dbPTM

TCPQ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TCPQ_HUMAN
UniProt AC	P50990
Protein Name	T-complex protein 1 subunit theta
Gene Name	CCT8
Organism	Homo sapiens (Human).
Sequence Length	548
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, cilium basal body .
Protein Description	Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin..
Protein Sequence	MALHVPKAPGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYEIACRKAHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQYGNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGISSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGKVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLTPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGILDTYLGKYWAIKLATNAAVTVLRVDQIIMAKPAGGPKPPSGKKDWDDDQND

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALHVPKAP ------CCCCCCCCC	13.33	-
7	Ubiquitination	-MALHVPKAPGFAQM -CCCCCCCCCCHHHH	67.15	21890473
7	Acetylation	-MALHVPKAPGFAQM -CCCCCCCCCCHHHH	67.15	19608861
7	Malonylation	-MALHVPKAPGFAQM -CCCCCCCCCCHHHH	67.15	26320211
7	Ubiquitination	-MALHVPKAPGFAQM -CCCCCCCCCCHHHH	67.15	21890473
14	Sulfoxidation	KAPGFAQMLKEGAKH CCCCHHHHHHHHHHH	5.32	28465586
16	Ubiquitination	PGFAQMLKEGAKHFS CCHHHHHHHHHHHCC	49.08	21890473
16	Acetylation	PGFAQMLKEGAKHFS CCHHHHHHHHHHHCC	49.08	25953088
16	Malonylation	PGFAQMLKEGAKHFS CCHHHHHHHHHHHCC	49.08	26320211
16	Ubiquitination	PGFAQMLKEGAKHFS CCHHHHHHHHHHHCC	49.08	21890473
18	Ubiquitination	FAQMLKEGAKHFSGL HHHHHHHHHHHCCCH	38.03	-
20	Ubiquitination	QMLKEGAKHFSGLEE HHHHHHHHHCCCHHH	56.91	21890473
20	Acetylation	QMLKEGAKHFSGLEE HHHHHHHHHCCCHHH	56.91	16916647
20	Malonylation	QMLKEGAKHFSGLEE HHHHHHHHHCCCHHH	56.91	26320211
20	Ubiquitination	QMLKEGAKHFSGLEE HHHHHHHHHCCCHHH	56.91	21890473
23	Phosphorylation	KEGAKHFSGLEEAVY HHHHHHCCCHHHHHH	42.03	30266825
30	Phosphorylation	SGLEEAVYRNIQACK CCHHHHHHHHHHHHH	12.65	25159151
35	Ubiquitination	AVYRNIQACKELAQT HHHHHHHHHHHHHHH	11.53	-
36	Glutathionylation	VYRNIQACKELAQTT HHHHHHHHHHHHHHH	1.70	22555962
36	S-palmitoylation	VYRNIQACKELAQTT HHHHHHHHHHHHHHH	1.70	26865113
37	2-Hydroxyisobutyrylation	YRNIQACKELAQTTR HHHHHHHHHHHHHHC	59.80	-
37	Acetylation	YRNIQACKELAQTTR HHHHHHHHHHHHHHC	59.80	26051181
37	Ubiquitination	YRNIQACKELAQTTR HHHHHHHHHHHHHHC	59.80	21906983
43	Ubiquitination	CKELAQTTRTAYGPN HHHHHHHHCCCCCCC	17.59	-
54	Ubiquitination	YGPNGMNKMVINHLE CCCCHHHHHHHHHHH	26.17	21890473
54	Ubiquitination	YGPNGMNKMVINHLE CCCCHHHHHHHHHHH	26.17	21890473
55	Sulfoxidation	GPNGMNKMVINHLEK CCCHHHHHHHHHHHH	2.88	30846556
62	Ubiquitination	MVINHLEKLFVTNDA HHHHHHHHHHCCCCH	54.29	21890473
62	2-Hydroxyisobutyrylation	MVINHLEKLFVTNDA HHHHHHHHHHCCCCH	54.29	-
62	Acetylation	MVINHLEKLFVTNDA HHHHHHHHHHCCCCH	54.29	25953088
62	Ubiquitination	MVINHLEKLFVTNDA HHHHHHHHHHCCCCH	54.29	21890473
66	Phosphorylation	HLEKLFVTNDAATIL HHHHHHCCCCHHHHH	21.75	22210691
71	Phosphorylation	FVTNDAATILRELEV HCCCCHHHHHHHHHC	23.43	27050516
119	Ubiquitination	LELAEELLRIGLSVS HHHHHHHHHHCCCHH	4.19	-
133	Ubiquitination	SEVIEGYEIACRKAH HHHHCCHHHHCHHHH	34.66	-
138	Acetylation	GYEIACRKAHEILPN CHHHHCHHHHHHHCC	54.71	26051181
138	Ubiquitination	GYEIACRKAHEILPN CHHHHCHHHHHHHCC	54.71	-
148	S-nitrosocysteine	EILPNLVCCSAKNLR HHHCCCEEEECCCCC	1.38	-
148	S-nitrosylation	EILPNLVCCSAKNLR HHHCCCEEEECCCCC	1.38	22178444
149	S-nitrosocysteine	ILPNLVCCSAKNLRD HHCCCEEEECCCCCC	3.27	-
149	Glutathionylation	ILPNLVCCSAKNLRD HHCCCEEEECCCCCC	3.27	22555962
149	S-nitrosylation	ILPNLVCCSAKNLRD HHCCCEEEECCCCCC	3.27	22178444
150	Phosphorylation	LPNLVCCSAKNLRDI HCCCEEEECCCCCCH	36.83	28450419
152	Ubiquitination	NLVCCSAKNLRDIDE CCEEEECCCCCCHHH	39.97	21890473
152	Ubiquitination	NLVCCSAKNLRDIDE CCEEEECCCCCCHHH	39.97	21890473
152	2-Hydroxyisobutyrylation	NLVCCSAKNLRDIDE CCEEEECCCCCCHHH	39.97	-
152	Acetylation	NLVCCSAKNLRDIDE CCEEEECCCCCCHHH	39.97	25953088
152	Malonylation	NLVCCSAKNLRDIDE CCEEEECCCCCCHHH	39.97	26320211
152	Ubiquitination	NLVCCSAKNLRDIDE CCEEEECCCCCCHHH	39.97	21890473
161	Phosphorylation	LRDIDEVSSLLRTSI CCCHHHHHHHHHHHH	17.14	20873877
162	Phosphorylation	RDIDEVSSLLRTSIM CCHHHHHHHHHHHHH	36.28	25262027
171	Ubiquitination	LRTSIMSKQYGNEVF HHHHHHHHHHCCHHH	30.11	21890473
171	2-Hydroxyisobutyrylation	LRTSIMSKQYGNEVF HHHHHHHHHHCCHHH	30.11	-
171	Acetylation	LRTSIMSKQYGNEVF HHHHHHHHHHCCHHH	30.11	27452117
171	Ubiquitination	LRTSIMSKQYGNEVF HHHHHHHHHHCCHHH	30.11	21906983
173	Phosphorylation	TSIMSKQYGNEVFLA HHHHHHHHCCHHHHH	26.17	28152594
206	Acetylation	VDNIRVCKILGSGIS CCCEEEEEECCCCCC	37.80	-
206	Ubiquitination	VDNIRVCKILGSGIS CCCEEEEEECCCCCC	37.80	-
206	Acetylation	VDNIRVCKILGSGIS CCCEEEEEECCCCCC	37.80	26051181
210	Phosphorylation	RVCKILGSGISSSSV EEEEECCCCCCCHHH	29.52	21406692
213	Phosphorylation	KILGSGISSSSVLHG EECCCCCCCHHHEEC	27.91	21406692
214	Phosphorylation	ILGSGISSSSVLHGM ECCCCCCCHHHEECE	25.39	21406692
215	Phosphorylation	LGSGISSSSVLHGMV CCCCCCCHHHEECEE	20.06	21406692
216	Ubiquitination	GSGISSSSVLHGMVF CCCCCCHHHEECEEE	30.55	-
216	Phosphorylation	GSGISSSSVLHGMVF CCCCCCHHHEECEEE	30.55	21406692
224	2-Hydroxyisobutyrylation	VLHGMVFKKETEGDV HEECEEEECCCCCCC	37.99	-
224	Acetylation	VLHGMVFKKETEGDV HEECEEEECCCCCCC	37.99	25038526
224	Sumoylation	VLHGMVFKKETEGDV HEECEEEECCCCCCC	37.99	28112733
224	Ubiquitination	VLHGMVFKKETEGDV HEECEEEECCCCCCC	37.99	-
225	Acetylation	LHGMVFKKETEGDVT EECEEEECCCCCCCC	59.40	23236377
225	Ubiquitination	LHGMVFKKETEGDVT EECEEEECCCCCCCC	59.40	17370265
227	Phosphorylation	GMVFKKETEGDVTSV CEEEECCCCCCCCCC	54.90	20068231
232	Phosphorylation	KETEGDVTSVKDAKI CCCCCCCCCCCCCEE	32.32	29255136
233	Phosphorylation	ETEGDVTSVKDAKIA CCCCCCCCCCCCEEE	27.33	29255136
235	Ubiquitination	EGDVTSVKDAKIAVY CCCCCCCCCCEEEEE	52.30	-
235	Acetylation	EGDVTSVKDAKIAVY CCCCCCCCCCEEEEE	52.30	25953088
235	Ubiquitination	EGDVTSVKDAKIAVY CCCCCCCCCCEEEEE	52.30	17370265
238	2-Hydroxyisobutyrylation	VTSVKDAKIAVYSCP CCCCCCCEEEEEECC	41.13	-
238	Acetylation	VTSVKDAKIAVYSCP CCCCCCCEEEEEECC	41.13	25038526
241	Ubiquitination	VKDAKIAVYSCPFDG CCCCEEEEEECCCCC	4.04	-
242	Phosphorylation	KDAKIAVYSCPFDGM CCCEEEEEECCCCCC	8.78	28152594
243	Phosphorylation	DAKIAVYSCPFDGMI CCEEEEEECCCCCCE	14.55	28152594
244	Glutathionylation	AKIAVYSCPFDGMIT CEEEEEECCCCCCEE	1.82	22555962
245	Acetylation	KIAVYSCPFDGMITE EEEEEECCCCCCEEC	25.15	19608861
245	Ubiquitination	KIAVYSCPFDGMITE EEEEEECCCCCCEEC	25.15	19608861
249	Sulfoxidation	YSCPFDGMITETKGT EECCCCCCEECCCCE	3.54	21406390
251	Acetylation	CPFDGMITETKGTVL CCCCCCEECCCCEEE	28.80	-
251	Ubiquitination	CPFDGMITETKGTVL CCCCCCEECCCCEEE	28.80	-
251	Phosphorylation	CPFDGMITETKGTVL CCCCCCEECCCCEEE	28.80	28450419
253	Phosphorylation	FDGMITETKGTVLIK CCCCEECCCCEEEEE	26.56	28857561
254	2-Hydroxyisobutyrylation	DGMITETKGTVLIKT CCCEECCCCEEEEEC	46.48	-
254	Sumoylation	DGMITETKGTVLIKT CCCEECCCCEEEEEC	46.48	28112733
254	Ubiquitination	DGMITETKGTVLIKT CCCEECCCCEEEEEC	46.48	-
256	Phosphorylation	MITETKGTVLIKTAE CEECCCCEEEEECHH	17.44	28857561
260	Ubiquitination	TKGTVLIKTAEELMN CCCEEEEECHHHHHC	37.21	21890473
260	Sumoylation	TKGTVLIKTAEELMN CCCEEEEECHHHHHC	37.21	28112733
260	Ubiquitination	TKGTVLIKTAEELMN CCCEEEEECHHHHHC	37.21	21906983
261	Phosphorylation	KGTVLIKTAEELMNF CCEEEEECHHHHHCC	32.10	-
266	Sulfoxidation	IKTAEELMNFSKGEE EECHHHHHCCCCCCC	5.57	21406390
269	Phosphorylation	AEELMNFSKGEENLM HHHHHCCCCCCCCHH	34.44	21815630
270	Acetylation	EELMNFSKGEENLMD HHHHCCCCCCCCHHH	67.23	23236377
270	Ubiquitination	EELMNFSKGEENLMD HHHHCCCCCCCCHHH	67.23	21906983
276	Sulfoxidation	SKGEENLMDAQVKAI CCCCCCHHHHHHHHH	6.39	21406390
277	Ubiquitination	KGEENLMDAQVKAIA CCCCCHHHHHHHHHH	36.69	-
281	2-Hydroxyisobutyrylation	NLMDAQVKAIADTGA CHHHHHHHHHHHCCC	23.22	-
286	Phosphorylation	QVKAIADTGANVVVT HHHHHHHCCCCEEEE	29.22	23911959
288	Ubiquitination	KAIADTGANVVVTGG HHHHHCCCCEEEECC	14.03	-
293	Phosphorylation	TGANVVVTGGKVADM CCCCEEEECCHHHHH	28.71	23911959
296	2-Hydroxyisobutyrylation	NVVVTGGKVADMALH CEEEECCHHHHHHHH	35.28	-
296	Acetylation	NVVVTGGKVADMALH CEEEECCHHHHHHHH	35.28	26051181
296	Malonylation	NVVVTGGKVADMALH CEEEECCHHHHHHHH	35.28	26320211
296	Ubiquitination	NVVVTGGKVADMALH CEEEECCHHHHHHHH	35.28	-
299	Acetylation	VTGGKVADMALHYAN EECCHHHHHHHHHHH	26.35	-
299	Ubiquitination	VTGGKVADMALHYAN EECCHHHHHHHHHHH	26.35	-
299	Acetylation	VTGGKVADMALHYAN EECCHHHHHHHHHHH	26.35	19608861
299	Ubiquitination	VTGGKVADMALHYAN EECCHHHHHHHHHHH	26.35	19608861
300	Sulfoxidation	TGGKVADMALHYANK ECCHHHHHHHHHHHH	2.85	30846556
304	Nitration	VADMALHYANKYNIM HHHHHHHHHHHCCEE	16.84	-
304	Phosphorylation	VADMALHYANKYNIM HHHHHHHHHHHCCEE	16.84	28152594
307	Acetylation	MALHYANKYNIMLVR HHHHHHHHCCEEEEE	31.35	-
307	Ubiquitination	MALHYANKYNIMLVR HHHHHHHHCCEEEEE	31.35	-
307	Acetylation	MALHYANKYNIMLVR HHHHHHHHCCEEEEE	31.35	25953088
307	Ubiquitination	MALHYANKYNIMLVR HHHHHHHHCCEEEEE	31.35	-
308	Phosphorylation	ALHYANKYNIMLVRL HHHHHHHCCEEEEEC	15.10	23882029
317	Phosphorylation	IMLVRLNSKWDLRRL EEEEECCCHHHHHHH	39.45	29978859
318	2-Hydroxyisobutyrylation	MLVRLNSKWDLRRLC EEEECCCHHHHHHHH	43.59	-
318	Acetylation	MLVRLNSKWDLRRLC EEEECCCHHHHHHHH	43.59	19608861
318	Malonylation	MLVRLNSKWDLRRLC EEEECCCHHHHHHHH	43.59	26320211
318	Ubiquitination	MLVRLNSKWDLRRLC EEEECCCHHHHHHHH	43.59	19608861
326	Ubiquitination	WDLRRLCKTVGATAL HHHHHHHHHHCCCCC	51.33	21890473
326	2-Hydroxyisobutyrylation	WDLRRLCKTVGATAL HHHHHHHHHHCCCCC	51.33	-
326	Acetylation	WDLRRLCKTVGATAL HHHHHHHHHHCCCCC	51.33	23749302
326	Malonylation	WDLRRLCKTVGATAL HHHHHHHHHHCCCCC	51.33	26320211
326	Ubiquitination	WDLRRLCKTVGATAL HHHHHHHHHHCCCCC	51.33	21890473
327	Acetylation	DLRRLCKTVGATALP HHHHHHHHHCCCCCC	24.15	19608861
327	Phosphorylation	DLRRLCKTVGATALP HHHHHHHHHCCCCCC	24.15	20068231
327	Ubiquitination	DLRRLCKTVGATALP HHHHHHHHHCCCCCC	24.15	19608861
331	Phosphorylation	LCKTVGATALPRLTP HHHHHCCCCCCCCCH	23.85	20068231
337	Phosphorylation	ATALPRLTPPVLEEM CCCCCCCCHHHHHHC	27.16	26126808
348	Acetylation	LEEMGHCDSVYLSEV HHHCCCCCEEEEECC	35.15	-
349	Phosphorylation	EEMGHCDSVYLSEVG HHCCCCCEEEEECCC	20.32	26126808
351	Phosphorylation	MGHCDSVYLSEVGDT CCCCCEEEEECCCCE	14.41	26126808
353	Phosphorylation	HCDSVYLSEVGDTQV CCCEEEEECCCCEEE	16.73	26126808
367	2-Hydroxyisobutyrylation	VVVFKHEKEDGAIST EEEEEEECCCCCEEE	61.91	-
367	Acetylation	VVVFKHEKEDGAIST EEEEEEECCCCCEEE	61.91	23236377
367	Malonylation	VVVFKHEKEDGAIST EEEEEEECCCCCEEE	61.91	26320211
367	Ubiquitination	VVVFKHEKEDGAIST EEEEEEECCCCCEEE	61.91	-
373	Phosphorylation	EKEDGAISTIVLRGS ECCCCCEEEEEEECC	16.14	20860994
378	Methylation	AISTIVLRGSTDNLM CEEEEEEECCCCCHH	26.56	-
380	Phosphorylation	STIVLRGSTDNLMDD EEEEEECCCCCHHHH	26.59	29255136
381	Acetylation	TIVLRGSTDNLMDDI EEEEECCCCCHHHHH	31.56	-
381	Ubiquitination	TIVLRGSTDNLMDDI EEEEECCCCCHHHHH	31.56	-
381	Acetylation	TIVLRGSTDNLMDDI EEEEECCCCCHHHHH	31.56	19608861
381	Phosphorylation	TIVLRGSTDNLMDDI EEEEECCCCCHHHHH	31.56	29255136
381	Ubiquitination	TIVLRGSTDNLMDDI EEEEECCCCCHHHHH	31.56	19608861
385	Sulfoxidation	RGSTDNLMDDIERAV ECCCCCHHHHHHHHH	5.65	21406390
393	Acetylation	DDIERAVDDGVNTFK HHHHHHHHCCCCEEE	46.06	19608861
393	Ubiquitination	DDIERAVDDGVNTFK HHHHHHHHCCCCEEE	46.06	19608861
398	Phosphorylation	AVDDGVNTFKVLTRD HHHCCCCEEEEEECC	23.56	21406692
400	Ubiquitination	DDGVNTFKVLTRDKR HCCCCEEEEEECCCC	34.01	21890473
400	2-Hydroxyisobutyrylation	DDGVNTFKVLTRDKR HCCCCEEEEEECCCC	34.01	-
400	Acetylation	DDGVNTFKVLTRDKR HCCCCEEEEEECCCC	34.01	19608861
400	Malonylation	DDGVNTFKVLTRDKR HCCCCEEEEEECCCC	34.01	26320211
400	Methylation	DDGVNTFKVLTRDKR HCCCCEEEEEECCCC	34.01	19608861
400	Ubiquitination	DDGVNTFKVLTRDKR HCCCCEEEEEECCCC	34.01	21890473
402	Ubiquitination	GVNTFKVLTRDKRLV CCCEEEEEECCCCCC	3.15	-
415	Phosphorylation	LVPGGGATEIELAKQ CCCCCCHHHHHHHHH	40.55	21406692
420	Ubiquitination	GATEIELAKQITSYG CHHHHHHHHHHHHCC	6.74	-
421	Ubiquitination	ATEIELAKQITSYGE HHHHHHHHHHHHCCC	55.66	21890473
421	Ubiquitination	ATEIELAKQITSYGE HHHHHHHHHHHHCCC	55.66	21890473
421	Acetylation	ATEIELAKQITSYGE HHHHHHHHHHHHCCC	55.66	26051181
421	Ubiquitination	ATEIELAKQITSYGE HHHHHHHHHHHHCCC	55.66	21906983
424	Phosphorylation	IELAKQITSYGETCP HHHHHHHHHCCCCCC	17.25	28152594
425	Phosphorylation	ELAKQITSYGETCPG HHHHHHHHCCCCCCC	32.54	28152594
426	Phosphorylation	LAKQITSYGETCPGL HHHHHHHCCCCCCCH	15.44	28152594
429	Phosphorylation	QITSYGETCPGLEQY HHHHCCCCCCCHHHH	21.45	28152594
430	S-nitrosocysteine	ITSYGETCPGLEQYA HHHCCCCCCCHHHHH	1.88	-
430	Glutathionylation	ITSYGETCPGLEQYA HHHCCCCCCCHHHHH	1.88	22555962
430	S-nitrosylation	ITSYGETCPGLEQYA HHHCCCCCCCHHHHH	1.88	19483679
436	Phosphorylation	TCPGLEQYAIKKFAE CCCCHHHHHHHHHHH	10.83	28152594
439	2-Hydroxyisobutyrylation	GLEQYAIKKFAEAFE CHHHHHHHHHHHHHH	33.40	-
439	Acetylation	GLEQYAIKKFAEAFE CHHHHHHHHHHHHHH	33.40	25953088
439	Ubiquitination	GLEQYAIKKFAEAFE CHHHHHHHHHHHHHH	33.40	-
440	Ubiquitination	LEQYAIKKFAEAFEA HHHHHHHHHHHHHHH	43.63	21890473
440	Ubiquitination	LEQYAIKKFAEAFEA HHHHHHHHHHHHHHH	43.63	21890473
440	Acetylation	LEQYAIKKFAEAFEA HHHHHHHHHHHHHHH	43.63	25953088
440	Succinylation	LEQYAIKKFAEAFEA HHHHHHHHHHHHHHH	43.63	23954790
440	Ubiquitination	LEQYAIKKFAEAFEA HHHHHHHHHHHHHHH	43.63	21890473
447	Acetylation	KFAEAFEAIPRALAE HHHHHHHHHHHHHHH	15.61	-
447	Ubiquitination	KFAEAFEAIPRALAE HHHHHHHHHHHHHHH	15.61	21890473
447	Acetylation	KFAEAFEAIPRALAE HHHHHHHHHHHHHHH	15.61	19608861
447	Ubiquitination	KFAEAFEAIPRALAE HHHHHHHHHHHHHHH	15.61	19608861
459	2-Hydroxyisobutyrylation	LAENSGVKANEVISK HHHCCCCCHHHHHHH	49.36	-
459	Sumoylation	LAENSGVKANEVISK HHHCCCCCHHHHHHH	49.36	25114211
459	Ubiquitination	LAENSGVKANEVISK HHHCCCCCHHHHHHH	49.36	21906983
466	Ubiquitination	KANEVISKLYAVHQE CHHHHHHHHHHHHHC	34.10	21890473
466	2-Hydroxyisobutyrylation	KANEVISKLYAVHQE CHHHHHHHHHHHHHC	34.10	-
466	Acetylation	KANEVISKLYAVHQE CHHHHHHHHHHHHHC	34.10	19608861
466	Malonylation	KANEVISKLYAVHQE CHHHHHHHHHHHHHC	34.10	26320211
466	Ubiquitination	KANEVISKLYAVHQE CHHHHHHHHHHHHHC	34.10	21890473
468	Nitration	NEVISKLYAVHQEGN HHHHHHHHHHHHCCC	15.43	-
468	Phosphorylation	NEVISKLYAVHQEGN HHHHHHHHHHHHCCC	15.43	28152594
492	Sulfoxidation	EVPAVKDMLEAGILD ECCHHHHHHHHCCHH	2.78	30846556
501	Phosphorylation	EAGILDTYLGKYWAI HHCCHHHHHHHHHHH	17.08	25147952
505	Phosphorylation	LDTYLGKYWAIKLAT HHHHHHHHHHHHHHH	9.77	22817900
509	Acetylation	LGKYWAIKLATNAAV HHHHHHHHHHHCCCE	25.07	-
509	Ubiquitination	LGKYWAIKLATNAAV HHHHHHHHHHHCCCE	25.07	21890473
512	Phosphorylation	YWAIKLATNAAVTVL HHHHHHHHCCCEEEE	35.51	20860994
515	Ubiquitination	IKLATNAAVTVLRVD HHHHHCCCEEEEEEC	10.28	-
517	Phosphorylation	LATNAAVTVLRVDQI HHHCCCEEEEEECEE	14.75	20860994
520	Ubiquitination	NAAVTVLRVDQIIMA CCCEEEEEECEEEEE	26.15	-
521	Ubiquitination	AAVTVLRVDQIIMAK CCEEEEEECEEEEEC	5.78	-
526	Sulfoxidation	LRVDQIIMAKPAGGP EEECEEEEECCCCCC	4.13	21406390
528	Ubiquitination	VDQIIMAKPAGGPKP ECEEEEECCCCCCCC	20.30	21890473
528	Acetylation	VDQIIMAKPAGGPKP ECEEEEECCCCCCCC	20.30	23749302
528	Malonylation	VDQIIMAKPAGGPKP ECEEEEECCCCCCCC	20.30	26320211
528	Methylation	VDQIIMAKPAGGPKP ECEEEEECCCCCCCC	20.30	-
528	Ubiquitination	VDQIIMAKPAGGPKP ECEEEEECCCCCCCC	20.30	21890473
534	Sumoylation	AKPAGGPKPPSGKKD ECCCCCCCCCCCCCC	73.22	-
534	Acetylation	AKPAGGPKPPSGKKD ECCCCCCCCCCCCCC	73.22	26210075
534	Sumoylation	AKPAGGPKPPSGKKD ECCCCCCCCCCCCCC	73.22	28112733
534	Ubiquitination	AKPAGGPKPPSGKKD ECCCCCCCCCCCCCC	73.22	-
537	Phosphorylation	AGGPKPPSGKKDWDD CCCCCCCCCCCCCCC	72.30	23401153
539	2-Hydroxyisobutyrylation	GPKPPSGKKDWDDDQ CCCCCCCCCCCCCCC	52.47	-
539	Acetylation	GPKPPSGKKDWDDDQ CCCCCCCCCCCCCCC	52.47	25953088
539	Sumoylation	GPKPPSGKKDWDDDQ CCCCCCCCCCCCCCC	52.47	28112733
539	Ubiquitination	GPKPPSGKKDWDDDQ CCCCCCCCCCCCCCC	52.47	-
540	Acetylation	PKPPSGKKDWDDDQN CCCCCCCCCCCCCCC	68.52	12430811
540	Ubiquitination	PKPPSGKKDWDDDQN CCCCCCCCCCCCCCC	68.52	21906983

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 TCPQ_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
TCPZ_HUMAN	CCT6A	physical	22939629
TIF1B_HUMAN	TRIM28	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
UBA5_HUMAN	UBA5	physical	22939629
TCPB_HUMAN	CCT2	physical	22863883
AT1A1_HUMAN	ATP1A1	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
MESD_HUMAN	MESDC2	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197

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 TCPQ_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-318; LYS-400 ANDLYS-466, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20, AND MASS SPECTROMETRY.	16916647 [Abstract]
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 SER-23 AND TYR-30, AND MASSSPECTROMETRY.	19690332 [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 SER-23, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227; THR-232 ANDSER-233, AND MASS SPECTROMETRY.	17924679 [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-505, AND MASSSPECTROMETRY.	15592455 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-225 AND LYS-235, AND MASSSPECTROMETRY.	17370265 [Abstract]