dbPTM

TCPZ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TCPZ_HUMAN
UniProt AC	P40227
Protein Name	T-complex protein 1 subunit zeta
Gene Name	CCT6A
Organism	Homo sapiens (Human).
Sequence Length	531
Subcellular Localization	Cytoplasm.
Protein Description	Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin..
Protein Sequence	MAAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLKG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAVKTLNP ------CCCCCCCCH	22.44	22814378
5	Ubiquitination	---MAAVKTLNPKAE ---CCCCCCCCHHHH	42.44	21890473
5	2-Hydroxyisobutyrylation	---MAAVKTLNPKAE ---CCCCCCCCHHHH	42.44	-
5	Acetylation	---MAAVKTLNPKAE ---CCCCCCCCHHHH	42.44	19608861
5	Methylation	---MAAVKTLNPKAE ---CCCCCCCCHHHH	42.44	19608861
5	Ubiquitination	---MAAVKTLNPKAE ---CCCCCCCCHHHH	42.44	21890473
6	Phosphorylation	--MAAVKTLNPKAEV --CCCCCCCCHHHHH	25.76	24719451
10	Ubiquitination	AVKTLNPKAEVARAQ CCCCCCHHHHHHHHH	56.98	21890473
10	Sumoylation	AVKTLNPKAEVARAQ CCCCCCHHHHHHHHH	56.98	-
10	Acetylation	AVKTLNPKAEVARAQ CCCCCCHHHHHHHHH	56.98	23954790
10	Malonylation	AVKTLNPKAEVARAQ CCCCCCHHHHHHHHH	56.98	26320211
10	Sumoylation	AVKTLNPKAEVARAQ CCCCCCHHHHHHHHH	56.98	19608861
10	Ubiquitination	AVKTLNPKAEVARAQ CCCCCCHHHHHHHHH	56.98	21890473
35	Methylation	RGLQDVLRTNLGPKG HCHHHHHHCCCCCCC	22.78	-
41	Acetylation	LRTNLGPKGTMKMLV HHCCCCCCCCEEEEE	66.28	26051181
41	Ubiquitination	LRTNLGPKGTMKMLV HHCCCCCCCCEEEEE	66.28	-
45	2-Hydroxyisobutyrylation	LGPKGTMKMLVSGAG CCCCCCEEEEECCCC	28.99	-
45	Ubiquitination	LGPKGTMKMLVSGAG CCCCCCEEEEECCCC	28.99	-
46	Sulfoxidation	GPKGTMKMLVSGAGD CCCCCEEEEECCCCC	2.87	21406390
55	Acetylation	VSGAGDIKLTKDGNV ECCCCCEEECCCCCE	55.64	25953088
55	Ubiquitination	VSGAGDIKLTKDGNV ECCCCCEEECCCCCE	55.64	21906983
57	Phosphorylation	GAGDIKLTKDGNVLL CCCCEEECCCCCEEE	23.30	20068231
58	Ubiquitination	AGDIKLTKDGNVLLH CCCEEECCCCCEEEE	74.25	21890473
58	2-Hydroxyisobutyrylation	AGDIKLTKDGNVLLH CCCEEECCCCCEEEE	74.25	-
58	Ubiquitination	AGDIKLTKDGNVLLH CCCEEECCCCCEEEE	74.25	21890473
58 (in isoform 2)	Ubiquitination	-	74.25	-
67	Sulfoxidation	GNVLLHEMQIQHPTA CCEEEEEEEECCCCH	2.71	30846556
73	Phosphorylation	EMQIQHPTASLIAKV EEEECCCCHHHHHHH	27.10	20068231
75	Phosphorylation	QIQHPTASLIAKVAT EECCCCHHHHHHHHC	23.84	20068231
79	Ubiquitination	PTASLIAKVATAQDD CCHHHHHHHHCCCCC	25.96	-
82	Phosphorylation	SLIAKVATAQDDITG HHHHHHHCCCCCCCC	28.04	21712546
93	Phosphorylation	DITGDGTTSNVLIIG CCCCCCCCCCEEECH	24.67	21712546
94	Phosphorylation	ITGDGTTSNVLIIGE CCCCCCCCCEEECHH	25.44	21712546
104	Ubiquitination	LIIGELLKQADLYIS EECHHHHHHCCEEEC	56.94	-
109	Phosphorylation	LLKQADLYISEGLHP HHHHCCEEECCCCCH	11.71	21406692
111	Phosphorylation	KQADLYISEGLHPRI HHCCEEECCCCCHHH	16.44	21406692
120	Phosphorylation	GLHPRIITEGFEAAK CCCHHHHHCCHHHHH	27.90	-
127	Acetylation	TEGFEAAKEKALQFL HCCHHHHHHHHHHHH	67.79	25038526
127	Ubiquitination	TEGFEAAKEKALQFL HCCHHHHHHHHHHHH	67.79	21906983
129	2-Hydroxyisobutyrylation	GFEAAKEKALQFLEE CHHHHHHHHHHHHHH	54.40	-
129	Acetylation	GFEAAKEKALQFLEE CHHHHHHHHHHHHHH	54.40	25953088
129	Ubiquitination	GFEAAKEKALQFLEE CHHHHHHHHHHHHHH	54.40	21906983
138	2-Hydroxyisobutyrylation	LQFLEEVKVSREMDR HHHHHHHHCCHHCCH	37.46	-
138	Ubiquitination	LQFLEEVKVSREMDR HHHHHHHHCCHHCCH	37.46	21906983
143	Sulfoxidation	EVKVSREMDRETLID HHHCCHHCCHHHHHH	5.98	21406390
154	Acetylation	TLIDVARTSLRTKVH HHHHHHHHHHHHHHH	23.52	19608861
154	Ubiquitination	TLIDVARTSLRTKVH HHHHHHHHHHHHHHH	23.52	19608861
159	Ubiquitination	ARTSLRTKVHAELAD HHHHHHHHHHHHHHH	26.11	-
180	2-Hydroxyisobutyrylation	VDSILAIKKQDEPID HHHHHHHHCCCCCCC	38.48	-
180	Ubiquitination	VDSILAIKKQDEPID HHHHHHHHCCCCCCC	38.48	-
190	Sulfoxidation	DEPIDLFMIEIMEMK CCCCCEEEEEHHHHH	3.32	30846556
194	Sulfoxidation	DLFMIEIMEMKHKSE CEEEEEHHHHHCCCC	2.39	30846556
196	Sulfoxidation	FMIEIMEMKHKSETD EEEEHHHHHCCCCCC	2.81	30846556
197	Acetylation	MIEIMEMKHKSETDT EEEHHHHHCCCCCCC	34.28	25038526
199	2-Hydroxyisobutyrylation	EIMEMKHKSETDTSL EHHHHHCCCCCCCHH	44.46	-
199	Acetylation	EIMEMKHKSETDTSL EHHHHHCCCCCCCHH	44.46	19608861
199	Malonylation	EIMEMKHKSETDTSL EHHHHHCCCCCCCHH	44.46	26320211
199	Ubiquitination	EIMEMKHKSETDTSL EHHHHHCCCCCCCHH	44.46	19608861
200	Phosphorylation	IMEMKHKSETDTSLI HHHHHCCCCCCCHHH	45.51	23403867
202	Phosphorylation	EMKHKSETDTSLIRG HHHCCCCCCCHHHHH	52.23	23403867
204	Phosphorylation	KHKSETDTSLIRGLV HCCCCCCCHHHHHHH	32.62	29255136
205	Phosphorylation	HKSETDTSLIRGLVL CCCCCCCHHHHHHHH	25.30	19664994
206	Ubiquitination	KSETDTSLIRGLVLD CCCCCCHHHHHHHHC	3.16	21890473
223	Ubiquitination	ARHPDMKKRVEDAYI CCCCCHHHHHHHEEE	55.85	-
229	Phosphorylation	KKRVEDAYILTCNVS HHHHHHEEEEEEEEE	14.58	28152594
232	Phosphorylation	VEDAYILTCNVSLEY HHHEEEEEEEEEEEE	7.77	28152594
239	Phosphorylation	TCNVSLEYEKTEVNS EEEEEEEEEEEEECC	28.19	22817900
241	Ubiquitination	NVSLEYEKTEVNSGF EEEEEEEEEEECCCC	49.43	-
242	Ubiquitination	VSLEYEKTEVNSGFF EEEEEEEEEECCCCC	32.97	21890473
246	Phosphorylation	YEKTEVNSGFFYKSA EEEEEECCCCCCCCH	42.00	21945579
250	Ubiquitination	EVNSGFFYKSAEERE EECCCCCCCCHHHHH	11.19	21890473
250	Phosphorylation	EVNSGFFYKSAEERE EECCCCCCCCHHHHH	11.19	21945579
251	2-Hydroxyisobutyrylation	VNSGFFYKSAEEREK ECCCCCCCCHHHHHH	37.72	-
251	Acetylation	VNSGFFYKSAEEREK ECCCCCCCCHHHHHH	37.72	23236377
251	Succinylation	VNSGFFYKSAEEREK ECCCCCCCCHHHHHH	37.72	23954790
251	Sumoylation	VNSGFFYKSAEEREK ECCCCCCCCHHHHHH	37.72	28112733
251	Ubiquitination	VNSGFFYKSAEEREK ECCCCCCCCHHHHHH	37.72	21890473
258	Ubiquitination	KSAEEREKLVKAERK CCHHHHHHHHHHHHH	65.87	-
262	Ubiquitination	EREKLVKAERKFIED HHHHHHHHHHHHHHH	17.85	21890473
265	Acetylation	KLVKAERKFIEDRVK HHHHHHHHHHHHHHH	42.05	26051181
265	Ubiquitination	KLVKAERKFIEDRVK HHHHHHHHHHHHHHH	42.05	-
272	Ubiquitination	KFIEDRVKKIIELKR HHHHHHHHHHHHHHH	38.87	-
278	Ubiquitination	VKKIIELKRKVCGDS HHHHHHHHHHHHCCC	37.07	-
280	Acetylation	KIIELKRKVCGDSDK HHHHHHHHHHCCCCC	40.05	7481305
280	Malonylation	KIIELKRKVCGDSDK HHHHHHHHHHCCCCC	40.05	26320211
280	Ubiquitination	KIIELKRKVCGDSDK HHHHHHHHHHCCCCC	40.05	-
282	Glutathionylation	IELKRKVCGDSDKGF HHHHHHHHCCCCCCE	5.86	22555962
285	Phosphorylation	KRKVCGDSDKGFVVI HHHHHCCCCCCEEEE	26.89	23401153
287	2-Hydroxyisobutyrylation	KVCGDSDKGFVVINQ HHHCCCCCCEEEEEC	59.19	-
287	Acetylation	KVCGDSDKGFVVINQ HHHCCCCCCEEEEEC	59.19	23749302
287	Ubiquitination	KVCGDSDKGFVVINQ HHHCCCCCCEEEEEC	59.19	21906983
295	Acetylation	GFVVINQKGIDPFSL CEEEEECCCCCCCCH	54.03	23954790
295	Ubiquitination	GFVVINQKGIDPFSL CEEEEECCCCCCCCH	54.03	21890473
301	Phosphorylation	QKGIDPFSLDALSKE CCCCCCCCHHHHCHH	30.63	23401153
306	Phosphorylation	PFSLDALSKEGIVAL CCCHHHHCHHHHHHH	30.31	21712546
307	2-Hydroxyisobutyrylation	FSLDALSKEGIVALR CCHHHHCHHHHHHHH	61.89	-
307	Ubiquitination	FSLDALSKEGIVALR CCHHHHCHHHHHHHH	61.89	21906983
314	Methylation	KEGIVALRRAKRRNM HHHHHHHHHHHHHCC	27.12	-
320	Acetylation	LRRAKRRNMERLTLA HHHHHHHCCHHHHHH	40.47	19608861
320	Ubiquitination	LRRAKRRNMERLTLA HHHHHHHCCHHHHHH	40.47	19608861
332	Ubiquitination	TLACGGVALNSFDDL HHHHCCCHHCCCCCC	12.33	21890473
332	Acetylation	TLACGGVALNSFDDL HHHHCCCHHCCCCCC	12.33	19608861
332	Ubiquitination	TLACGGVALNSFDDL HHHHCCCHHCCCCCC	12.33	19608861
336	Ubiquitination	GGVALNSFDDLSPDC CCCHHCCCCCCCCCC	9.13	21890473
343	Acetylation	FDDLSPDCLGHAGLV CCCCCCCCCCCCEEE	5.79	19608861
365	2-Hydroxyisobutyrylation	EKFTFIEKCNNPRSV CEEEEEECCCCCCEE	37.13	-
365	Acetylation	EKFTFIEKCNNPRSV CEEEEEECCCCCCEE	37.13	19608861
365	Malonylation	EKFTFIEKCNNPRSV CEEEEEECCCCCCEE	37.13	26320211
365	Succinylation	EKFTFIEKCNNPRSV CEEEEEECCCCCCEE	37.13	27452117
365	Ubiquitination	EKFTFIEKCNNPRSV CEEEEEECCCCCCEE	37.13	19608861
377	Acetylation	RSVTLLIKGPNKHTL CEEEEEEECCCCCCH	69.18	19608861
377	Malonylation	RSVTLLIKGPNKHTL CEEEEEEECCCCCCH	69.18	26320211
377	Ubiquitination	RSVTLLIKGPNKHTL CEEEEEEECCCCCCH	69.18	21890473
381	2-Hydroxyisobutyrylation	LLIKGPNKHTLTQIK EEEECCCCCCHHHHH	40.89	-
381	Acetylation	LLIKGPNKHTLTQIK EEEECCCCCCHHHHH	40.89	25953088
381	Malonylation	LLIKGPNKHTLTQIK EEEECCCCCCHHHHH	40.89	26320211
381	Ubiquitination	LLIKGPNKHTLTQIK EEEECCCCCCHHHHH	40.89	21890473
383	Phosphorylation	IKGPNKHTLTQIKDA EECCCCCCHHHHHHH	32.86	23312004
388	2-Hydroxyisobutyrylation	KHTLTQIKDAVRDGL CCCHHHHHHHHHHHH	29.80	-
388	Acetylation	KHTLTQIKDAVRDGL CCCHHHHHHHHHHHH	29.80	19608861
388	Malonylation	KHTLTQIKDAVRDGL CCCHHHHHHHHHHHH	29.80	26320211
388	Succinylation	KHTLTQIKDAVRDGL CCCHHHHHHHHHHHH	29.80	23954790
388	Ubiquitination	KHTLTQIKDAVRDGL CCCHHHHHHHHHHHH	29.80	19608861
396	Methylation	DAVRDGLRAVKNAID HHHHHHHHHHHHHCC	42.75	-
399	2-Hydroxyisobutyrylation	RDGLRAVKNAIDDGC HHHHHHHHHHCCCCC	39.41	-
399	Ubiquitination	RDGLRAVKNAIDDGC HHHHHHHHHHCCCCC	39.41	-
406	S-nitrosocysteine	KNAIDDGCVVPGAGA HHHCCCCCCCCCCCH	3.43	-
406	Glutathionylation	KNAIDDGCVVPGAGA HHHCCCCCCCCCCCH	3.43	22555962
406	S-nitrosylation	KNAIDDGCVVPGAGA HHHCCCCCCCCCCCH	3.43	22178444
418	Sulfoxidation	AGAVEVAMAEALIKH CCHHHHHHHHHHHHC	4.12	30846556
424	Ubiquitination	AMAEALIKHKPSVKG HHHHHHHHCCCCCCC	46.56	-
426	Ubiquitination	AEALIKHKPSVKGRA HHHHHHCCCCCCCCH	33.70	-
455	Phosphorylation	PKVLAQNSGFDLQET HHHHHHCCCCCHHHH	28.85	25693802
485	Ubiquitination	GVDLNTGEPMVAAEV EEECCCCCCEEEEEC	28.34	21890473
527	Phosphorylation	EIMRAGMSSLKG--- HHHHHHHHHCCC---	31.44	28348404
528	Phosphorylation	IMRAGMSSLKG---- HHHHHHHHCCC----	25.80	28348404
530	Acetylation	RAGMSSLKG------ HHHHHHCCC------	65.60	27452117
530	Ubiquitination	RAGMSSLKG------ HHHHHHCCC------	65.60	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 TCPZ_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBP5_HUMAN	USP5	physical	22939629
VIME_HUMAN	VIM	physical	22939629
TCPG_HUMAN	CCT3	physical	22863883
TCPD_HUMAN	CCT4	physical	22863883
TCPQ_HUMAN	CCT8	physical	22863883
EF1D_HUMAN	EEF1D	physical	22863883
AT1A1_HUMAN	ATP1A1	physical	26344197
ATPG_HUMAN	ATP5C1	physical	26344197
TCPB_HUMAN	CCT2	physical	26344197
TCPG_HUMAN	CCT3	physical	26344197
TCPD_HUMAN	CCT4	physical	26344197
TCPH_HUMAN	CCT7	physical	26344197
TCPQ_HUMAN	CCT8	physical	26344197
DNJA1_HUMAN	DNAJA1	physical	26344197
DNJA4_HUMAN	DNAJA4	physical	26344197
FAS_HUMAN	FASN	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
PKN2_HUMAN	PKN2	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
TCPA_HUMAN	TCP1	physical	26344197
QCR2_HUMAN	UQCRC2	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 TCPZ_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-5; LYS-10; LYS-199; LYS-365;LYS-377 AND LYS-388, AND MASS SPECTROMETRY.	19608861 [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-205, AND MASSSPECTROMETRY.	19690332 [Abstract]