dbPTM

PA2G4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PA2G4_HUMAN
UniProt AC	Q9UQ80
Protein Name	Proliferation-associated protein 2G4
Gene Name	PA2G4
Organism	Homo sapiens (Human).
Sequence Length	394
Subcellular Localization	Isoform 1: Cytoplasm . Nucleus, nucleolus . Translocates to the nucleus upon treatment with HRG. Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization. Isoform 2: Cytoplasm .
Protein Description	May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity)..
Protein Sequence	MSGEDEQQEQTIAEDLVVTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDAMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDVAQGTQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAKDAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDAMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRITSGPFEPDLYKSEMEVQDAELKALLQSSASRKTQKKKKKKASKTAENATSGETLEENEAGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGEDEQQE ------CCCCHHHHH	51.38	20068231
2	Phosphorylation	------MSGEDEQQE ------CCCCHHHHH	51.38	29255136
11	Phosphorylation	EDEQQEQTIAEDLVV CHHHHHHHHHHHHHH	22.77	22167270
19	Phosphorylation	IAEDLVVTKYKMGGD HHHHHHHEEECCCHH	22.60	22167270
20	Ubiquitination	AEDLVVTKYKMGGDI HHHHHHEEECCCHHH	31.12	21906983
20	2-Hydroxyisobutyrylation	AEDLVVTKYKMGGDI HHHHHHEEECCCHHH	31.12	-
20	Acetylation	AEDLVVTKYKMGGDI HHHHHHEEECCCHHH	31.12	27452117
22	Ubiquitination	DLVVTKYKMGGDIAN HHHHEEECCCHHHHH	32.40	-
22	2-Hydroxyisobutyrylation	DLVVTKYKMGGDIAN HHHHEEECCCHHHHH	32.40	-
22	Acetylation	DLVVTKYKMGGDIAN HHHHEEECCCHHHHH	32.40	25953088
23	Sulfoxidation	LVVTKYKMGGDIANR HHHEEECCCHHHHHH	7.05	30846556
30	Methylation	MGGDIANRVLRSLVE CCHHHHHHHHHHHHH	21.59	-
34	Phosphorylation	IANRVLRSLVEASSS HHHHHHHHHHHHHHC	32.38	-
44	Phosphorylation	EASSSGVSVLSLCEK HHHHCCCEEHHHHHH	22.36	-
55	Sulfoxidation	LCEKGDAMIMEETGK HHHHCCEEEEECCCC	3.40	21406390
57	Sulfoxidation	EKGDAMIMEETGKIF HHCCEEEEECCCCHH	2.15	30846556
60	Phosphorylation	DAMIMEETGKIFKKE CEEEEECCCCHHHHH	30.39	-
62	Ubiquitination	MIMEETGKIFKKEKE EEEECCCCHHHHHHH	53.00	-
66	Ubiquitination	ETGKIFKKEKEMKKG CCCCHHHHHHHHHCC	64.37	-
72	Ubiquitination	KKEKEMKKGIAFPTS HHHHHHHCCCCCCCE	54.99	-
72	Acetylation	KKEKEMKKGIAFPTS HHHHHHHCCCCCCCE	54.99	26051181
78	Phosphorylation	KKGIAFPTSISVNNC HCCCCCCCEEEECCE	32.04	20873877
79	Phosphorylation	KGIAFPTSISVNNCV CCCCCCCEEEECCEE	17.07	20873877
81	Phosphorylation	IAFPTSISVNNCVCH CCCCCEEEECCEEEE	20.68	20873877
90	Phosphorylation	NNCVCHFSPLKSDQD CCEEEECCCCCCCCC	12.98	20873877
93	Sumoylation	VCHFSPLKSDQDYIL EEECCCCCCCCCEEE	56.20	-
93	Sumoylation	VCHFSPLKSDQDYIL EEECCCCCCCCCEEE	56.20	-
93	Ubiquitination	VCHFSPLKSDQDYIL EEECCCCCCCCCEEE	56.20	-
93	Acetylation	VCHFSPLKSDQDYIL EEECCCCCCCCCEEE	56.20	26051181
94	Phosphorylation	CHFSPLKSDQDYILK EECCCCCCCCCEEEC	48.46	28152594
98	Phosphorylation	PLKSDQDYILKEGDL CCCCCCCEEECCCCE	11.52	19702290
101	Ubiquitination	SDQDYILKEGDLVKI CCCCEEECCCCEEEE	50.52	-
101	Acetylation	SDQDYILKEGDLVKI CCCCEEECCCCEEEE	50.52	25953088
101	Succinylation	SDQDYILKEGDLVKI CCCCEEECCCCEEEE	50.52	23954790
144	Ubiquitination	GRKADVIKAAHLCAE CCHHHHHHHHHHHHH	39.09	-
144	2-Hydroxyisobutyrylation	GRKADVIKAAHLCAE CCHHHHHHHHHHHHH	39.09	-
144	Acetylation	GRKADVIKAAHLCAE CCHHHHHHHHHHHHH	39.09	26051181
149	Glutathionylation	VIKAAHLCAEAALRL HHHHHHHHHHHHHHH	2.00	22555962
158	Ubiquitination	EAALRLVKPGNQNTQ HHHHHHCCCCCCCCH	52.37	21906983
158	Acetylation	EAALRLVKPGNQNTQ HHHHHHCCCCCCCCH	52.37	26051181
172	Methylation	QVTEAWNKVAHSFNC HHHHHHHHHHHHCCC	30.05	-
172	Ubiquitination	QVTEAWNKVAHSFNC HHHHHHHHHHHHCCC	30.05	-
172	Acetylation	QVTEAWNKVAHSFNC HHHHHHHHHHHHCCC	30.05	26051181
176	Phosphorylation	AWNKVAHSFNCTPIE HHHHHHHHCCCCCCC	14.39	20873877
179	Glutathionylation	KVAHSFNCTPIEGML HHHHHCCCCCCCCHH	4.51	22555962
180	Phosphorylation	VAHSFNCTPIEGMLS HHHHCCCCCCCCHHH	28.53	28857561
187	Phosphorylation	TPIEGMLSHQLKQHV CCCCCHHHHHHHHHC	10.57	20873877
191	Ubiquitination	GMLSHQLKQHVIDGE CHHHHHHHHHCCCCC	31.61	-
191	Acetylation	GMLSHQLKQHVIDGE CHHHHHHHHHCCCCC	31.61	26051181
199	"N6,N6-dimethyllysine"	QHVIDGEKTIIQNPT HHCCCCCCEEEECCC	51.02	-
199	Ubiquitination	QHVIDGEKTIIQNPT HHCCCCCCEEEECCC	51.02	21906983
199	2-Hydroxyisobutyrylation	QHVIDGEKTIIQNPT HHCCCCCCEEEECCC	51.02	-
199	Acetylation	QHVIDGEKTIIQNPT HHCCCCCCEEEECCC	51.02	26051181
199	Methylation	QHVIDGEKTIIQNPT HHCCCCCCEEEECCC	51.02	-
206	Phosphorylation	KTIIQNPTDQQKKDH CEEEECCCHHHHHHH	54.73	21712546
210	Ubiquitination	QNPTDQQKKDHEKAE ECCCHHHHHHHHHHE	55.31	21906983
210	2-Hydroxyisobutyrylation	QNPTDQQKKDHEKAE ECCCHHHHHHHHHHE	55.31	-
210	Acetylation	QNPTDQQKKDHEKAE ECCCHHHHHHHHHHE	55.31	26051181
211	Ubiquitination	NPTDQQKKDHEKAEF CCCHHHHHHHHHHEE	61.04	-
238	Ubiquitination	SSGEGKAKDAGQRTT ECCCCCCCCCCCCCE	52.15	-
248	Ubiquitination	GQRTTIYKRDPSKQY CCCCEEEECCHHHCC	46.61	-
252	Phosphorylation	TIYKRDPSKQYGLKM EEEECCHHHCCCCEE	36.36	28152594
253	Ubiquitination	IYKRDPSKQYGLKMK EEECCHHHCCCCEEH	53.58	-
253	2-Hydroxyisobutyrylation	IYKRDPSKQYGLKMK EEECCHHHCCCCEEH	53.58	-
253	Acetylation	IYKRDPSKQYGLKMK EEECCHHHCCCCEEH	53.58	26051181
255	Phosphorylation	KRDPSKQYGLKMKTS ECCHHHCCCCEEHHC	28.32	28152594
258	Ubiquitination	PSKQYGLKMKTSRAF HHHCCCCEEHHCHHH	33.71	-
258	2-Hydroxyisobutyrylation	PSKQYGLKMKTSRAF HHHCCCCEEHHCHHH	33.71	-
258	Acetylation	PSKQYGLKMKTSRAF HHHCCCCEEHHCHHH	33.71	25953088
260	Methylation	KQYGLKMKTSRAFFS HCCCCEEHHCHHHHH	41.58	-
261	Phosphorylation	QYGLKMKTSRAFFSE CCCCEEHHCHHHHHH	21.68	18283314
262	Phosphorylation	YGLKMKTSRAFFSEV CCCEEHHCHHHHHHH	18.98	28509920
267	Phosphorylation	KTSRAFFSEVERRFD HHCHHHHHHHHHHHH	33.99	28857561
271	Methylation	AFFSEVERRFDAMPF HHHHHHHHHHHCCCE	50.14	-
276	Sulfoxidation	VERRFDAMPFTLRAF HHHHHHCCCEEEHHH	2.78	21406390
279	Phosphorylation	RFDAMPFTLRAFEDE HHHCCCEEEHHHHCH	14.95	24719451
281	Methylation	DAMPFTLRAFEDEKK HCCCEEEHHHHCHHH	33.89	-
287	Acetylation	LRAFEDEKKARMGVV EHHHHCHHHHHCCHH	65.14	23749302
287	Ubiquitination	LRAFEDEKKARMGVV EHHHHCHHHHHCCHH	65.14	-
288	Ubiquitination	RAFEDEKKARMGVVE HHHHCHHHHHCCHHH	38.90	-
296	Glutathionylation	ARMGVVECAKHELLQ HHCCHHHHHHHHHHH	4.06	22555962
298	Acetylation	MGVVECAKHELLQPF CCHHHHHHHHHHHCC	49.63	23954790
298	Sumoylation	MGVVECAKHELLQPF CCHHHHHHHHHHHCC	49.63	-
298	Ubiquitination	MGVVECAKHELLQPF CCHHHHHHHHHHHCC	49.63	-
298	Sumoylation	MGVVECAKHELLQPF CCHHHHHHHHHHHCC	49.63	28112733
309	Phosphorylation	LQPFNVLYEKEGEFV HHCCCEEEEECCCEE	22.22	28152594
311	Ubiquitination	PFNVLYEKEGEFVAQ CCCEEEEECCCEEEE	58.42	-
326	Sulfoxidation	FKFTVLLMPNGPMRI EEEEEEECCCCCEEE	1.80	21406390
334	Phosphorylation	PNGPMRITSGPFEPD CCCCEEECCCCCCCC	19.78	20068231
335	Phosphorylation	NGPMRITSGPFEPDL CCCEEECCCCCCCCH	41.94	20068231
343	Phosphorylation	GPFEPDLYKSEMEVQ CCCCCCHHCCHHHHC	21.61	20068231
344	Ubiquitination	PFEPDLYKSEMEVQD CCCCCHHCCHHHHCH	47.43	21906983
344	Sumoylation	PFEPDLYKSEMEVQD CCCCCHHCCHHHHCH	47.43	-
344	2-Hydroxyisobutyrylation	PFEPDLYKSEMEVQD CCCCCHHCCHHHHCH	47.43	-
344	Acetylation	PFEPDLYKSEMEVQD CCCCCHHCCHHHHCH	47.43	26051181
345	Phosphorylation	FEPDLYKSEMEVQDA CCCCHHCCHHHHCHH	28.72	21712546
347	Sulfoxidation	PDLYKSEMEVQDAEL CCHHCCHHHHCHHHH	8.69	21406390
355	Ubiquitination	EVQDAELKALLQSSA HHCHHHHHHHHHHHH	28.61	21906983
355	2-Hydroxyisobutyrylation	EVQDAELKALLQSSA HHCHHHHHHHHHHHH	28.61	-
360	Phosphorylation	ELKALLQSSASRKTQ HHHHHHHHHHHHHHH	28.04	30266825
361	Phosphorylation	LKALLQSSASRKTQK HHHHHHHHHHHHHHH	19.80	29255136
363	Phosphorylation	ALLQSSASRKTQKKK HHHHHHHHHHHHHHH	35.94	30266825
366	Phosphorylation	QSSASRKTQKKKKKK HHHHHHHHHHHHHHH	44.50	26434776
373	Ubiquitination	TQKKKKKKASKTAEN HHHHHHHHHHHHHCC	67.77	-
375	Phosphorylation	KKKKKKASKTAENAT HHHHHHHHHHHCCCC	39.14	24732914
376	Ubiquitination	KKKKKASKTAENATS HHHHHHHHHHCCCCC	57.52	21906983
377	Phosphorylation	KKKKASKTAENATSG HHHHHHHHHCCCCCC	36.39	25159151
382	Phosphorylation	SKTAENATSGETLEE HHHHCCCCCCCCCHH	49.17	30278072
383	Phosphorylation	KTAENATSGETLEEN HHHCCCCCCCCCHHC	32.02	30278072
386	Phosphorylation	ENATSGETLEENEAG CCCCCCCCCHHCCCC	42.89	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
34	S	Phosphorylation	Kinase	CDK2	P24941	PSP
261	T	Phosphorylation	Kinase	PAK1	Q13153	PSP
360	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
360	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
361	S	Phosphorylation	Kinase	PRKCD	Q05655	Uniprot
366	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RNF40	O75150	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	RNF20	Q5VTR2	PMID:19037095
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
361	S	Phosphorylation		16832058
Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization.

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 PA2G4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC2_HUMAN	HDAC2	physical	12682367
RB_HUMAN	RB1	physical	11268000
ANDR_HUMAN	AR	physical	12165860
BRE1A_HUMAN	RNF20	physical	19037095
NEMO_HUMAN	IKBKG	physical	20211142
SIN3A_HUMAN	SIN3A	physical	16254079
MDM2_HUMAN	MDM2	physical	21930127
AKT1_HUMAN	AKT1	physical	21930127
MDM2_HUMAN	MDM2	physical	21098709
FUS_HUMAN	FUS	physical	19946338
UBC9_HUMAN	UBE2I	physical	19946338
NPM_HUMAN	NPM1	physical	17951246
VPP1_HUMAN	ATP6V0A1	physical	22939629
PAIRB_HUMAN	SERBP1	physical	22939629
NUCL_HUMAN	NCL	physical	15064750
TOP1_HUMAN	TOP1	physical	15064750
IF2B2_HUMAN	IGF2BP2	physical	15064750
RLA0_HUMAN	RPLP0	physical	15064750
H11_HUMAN	HIST1H1A	physical	15064750
RL4_HUMAN	RPL4	physical	15064750
RL8_HUMAN	RPL8	physical	15064750
RL15_HUMAN	RPL15	physical	15064750
RL18_HUMAN	RPL18	physical	15064750
RL18A_HUMAN	RPL18A	physical	15064750
RL21_HUMAN	RPL21	physical	15064750
RL11_HUMAN	RPL11	physical	15064750
RL12_HUMAN	RPL12	physical	15064750
RL28_HUMAN	RPL28	physical	15064750
RL27_HUMAN	RPL27	physical	15064750
RL30_HUMAN	RPL30	physical	15064750
RLA2_HUMAN	RPLP2	physical	15064750
HMGA1_HUMAN	HMGA1	physical	18850631
HMGA2_HUMAN	HMGA2	physical	18850631
NELFB_HUMAN	NELFB	physical	22863883
DIM1_HUMAN	DIMT1	physical	22863883
EIF3K_HUMAN	EIF3K	physical	22863883
MTAP2_HUMAN	MAP2	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
YBOX1_HUMAN	YBX1	physical	22863883
NPM_HUMAN	NPM1	physical	19037095
ERBB3_HUMAN	ERBB3	physical	19037095
DHX9_HUMAN	DHX9	physical	19037095
LAMB1_HUMAN	LAMB1	physical	19037095
NUCL_HUMAN	NCL	physical	19037095
DDX21_HUMAN	DDX21	physical	19037095
PKN1_HUMAN	PKN1	physical	19037095
VIME_HUMAN	VIM	physical	19037095
ACTB_HUMAN	ACTB	physical	19037095
ROA2_HUMAN	HNRNPA2B1	physical	19037095
NPM_HUMAN	NPM1	physical	19946338
BRE1A_HUMAN	RNF20	physical	19946338
CDN2A_HUMAN	CDKN2A	physical	19946338
ARF_HUMAN	CDKN2A	physical	19946338
RL18_HUMAN	RPL18	physical	19946338
RL4_HUMAN	RPL4	physical	19946338
HNRPK_HUMAN	HNRNPK	physical	19946338
NUCL_HUMAN	NCL	physical	19946338
RB_HUMAN	RB1	physical	19946338
RL15_HUMAN	RPL15	physical	19946338
TMED7_HUMAN	TMED7	physical	26186194
MYCBP_HUMAN	MYCBP	physical	26344197
ERBB3_HUMAN	ERBB3	physical	11708806
FBXW7_HUMAN	FBXW7	physical	28209614
HSP74_HUMAN	HSPA4	physical	27464702
CHIP_HUMAN	STUB1	physical	27464702
TMED7_HUMAN	TMED7	physical	28514442
ANXA5_HUMAN	ANXA5	physical	27173435
G6PI_HUMAN	GPI	physical	27173435
TRAP1_HUMAN	TRAP1	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435
SND1_HUMAN	SND1	physical	27173435
SIAS_HUMAN	NANS	physical	27173435
PLST_HUMAN	PLS3	physical	27173435
IF2P_HUMAN	EIF5B	physical	27173435
IDHP_HUMAN	IDH2	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435
RM12_HUMAN	MRPL12	physical	27173435
CRNN_HUMAN	CRNN	physical	27173435
ZN207_HUMAN	ZNF207	physical	27173435
CPNE3_HUMAN	CPNE3	physical	27173435
PYGL_HUMAN	PYGL	physical	27173435
SF3A3_HUMAN	SF3A3	physical	27173435
DNJC8_HUMAN	DNAJC8	physical	27173435
CPSF6_HUMAN	CPSF6	physical	27173435
HPRT_HUMAN	HPRT1	physical	27173435
SF3A1_HUMAN	SF3A1	physical	27173435
ECHM_HUMAN	ECHS1	physical	27173435
SRP68_HUMAN	SRP68	physical	27173435
AIMP1_HUMAN	AIMP1	physical	27173435
CBS_HUMAN	CBS	physical	27173435

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 PA2G4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-11; SER-383 ANDTHR-386, 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-361 AND THR-386, ANDMASS SPECTROMETRY.	18669648 [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 THR-386, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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 THR-386, AND MASSSPECTROMETRY.	19690332 [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 THR-386, AND MASSSPECTROMETRY.	16964243 [Abstract]

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