dbPTM

PTMA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTMA_HUMAN
UniProt AC	P06454
Protein Name	Prothymosin alpha
Gene Name	PTMA
Organism	Homo sapiens (Human).
Sequence Length	111
Subcellular Localization	Nucleus.
Protein Description	Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections..
Protein Sequence	MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAENEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAESATGKRAAEDDEDDDVDTKKQKTDEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MSDAAVDT -------CCCCCCCC	8.05	20068231
2	Acetylation	------MSDAAVDTS ------CCCCCCCCC	35.64	20068231
2	Phosphorylation	------MSDAAVDTS ------CCCCCCCCC	35.64	29255136
8	Phosphorylation	MSDAAVDTSSEITTK CCCCCCCCCCCCCHH	27.79	29255136
9	Phosphorylation	SDAAVDTSSEITTKD CCCCCCCCCCCCHHH	22.85	29255136
10	Phosphorylation	DAAVDTSSEITTKDL CCCCCCCCCCCHHHH	34.80	29255136
13	Phosphorylation	VDTSSEITTKDLKEK CCCCCCCCHHHHHHH	24.60	29255136
14	Phosphorylation	DTSSEITTKDLKEKK CCCCCCCHHHHHHHH	28.37	25159151
15	2-Hydroxyisobutyrylation	TSSEITTKDLKEKKE CCCCCCHHHHHHHHH	53.03	-
15	Succinylation	TSSEITTKDLKEKKE CCCCCCHHHHHHHHH	53.03	23954790
15 (in isoform 1)	Ubiquitination	-	53.03	21890473
15 (in isoform 2)	Ubiquitination	-	53.03	21890473
15	Ubiquitination	TSSEITTKDLKEKKE CCCCCCHHHHHHHHH	53.03	21890473
15	Succinylation	TSSEITTKDLKEKKE CCCCCCHHHHHHHHH	53.03	-
15	Acetylation	TSSEITTKDLKEKKE CCCCCCHHHHHHHHH	53.03	19608861
18	Acetylation	EITTKDLKEKKEVVE CCCHHHHHHHHHHHH	77.08	19352641
20	Acetylation	TTKDLKEKKEVVEEA CHHHHHHHHHHHHHH	53.28	25953088
20	Ubiquitination	TTKDLKEKKEVVEEA CHHHHHHHHHHHHHH	53.28	21906983
20 (in isoform 2)	Ubiquitination	-	53.28	21890473
20 (in isoform 1)	Ubiquitination	-	53.28	21890473
21 (in isoform 1)	Ubiquitination	-	57.75	21890473
21 (in isoform 2)	Ubiquitination	-	57.75	21890473
21	Acetylation	TKDLKEKKEVVEEAE HHHHHHHHHHHHHHH	57.75	23749302
21	Ubiquitination	TKDLKEKKEVVEEAE HHHHHHHHHHHHHHH	57.75	21890473
84 (in isoform 2)	Phosphorylation	-	44.16	28634120
85	Phosphorylation	DEDEEAESATGKRAA CHHHHHHHHHCCCCC	37.87	28985074
86 (in isoform 2)	Phosphorylation	-	16.33	18669648
87	Phosphorylation	DEEAESATGKRAAED HHHHHHHHCCCCCCC	53.14	18669648
90	Methylation	AESATGKRAAEDDED HHHHHCCCCCCCCCC	40.13	115489591
102	Acetylation	DEDDDVDTKKQKTDE CCCCCCCHHHCCCCC	39.73	19608861
102	Phosphorylation	DEDDDVDTKKQKTDE CCCCCCCHHHCCCCC	39.73	29255136
102	Ubiquitination	DEDDDVDTKKQKTDE CCCCCCCHHHCCCCC	39.73	19608861
102 (in isoform 2)	Ubiquitination	-	39.73	21890473
103	Succinylation	EDDDVDTKKQKTDED CCCCCCHHHCCCCCC	49.06	23954790
103	Sumoylation	EDDDVDTKKQKTDED CCCCCCHHHCCCCCC	49.06	28112733
103	Ubiquitination	EDDDVDTKKQKTDED CCCCCCHHHCCCCCC	49.06	19608861
103	Acetylation	EDDDVDTKKQKTDED CCCCCCHHHCCCCCC	49.06	23954790
103 (in isoform 1)	Ubiquitination	-	49.06	21890473
104	Acetylation	DDDVDTKKQKTDEDD CCCCCHHHCCCCCCC	60.15	70363
104	Ubiquitination	DDDVDTKKQKTDEDD CCCCCHHHCCCCCCC	60.15	-
106	Acetylation	DVDTKKQKTDEDD-- CCCHHHCCCCCCC--	67.81	164561
106	Ubiquitination	DVDTKKQKTDEDD-- CCCHHHCCCCCCC--	67.81	-
107	Phosphorylation	VDTKKQKTDEDD--- CCHHHCCCCCCC---	41.97	23911959

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
8	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
8	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
13	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
13	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
14	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
14	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR1_HUMAN	ESR1	physical	12943695
HDAC1_HUMAN	HDAC1	physical	12634383
HDAC2_HUMAN	HDAC2	physical	12634383
NCOR1_HUMAN	NCOR1	physical	12634383
SIN3A_HUMAN	SIN3A	physical	12634383
CBP_HUMAN	CREBBP	physical	11897665
EP300_HUMAN	EP300	genetic	11967287
SET_HUMAN	SET	physical	15556635
KEAP1_MOUSE	Keap1	physical	19279002
PTMS_HUMAN	PTMS	physical	22939629
SRSF2_HUMAN	SRSF2	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
IMA1_HUMAN	KPNA2	physical	11310559
RAN_HUMAN	RAN	physical	11310559
RCC1_HUMAN	RCC1	physical	11310559
IMB1_HUMAN	KPNB1	physical	11310559
PCNA_HUMAN	PCNA	physical	11310559
CDK2_HUMAN	CDK2	physical	11310559
CDK4_HUMAN	CDK4	physical	11310559
CDK1_HUMAN	CDK1	physical	11310559
CCNB1_HUMAN	CCNB1	physical	11310559
ASNS_HUMAN	ASNS	physical	22863883
PUR9_HUMAN	ATIC	physical	22863883
CPNS1_HUMAN	CAPNS1	physical	22863883
CAZA2_HUMAN	CAPZA2	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
MCTS1_HUMAN	MCTS1	physical	22863883
MOES_HUMAN	MSN	physical	22863883
NSF1C_HUMAN	NSFL1C	physical	22863883
PDIA4_HUMAN	PDIA4	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
TBCB_HUMAN	TBCB	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
KEAP1_HUMAN	KEAP1	physical	23318954
KEAP1_HUMAN	KEAP1	physical	25416956
H11_HUMAN	HIST1H1A	physical	10891508
EP300_HUMAN	EP300	physical	10891508

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 PTMA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Phosphorylation of human and bovine prothymosin alpha in vivo."; Sburlati A.R., De La Rosa A., Batey D.W., Kurys G.L., Manrow R.E.,Pannell L.K., Martin B.M., Sheeley D.M., Berger S.L.; Biochemistry 32:4587-4596(1993). Cited for: PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2.	8485135 [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-15, 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-2, AND MASSSPECTROMETRY.	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-2, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-9 AND SER-10, ANDMASS SPECTROMETRY.	19413330 [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-2, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Phosphorylation of human and bovine prothymosin alpha in vivo."; Sburlati A.R., De La Rosa A., Batey D.W., Kurys G.L., Manrow R.E.,Pannell L.K., Martin B.M., Sheeley D.M., Berger S.L.; Biochemistry 32:4587-4596(1993). Cited for: PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2.	8485135 [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 THR-107, AND MASSSPECTROMETRY.	18669648 [Abstract]