dbPTM

GOGA5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GOGA5_HUMAN
UniProt AC	Q8TBA6
Protein Name	Golgin subfamily A member 5
Gene Name	GOLGA5
Organism	Homo sapiens (Human).
Sequence Length	731
Subcellular Localization	Golgi apparatus membrane Single-pass type IV membrane protein . Found throughout the Golgi, both on cisternae and, at higher abundance, on the tubulo-vesicular structures of the cis-Golgi network.
Protein Description	Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport..
Protein Sequence	MSWFVDLAGKAEDLLNRVDQGAATALSRKDNASNIYSKNTDYTELHQQNTDLIYQTGPKSTYISSAADNIRNQKATILAGTANVKVGSRTPVEASHPVENASVPRPSSHFVRRKKSEPDDELLFDFLNSSQKEPTGRVEIRKEKGKTPVFQSSQTSSVSSVNPSVTTIKTIEENSFGSQTHEAASNSDSSHEGQEESSKENVSSNAACPDHTPTPNDDGKSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQMNSASGSSSNGSSINMSGIDNGEGTRLRNVPVLFNDTETNLAGMYGKVRKAASSIDQFSIRLGIFLRRYPIARVFVIIYMALLHLWVMIVLLTYTPEMHHDQPYGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSWFVDLAG ------CCCCCCCCC	29.26	28348404
2	Acetylation	------MSWFVDLAG ------CCCCCCCCC	29.26	22223895
33	Phosphorylation	LSRKDNASNIYSKNT HHCCCCHHHCCCCCC	29.98	27251275
36	Phosphorylation	KDNASNIYSKNTDYT CCCHHHCCCCCCCHH	20.17	27642862
37	Phosphorylation	DNASNIYSKNTDYTE CCHHHCCCCCCCHHH	18.68	-
38	Ubiquitination	NASNIYSKNTDYTEL CHHHCCCCCCCHHHH	47.06	29967540
40	Phosphorylation	SNIYSKNTDYTELHQ HHCCCCCCCHHHHHH	33.83	21945579
42	Phosphorylation	IYSKNTDYTELHQQN CCCCCCCHHHHHHHC	10.48	21945579
43	Phosphorylation	YSKNTDYTELHQQNT CCCCCCHHHHHHHCC	34.58	21945579
50	Phosphorylation	TELHQQNTDLIYQTG HHHHHHCCCEEEECC	28.04	21945579
54	Phosphorylation	QQNTDLIYQTGPKST HHCCCEEEECCCCCH	13.81	21945579
56	Phosphorylation	NTDLIYQTGPKSTYI CCCEEEECCCCCHHC	38.18	21945579
60	Phosphorylation	IYQTGPKSTYISSAA EEECCCCCHHCCHHH	29.58	28796482
61	Phosphorylation	YQTGPKSTYISSAAD EECCCCCHHCCHHHH	30.88	28796482
62	Phosphorylation	QTGPKSTYISSAADN ECCCCCHHCCHHHHH	13.09	28796482
64	Phosphorylation	GPKSTYISSAADNIR CCCCHHCCHHHHHHH	11.96	-
74	Methylation	ADNIRNQKATILAGT HHHHHHCCCEEEEEC	51.55	-
81	Phosphorylation	KATILAGTANVKVGS CCEEEEECCCEEECC	14.95	-
88	Phosphorylation	TANVKVGSRTPVEAS CCCEEECCCCCCCCC	35.65	29978859
89	Methylation	ANVKVGSRTPVEASH CCEEECCCCCCCCCC	36.80	-
90	Phosphorylation	NVKVGSRTPVEASHP CEEECCCCCCCCCCC	33.12	25849741
95	Phosphorylation	SRTPVEASHPVENAS CCCCCCCCCCCCCCC	18.15	26657352
102	Phosphorylation	SHPVENASVPRPSSH CCCCCCCCCCCCCCH	44.21	26425664
107	Phosphorylation	NASVPRPSSHFVRRK CCCCCCCCCHHCCCC	37.41	22210691
116	Phosphorylation	HFVRRKKSEPDDELL HHCCCCCCCCCCHHH	58.35	29255136
129	Phosphorylation	LLFDFLNSSQKEPTG HHHHHHHCCCCCCCC	35.97	29507054
130	Phosphorylation	LFDFLNSSQKEPTGR HHHHHHCCCCCCCCC	44.17	25159151
135	Phosphorylation	NSSQKEPTGRVEIRK HCCCCCCCCCEEEEH	38.42	21712546
147	Phosphorylation	IRKEKGKTPVFQSSQ EEHHCCCCCEECCCC	33.10	22210691
152	Phosphorylation	GKTPVFQSSQTSSVS CCCCEECCCCCCCCC	16.98	22210691
153	Phosphorylation	KTPVFQSSQTSSVSS CCCEECCCCCCCCCC	27.05	22210691
156	Phosphorylation	VFQSSQTSSVSSVNP EECCCCCCCCCCCCC	22.55	27251275
157	Phosphorylation	FQSSQTSSVSSVNPS ECCCCCCCCCCCCCC	29.43	27251275
159	Phosphorylation	SSQTSSVSSVNPSVT CCCCCCCCCCCCCCE	30.43	22210691
160	Phosphorylation	SQTSSVSSVNPSVTT CCCCCCCCCCCCCEE	24.61	27251275
170	Phosphorylation	PSVTTIKTIEENSFG CCCEEEEEEECCCCC	29.75	27251275
175	Phosphorylation	IKTIEENSFGSQTHE EEEEECCCCCHHHCC	33.97	27251275
178	Phosphorylation	IEENSFGSQTHEAAS EECCCCCHHHCCHHH	29.87	23927012
180	Phosphorylation	ENSFGSQTHEAASNS CCCCCHHHCCHHHCC	24.31	27251275
185	Phosphorylation	SQTHEAASNSDSSHE HHHCCHHHCCCCCCC	43.87	23927012
187	Phosphorylation	THEAASNSDSSHEGQ HCCHHHCCCCCCCCC	36.05	23927012
189	Phosphorylation	EAASNSDSSHEGQEE CHHHCCCCCCCCCHH	33.15	23927012
190	Phosphorylation	AASNSDSSHEGQEES HHHCCCCCCCCCHHH	30.46	23927012
197	Phosphorylation	SHEGQEESSKENVSS CCCCCHHHHHHCCCC	46.05	27251275
198	Phosphorylation	HEGQEESSKENVSSN CCCCHHHHHHCCCCC	47.47	27251275
203	Phosphorylation	ESSKENVSSNAACPD HHHHHCCCCCCCCCC	29.47	25159151
204	Phosphorylation	SSKENVSSNAACPDH HHHHCCCCCCCCCCC	26.63	23312004
212	Phosphorylation	NAACPDHTPTPNDDG CCCCCCCCCCCCCCC	35.92	28450419
214	Phosphorylation	ACPDHTPTPNDDGKS CCCCCCCCCCCCCCC	35.56	28450419
225	Phosphorylation	DGKSHELSNLRLENQ CCCCHHHHHHHHHHH	30.73	24719451
275	2-Hydroxyisobutyrylation	KWNADHSKSDRMTRG HHCCCCCHHHHHHHH	53.61	-
276	Phosphorylation	WNADHSKSDRMTRGL HCCCCCHHHHHHHHH	33.20	20068231
280	Phosphorylation	HSKSDRMTRGLRAQV CCHHHHHHHHHHHHH	23.60	20068231
291	Phosphorylation	RAQVDDLTEAVAAKD HHHHHHHHHHHHHCC	28.97	22210691
299	Phosphorylation	EAVAAKDSQLAVLKV HHHHHCCCCEEEEEH	26.79	22210691
305	2-Hydroxyisobutyrylation	DSQLAVLKVRLQEAD CCCEEEEEHHHHHHH	20.79	-
337	Phosphorylation	SRIMQDQSEGNSLQN HHHCCCHHHCCHHHH	56.62	24275569
341	Phosphorylation	QDQSEGNSLQNQALQ CCHHHCCHHHHHHHH	42.04	27251275
367	Phosphorylation	TLKREQESYKQMQSE HHHHHHHHHHHHHHH	37.01	28857561
417	Phosphorylation	LQQQVKLYKLNLESS HHHHHHHHCCCCCCC	14.01	-
418	Malonylation	QQQVKLYKLNLESSK HHHHHHHCCCCCCCH	41.14	32601280
444	Malonylation	RILQSKEKLINSLKE HHHHCHHHHHHHHHC	59.40	26320211
453	Phosphorylation	INSLKEGSGFEGLDS HHHHHCCCCCCCCCC	41.21	26425664
460	Phosphorylation	SGFEGLDSSTASSME CCCCCCCCCCCCHHH	34.33	28348404
461	Phosphorylation	GFEGLDSSTASSMEL CCCCCCCCCCCHHHH	27.88	25849741
462	Phosphorylation	FEGLDSSTASSMELE CCCCCCCCCCHHHHH	34.21	27251275
464	Phosphorylation	GLDSSTASSMELEEL CCCCCCCCHHHHHHH	30.24	28985074
465	Phosphorylation	LDSSTASSMELEELR CCCCCCCHHHHHHHH	17.51	27251275
544	Phosphorylation	RLKQEFHYIEEDLYR HHHHHHHHHHHHHHH	18.49	25884760
550	Phosphorylation	HYIEEDLYRTKNTLQ HHHHHHHHHCHHHHH	28.67	-
558	Phosphorylation	RTKNTLQSRIKDRDE HCHHHHHHHHCCHHH	38.80	23403867
577	Ubiquitination	LRNQLTNKTLSNSSQ HHHHHHHCCCCCCCH	45.68	32015554
582	Phosphorylation	TNKTLSNSSQSELEN HHCCCCCCCHHHHHH	26.78	27251275
583	Phosphorylation	NKTLSNSSQSELENR HCCCCCCCHHHHHHH	41.81	25159151
585	Phosphorylation	TLSNSSQSELENRLH CCCCCCHHHHHHHHH	46.20	26471730
601	Ubiquitination	LTETLIQKQTMLESL HHHHHHHHHHHHHHC	40.52	32015554
612	Ubiquitination	LESLSTEKNSLVFQL HHHCCCCCCHHHHHH	52.50	32015554
614	Phosphorylation	SLSTEKNSLVFQLER HCCCCCCHHHHHHHH	36.66	28555341
630	Phosphorylation	EQQMNSASGSSSNGS HHHHHHCCCCCCCCC	38.74	22210691
632	Phosphorylation	QMNSASGSSSNGSSI HHHHCCCCCCCCCCC	28.26	27251275
633	Phosphorylation	MNSASGSSSNGSSIN HHHCCCCCCCCCCCC	31.20	27251275
634	Phosphorylation	NSASGSSSNGSSINM HHCCCCCCCCCCCCC	47.08	27251275
637	Phosphorylation	SGSSSNGSSINMSGI CCCCCCCCCCCCCCC	32.09	22468782
638	Phosphorylation	GSSSNGSSINMSGID CCCCCCCCCCCCCCC	21.27	22210691
650	Phosphorylation	GIDNGEGTRLRNVPV CCCCCCCCCCCCCCE	23.41	22210691
662	Phosphorylation	VPVLFNDTETNLAGM CCEEECCCCCCHHHH	45.90	26657352
664	Phosphorylation	VLFNDTETNLAGMYG EEECCCCCCHHHHHH	37.31	27251275
670	Phosphorylation	ETNLAGMYGKVRKAA CCCHHHHHHHHHHHH	16.93	-
672	Ubiquitination	NLAGMYGKVRKAASS CHHHHHHHHHHHHHC	22.75	32015554
675	Ubiquitination	GMYGKVRKAASSIDQ HHHHHHHHHHHCCCH	51.82	33845483

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 GOGA5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GOGA5_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 GOGA5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PKN3_HUMAN	PKN3	physical	27173435
TFPT_HUMAN	TFPT	physical	27173435
YETS4_HUMAN	YEATS4	physical	27173435
CLOCK_HUMAN	CLOCK	physical	27173435
PSMD9_HUMAN	PSMD9	physical	27173435
VPS50_HUMAN	CCDC132	physical	27173435
CAVN1_HUMAN	PTRF	physical	27173435
HAUS6_HUMAN	HAUS6	physical	27173435
RPR1A_HUMAN	RPRD1A	physical	27173435
BMAL1_HUMAN	ARNTL	physical	27173435
RABX5_HUMAN	RABGEF1	physical	27173435
NUF2_HUMAN	NUF2	physical	27173435
EIPR1_HUMAN	TSSC1	physical	27173435
STRN_HUMAN	STRN	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
188550	Thyroid papillary carcinoma (TPC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GOGA5_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-116, AND MASSSPECTROMETRY.	18669648 [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 SER-116, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42 AND TYR-54, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42 AND TYR-54, AND MASSSPECTROMETRY.	15144186 [Abstract]