dbPTM

RBM34_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM34_HUMAN
UniProt AC	P42696
Protein Name	RNA-binding protein 34
Gene Name	RBM34
Organism	Homo sapiens (Human).
Sequence Length	430
Subcellular Localization	Nucleus, nucleolus .
Protein Description
Protein Sequence	MALEGMSKRKRKRSVQEGENPDDGVRGSPPEDYRLGQVASSLFRGEHHSRGGTGRLASLFSSLEPQIQPVYVPVPKQTIKKTKRNEEEESTSQIERPLSQEPAKKVKAKKKHTNAEKKLADRESALASADLEEEIHQKQGQKRKNSQPGVKVADRKILDDTEDTVVSQRKKIQINQEEERLKNERTVFVGNLPVTCNKKKLKSFFKEYGQIESVRFRSLIPAEGTLSKKLAAIKRKIHPDQKNINAYVVFKEESAATQALKRNGAQIADGFRIRVDLASETSSRDKRSVFVGNLPYKVEESAIEKHFLDCGSIMAVRIVRDKMTGIGKGFGYVLFENTDSVHLALKLNNSELMGRKLRVMRSVNKEKFKQQNSNPRLKNVSKPKQGLNFTSKTAEGHPKSLFIGEKAVLLKTKKKGQKKSGRPKKQRKQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MALEGMSKRKRKRS -CCCCCCCHHHHHCC	39.92	24425749
8	Acetylation	MALEGMSKRKRKRSV CCCCCCCHHHHHCCC	53.71	25953088
8	Ubiquitination	MALEGMSKRKRKRSV CCCCCCCHHHHHCCC	53.71	24816145
14	Phosphorylation	SKRKRKRSVQEGENP CHHHHHCCCCCCCCC	31.05	29255136
26	Methylation	ENPDDGVRGSPPEDY CCCCCCCCCCCCHHH	45.46	115490751
28	Phosphorylation	PDDGVRGSPPEDYRL CCCCCCCCCCHHHHH	27.07	29255136
33	Phosphorylation	RGSPPEDYRLGQVAS CCCCCHHHHHHHHHH	13.18	28176443
40	Phosphorylation	YRLGQVASSLFRGEH HHHHHHHHHHHCCCC	28.81	26074081
41	Phosphorylation	RLGQVASSLFRGEHH HHHHHHHHHHCCCCC	23.07	30576142
58	Phosphorylation	GGTGRLASLFSSLEP CCCHHHHHHHHCCCC	34.24	24719451
61	Phosphorylation	GRLASLFSSLEPQIQ HHHHHHHHCCCCCCC	39.03	23663014
62	Phosphorylation	RLASLFSSLEPQIQP HHHHHHHCCCCCCCC	29.44	23663014
71	Phosphorylation	EPQIQPVYVPVPKQT CCCCCCEEECCCHHH	13.01	17360941
90	Phosphorylation	KRNEEEESTSQIERP CCCHHHHCHHHCCCC	36.32	30576142
91	Phosphorylation	RNEEEESTSQIERPL CCHHHHCHHHCCCCC	28.12	25850435
92	Phosphorylation	NEEEESTSQIERPLS CHHHHCHHHCCCCCC	38.14	17525332
99	Phosphorylation	SQIERPLSQEPAKKV HHCCCCCCCCHHHHH	34.87	17525332
104	Acetylation	PLSQEPAKKVKAKKK CCCCCHHHHHHHHHH	69.67	25953088
105	Acetylation	LSQEPAKKVKAKKKH CCCCHHHHHHHHHHC	51.58	90333
107	Acetylation	QEPAKKVKAKKKHTN CCHHHHHHHHHHCCC	64.47	90337
110	Acetylation	AKKVKAKKKHTNAEK HHHHHHHHHCCCHHH	55.43	90341
124	Phosphorylation	KKLADRESALASADL HHHCHHHHHHHHCCH	29.49	30266825
128	Phosphorylation	DRESALASADLEEEI HHHHHHHHCCHHHHH	24.14	30266825
142	Ubiquitination	IHQKQGQKRKNSQPG HHHHHCHHCCCCCCC	72.64	24816145
146	Phosphorylation	QGQKRKNSQPGVKVA HCHHCCCCCCCCCHH	40.56	22798277
151	Acetylation	KNSQPGVKVADRKIL CCCCCCCCHHCCCCC	37.31	-
151	Ubiquitination	KNSQPGVKVADRKIL CCCCCCCCHHCCCCC	37.31	24816145
156	Ubiquitination	GVKVADRKILDDTED CCCHHCCCCCCCCCC	48.44	24816145
167	Phosphorylation	DTEDTVVSQRKKIQI CCCCCHHHHHHHEEC	21.67	25159151
171	Ubiquitination	TVVSQRKKIQINQEE CHHHHHHHEECCHHH	41.87	24816145
195	Phosphorylation	FVGNLPVTCNKKKLK EEECCCCCCCHHHHH	14.39	25159151
198	Acetylation	NLPVTCNKKKLKSFF CCCCCCCHHHHHHHH	54.13	26051181
203	Phosphorylation	CNKKKLKSFFKEYGQ CCHHHHHHHHHHHCC	46.48	-
218	Phosphorylation	IESVRFRSLIPAEGT EEEEEEHHCCCCCCC	28.12	-
225	Phosphorylation	SLIPAEGTLSKKLAA HCCCCCCCHHHHHHH	21.26	28555341
227	Phosphorylation	IPAEGTLSKKLAAIK CCCCCCHHHHHHHHH	27.81	20860994
228	Ubiquitination	PAEGTLSKKLAAIKR CCCCCHHHHHHHHHH	55.72	29967540
229	Ubiquitination	AEGTLSKKLAAIKRK CCCCHHHHHHHHHHH	39.73	-
242	Sumoylation	RKIHPDQKNINAYVV HHCCCCCCCCCEEEE	68.15	28112733
247	Phosphorylation	DQKNINAYVVFKEES CCCCCCEEEEECHHH	7.83	18083107
251	Sumoylation	INAYVVFKEESAATQ CCEEEEECHHHHHHH	49.30	-
254	Phosphorylation	YVVFKEESAATQALK EEEECHHHHHHHHHH	25.05	20068231
257	Phosphorylation	FKEESAATQALKRNG ECHHHHHHHHHHHCC	17.68	20068231
261	2-Hydroxyisobutyrylation	SAATQALKRNGAQIA HHHHHHHHHCCCCCC	47.00	-
261	Ubiquitination	SAATQALKRNGAQIA HHHHHHHHHCCCCCC	47.00	29967540
288	Phosphorylation	TSSRDKRSVFVGNLP CCCCCCCEEEECCCC	26.16	28112733
296	Phosphorylation	VFVGNLPYKVEESAI EEECCCCCCCCHHHH	30.72	22461510
297	Ubiquitination	FVGNLPYKVEESAIE EECCCCCCCCHHHHH	41.03	29967540
297	Acetylation	FVGNLPYKVEESAIE EECCCCCCCCHHHHH	41.03	26051181
322	Acetylation	AVRIVRDKMTGIGKG EEEEEHHHCCCCCCC	28.00	25953088
349	Ubiquitination	HLALKLNNSELMGRK EEEEEECCHHHHCHH	47.50	24816145
353	Sulfoxidation	KLNNSELMGRKLRVM EECCHHHHCHHHHHH	4.24	21406390
368	Ubiquitination	RSVNKEKFKQQNSNP HHHCHHHHHHCCCCC	10.15	24816145
369	Ubiquitination	SVNKEKFKQQNSNPR HHCHHHHHHCCCCCC	63.14	24816145
373	Phosphorylation	EKFKQQNSNPRLKNV HHHHHCCCCCCCCCC	43.82	26434552
383	Ubiquitination	RLKNVSKPKQGLNFT CCCCCCCCCCCCCCC	27.05	29967540
384	Ubiquitination	LKNVSKPKQGLNFTS CCCCCCCCCCCCCCC	61.81	29967540
391	Ubiquitination	KQGLNFTSKTAEGHP CCCCCCCCCCCCCCC	24.70	29967540
392	Ubiquitination	QGLNFTSKTAEGHPK CCCCCCCCCCCCCCC	49.01	29967540
398	Ubiquitination	SKTAEGHPKSLFIGE CCCCCCCCCEEEEEC	38.49	29967540
399	Ubiquitination	KTAEGHPKSLFIGEK CCCCCCCCEEEEECE	54.86	29967540
406	Acetylation	KSLFIGEKAVLLKTK CEEEEECEEEEEECC	38.28	26051181

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 RBM34_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBM34_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 RBM34_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LN28A_HUMAN	LIN28A	physical	24778252
POP1_HUMAN	POP1	physical	24778252
PRKRA_HUMAN	PRKRA	physical	24778252
THOC4_HUMAN	ALYREF	physical	26344197
PWP1_HUMAN	PWP1	physical	26344197
RBBP6_HUMAN	RBBP6	physical	26344197
H2B2F_HUMAN	HIST2H2BF	physical	28514442
CENPI_HUMAN	CENPI	physical	28514442
CENPC_HUMAN	CENPC	physical	28514442
RL36L_HUMAN	RPL36AL	physical	28514442
SDA1_HUMAN	SDAD1	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
TAF1D_HUMAN	TAF1D	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
SPT2_HUMAN	SPTY2D1	physical	28514442
SRP68_HUMAN	SRP68	physical	28514442
TAF1A_HUMAN	TAF1A	physical	28514442
ZFP62_HUMAN	ZFP62	physical	28514442
STAU1_HUMAN	STAU1	physical	28514442
CC137_HUMAN	CCDC137	physical	28514442
CEBPZ_HUMAN	CEBPZ	physical	28514442
DDX31_HUMAN	DDX31	physical	28514442
CENPU_HUMAN	CENPU	physical	28514442
DDX54_HUMAN	DDX54	physical	28514442
DDX27_HUMAN	DDX27	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
URB2_HUMAN	URB2	physical	28514442
DDX10_HUMAN	DDX10	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
REXO4_HUMAN	REXO4	physical	28514442
ZNF48_HUMAN	ZNF48	physical	28514442
KNOP1_HUMAN	KNOP1	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
MBB1A_HUMAN	MYBBP1A	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
NOC3L_HUMAN	NOC3L	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
RLA0_HUMAN	RPLP0	physical	28514442
DDX51_HUMAN	DDX51	physical	28514442
RL32_HUMAN	RPL32	physical	28514442
ZN777_HUMAN	ZNF777	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
TTF1_HUMAN	TTF1	physical	28514442
RSBNL_HUMAN	RSBN1L	physical	28514442
DDX21_HUMAN	DDX21	physical	28514442
NOC2L_HUMAN	NOC2L	physical	28514442
NVL_HUMAN	NVL	physical	28514442
RS13_HUMAN	RPS13	physical	28514442
IMP4_HUMAN	IMP4	physical	28514442
PK1IP_HUMAN	PAK1IP1	physical	28514442
PRP4B_HUMAN	PRPF4B	physical	28514442
RL15_HUMAN	RPL15	physical	28514442
SRRM1_HUMAN	SRRM1	physical	28514442
PRKRA_HUMAN	PRKRA	physical	28514442
NPA1P_HUMAN	URB1	physical	28514442
RLA2_HUMAN	RPLP2	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
DDX50_HUMAN	DDX50	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
NOP53_HUMAN	GLTSCR2	physical	28514442
RL35A_HUMAN	RPL35A	physical	28514442
DDX56_HUMAN	DDX56	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
DHX30_HUMAN	DHX30	physical	28514442
ZSC25_HUMAN	ZSCAN25	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
ZN512_HUMAN	ZNF512	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
NOP10_HUMAN	NOP10	physical	28514442
RL7L_HUMAN	RPL7L1	physical	28514442
GLYR1_HUMAN	GLYR1	physical	28514442
RL13A_HUMAN	RPL13A	physical	28514442
RBM4_HUMAN	RBM4	physical	28514442
TAF1C_HUMAN	TAF1C	physical	28514442
ZN768_HUMAN	ZNF768	physical	28514442

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 RBM34_HUMAN

Related Literatures of Post-Translational Modification

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-14 AND SER-28, 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-14 AND SER-28, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.	19007248 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-99, AND MASSSPECTROMETRY.	17525332 [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-14, AND MASSSPECTROMETRY.	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-14 AND SER-28, AND MASSSPECTROMETRY.	17081983 [Abstract]