSDP HHHCCCCCCCCCCCC	32.45	28348404
391	O-linked_Glycosylation	LSSLPPTSNAPSDPA HHCCCCCCCCCCCCC	36.45	23301498
391	Phosphorylation	LSSLPPTSNAPSDPA HHCCCCCCCCCCCCC	36.45	28348404
408	Phosphorylation	TAKADAASSLTVDVT CCCCHHHHCCEEECC	27.83	23401153
409	Phosphorylation	AKADAASSLTVDVTP CCCHHHHCCEEECCC	24.27	28355574
409	O-linked_Glycosylation	AKADAASSLTVDVTP CCCHHHHCCEEECCC	24.27	23301498
411	Phosphorylation	ADAASSLTVDVTPPT CHHHHCCEEECCCCC	19.33	30278072
415	Phosphorylation	SSLTVDVTPPTAKAP HCCEEECCCCCCCCC	21.06	19664994
418	Phosphorylation	TVDVTPPTAKAPTTV EEECCCCCCCCCCCC	41.83	30266825
420	Ubiquitination	DVTPPTAKAPTTVED ECCCCCCCCCCCCCC	58.33	23503661
423	Phosphorylation	PPTAKAPTTVEDRVG CCCCCCCCCCCCCCC	48.62	28176443
424	Phosphorylation	PTAKAPTTVEDRVGD CCCCCCCCCCCCCCC	22.34	28450419
424	O-linked_Glycosylation	PTAKAPTTVEDRVGD CCCCCCCCCCCCCCC	22.34	23301498
428	Methylation	APTTVEDRVGDSTPV CCCCCCCCCCCCCCC	22.32	-
432	Phosphorylation	VEDRVGDSTPVSEKP CCCCCCCCCCCCCCC	28.78	25159151
432	Ubiquitination	VEDRVGDSTPVSEKP CCCCCCCCCCCCCCC	28.78	-
433	Phosphorylation	EDRVGDSTPVSEKPV CCCCCCCCCCCCCCC	32.23	19664994
436	Phosphorylation	VGDSTPVSEKPVSAA CCCCCCCCCCCCCEE	40.90	25159151
438	Acetylation	DSTPVSEKPVSAAVD CCCCCCCCCCCEECC	43.12	26051181
441	Phosphorylation	PVSEKPVSAAVDANA CCCCCCCCEECCCCC	21.02	30278072
449	Phosphorylation	AAVDANASESP---- EECCCCCCCCC----	38.11	29255136
451	Phosphorylation	VDANASESP------ CCCCCCCCC------	33.15	19664994

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
222	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
222	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
225	T	Phosphorylation	Kinase	CDK2	P24941	PSP
225	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
225	T	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
441	S	Phosphorylation		21884936
ER stress-induced phosphorylation at Ser-441 induces monomerization and subsequent relocalization from Golgi to ER which is essential for mediating unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane.

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 GORS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
T22D4_HUMAN	TSC22D4	physical	16189514
TMED2_HUMAN	TMED2	physical	11739402
GO45_HUMAN	BLZF1	physical	11739402
TMED3_HUMAN	TMED3	physical	11739402
TGFA_HUMAN	TGFA	physical	11739402
TMEDA_HUMAN	TMED10	physical	11739402
GOGA2_HUMAN	GOLGA2	physical	11739402
GOGA2_HUMAN	GOLGA2	physical	11739401
GOGA2_HUMAN	GOLGA2	physical	21900206
A4_HUMAN	APP	physical	21832049
NONO_HUMAN	NONO	physical	22939629
LTOR5_HUMAN	LAMTOR5	physical	22939629
RMD3_HUMAN	RMDN3	physical	22939629
LTBP3_HUMAN	LTBP3	physical	21988832
GCP60_HUMAN	ACBD3	physical	22863883
BLMH_HUMAN	BLMH	physical	22863883
BOP1_HUMAN	BOP1	physical	22863883
CUL3_HUMAN	CUL3	physical	22863883
GARS_HUMAN	GARS	physical	22863883
MAOX_HUMAN	ME1	physical	22863883
RUSD2_HUMAN	RPUSD2	physical	22863883
TBCD_HUMAN	TBCD	physical	22863883
UGDH_HUMAN	UGDH	physical	22863883
AAMDC_HUMAN	AAMDC	physical	25416956
SCND1_HUMAN	SCAND1	physical	25416956
KCTD9_HUMAN	KCTD9	physical	25416956
ENOX1_HUMAN	ENOX1	physical	25416956
DUS21_HUMAN	DUSP21	physical	25416956
TEKT3_HUMAN	TEKT3	physical	25416956
BEND5_HUMAN	BEND5	physical	25416956
MLP3B_HUMAN	MAP1LC3B	physical	25416956
ZMAT1_HUMAN	ZMAT1	physical	25416956
CA094_HUMAN	C1orf94	physical	25416956
LONF1_HUMAN	LONRF1	physical	25416956
ACY3_HUMAN	ACY3	physical	25416956
PNMA5_HUMAN	PNMA5	physical	25416956
GABP2_HUMAN	GABPB2	physical	25416956
TXLNA_HUMAN	TXLNA	physical	25416956
STOX1_HUMAN	STOX1	physical	25416956
CC153_HUMAN	CCDC153	physical	25416956
MORN2_HUMAN	MORN2	physical	25416956
AHNK_HUMAN	AHNAK	physical	26344197
DDX43_HUMAN	DDX43	physical	26344197
FA98B_HUMAN	FAM98B	physical	26344197
GLYM_HUMAN	SHMT2	physical	26344197
RGS3_HUMAN	RGS3	physical	21516116
TEKT3_HUMAN	TEKT3	physical	21516116
BEND5_HUMAN	BEND5	physical	21516116
ACY3_HUMAN	ACY3	physical	21516116
KIF14_HUMAN	KIF14	physical	28514442
GOGA2_HUMAN	GOLGA2	physical	28514442
ISCA1_HUMAN	ISCA1	physical	28514442
TMED7_HUMAN	TMED7	physical	28514442
KBP_HUMAN	KIAA1279	physical	28514442
TMED4_HUMAN	TMED4	physical	28514442
FLOT2_HUMAN	FLOT2	physical	28514442
FLOT1_HUMAN	FLOT1	physical	28514442

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 GORS2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-415 AND SER-451, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222; THR-225; THR-415;THR-433 AND SER-451, AND MASS SPECTROMETRY.	19413330 [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-415; THR-433; SER-436;SER-449 AND SER-451, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; THR-222 ANDTHR-225, AND MASS SPECTROMETRY.	17287340 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-415 AND SER-451, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"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 THR-222; THR-225 ANDTHR-415, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Mitotic phosphorylation of Golgi reassembly stacking protein 55 bymitogen-activated protein kinase ERK2."; Jesch S.A., Lewis T.S., Ahn N.G., Linstedt A.D.; Mol. Biol. Cell 12:1811-1817(2001). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-225,AND MUTAGENESIS.	11408587 [Abstract]

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