dbPTM

TPD54_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPD54_HUMAN
UniProt AC	O43399
Protein Name	Tumor protein D54
Gene Name	TPD52L2
Organism	Homo sapiens (Human).
Sequence Length	206
Subcellular Localization
Protein Description
Protein Sequence	MDSAGQDINLNSPNKGLLSDSMTDVPVDTGVAARTPAVEGLTEAEEEELRAELTKVEEEIVTLRQVLAAKERHCGELKRRLGLSTLGELKQNLSRSWHDVQVSSAYVKTSEKLGEWNEKVTQSDLYKKTQETLSQAGQKTSAALSTVGSAISRKLGDMRNSATFKSFEDRVGTIKSKVVGDRENGSDNLPSSAGSGDKPLSDPAPF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDSAGQDI -------CCCCCCCC	9.19	20068231
1	Sulfoxidation	-------MDSAGQDI -------CCCCCCCC	9.19	28465586
3	Phosphorylation	-----MDSAGQDINL -----CCCCCCCCCC	32.76	28355574
12	Phosphorylation	GQDINLNSPNKGLLS CCCCCCCCCCCCCCC	32.77	29255136
19	Phosphorylation	SPNKGLLSDSMTDVP CCCCCCCCCCCCCCC	32.45	29255136
21	Phosphorylation	NKGLLSDSMTDVPVD CCCCCCCCCCCCCCC	21.87	29255136
22	Sulfoxidation	KGLLSDSMTDVPVDT CCCCCCCCCCCCCCC	4.44	21406390
23	Phosphorylation	GLLSDSMTDVPVDTG CCCCCCCCCCCCCCC	37.48	29255136
29	Phosphorylation	MTDVPVDTGVAARTP CCCCCCCCCHHCCCC	33.51	22167270
35	Phosphorylation	DTGVAARTPAVEGLT CCCHHCCCCCCCCCC	15.75	21815630
42	Phosphorylation	TPAVEGLTEAEEEEL CCCCCCCCHHHHHHH	43.96	-
50	Methylation	EAEEEELRAELTKVE HHHHHHHHHHHHHHH	29.33	115918789
55	Ubiquitination	ELRAELTKVEEEIVT HHHHHHHHHHHHHHH	61.34	22053931
55 (in isoform 2)	Ubiquitination	-	61.34	21890473
62	Phosphorylation	KVEEEIVTLRQVLAA HHHHHHHHHHHHHHH	23.14	30576742
70	Acetylation	LRQVLAAKERHCGEL HHHHHHHHHHHHHHH	50.07	27452117
70	Succinylation	LRQVLAAKERHCGEL HHHHHHHHHHHHHHH	50.07	23954790
70	Ubiquitination	LRQVLAAKERHCGEL HHHHHHHHHHHHHHH	50.07	-
71 (in isoform 6)	Phosphorylation	-	42.82	25159151
73 (in isoform 6)	Phosphorylation	-	25.65	25159151
78	Acetylation	ERHCGELKRRLGLST HHHHHHHHHHHCCCH	31.04	24847115
80 (in isoform 6)	Phosphorylation	-	31.36	20068231
81 (in isoform 6)	Phosphorylation	-	10.58	29507054
83 (in isoform 6)	Phosphorylation	-	4.12	20068231
84	Phosphorylation	LKRRLGLSTLGELKQ HHHHHCCCHHHHHHH	21.56	20068231
85	Phosphorylation	KRRLGLSTLGELKQN HHHHCCCHHHHHHHH	43.77	20068231
90	Ubiquitination	LSTLGELKQNLSRSW CCHHHHHHHHHCCCC	32.60	21890473
90	Methylation	LSTLGELKQNLSRSW CCHHHHHHHHHCCCC	32.60	72668545
90	Ubiquitination	LSTLGELKQNLSRSW CCHHHHHHHHHCCCC	32.60	21890473
90 (in isoform 1)	Ubiquitination	-	32.60	21890473
90 (in isoform 2)	Ubiquitination	-	32.60	21890473
90 (in isoform 3)	Ubiquitination	-	32.60	21890473
90 (in isoform 4)	Ubiquitination	-	32.60	21890473
91 (in isoform 6)	Phosphorylation	-	69.58	25159151
94	Phosphorylation	GELKQNLSRSWHDVQ HHHHHHHCCCCCCHH	31.64	23401153
94 (in isoform 2)	Phosphorylation	-	31.64	25159151
94 (in isoform 3)	Phosphorylation	-	31.64	25159151
94 (in isoform 4)	Phosphorylation	-	31.64	25159151
96	O-linked_Glycosylation	LKQNLSRSWHDVQVS HHHHHCCCCCCHHCC	25.95	30059200
96	Phosphorylation	LKQNLSRSWHDVQVS HHHHHCCCCCCHHCC	25.95	23927012
96 (in isoform 2)	Phosphorylation	-	25.95	25159151
96 (in isoform 3)	Phosphorylation	-	25.95	25159151
96 (in isoform 4)	Phosphorylation	-	25.95	25159151
103	O-linked_Glycosylation	SWHDVQVSSAYVKTS CCCCHHCCEEEEHHH	7.67	30059200
103	Phosphorylation	SWHDVQVSSAYVKTS CCCCHHCCEEEEHHH	7.67	21945579
103 (in isoform 2)	Phosphorylation	-	7.67	20068231
103 (in isoform 3)	Phosphorylation	-	7.67	20068231
103 (in isoform 4)	Phosphorylation	-	7.67	20068231
104	O-linked_Glycosylation	WHDVQVSSAYVKTSE CCCHHCCEEEEHHHH	25.43	30059200
104	Phosphorylation	WHDVQVSSAYVKTSE CCCHHCCEEEEHHHH	25.43	21945579
104 (in isoform 2)	Phosphorylation	-	25.43	29507054
104 (in isoform 3)	Phosphorylation	-	25.43	29507054
104 (in isoform 4)	Phosphorylation	-	25.43	29507054
106	Phosphorylation	DVQVSSAYVKTSEKL CHHCCEEEEHHHHHH	12.39	21945579
106 (in isoform 2)	Phosphorylation	-	12.39	20068231
106 (in isoform 3)	Phosphorylation	-	12.39	20068231
106 (in isoform 4)	Phosphorylation	-	12.39	20068231
108	Ubiquitination	QVSSAYVKTSEKLGE HCCEEEEHHHHHHHH	33.39	21890473
108 (in isoform 1)	Ubiquitination	-	33.39	21890473
108 (in isoform 2)	Ubiquitination	-	33.39	21890473
108 (in isoform 3)	Ubiquitination	-	33.39	21890473
108	Ubiquitination	QVSSAYVKTSEKLGE HCCEEEEHHHHHHHH	33.39	21890473
108	Ubiquitination	QVSSAYVKTSEKLGE HCCEEEEHHHHHHHH	33.39	21890473
112	Ubiquitination	AYVKTSEKLGEWNEK EEEHHHHHHHHHCHH	62.65	21906983
112 (in isoform 1)	Ubiquitination	-	62.65	21890473
114 (in isoform 2)	Phosphorylation	-	49.28	25159151
114 (in isoform 3)	Phosphorylation	-	49.28	25159151
114 (in isoform 4)	Phosphorylation	-	49.28	25159151
119	Acetylation	KLGEWNEKVTQSDLY HHHHHCHHCCHHHHH	47.58	27452117
119	Ubiquitination	KLGEWNEKVTQSDLY HHHHHCHHCCHHHHH	47.58	-
119 (in isoform 2)	Ubiquitination	-	47.58	21890473
119 (in isoform 3)	Ubiquitination	-	47.58	21890473
119 (in isoform 5)	Ubiquitination	-	47.58	20972266
121	O-linked_Glycosylation	GEWNEKVTQSDLYKK HHHCHHCCHHHHHHH	33.16	30059200
123	Phosphorylation	WNEKVTQSDLYKKTQ HCHHCCHHHHHHHHH	21.88	28152594
126	Phosphorylation	KVTQSDLYKKTQETL HCCHHHHHHHHHHHH	18.54	25394399
127	Acetylation	VTQSDLYKKTQETLS CCHHHHHHHHHHHHH	57.55	27452117
127	Succinylation	VTQSDLYKKTQETLS CCHHHHHHHHHHHHH	57.55	23954790
128	Ubiquitination	TQSDLYKKTQETLSQ CHHHHHHHHHHHHHH	41.71	21906983
128 (in isoform 1)	Ubiquitination	-	41.71	21890473
129	Phosphorylation	QSDLYKKTQETLSQA HHHHHHHHHHHHHHH	27.73	-
132	Phosphorylation	LYKKTQETLSQAGQK HHHHHHHHHHHHHHH	23.15	29396449
134	O-linked_Glycosylation	KKTQETLSQAGQKTS HHHHHHHHHHHHHHH	25.96	30059200
134	Phosphorylation	KKTQETLSQAGQKTS HHHHHHHHHHHHHHH	25.96	25159151
139	Ubiquitination	TLSQAGQKTSAALST HHHHHHHHHHHHHHH	43.46	20972266
139 (in isoform 1)	Ubiquitination	-	43.46	21890473
140	Phosphorylation	LSQAGQKTSAALSTV HHHHHHHHHHHHHHH	18.73	29396449
141	Phosphorylation	SQAGQKTSAALSTVG HHHHHHHHHHHHHHH	20.69	20068231
144 (in isoform 3)	Phosphorylation	-	4.39	24117733
145	O-linked_Glycosylation	QKTSAALSTVGSAIS HHHHHHHHHHHHHHH	19.13	OGP
145	Phosphorylation	QKTSAALSTVGSAIS HHHHHHHHHHHHHHH	19.13	25159151
146	O-linked_Glycosylation	KTSAALSTVGSAISR HHHHHHHHHHHHHHH	29.72	OGP
146	Phosphorylation	KTSAALSTVGSAISR HHHHHHHHHHHHHHH	29.72	25159151
146 (in isoform 3)	Phosphorylation	-	29.72	24117733
146 (in isoform 4)	Phosphorylation	-	29.72	25849741
148 (in isoform 3)	Phosphorylation	-	16.08	24117733
148 (in isoform 4)	Phosphorylation	-	16.08	25849741
149	O-linked_Glycosylation	AALSTVGSAISRKLG HHHHHHHHHHHHHHH	20.35	OGP
149	Phosphorylation	AALSTVGSAISRKLG HHHHHHHHHHHHHHH	20.35	25159151
149 (in isoform 3)	Phosphorylation	-	20.35	24117733
151 (in isoform 3)	Phosphorylation	-	4.36	24117733
152	O-linked_Glycosylation	STVGSAISRKLGDMR HHHHHHHHHHHHCCC	24.07	OGP
152	Phosphorylation	STVGSAISRKLGDMR HHHHHHHHHHHHCCC	24.07	23401153
155 (in isoform 3)	Phosphorylation	-	7.36	24275569
155 (in isoform 4)	Phosphorylation	-	7.36	27762562
157 (in isoform 3)	Phosphorylation	-	43.22	27135362
157 (in isoform 4)	Phosphorylation	-	43.22	25849741
160 (in isoform 4)	Phosphorylation	-	29.38	25849741
161	Phosphorylation	KLGDMRNSATFKSFE HHHCCCCCCCHHCHH	20.51	22167270
163	Phosphorylation	GDMRNSATFKSFEDR HCCCCCCCHHCHHHH	31.27	29255136
164 (in isoform 3)	Phosphorylation	-	6.62	27762562
164 (in isoform 7)	Phosphorylation	-	6.62	24117733
165	Acetylation	MRNSATFKSFEDRVG CCCCCCHHCHHHHHC	50.29	25953088
165	Methylation	MRNSATFKSFEDRVG CCCCCCHHCHHHHHC	50.29	90159
165	Ubiquitination	MRNSATFKSFEDRVG CCCCCCHHCHHHHHC	50.29	-
166	Phosphorylation	RNSATFKSFEDRVGT CCCCCHHCHHHHHCC	29.67	29255136
166 (in isoform 3)	Phosphorylation	-	29.67	25849741
166 (in isoform 5)	Phosphorylation	-	29.67	25849741
168 (in isoform 5)	Phosphorylation	-	52.58	25849741
169 (in isoform 3)	Phosphorylation	-	48.86	25849741
169 (in isoform 7)	Phosphorylation	-	48.86	24117733
170	Methylation	TFKSFEDRVGTIKSK CHHCHHHHHCCCEEE	22.90	115918785
171 (in isoform 7)	Phosphorylation	-	14.18	24117733
173	Phosphorylation	SFEDRVGTIKSKVVG CHHHHHCCCEEEECC	23.52	28355574
175 (in isoform 5)	Phosphorylation	-	44.02	27762562
176	Phosphorylation	DRVGTIKSKVVGDRE HHHCCCEEEECCCCC	27.17	21601212
177 (in isoform 5)	Phosphorylation	-	35.62	25849741
180 (in isoform 5)	Phosphorylation	-	31.11	25849741
184 (in isoform 7)	Phosphorylation	-	57.04	27762562
186	Phosphorylation	VGDRENGSDNLPSSA CCCCCCCCCCCCCCC	34.60	25849741
191	Phosphorylation	NGSDNLPSSAGSGDK CCCCCCCCCCCCCCC	35.67	23401153
192	Phosphorylation	GSDNLPSSAGSGDKP CCCCCCCCCCCCCCC	34.41	25159151
195	Phosphorylation	NLPSSAGSGDKPLSD CCCCCCCCCCCCCCC	43.46	25159151
198	Ubiquitination	SSAGSGDKPLSDPAP CCCCCCCCCCCCCCC	51.92	-
201	Phosphorylation	GSGDKPLSDPAPF-- CCCCCCCCCCCCC--	50.50	25159151

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 TPD54_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TPD54_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 TPD54_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TPD52_HUMAN	TPD52	physical	9484778
TPD53_HUMAN	TPD52L1	physical	9484778
TPD54_HUMAN	TPD52L2	physical	9484778
TRXR1_HUMAN	TXNRD1	physical	22939629
IPO11_HUMAN	IPO11	physical	22863883
METH_HUMAN	MTR	physical	22863883
PDIA1_HUMAN	P4HB	physical	22863883
PFD2_HUMAN	PFDN2	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
THG1_HUMAN	THG1L	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
UBQL2_HUMAN	UBQLN2	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	25416956
CGL_HUMAN	CTH	physical	26344197
ECHM_HUMAN	ECHS1	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
OGT1_HUMAN	OGT	physical	26344197
PA1B2_HUMAN	PAFAH1B2	physical	26344197
PPM1G_HUMAN	PPM1G	physical	26344197
TEBP_HUMAN	PTGES3	physical	26344197
SC31A_HUMAN	SEC31A	physical	26344197
SYTC_HUMAN	TARS	physical	26344197
TRI25_HUMAN	TRIM25	physical	26344197
VAV2_HUMAN	VAV2	physical	26344197
TPD53_HUMAN	TPD52L1	physical	28514442
SHIP2_HUMAN	INPPL1	physical	28514442
TPD52_HUMAN	TPD52	physical	28514442
CSN5_HUMAN	COPS5	physical	28514442
GABPA_HUMAN	GABPA	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TPD54_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-12, AND MASS SPECTROMETRY.	19413330 [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-96; SER-149 AND SER-166,AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-12, AND MASS SPECTROMETRY.	19413330 [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-3; SER-12; SER-21;SER-96 AND SER-166, 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-12 AND SER-166, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-166 ANDTHR-173, AND MASS SPECTROMETRY.	17287340 [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-12; SER-96 AND SER-166,AND MASS SPECTROMETRY.	17081983 [Abstract]