dbPTM

GOGA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GOGA2_HUMAN
UniProt AC	Q08379
Protein Name	Golgin subfamily A member 2
Gene Name	GOLGA2
Organism	Homo sapiens (Human).
Sequence Length	1002
Subcellular Localization	Golgi apparatus, cis-Golgi network membrane Peripheral membrane protein . Cytoplasm, cytoskeleton, spindle pole . Peripheral membrane protein associated with cis-Golgi stacks (By similarity). Associates with the mitotic spindle during mitosis (PubM
Protein Description	Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane. Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (By similarity). Also plays a key role in spindle pole assembly and centrosome organization. [PubMed: 26165940 Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle]
Protein Sequence	MWPQPRLPPRPAMSEETRQSKLAAAKKKLREYQQRNSPGVPTGAKKKKKIKNGSNPETTTSGGCHSPEDTPKDNAATLQPSDDTVLPGGVPSPGASLTSMAASQNHDADNVPNLMDETKTFSSTESLRQLSQQLNGLVCESATCVNGEGPASSANLKDLESRYQQLAVALDSSYVTNKQLNITIEKLKQQNQEITDQLEEEKKECHQKQGALREQLQVHIQTIGILVSEKAELQTALAHTQHAARQKEGESEDLASRLQYSRRRVGELERALSAVSTQQKKADRYNKELTKERDALRLELYKNTQSNEDLKQEKSELEEKLRVLVTEKAGMQLNLEELQKKLEMTELLLQQFSSRCEAPDANQQLQQAMEERAQLEAHLGQVMESVRQLQMERDKYAENLKGESAMWRQRMQQMSEQVHTLREEKECSMSRVQELETSLAELRNQMAEPPPPEPPAGPSEVEQQLQAEAEHLRKELEGLAGQLQAQVQDNEGLSRLNREQEERLLELERAAELWGEQAEARRQILETMQNDRTTISRALSQNRELKEQLAELQSGFVKLTNENMEITSALQSEQHVKRELGKKLGELQEKLSELKETVELKSQEAQSLQQQRDQYLGHLQQYVAAYQQLTSEKEVLHNQLLLQTQLVDQLQQQEAQGKAVAEMARQELQETQERLEAATQQNQQLRAQLSLMAHPGEGDGLDREEEEDEEEEEEEAVAVPQPMPSIPEDLESREAMVAFFNSAVASAEEEQARLRGQLKEQRVRCRRLAHLLASAQKEPEAAAPAPGTGGDSVCGETHRALQGAMEKLQSRFMELMQEKADLKERVEELEHRCIQLSGETDTIGEYIALYQSQRAVLKERHREKEEYISRLAQDKEEMKVKLLELQELVLRLVGDRNEWHGRFLAAAQNPADEPTSGAPAPQELGAANQQGDLCEVSLAGSVEPAQGEAREGSPRDNPTAQQIMQLLREMQNPRERPGLGSNPCIPFFYRADENDEVKITVI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MWPQPRLPPRPAMSE CCCCCCCCCCCCCCH	24.92	16097034
14	Phosphorylation	LPPRPAMSEETRQSK CCCCCCCCHHHHHHH	34.09	28555341
18	Methylation	PAMSEETRQSKLAAA CCCCHHHHHHHHHHH	41.89	20421892
20	Phosphorylation	MSEETRQSKLAAAKK CCHHHHHHHHHHHHH	26.75	16097034
21	Acetylation	SEETRQSKLAAAKKK CHHHHHHHHHHHHHH	33.53	25953088
25	Phosphorylation	RQSKLAAAKKKLREY HHHHHHHHHHHHHHH	20.70	18669648
27	Ubiquitination	SKLAAAKKKLREYQQ HHHHHHHHHHHHHHH	52.92	24816145
30	Methylation	AAAKKKLREYQQRNS HHHHHHHHHHHHHCC	49.83	20421892
32	Phosphorylation	AKKKLREYQQRNSPG HHHHHHHHHHHCCCC	11.96	20860994
35	Methylation	KLREYQQRNSPGVPT HHHHHHHHCCCCCCC	30.02	20421892
37	Dephosphorylation	REYQQRNSPGVPTGA HHHHHHCCCCCCCCH	25.81	10769027
37	Phosphorylation	REYQQRNSPGVPTGA HHHHHHCCCCCCCCH	25.81	30266825
42	Phosphorylation	RNSPGVPTGAKKKKK HCCCCCCCCHHCCCC	47.57	23403867
45	Acetylation	PGVPTGAKKKKKIKN CCCCCCHHCCCCCCC	67.48	25953088
47	Acetylation	VPTGAKKKKKIKNGS CCCCHHCCCCCCCCC	59.60	7469369
51	Ubiquitination	AKKKKKIKNGSNPET HHCCCCCCCCCCCCC	65.22	-
54	Phosphorylation	KKKIKNGSNPETTTS CCCCCCCCCCCCCCC	59.61	25159151
58	Phosphorylation	KNGSNPETTTSGGCH CCCCCCCCCCCCCCC	36.31	23663014
59	Phosphorylation	NGSNPETTTSGGCHS CCCCCCCCCCCCCCC	19.80	25159151
60	Phosphorylation	GSNPETTTSGGCHSP CCCCCCCCCCCCCCC	32.56	22115753
61	Phosphorylation	SNPETTTSGGCHSPE CCCCCCCCCCCCCCC	30.97	22617229
63 (in isoform 2)	Ubiquitination	-	13.01	21906983
66	Phosphorylation	TTSGGCHSPEDTPKD CCCCCCCCCCCCCCC	33.78	25159151
70	Phosphorylation	GCHSPEDTPKDNAAT CCCCCCCCCCCCCCC	30.49	23663014
77	Phosphorylation	TPKDNAATLQPSDDT CCCCCCCCCCCCCCC	24.42	20068231
81	Phosphorylation	NAATLQPSDDTVLPG CCCCCCCCCCCCCCC	34.85	20068231
84	Phosphorylation	TLQPSDDTVLPGGVP CCCCCCCCCCCCCCC	29.00	20068231
92	Phosphorylation	VLPGGVPSPGASLTS CCCCCCCCCCCCHHH	33.29	29496963
96	Phosphorylation	GVPSPGASLTSMAAS CCCCCCCCHHHHHHH	37.79	26074081
98	Phosphorylation	PSPGASLTSMAASQN CCCCCCHHHHHHHCC	17.60	20068231
99	Phosphorylation	SPGASLTSMAASQNH CCCCCHHHHHHHCCC	16.24	20068231
103	Phosphorylation	SLTSMAASQNHDADN CHHHHHHHCCCCCCC	23.21	20068231
118	Phosphorylation	VPNLMDETKTFSSTE CCCCCCHHCCCCCHH	30.99	30278072
120	Phosphorylation	NLMDETKTFSSTESL CCCCHHCCCCCHHHH	35.85	27732954
122	Phosphorylation	MDETKTFSSTESLRQ CCHHCCCCCHHHHHH	41.40	30108239
123	Phosphorylation	DETKTFSSTESLRQL CHHCCCCCHHHHHHH	31.81	30108239
124	Phosphorylation	ETKTFSSTESLRQLS HHCCCCCHHHHHHHH	28.53	30108239
126	Phosphorylation	KTFSSTESLRQLSQQ CCCCCHHHHHHHHHH	29.01	30108239
131	Phosphorylation	TESLRQLSQQLNGLV HHHHHHHHHHHCCCC	13.93	27251275
152	Phosphorylation	VNGEGPASSANLKDL CCCCCCCCCCCHHHH	32.87	27251275
163	Phosphorylation	LKDLESRYQQLAVAL HHHHHHHHHHHHHHH	15.19	27642862
174	Phosphorylation	AVALDSSYVTNKQLN HHHHCCHHHCCHHHC	18.42	25884760
195	Phosphorylation	KQQNQEITDQLEEEK HHHCHHHHHHHHHHH	19.55	30619164
202 (in isoform 1)	Ubiquitination	-	58.09	21906983
202	Ubiquitination	TDQLEEEKKECHQKQ HHHHHHHHHHHHHHH	58.09	21906983
220	Ubiquitination	REQLQVHIQTIGILV HHHHHHHHHHHHHHH	3.98	24816145
247	Ubiquitination	TQHAARQKEGESEDL HHHHHHHCCCCCHHH	63.23	24816145
251	Phosphorylation	ARQKEGESEDLASRL HHHCCCCCHHHHHHH	47.47	21406692
253	Ubiquitination	QKEGESEDLASRLQY HCCCCCHHHHHHHHH	57.73	24816145
256	Phosphorylation	GESEDLASRLQYSRR CCCHHHHHHHHHHHH	40.60	21406692
273	Phosphorylation	GELERALSAVSTQQK HHHHHHHHHHHHHHH	26.16	28450419
274	Ubiquitination	ELERALSAVSTQQKK HHHHHHHHHHHHHHH	10.50	24816145
276	Phosphorylation	ERALSAVSTQQKKAD HHHHHHHHHHHHHHH	21.88	25072903
277	Phosphorylation	RALSAVSTQQKKADR HHHHHHHHHHHHHHH	28.55	25072903
280	2-Hydroxyisobutyrylation	SAVSTQQKKADRYNK HHHHHHHHHHHHHHH	39.86	-
280	Ubiquitination	SAVSTQQKKADRYNK HHHHHHHHHHHHHHH	39.86	24816145
302	Ubiquitination	ALRLELYKNTQSNED HHHHHHHHCCCCCHH	67.17	-
307	Ubiquitination	LYKNTQSNEDLKQEK HHHCCCCCHHHHHHH	36.66	24816145
320	Ubiquitination	EKSELEEKLRVLVTE HHHHHHHHHHHHHHH	32.02	-
320	2-Hydroxyisobutyrylation	EKSELEEKLRVLVTE HHHHHHHHHHHHHHH	32.02	-
415	Phosphorylation	RQRMQQMSEQVHTLR HHHHHHHHHHHHHHH	22.12	28555341
420	Phosphorylation	QMSEQVHTLREEKEC HHHHHHHHHHHHHHH	28.75	28509920
426	Phosphorylation	HTLREEKECSMSRVQ HHHHHHHHHCHHHHH	34.79	18669648
437	Phosphorylation	SRVQELETSLAELRN HHHHHHHHHHHHHHH	41.48	30266825
438	Phosphorylation	RVQELETSLAELRNQ HHHHHHHHHHHHHHH	19.06	30266825
474	Ubiquitination	AEAEHLRKELEGLAG HHHHHHHHHHHHHHH	73.36	-
532	Methylation	LETMQNDRTTISRAL HHHHHHCHHHHHHHH	41.12	-
540	Phosphorylation	TTISRALSQNRELKE HHHHHHHHCCHHHHH	25.15	24719451
546	Ubiquitination	LSQNRELKEQLAELQ HHCCHHHHHHHHHHH	38.37	-
577	2-Hydroxyisobutyrylation	LQSEQHVKRELGKKL HHCHHHHHHHHHHHH	37.72	-
583	Ubiquitination	VKRELGKKLGELQEK HHHHHHHHHHHHHHH	60.98	29967540
590	Ubiquitination	KLGELQEKLSELKET HHHHHHHHHHHHHHH	44.33	2190698
590 (in isoform 1)	Ubiquitination	-	44.33	21906983
595	Ubiquitination	QEKLSELKETVELKS HHHHHHHHHHHHHHH	47.49	-
690	Phosphorylation	QQLRAQLSLMAHPGE HHHHHHHHHHCCCCC	12.20	22067460
774	Phosphorylation	RLAHLLASAQKEPEA HHHHHHHHHHCCCHH	31.07	18491316
777	Ubiquitination	HLLASAQKEPEAAAP HHHHHHHCCCHHCCC	74.97	-
780	Ubiquitination	ASAQKEPEAAAPAPG HHHHCCCHHCCCCCC	52.62	24816145
788	Phosphorylation	AAAPAPGTGGDSVCG HCCCCCCCCCCCCCH	36.61	27251275
792	Phosphorylation	APGTGGDSVCGETHR CCCCCCCCCCHHHHH	23.68	25849741
795	Ubiquitination	TGGDSVCGETHRALQ CCCCCCCHHHHHHHH	40.45	32015554
797	Phosphorylation	GDSVCGETHRALQGA CCCCCHHHHHHHHHH	11.27	27251275
807	Ubiquitination	ALQGAMEKLQSRFME HHHHHHHHHHHHHHH	38.45	32015554
819	Ubiquitination	FMELMQEKADLKERV HHHHHHHHHHHHHHH	30.24	-
819	2-Hydroxyisobutyrylation	FMELMQEKADLKERV HHHHHHHHHHHHHHH	30.24	-
822	Ubiquitination	LMQEKADLKERVEEL HHHHHHHHHHHHHHH	8.09	32015554
834	Ubiquitination	EELEHRCIQLSGETD HHHHHHHHHHCCCCC	4.68	24816145
850	Phosphorylation	IGEYIALYQSQRAVL HHHHHHHHHHHHHHH	9.33	-
864	2-Hydroxyisobutyrylation	LKERHREKEEYISRL HHHHHHHHHHHHHHH	56.66	-
881	Ubiquitination	DKEEMKVKLLELQEL CHHHHHHHHHHHHHH	41.66	-
937	Phosphorylation	QGDLCEVSLAGSVEP CCCCEEEEECCCCCC	7.10	24275569
941	Phosphorylation	CEVSLAGSVEPAQGE EEEEECCCCCCCCCC	20.07	17081983
947	Phosphorylation	GSVEPAQGEAREGSP CCCCCCCCCCCCCCC	32.41	18669648
953	Phosphorylation	QGEAREGSPRDNPTA CCCCCCCCCCCCHHH	16.41	25159151
959	Phosphorylation	GSPRDNPTAQQIMQL CCCCCCHHHHHHHHH	43.27	22617229
981	Phosphorylation	RERPGLGSNPCIPFF CCCCCCCCCCCEEEE	42.51	26363069

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
25	S	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
37	S	Phosphorylation	Kinase	CDK1	P06493	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
18	R	Methylation	20421892
While dimethylation at Arg-30 and Arg-35 are confirmed in vivo, it is unclear whether Arg-18 is methylated in vivo.
30	R	Methylation	20421892
While dimethylation at Arg-30 and Arg-35 are confirmed in vivo, it is unclear whether Arg-18 is methylated in vivo.
35	R	Methylation	20421892
While dimethylation at Arg-30 and Arg-35 are confirmed in vivo, it is unclear whether Arg-18 is methylated in vivo.
37	S	Phosphorylation	16964243
Phosphorylated at Ser-37 by CDK1 at the onset of mitosis, inhibiting the interaction with p115/USO1 and triggering Golgi disassembly.
37	S	Phosphorylation	16964243
Phosphorylated at Ser-37 in prophase as the Golgi complex starts to break down, and remains phosphorylated during further breakdown and partitioning of the Golgi fragments in metaphase and anaphase.

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 GOGA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GORS2_HUMAN	GORASP2	physical	10487747
ABLM1_HUMAN	ABLIM1	physical	16189514
ZN250_HUMAN	ZNF250	physical	16189514
GCP4_HUMAN	TUBGCP4	physical	16189514
TRI29_HUMAN	TRIM29	physical	16189514
P121A_HUMAN	POM121	physical	16189514
RAB2A_HUMAN	RAB2A	physical	16189514
USO1_HUMAN	USO1	physical	10931861
TMED2_HUMAN	TMED2	physical	11739402
GORS1_HUMAN	GORASP1	physical	11739402
GORS1_HUMAN	GORASP1	physical	11781572
GORS1_HUMAN	GORASP1	physical	10487747
RBL1_HUMAN	RBL1	physical	21988832
YTDC1_HUMAN	YTHDC1	physical	21988832
HXB9_HUMAN	HOXB9	physical	25416956
IP3KB_HUMAN	ITPKB	physical	25416956
KIFC3_HUMAN	KIFC3	physical	25416956
K2C6A_HUMAN	KRT6A	physical	25416956
K2C6B_HUMAN	KRT6B	physical	25416956
K1C18_HUMAN	KRT18	physical	25416956
LASP1_HUMAN	LASP1	physical	25416956
LCP2_HUMAN	LCP2	physical	25416956
LEG3_HUMAN	LGALS3	physical	25416956
RBTN1_HUMAN	LMO1	physical	25416956
RBTN2_HUMAN	LMO2	physical	25416956
MGN_HUMAN	MAGOH	physical	25416956
MCM7_HUMAN	MCM7	physical	25416956
MCSP_HUMAN	SMCP	physical	25416956
MFAP1_HUMAN	MFAP1	physical	25416956
MOS_HUMAN	MOS	physical	25416956
NCF2_HUMAN	NCF2	physical	25416956
NOS3_HUMAN	NOS3	physical	25416956
ORC1_HUMAN	ORC1	physical	25416956
CDK18_HUMAN	CDK18	physical	25416956
P85B_HUMAN	PIK3R2	physical	25416956
PIN1_HUMAN	PIN1	physical	25416956
AAPK1_HUMAN	PRKAA1	physical	25416956
AAKB2_HUMAN	PRKAB2	physical	25416956
PKN1_HUMAN	PKN1	physical	25416956
PSA1_HUMAN	PSMA1	physical	25416956
PSA4_HUMAN	PSMA4	physical	25416956
RAB2A_HUMAN	RAB2A	physical	25416956
SRSF2_HUMAN	SRSF2	physical	25416956
SMCE1_HUMAN	SMARCE1	physical	25416956
RSMB_HUMAN	SNRPB	physical	25416956
RU2B_HUMAN	SNRPB2	physical	25416956
RU1C_HUMAN	SNRPC	physical	25416956
TBP_HUMAN	TBP	physical	25416956
TCEA2_HUMAN	TCEA2	physical	25416956
TCF19_HUMAN	TCF19	physical	25416956
TEAD4_HUMAN	TEAD4	physical	25416956
TFAP4_HUMAN	TFAP4	physical	25416956
TPM1_HUMAN	TPM1	physical	25416956
UBC9_HUMAN	UBE2I	physical	25416956
ZN124_HUMAN	ZNF124	physical	25416956
ZBT16_HUMAN	ZBTB16	physical	25416956
GPAN1_HUMAN	GPANK1	physical	25416956
CUL5_HUMAN	CUL5	physical	25416956
TCL1A_HUMAN	TCL1A	physical	25416956
PKP4_HUMAN	PKP4	physical	25416956
LMO4_HUMAN	LMO4	physical	25416956
EIF3G_HUMAN	EIF3G	physical	25416956
SCEL_HUMAN	SCEL	physical	25416956
LIN7A_HUMAN	LIN7A	physical	25416956
PIAS2_HUMAN	PIAS2	physical	25416956
UBP2_HUMAN	USP2	physical	25416956
LATS1_HUMAN	LATS1	physical	25416956
VATG1_HUMAN	ATP6V1G1	physical	25416956
RBM39_HUMAN	RBM39	physical	25416956
MO4L2_HUMAN	MORF4L2	physical	25416956
UBE3C_HUMAN	UBE3C	physical	25416956
UT14C_HUMAN	UTP14C	physical	25416956
HDAC4_HUMAN	HDAC4	physical	25416956
DLGP5_HUMAN	DLGAP5	physical	25416956
SPAT2_HUMAN	SPATA2	physical	25416956
TSSC4_HUMAN	TSSC4	physical	25416956
PQBP1_HUMAN	PQBP1	physical	25416956
ARPC3_HUMAN	ARPC3	physical	25416956
ARL4A_HUMAN	ARL4A	physical	25416956
SPF27_HUMAN	BCAS2	physical	25416956
LYPA1_HUMAN	LYPLA1	physical	25416956
STK25_HUMAN	STK25	physical	25416956
KAT5_HUMAN	KAT5	physical	25416956
NEBL_HUMAN	NEBL	physical	25416956
SLU7_HUMAN	SLU7	physical	25416956
MB212_HUMAN	MAB21L2	physical	25416956
ARI5A_HUMAN	ARID5A	physical	25416956
MO4L1_HUMAN	MORF4L1	physical	25416956
IFT27_HUMAN	IFT27	physical	25416956
ADAP1_HUMAN	ADAP1	physical	25416956
TRIM1_HUMAN	MID2	physical	25416956
CPSF5_HUMAN	NUDT21	physical	25416956
COR1A_HUMAN	CORO1A	physical	25416956
SNF8_HUMAN	SNF8	physical	25416956
SCAF8_HUMAN	SCAF8	physical	25416956
BAHD1_HUMAN	BAHD1	physical	25416956
SNW1_HUMAN	SNW1	physical	25416956
TPX2_HUMAN	TPX2	physical	25416956
KDM1A_HUMAN	KDM1A	physical	25416956
SMAG1_HUMAN	SAMD4A	physical	25416956
GSE1_HUMAN	GSE1	physical	25416956
FBX28_HUMAN	FBXO28	physical	25416956
ISCU_HUMAN	ISCU	physical	25416956
ZFY26_HUMAN	ZFYVE26	physical	25416956
TRI29_HUMAN	TRIM29	physical	25416956
KANK2_HUMAN	KANK2	physical	25416956
GORS2_HUMAN	GORASP2	physical	25416956
PP16B_HUMAN	PPP1R16B	physical	25416956
PRP31_HUMAN	PRPF31	physical	25416956
FA50B_HUMAN	FAM50B	physical	25416956
PI5PA_HUMAN	INPP5J	physical	25416956
AFF4_HUMAN	AFF4	physical	25416956
RSP14_HUMAN	RSPH14	physical	25416956
GPKOW_HUMAN	GPKOW	physical	25416956
S30BP_HUMAN	SAP30BP	physical	25416956
NDK7_HUMAN	NME7	physical	25416956
MYEF2_HUMAN	MYEF2	physical	25416956
WASC3_HUMAN	CCDC53	physical	25416956
CHCH2_HUMAN	CHCHD2	physical	25416956
VPS28_HUMAN	VPS28	physical	25416956
DCTN4_HUMAN	DCTN4	physical	25416956
CDKL3_HUMAN	CDKL3	physical	25416956
VATD_HUMAN	ATP6V1D	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
ZN581_HUMAN	ZNF581	physical	25416956
CINP_HUMAN	CINP	physical	25416956
NB5R2_HUMAN	CYB5R2	physical	25416956
STK26_HUMAN	STK26	physical	25416956
SHC3_HUMAN	SHC3	physical	25416956
MBD3_HUMAN	MBD3	physical	25416956
CCHCR_HUMAN	CCHCR1	physical	25416956
F193B_HUMAN	FAM193B	physical	25416956
RB39A_HUMAN	RAB39A	physical	25416956
MIC19_HUMAN	CHCHD3	physical	25416956
CA109_HUMAN	C1orf109	physical	25416956
PCLI1_HUMAN	PID1	physical	25416956
VP37C_HUMAN	VPS37C	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
MGN2_HUMAN	MAGOHB	physical	25416956
F90A1_HUMAN	FAM90A1	physical	25416956
CN105_HUMAN	C14orf105	physical	25416956
CCD87_HUMAN	CCDC87	physical	25416956
RBM41_HUMAN	RBM41	physical	25416956
MCM10_HUMAN	MCM10	physical	25416956
LIMS2_HUMAN	LIMS2	physical	25416956
CCD94_HUMAN	CCDC94	physical	25416956
CCAR1_HUMAN	CCAR1	physical	25416956
RCOR3_HUMAN	RCOR3	physical	25416956
NXT2_HUMAN	NXT2	physical	25416956
F214A_HUMAN	FAM214A	physical	25416956
SKT_HUMAN	KIAA1217	physical	25416956
EXOS5_HUMAN	EXOSC5	physical	25416956
CBX8_HUMAN	CBX8	physical	25416956
P66B_HUMAN	GATAD2B	physical	25416956
STALP_HUMAN	STAMBPL1	physical	25416956
CC146_HUMAN	CCDC146	physical	25416956
RN213_HUMAN	RNF213	physical	25416956
ZN410_HUMAN	ZNF410	physical	25416956
ZN250_HUMAN	ZNF250	physical	25416956
SH24A_HUMAN	SH2D4A	physical	25416956
TTC23_HUMAN	TTC23	physical	25416956
RSRC2_HUMAN	RSRC2	physical	25416956
SCNM1_HUMAN	SCNM1	physical	25416956
FND11_HUMAN	C20orf195	physical	25416956
SEBP2_HUMAN	SECISBP2	physical	25416956
LENG1_HUMAN	LENG1	physical	25416956
MMTA2_HUMAN	C1orf35	physical	25416956
GCC1_HUMAN	GCC1	physical	25416956
CDC73_HUMAN	CDC73	physical	25416956
F184A_HUMAN	FAM184A	physical	25416956
F124B_HUMAN	FAM124B	physical	25416956
CSPP1_HUMAN	CSPP1	physical	25416956
FXL18_HUMAN	FBXL18	physical	25416956
ZFP2_HUMAN	ZFP2	physical	25416956
THAP7_HUMAN	THAP7	physical	25416956
NDEL1_HUMAN	NDEL1	physical	25416956
FIP1_HUMAN	FIP1L1	physical	25416956
T22D4_HUMAN	TSC22D4	physical	25416956
TSSK3_HUMAN	TSSK3	physical	25416956
CCD70_HUMAN	CCDC70	physical	25416956
TTC25_HUMAN	TTC25	physical	25416956
F110A_HUMAN	FAM110A	physical	25416956
RHNO1_HUMAN	RHNO1	physical	25416956
PDIP3_HUMAN	POLDIP3	physical	25416956
RN135_HUMAN	RNF135	physical	25416956
ZN414_HUMAN	ZNF414	physical	25416956
PAR6B_HUMAN	PARD6B	physical	25416956
ZGPAT_HUMAN	ZGPAT	physical	25416956
SPT22_HUMAN	SPATA22	physical	25416956
LIGO1_HUMAN	LINGO1	physical	25416956
ZN587_HUMAN	ZNF587	physical	25416956
RAB2B_HUMAN	RAB2B	physical	25416956
RITA1_HUMAN	RITA1	physical	25416956
SPF45_HUMAN	RBM17	physical	25416956
FBF1_HUMAN	FBF1	physical	25416956
F207A_HUMAN	FAM207A	physical	25416956
RGS8_HUMAN	RGS8	physical	25416956
GTPBA_HUMAN	GTPBP10	physical	25416956
IFT20_HUMAN	IFT20	physical	25416956
MTFR2_HUMAN	MTFR2	physical	25416956
DTX2_HUMAN	DTX2	physical	25416956
HAUS1_HUMAN	HAUS1	physical	25416956
RB39B_HUMAN	RAB39B	physical	25416956
SNP47_HUMAN	SNAP47	physical	25416956
HRSL5_HUMAN	HRASLS5	physical	25416956
ZN488_HUMAN	ZNF488	physical	25416956
GLCTK_HUMAN	GLYCTK	physical	25416956
ZN572_HUMAN	ZNF572	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
SYT6_HUMAN	SYT6	physical	25416956
UBE2U_HUMAN	UBE2U	physical	25416956
CCD17_HUMAN	CCDC17	physical	25416956
C2CD6_HUMAN	ALS2CR11	physical	25416956
ZMAT2_HUMAN	ZMAT2	physical	25416956
SH3R2_HUMAN	SH3RF2	physical	25416956
RIBC1_HUMAN	RIBC1	physical	25416956
DEUP1_HUMAN	CCDC67	physical	25416956
CL050_HUMAN	C12orf50	physical	25416956
CD20B_HUMAN	CDC20B	physical	25416956
TEANC_HUMAN	TCEANC	physical	25416956
PPR18_HUMAN	PPP1R18	physical	25416956
ZC3H1_HUMAN	ZFC3H1	physical	25416956
TXLNA_HUMAN	TXLNA	physical	25416956
HYLS1_HUMAN	HYLS1	physical	25416956
PATL1_HUMAN	PATL1	physical	25416956
ALKB3_HUMAN	ALKBH3	physical	25416956
VATC2_HUMAN	ATP6V1C2	physical	25416956
MSRB3_HUMAN	MSRB3	physical	25416956
BCL6B_HUMAN	BCL6B	physical	25416956
RN214_HUMAN	RNF214	physical	25416956
TTC9C_HUMAN	TTC9C	physical	25416956
MORN3_HUMAN	MORN3	physical	25416956
KANL1_HUMAN	KANSL1	physical	25416956
CC150_HUMAN	CCDC150	physical	25416956
RTP5_HUMAN	RTP5	physical	25416956
F126B_HUMAN	FAM126B	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
K2C6C_HUMAN	KRT6C	physical	25416956
TRI42_HUMAN	TRIM42	physical	25416956
ARL16_HUMAN	ARL16	physical	25416956
ZN774_HUMAN	ZNF774	physical	25416956
SELV_HUMAN	SELV	physical	25416956
LYSM1_HUMAN	LYSMD1	physical	25416956
CENPP_HUMAN	CENPP	physical	25416956
KANL1_HUMAN	KANSL1	physical	21516116
F126B_HUMAN	FAM126B	physical	21516116
THYN1_HUMAN	THYN1	physical	21516116
IP3KB_HUMAN	ITPKB	physical	21516116
DCTN4_HUMAN	DCTN4	physical	21516116
PTBP2_HUMAN	PTBP2	physical	21516116
TCF19_HUMAN	TCF19	physical	21516116
MMTA2_HUMAN	C1orf35	physical	21516116
CUL5_HUMAN	CUL5	physical	21516116
TSSK3_HUMAN	TSSK3	physical	21516116
AB17A_HUMAN	ABHD17A	physical	21516116
ZMAT1_HUMAN	ZMAT1	physical	21516116
RITA1_HUMAN	RITA1	physical	21516116
SPF45_HUMAN	RBM17	physical	21516116
SCEL_HUMAN	SCEL	physical	21516116
CCNH_HUMAN	CCNH	physical	21516116
UBE3C_HUMAN	UBE3C	physical	21516116
SFI1_HUMAN	SFI1	physical	21516116
ASAP3_HUMAN	ASAP3	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 GOGA2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-37 AND SER-438, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-438, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.	19007248 [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 SER-37, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	16097034 [Abstract]

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