dbPTM

GCC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GCC2_HUMAN
UniProt AC	Q8IWJ2
Protein Name	GRIP and coiled-coil domain-containing protein 2
Gene Name	GCC2
Organism	Homo sapiens (Human).
Sequence Length	1684
Subcellular Localization	Cytoplasm. Golgi apparatus, trans-Golgi network membrane Peripheral membrane protein.
Protein Description	Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2..
Protein Sequence	MEDLVQDGVASPATPGTGKSKLETLPKEDLIKFAKKQMMLIQKAKSRCTELEKEIEELRSKPVTEGTGDIIKALTERLDALLLEKAETEQQCLSLKKENIKMKQEVEDSVTKMGDAHKELEQSHINYVKEIENLKNELMAVRSKYSEDKANLQKQLEEAMNTQLELSEQLKFQNNSEDNVKKLQEEIEKIRPGFEEQILYLQKQLDATTDEKKETVTQLQNIIEANSQHYQKNINSLQEELLQLKAIHQEEVKELMCQIEASAKEHEAEINKLNELKENLVKQCEASEKNIQKKYECELENLRKATSNANQDNQICSILLQENTFVEQVVNEKVKHLEDTLKELESQHSILKDEVTYMNNLKLKLEMDAQHIKDEFFHEREDLEFKINELLLAKEEQGCVIEKLKSELAGLNKQFCYTVEQHNREVQSLKEQHQKEISELNETFLSDSEKEKLTLMFEIQGLKEQCENLQQEKQEAILNYESLREIMEILQTELGESAGKISQEFESMKQQQASDVHELQQKLRTAFTEKDALLETVNRLQGENEKLLSQQELVPELENTIKNLQEKNGVYLLSLSQRDTMLKELEGKINSLTEEKDDFINKLKNSHEEMDNFHKKCEREERLILELGKKVEQTIQYNSELEQKVNELTGGLEETLKEKDQNDQKLEKLMVQMKVLSEDKEVLSAEVKSLYEENNKLSSEKKQLSRDLEVFLSQKEDVILKEHITQLEKKLQLMVEEQDNLNKLLENEQVQKLFVKTQLYGFLKEMGSEVSEDSEEKDVVNVLQAVGESLAKINEEKCNLAFQRDEKVLELEKEIKCLQEESVVQCEELKSLLRDYEQEKVLLRKELEEIQSEKEALQSDLLEMKNANEKTRLENQNLLIQVEEVSQTCSKSEIHNEKEKCFIKEHENLKPLLEQKELRDRRAELILLKDSLAKSPSVKNDPLSSVKELEEKIENLEKECKEKEEKINKIKLVAVKAKKELDSSRKETQTVKEELESLRSEKDQLSASMRDLIQGAESYKNLLLEYEKQSEQLDVEKERANNFEHRIEDLTRQLRNSTLQCETINSDNEDLLARIETLQSNAKLLEVQILEVQRAKAMVDKELEAEKLQKEQKIKEHATTVNELEELQVQLQKQKKQLQKTMQELELVKKDAQQTTLMNMEIADYERLMKELNQKLTNKNNKIEDLEQEIKIQKQKQETLQEEITSLQSSVQQYEEKNTKIKQLLVKTKKELADSKQAETDHLILQASLKGELEASQQQVEVYKIQLAEITSEKHKIHEHLKTSAEQHQRTLSAYQQRVTALQEECRAAKAEQATVTSEFESYKVRVHNVLKQQKNKSMSQAETEGAKQEREHLEMLIDQLKIKLQDSQNNLQINVSELQTLQSEHDTLLERHNKMLQETVSKEAELREKLCSIQSENMMMKSEHTQTVSQLTSQNEVLRNSFRDQVRHLQEEHRKTVETLQQQLSKMEAQLFQLKNEPTTRSPVSSQQSLKNLRERRNTDLPLLDMHTVTREEGEGMETTDTESVSSASTYTQSLEQLLNSPETKLEPPLWHAEFTKEELVQKLSSTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQEREKSAANLEYLKNVLLQFIFLKPGSERERLLPVINTMLQLSPEEKGKLAAVAQGEEENASRSSGWASYLHSWSGLR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDLVQDG -------CHHHHCCC	40.26	20068231
11	Phosphorylation	LVQDGVASPATPGTG HHCCCCCCCCCCCCC	16.80	22199227
11 (in isoform 3)	Phosphorylation	-	16.80	25159151
14	Phosphorylation	DGVASPATPGTGKSK CCCCCCCCCCCCCHH	26.15	22199227
14 (in isoform 3)	Phosphorylation	-	26.15	25159151
17	Phosphorylation	ASPATPGTGKSKLET CCCCCCCCCCHHHCC	42.51	22199227
32	Ubiquitination	LPKEDLIKFAKKQMM CCHHHHHHHHHHHHH	46.71	21890473
36	Malonylation	DLIKFAKKQMMLIQK HHHHHHHHHHHHHHH	39.74	26320211
36	Ubiquitination	DLIKFAKKQMMLIQK HHHHHHHHHHHHHHH	39.74	-
53	Ubiquitination	SRCTELEKEIEELRS HHHHHHHHHHHHHHC	76.30	-
72	Ubiquitination	EGTGDIIKALTERLD CCHHHHHHHHHHHHH	37.36	2189047
88	Phosphorylation	LLLEKAETEQQCLSL HHHHHHHHHHHHHHH	43.91	30206219
94	Phosphorylation	ETEQQCLSLKKENIK HHHHHHHHHHHHCCC	45.85	30206219
96	2-Hydroxyisobutyrylation	EQQCLSLKKENIKMK HHHHHHHHHHCCCCC	55.45	-
109	Phosphorylation	MKQEVEDSVTKMGDA CCHHHHHHHHHHHHH	20.41	29978859
111	Phosphorylation	QEVEDSVTKMGDAHK HHHHHHHHHHHHHHH	21.18	29978859
135	2-Hydroxyisobutyrylation	VKEIENLKNELMAVR HHHHHHHHHHHHHHH	61.02	-
143	Phosphorylation	NELMAVRSKYSEDKA HHHHHHHHHHHHHHH	29.37	20068231
149	2-Hydroxyisobutyrylation	RSKYSEDKANLQKQL HHHHHHHHHHHHHHH	34.81	-
236	Phosphorylation	HYQKNINSLQEELLQ HHHHHHHHHHHHHHH	27.86	23663014
245	Ubiquitination	QEELLQLKAIHQEEV HHHHHHHHHHCHHHH	32.13	-
272	Ubiquitination	EHEAEINKLNELKEN HHHHHHHHHHHHHHH	59.35	-
287	Phosphorylation	LVKQCEASEKNIQKK HHHHHHHHHHHHHHH	27.15	17192257
294	Acetylation	SEKNIQKKYECELEN HHHHHHHHHHHHHHH	29.88	27452117
295	Phosphorylation	EKNIQKKYECELENL HHHHHHHHHHHHHHH	32.61	27642862
349	Phosphorylation	KELESQHSILKDEVT HHHHHHHHHHHHHHH	23.21	24719451
403	Acetylation	EQGCVIEKLKSELAG HCCCHHHHHHHHHCC	50.52	23749302
417	Phosphorylation	GLNKQFCYTVEQHNR CCCHHHHHHHHHHHH	18.34	-
443	Phosphorylation	EISELNETFLSDSEK HHHHHHHHHCCHHHH	28.89	29523821
446	Phosphorylation	ELNETFLSDSEKEKL HHHHHHCCHHHHHHH	34.59	26657352
448	Phosphorylation	NETFLSDSEKEKLTL HHHHCCHHHHHHHHH	47.38	29523821
450	Ubiquitination	TFLSDSEKEKLTLMF HHCCHHHHHHHHHHH	65.19	-
480	Phosphorylation	KQEAILNYESLREIM HHHHHHCHHHHHHHH	11.93	23403867
482	Phosphorylation	EAILNYESLREIMEI HHHHCHHHHHHHHHH	23.51	30243723
492	Phosphorylation	EIMEILQTELGESAG HHHHHHHHHHHHHHH	29.72	-
497	Phosphorylation	LQTELGESAGKISQE HHHHHHHHHHHHHHH	40.29	23403867
500	Ubiquitination	ELGESAGKISQEFES HHHHHHHHHHHHHHH	38.61	-
507	Phosphorylation	KISQEFESMKQQQAS HHHHHHHHHHHHHCH	36.28	28555341
522	Ubiquitination	DVHELQQKLRTAFTE HHHHHHHHHHHHHHH	27.29	-
525	Phosphorylation	ELQQKLRTAFTEKDA HHHHHHHHHHHHHHH	36.24	29083192
528	Phosphorylation	QKLRTAFTEKDALLE HHHHHHHHHHHHHHH	39.39	29083192
530	Ubiquitination	LRTAFTEKDALLETV HHHHHHHHHHHHHHH	45.29	-
536	Phosphorylation	EKDALLETVNRLQGE HHHHHHHHHHHHCCH	24.05	29083192
571	Phosphorylation	LQEKNGVYLLSLSQR HHHHCCEEEEEHHHH	11.88	25219547
574	Phosphorylation	KNGVYLLSLSQRDTM HCCEEEEEHHHHHHH	24.31	26074081
576	Phosphorylation	GVYLLSLSQRDTMLK CEEEEEHHHHHHHHH	21.57	26074081
580	Phosphorylation	LSLSQRDTMLKELEG EEHHHHHHHHHHHHH	26.96	26074081
591	Phosphorylation	ELEGKINSLTEEKDD HHHHHHHCCCHHHHH	39.89	23663014
593	Phosphorylation	EGKINSLTEEKDDFI HHHHHCCCHHHHHHH	41.75	25219547
596	2-Hydroxyisobutyrylation	INSLTEEKDDFINKL HHCCCHHHHHHHHHH	57.26	-
606	Phosphorylation	FINKLKNSHEEMDNF HHHHHHCCHHHHHHH	30.59	-
677	Phosphorylation	MVQMKVLSEDKEVLS HHHHHHHCCCHHHHH	46.89	30108239
680	2-Hydroxyisobutyrylation	MKVLSEDKEVLSAEV HHHHCCCHHHHHHHH	45.75	-
689	Phosphorylation	VLSAEVKSLYEENNK HHHHHHHHHHHHHCC	41.16	24961811
698	Phosphorylation	YEENNKLSSEKKQLS HHHHCCCCHHHHHHH	37.75	21406692
699	Phosphorylation	EENNKLSSEKKQLSR HHHCCCCHHHHHHHH	64.96	21406692
713	Phosphorylation	RDLEVFLSQKEDVIL HHHHHHHHHHHHHHH	27.95	21406692
752	Ubiquitination	LENEQVQKLFVKTQL HCHHHHHHHHHHHHH	45.06	-
760	Phosphorylation	LFVKTQLYGFLKEMG HHHHHHHHHHHHHHC	8.94	27642862
792	Ubiquitination	AVGESLAKINEEKCN HHHHHHHHHCHHHHC	51.89	-
807	Ubiquitination	LAFQRDEKVLELEKE HHCCCCHHHHHHHHH	57.31	-
813	Ubiquitination	EKVLELEKEIKCLQE HHHHHHHHHHHHHHH	76.88	-
816	Ubiquitination	LELEKEIKCLQEESV HHHHHHHHHHHHCCC	29.95	-
830	Ubiquitination	VVQCEELKSLLRDYE CCCHHHHHHHHCHHH	42.19	-
831	Phosphorylation	VQCEELKSLLRDYEQ CCHHHHHHHHCHHHH	45.31	24719451
840	Ubiquitination	LRDYEQEKVLLRKEL HCHHHHHHHHHHHHH	37.57	-
892	Phosphorylation	VSQTCSKSEIHNEKE HHHHCCHHHHCCCHH	26.03	28258704
931	Phosphorylation	ELILLKDSLAKSPSV HHHHHHHHHCCCCCC	28.74	28555341
935	Phosphorylation	LKDSLAKSPSVKNDP HHHHHCCCCCCCCCC	19.46	29496963
937	Phosphorylation	DSLAKSPSVKNDPLS HHHCCCCCCCCCCCH	53.46	18491316
944	Phosphorylation	SVKNDPLSSVKELEE CCCCCCCHHHHHHHH	38.17	23532336
945	Phosphorylation	VKNDPLSSVKELEEK CCCCCCHHHHHHHHH	44.91	20068231
952	Acetylation	SVKELEEKIENLEKE HHHHHHHHHHHHHHH	46.04	20167786
958	Acetylation	EKIENLEKECKEKEE HHHHHHHHHHHHHHH	72.13	20167786
971	Acetylation	EEKINKIKLVAVKAK HHHHHHHHHEEHHHH	38.22	25953088
971	Malonylation	EEKINKIKLVAVKAK HHHHHHHHHEEHHHH	38.22	26320211
988	Phosphorylation	LDSSRKETQTVKEEL HCCCCHHHHHHHHHH	32.35	18491316
1002	2-Hydroxyisobutyrylation	LESLRSEKDQLSASM HHHHHCHHHHHHHHH	52.61	-
1010	Methylation	DQLSASMRDLIQGAE HHHHHHHHHHHHHHH	32.84	-
1018	Phosphorylation	DLIQGAESYKNLLLE HHHHHHHHHHHHHHH	40.65	30576142
1019	Phosphorylation	LIQGAESYKNLLLEY HHHHHHHHHHHHHHH	8.73	30576142
1030	Phosphorylation	LLEYEKQSEQLDVEK HHHHHHHHHHCCHHH	38.08	20873877
1077	Phosphorylation	DLLARIETLQSNAKL HHHHHHHHHHHCCCC	27.94	21406692
1080	Phosphorylation	ARIETLQSNAKLLEV HHHHHHHHCCCCHHH	41.70	21406692
1098	Sulfoxidation	EVQRAKAMVDKELEA HHHHHHHHHCHHHHH	3.84	21406390
1141	Phosphorylation	QKKQLQKTMQELELV HHHHHHHHHHHHHHH	15.89	21082442
1155	Phosphorylation	VKKDAQQTTLMNMEI HHHHHHHHHHHHHHH	15.15	26552605
1156	Phosphorylation	KKDAQQTTLMNMEIA HHHHHHHHHHHHHHH	21.48	26552605
1165	Phosphorylation	MNMEIADYERLMKEL HHHHHHHHHHHHHHH	8.23	26552605
1222	Malonylation	EEKNTKIKQLLVKTK HHHHHHHHHHHHHCH	36.13	26320211
1227	Acetylation	KIKQLLVKTKKELAD HHHHHHHHCHHHHCC	55.38	25953088
1274	Acetylation	LAEITSEKHKIHEHL HHHHHCCHHHHHHHH	50.38	25953088
1382	Phosphorylation	NVSELQTLQSEHDTL EHHHHHHHHHHHHHH	3.21	18669648
1410	Acetylation	KEAELREKLCSIQSE HHHHHHHHHHHHHHH	48.65	19819133
1416	Phosphorylation	EKLCSIQSENMMMKS HHHHHHHHHCCCCCC	29.30	25954137
1423	Phosphorylation	SENMMMKSEHTQTVS HHCCCCCCCHHHHHH	19.40	25954137
1428	Phosphorylation	MKSEHTQTVSQLTSQ CCCCHHHHHHHHHHH	24.23	25954137
1430	Phosphorylation	SEHTQTVSQLTSQNE CCHHHHHHHHHHHHH	23.90	25954137
1433	Phosphorylation	TQTVSQLTSQNEVLR HHHHHHHHHHHHHHH	22.19	25954137
1434	Phosphorylation	QTVSQLTSQNEVLRN HHHHHHHHHHHHHHH	39.33	25954137
1441	Phosphorylation	SQNEVLRNSFRDQVR HHHHHHHHHHHHHHH	41.14	18669648
1456	Ubiquitination	HLQEEHRKTVETLQQ HHHHHHHHHHHHHHH	59.85	-
1480	Phosphorylation	FQLKNEPTTRSPVSS HHCCCCCCCCCCCCC	28.76	26657352
1481	Phosphorylation	QLKNEPTTRSPVSSQ HCCCCCCCCCCCCCH	39.61	25159151
1483	Phosphorylation	KNEPTTRSPVSSQQS CCCCCCCCCCCCHHH	27.79	25159151
1486	Phosphorylation	PTTRSPVSSQQSLKN CCCCCCCCCHHHHHH	26.30	28450419
1487	Phosphorylation	TTRSPVSSQQSLKNL CCCCCCCCHHHHHHH	32.26	25159151
1490	Phosphorylation	SPVSSQQSLKNLRER CCCCCHHHHHHHHHH	33.40	25159151
1492	Ubiquitination	VSSQQSLKNLRERRN CCCHHHHHHHHHHCC	60.22	-
1500	Phosphorylation	NLRERRNTDLPLLDM HHHHHCCCCCCEEEC	36.78	25849741
1509	Phosphorylation	LPLLDMHTVTREEGE CCEEECEEEECCCCC	19.55	-
1542	Phosphorylation	SLEQLLNSPETKLEP HHHHHHCCCCCCCCC	24.88	29496963
1545	Phosphorylation	QLLNSPETKLEPPLW HHHCCCCCCCCCCCC	44.29	26074081
1548	Phosphorylation	NSPETKLEPPLWHAE CCCCCCCCCCCCCCC	46.56	18669648
1558	Ubiquitination	LWHAEFTKEELVQKL CCCCCCCHHHHHHHH	55.29	-
1564	Ubiquitination	TKEELVQKLSSTTKS CHHHHHHHHHHCCCC	42.74	-
1566	Phosphorylation	EELVQKLSSTTKSAD HHHHHHHHHCCCCHH	32.45	30108239
1567	Phosphorylation	ELVQKLSSTTKSADH HHHHHHHHCCCCHHH	51.00	30108239
1568	Phosphorylation	LVQKLSSTTKSADHL HHHHHHHCCCCHHHH	34.56	30108239
1569	Phosphorylation	VQKLSSTTKSADHLN HHHHHHCCCCHHHHH	25.58	30108239
1570	Ubiquitination	QKLSSTTKSADHLNG HHHHHCCCCHHHHHH	43.67	-
1571	Phosphorylation	KLSSTTKSADHLNGL HHHHCCCCHHHHHHH	36.52	25159151
1590	Sulfoxidation	EATNAILMEQIKLLK HHHHHHHHHHHHHHH	2.66	21406390
1594	Ubiquitination	AILMEQIKLLKSEIR HHHHHHHHHHHHHHH	47.68	-
1597	Ubiquitination	MEQIKLLKSEIRRLE HHHHHHHHHHHHHHH	57.38	-
1611	Ubiquitination	ERNQEREKSAANLEY HHHHHHHHHHHHHHH	52.17	-
1612	Phosphorylation	RNQEREKSAANLEYL HHHHHHHHHHHHHHH	28.06	-
1618	Phosphorylation	KSAANLEYLKNVLLQ HHHHHHHHHHHHHHH	26.58	22817900
1630	Ubiquitination	LLQFIFLKPGSERER HHHHHHCCCCCHHHH	36.26	-
1644	Phosphorylation	RLLPVINTMLQLSPE HHHHHHHHHHHCCHH	14.24	27251275
1649	Phosphorylation	INTMLQLSPEEKGKL HHHHHHCCHHHHCHH	19.80	22617229
1668	Phosphorylation	QGEEENASRSSGWAS CCCHHCCCCCCCHHH	44.25	23663014
1670	Phosphorylation	EEENASRSSGWASYL CHHCCCCCCCHHHHH	30.61	-
1671	Phosphorylation	EENASRSSGWASYLH HHCCCCCCCHHHHHH	36.93	23663014

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 GCC2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GCC2_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 GCC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of GCC2_HUMAN !!

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 GCC2_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-1483; SER-1542 ANDSER-1649, AND MASS SPECTROMETRY.	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-287 AND SER-1649, ANDMASS SPECTROMETRY.	18691976 [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-1483, AND MASSSPECTROMETRY.	16964243 [Abstract]