dbPTM

ZRAB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZRAB2_HUMAN
UniProt AC	O95218
Protein Name	Zinc finger Ran-binding domain-containing protein 2
Gene Name	ZRANB2
Organism	Homo sapiens (Human).
Sequence Length	330
Subcellular Localization	Nucleus .
Protein Description	Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice site selection..
Protein Sequence	MSTKNFRVSDGDWICPDKKCGNVNFARRTSCNRCGREKTTEAKMMKAGGTEIGKTLAEKSRGLFSANDWQCKTCSNVNWARRSECNMCNTPKYAKLEERTGYGGGFNERENVEYIEREESDGEYDEFGRKKKKYRGKAVGPASILKEVEDKESEGEEEDEDEDLSKYKLDEDEDEDDADLSKYNLDASEEEDSNKKKSNRRSRSKSRSSHSRSSSRSSSPSSSRSRSRSRSRSSSSSQSRSRSSSRERSRSRGSKSRSSSRSHRGSSSPRKRSYSSSSSSPERNRKRSRSRSSSSGDRKKRRTRSRSPERRHRSSSGSSHSGSRSSSKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSTKNFRVS ------CCCCCEECC	48.35	23403867
3	Phosphorylation	-----MSTKNFRVSD -----CCCCCEECCC	28.80	23403867
9	Phosphorylation	STKNFRVSDGDWICP CCCCEECCCCCEECC	31.45	25159151
9 (in isoform 2)	Phosphorylation	-	31.45	18669648
18	Acetylation	GDWICPDKKCGNVNF CCEECCCCCCCCCEE	34.80	25953088
18	2-Hydroxyisobutyrylation	GDWICPDKKCGNVNF CCEECCCCCCCCCEE	34.80	-
19	Acetylation	DWICPDKKCGNVNFA CEECCCCCCCCCEEC	55.55	27452117
40	Phosphorylation	RCGREKTTEAKMMKA CCCCCCCHHHHHHHC	45.04	21601212
43	Acetylation	REKTTEAKMMKAGGT CCCCHHHHHHHCCCC	33.04	25953088
46	Ubiquitination	TTEAKMMKAGGTEIG CHHHHHHHCCCCHHH	40.14	24816145
46	Acetylation	TTEAKMMKAGGTEIG CHHHHHHHCCCCHHH	40.14	25953088
50	Phosphorylation	KMMKAGGTEIGKTLA HHHHCCCCHHHHHHH	24.42	-
54	Acetylation	AGGTEIGKTLAEKSR CCCCHHHHHHHHHHC	46.13	19608861
54	Ubiquitination	AGGTEIGKTLAEKSR CCCCHHHHHHHHHHC	46.13	33845483
55	Phosphorylation	GGTEIGKTLAEKSRG CCCHHHHHHHHHHCC	26.45	21601212
59	Acetylation	IGKTLAEKSRGLFSA HHHHHHHHHCCCCCC	39.59	23749302
59	Ubiquitination	IGKTLAEKSRGLFSA HHHHHHHHHCCCCCC	39.59	33845483
59	2-Hydroxyisobutyrylation	IGKTLAEKSRGLFSA HHHHHHHHHCCCCCC	39.59	-
60	Phosphorylation	GKTLAEKSRGLFSAN HHHHHHHHCCCCCCC	24.08	28555341
61	Methylation	KTLAEKSRGLFSAND HHHHHHHCCCCCCCC	57.83	115920429
65	Phosphorylation	EKSRGLFSANDWQCK HHHCCCCCCCCCCCC	31.07	27251789
72	Ubiquitination	SANDWQCKTCSNVNW CCCCCCCCCCCCCCC	37.15	32015554
83	Phosphorylation	NVNWARRSECNMCNT CCCCHHHHHCCCCCC	40.73	23401153
87	Sulfoxidation	ARRSECNMCNTPKYA HHHHHCCCCCCHHCC	2.56	30846556
90	Phosphorylation	SECNMCNTPKYAKLE HHCCCCCCHHCCCHH	19.07	25159151
92	Acetylation	CNMCNTPKYAKLEER CCCCCCHHCCCHHHH	56.66	25953088
93	Phosphorylation	NMCNTPKYAKLEERT CCCCCHHCCCHHHHC	15.35	-
95	Sumoylation	CNTPKYAKLEERTGY CCCHHCCCHHHHCCC	54.03	-
95	Sumoylation	CNTPKYAKLEERTGY CCCHHCCCHHHHCCC	54.03	-
95	Ubiquitination	CNTPKYAKLEERTGY CCCHHCCCHHHHCCC	54.03	24816145
95	Acetylation	CNTPKYAKLEERTGY CCCHHCCCHHHHCCC	54.03	25953088
100	Phosphorylation	YAKLEERTGYGGGFN CCCHHHHCCCCCCCC	37.73	26074081
102	Phosphorylation	KLEERTGYGGGFNER CHHHHCCCCCCCCCH	16.40	26074081
114	Phosphorylation	NERENVEYIEREESD CCHHCCEEEECCCCC	12.09	23927012
114 (in isoform 2)	Phosphorylation	-	12.09	18669648
120	Phosphorylation	EYIEREESDGEYDEF EEEECCCCCCCCCCC	46.27	19664994
120 (in isoform 2)	Phosphorylation	-	46.27	18669648
124	Phosphorylation	REESDGEYDEFGRKK CCCCCCCCCCCCCCC	26.71	23927012
137	Methylation	KKKKYRGKAVGPASI CCCCCCCCCCCCHHH	30.79	115978261
137	Ubiquitination	KKKKYRGKAVGPASI CCCCCCCCCCCCHHH	30.79	32142685
143	Phosphorylation	GKAVGPASILKEVED CCCCCCHHHHHHHHC	31.42	25159151
153	Phosphorylation	KEVEDKESEGEEEDE HHHHCCCCCCCCCCC	57.55	29255136
153 (in isoform 2)	Phosphorylation	-	57.55	18669648
165	Phosphorylation	EDEDEDLSKYKLDED CCCCCCHHHHCCCCC	46.38	23927012
167	Phosphorylation	EDEDLSKYKLDEDED CCCCHHHHCCCCCCC	17.26	30576142
168	Ubiquitination	DEDLSKYKLDEDEDE CCCHHHHCCCCCCCC	53.88	29967540
181	Phosphorylation	DEDDADLSKYNLDAS CCCCCCHHHHCCCCC	33.37	25159151
181 (in isoform 2)	Phosphorylation	-	33.37	18669648
182	Ubiquitination	EDDADLSKYNLDASE CCCCCHHHHCCCCCH	45.51	29967540
183	Phosphorylation	DDADLSKYNLDASEE CCCCHHHHCCCCCHH	19.99	23927012
183 (in isoform 2)	Phosphorylation	-	19.99	18669648
188	Phosphorylation	SKYNLDASEEEDSNK HHHCCCCCHHHHHHH	45.25	19664994
188 (in isoform 2)	Phosphorylation	-	45.25	18669648
193	Phosphorylation	DASEEEDSNKKKSNR CCCHHHHHHHHHHCH	54.55	22167270
195	Acetylation	SEEEDSNKKKSNRRS CHHHHHHHHHHCHHH	66.58	26051181
196	Acetylation	EEEDSNKKKSNRRSR HHHHHHHHHHCHHHH	66.73	25953088
202	Phosphorylation	KKKSNRRSRSKSRSS HHHHCHHHHHHHHHC	37.35	24505115
206	Phosphorylation	NRRSRSKSRSSHSRS CHHHHHHHHHCCCCC	38.35	-
208	Phosphorylation	RSRSKSRSSHSRSSS HHHHHHHHCCCCCCC	39.22	24505115
209	Phosphorylation	SRSKSRSSHSRSSSR HHHHHHHCCCCCCCC	25.11	24505115
213	Phosphorylation	SRSSHSRSSSRSSSP HHHCCCCCCCCCCCC	35.36	20044836
217	Phosphorylation	HSRSSSRSSSPSSSR CCCCCCCCCCCCHHH	36.80	20044836
218	Phosphorylation	SRSSSRSSSPSSSRS CCCCCCCCCCCHHHH	45.20	20044836
221	Phosphorylation	SSRSSSPSSSRSRSR CCCCCCCCHHHHHHH	42.78	26074081
222	Phosphorylation	SRSSSPSSSRSRSRS CCCCCCCHHHHHHHH	32.91	26074081
223	Phosphorylation	RSSSPSSSRSRSRSR CCCCCCHHHHHHHHC	38.32	26074081
225	Phosphorylation	SSPSSSRSRSRSRSR CCCCHHHHHHHHCCC	36.23	26074081
227	Phosphorylation	PSSSRSRSRSRSRSS CCHHHHHHHHCCCCC	35.54	26074081
229	Phosphorylation	SSRSRSRSRSRSSSS HHHHHHHHCCCCCCC	35.54	26074081
231	Phosphorylation	RSRSRSRSRSSSSSQ HHHHHHCCCCCCCHH	37.45	26074081
241	Phosphorylation	SSSSQSRSRSSSRER CCCHHHHHHHHHHHH	41.58	29396449
243	Phosphorylation	SSQSRSRSSSRERSR CHHHHHHHHHHHHHH	33.63	29396449
245	Phosphorylation	QSRSRSSSRERSRSR HHHHHHHHHHHHHHC	39.13	19651622
249	Phosphorylation	RSSSRERSRSRGSKS HHHHHHHHHHCCCCC	29.83	19651622
256	Phosphorylation	SRSRGSKSRSSSRSH HHHCCCCCCCCCCCC	38.81	21601212
262	Phosphorylation	KSRSSSRSHRGSSSP CCCCCCCCCCCCCCC	21.34	24144214
266	Phosphorylation	SSRSHRGSSSPRKRS CCCCCCCCCCCCCCC	27.83	24144214
267	Phosphorylation	SRSHRGSSSPRKRSY CCCCCCCCCCCCCCC	47.38	24144214
268	Phosphorylation	RSHRGSSSPRKRSYS CCCCCCCCCCCCCCC	30.35	24144214
273	Phosphorylation	SSSPRKRSYSSSSSS CCCCCCCCCCCCCCC	32.19	28450419
274	Phosphorylation	SSPRKRSYSSSSSSP CCCCCCCCCCCCCCH	19.32	30576142
275	Phosphorylation	SPRKRSYSSSSSSPE CCCCCCCCCCCCCHH	25.62	25159151
276	Phosphorylation	PRKRSYSSSSSSPER CCCCCCCCCCCCHHH	26.46	28176443
277	Phosphorylation	RKRSYSSSSSSPERN CCCCCCCCCCCHHHH	28.44	28176443
278	Phosphorylation	KRSYSSSSSSPERNR CCCCCCCCCCHHHHH	36.46	25159151
279	Phosphorylation	RSYSSSSSSPERNRK CCCCCCCCCHHHHHH	52.43	25159151
280	Phosphorylation	SYSSSSSSPERNRKR CCCCCCCCHHHHHHH	32.50	23401153
288	Phosphorylation	PERNRKRSRSRSSSS HHHHHHHHHHCCCCC	37.33	-
290	Phosphorylation	RNRKRSRSRSSSSGD HHHHHHHHCCCCCHH	37.45	-
303	Phosphorylation	GDRKKRRTRSRSPER HHHHHHHHCCCCHHH	36.71	23663014
303 (in isoform 2)	Phosphorylation	-	36.71	30266825
305	Phosphorylation	RKKRRTRSRSPERRH HHHHHHCCCCHHHHH	36.18	19664994
305 (in isoform 2)	Phosphorylation	-	36.18	19664994
307	Phosphorylation	KRRTRSRSPERRHRS HHHHCCCCHHHHHCC	32.15	19664994
307 (in isoform 2)	Phosphorylation	-	32.15	19664994
310 (in isoform 2)	Phosphorylation	-	42.99	22167270
314	Phosphorylation	SPERRHRSSSGSSHS CHHHHHCCCCCCCCC	23.80	28634120
315	Phosphorylation	PERRHRSSSGSSHSG HHHHHCCCCCCCCCC	38.38	28634120
316	Phosphorylation	ERRHRSSSGSSHSGS HHHHCCCCCCCCCCC	43.89	30278072
317 (in isoform 2)	Phosphorylation	-	34.81	22167270
318	Phosphorylation	RHRSSSGSSHSGSRS HHCCCCCCCCCCCCC	27.16	22496350
319	Phosphorylation	HRSSSGSSHSGSRSS HCCCCCCCCCCCCCC	25.79	23090842
321	Phosphorylation	SSSGSSHSGSRSSSK CCCCCCCCCCCCCCC	40.17	23090842
323	Phosphorylation	SGSSHSGSRSSSKKK CCCCCCCCCCCCCCC	31.81	23090842
325	Phosphorylation	SSHSGSRSSSKKK-- CCCCCCCCCCCCC--	40.43	23090842
326	Phosphorylation	SHSGSRSSSKKK--- CCCCCCCCCCCC---	45.10	28985074
327	Phosphorylation	HSGSRSSSKKK---- CCCCCCCCCCC----	50.14	23090842

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 ZRAB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
310	S	Phosphorylation		17525332
Isoform 2 is phosphorylated on Ser-310 upon DNA damage, probably by ATM or ATR.

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 ZRAB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
U2AF1_HUMAN	U2AF1	physical	11448987
RU17_HUMAN	SNRNP70	physical	11448987
TRA2B_HUMAN	TRA2B	physical	11448987
COR1B_HUMAN	CORO1B	physical	22863883
PARVA_HUMAN	PARVA	physical	22863883
SWP70_HUMAN	SWAP70	physical	22863883
TBC17_HUMAN	TBC1D17	physical	22863883
TOP1_HUMAN	TOP1	physical	26186194
PRP4B_HUMAN	PRPF4B	physical	26186194
LC7L2_HUMAN	LUC7L2	physical	26186194
LUC7L_HUMAN	LUC7L	physical	26186194
IMA6_HUMAN	KPNA5	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
RSBNL_HUMAN	RSBN1L	physical	26186194
RSBN1_HUMAN	RSBN1	physical	26186194
LC7L3_HUMAN	LUC7L3	physical	26186194
VANG1_HUMAN	VANGL1	physical	26186194
PI42C_HUMAN	PIP4K2C	physical	26186194
PI42B_HUMAN	PIP4K2B	physical	26186194
PI42A_HUMAN	PIP4K2A	physical	26186194
SRS11_HUMAN	SRSF11	physical	26186194
PLD1_HUMAN	PLD1	physical	26186194
SREK1_HUMAN	SREK1	physical	26186194
ACL6A_HUMAN	ACTL6A	physical	26186194
IKBL1_HUMAN	NFKBIL1	physical	26186194
PI42A_HUMAN	PIP4K2A	physical	28514442
IKBL1_HUMAN	NFKBIL1	physical	28514442
LC7L2_HUMAN	LUC7L2	physical	28514442
PI42B_HUMAN	PIP4K2B	physical	28514442
SREK1_HUMAN	SREK1	physical	28514442
PI42C_HUMAN	PIP4K2C	physical	28514442
PLD1_HUMAN	PLD1	physical	28514442
TOP1_HUMAN	TOP1	physical	28514442
LUC7L_HUMAN	LUC7L	physical	28514442
RSBN1_HUMAN	RSBN1	physical	28514442
RSBNL_HUMAN	RSBN1L	physical	28514442
U2AF2_HUMAN	U2AF2	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
ACL6A_HUMAN	ACTL6A	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 ZRAB2_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-54, 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-120; SER-153; SER-188;SER-305 AND SER-307, AND MASS SPECTROMETRY.	19690332 [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-188 AND SER-193, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-153, ANDMASS SPECTROMETRY.	18318008 [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-9; SER-120; SER-181;SER-188; THR-303; SER-153; SER-305 AND SER-307, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-310 (ISOFORM 2), AND MASS SPECTROMETRY.	18669648 [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-120, 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-120, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.	18187866 [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-120, 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-305 AND SER-307,PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 (ISOFORM 2), ANDMASS SPECTROMETRY.	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-181 AND SER-188, ANDMASS 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-120; SER-153; SER-181;SER-188; SER-193; THR-303; SER-305 AND SER-307, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.	15302935 [Abstract]

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