dbPTM

WRIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	WRIP1_HUMAN
UniProt AC	Q96S55
Protein Name	ATPase WRNIP1
Gene Name	WRNIP1 {ECO:0000312\|HGNC:HGNC:20876}
Organism	Homo sapiens (Human).
Sequence Length	665
Subcellular Localization	Nucleus . Cytoplasm . Colocalizes with WRN in granular structures in the nucleus.
Protein Description	Functions as a modulator of initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. In the presence of ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is decreased. Plays also a role in the innate immune defense against viruses. Stabilizes the RIG-I/DDX58 dsRNA interaction and promotes RIG-I/DDX58 'Lys-63'-linked polyubiquitination. In turn, RIG-I/DDX58 transmits the signal through mitochondrial MAVS..
Protein Sequence	MEVSGPEDDPFLSQLHQVQCPVCQQMMPAAHINSHLDRCLLLHPAGHAEPAAGSHRAGERAKGPSPPGAKRRRLSESSALKQPATPTAAESSEGEGEEGDDGGETESRESYDAPPTPSGARLIPDFPVARSSSPGRKGSGKRPAAAAAAGSASPRSWDEAEAQEEEEAVGDGDGDGDADADGEDDPGHWDADAAEAATAFGASGGGRPHPRALAAEEIRQMLQGKPLADTMRPDTLQDYFGQSKAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIASNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFFKRKTILFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEAMVTILMRAINSLGIHVLDSSRPTDPLSHSSNSSSEPAMFIEDKAVDTLAYLSDGDARAGLNGLQLAVLARLSSRKMFCKKSGQSYSPSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFASEDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRNHQGPLPPVPLHLRNAPTRLMKDLGYGKGYKYNPMYSEPVDQEYLPEELRGVDFFKQRRC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MEVSGPEDDPF ----CCCCCCCCCHH	35.01	28348404
54	Phosphorylation	HAEPAAGSHRAGERA CCCCCCCCCCCHHHC	12.69	28348404
62	Ubiquitination	HRAGERAKGPSPPGA CCCHHHCCCCCCCCH	77.04	27667366
65	Phosphorylation	GERAKGPSPPGAKRR HHHCCCCCCCCHHHH	53.01	25159151
66 (in isoform 3)	Ubiquitination	-	34.18	21890473
70	Acetylation	GPSPPGAKRRRLSES CCCCCCHHHHCCCCC	52.96	25953088
70	Ubiquitination	GPSPPGAKRRRLSES CCCCCCHHHHCCCCC	52.96	21906983
70 (in isoform 1)	Ubiquitination	-	52.96	21890473
70 (in isoform 2)	Ubiquitination	-	52.96	21890473
75	Phosphorylation	GAKRRRLSESSALKQ CHHHHCCCCCCCCCC	33.35	29255136
77	Phosphorylation	KRRRLSESSALKQPA HHHCCCCCCCCCCCC	19.96	29255136
78	Phosphorylation	RRRLSESSALKQPAT HHCCCCCCCCCCCCC	33.30	29255136
81	Sumoylation	LSESSALKQPATPTA CCCCCCCCCCCCCCC	54.69	-
81	Ubiquitination	LSESSALKQPATPTA CCCCCCCCCCCCCCC	54.69	17550899
81 (in isoform 3)	Ubiquitination	-	54.69	21890473
85	Phosphorylation	SALKQPATPTAAESS CCCCCCCCCCCCCCC	28.05	27273156
87	Phosphorylation	LKQPATPTAAESSEG CCCCCCCCCCCCCCC	33.86	23927012
90 (in isoform 3)	Ubiquitination	-	52.94	21890473
91	Phosphorylation	ATPTAAESSEGEGEE CCCCCCCCCCCCCCC	29.03	23401153
92	Phosphorylation	TPTAAESSEGEGEEG CCCCCCCCCCCCCCC	40.92	27273156
96 (in isoform 3)	Ubiquitination	-	49.46	21890473
98 (in isoform 4)	Ubiquitination	-	77.95	21890473
105	Phosphorylation	EGDDGGETESRESYD CCCCCCCCCCCCCCC	42.40	28450419
107	Phosphorylation	DDGGETESRESYDAP CCCCCCCCCCCCCCC	49.09	28450419
110	Phosphorylation	GETESRESYDAPPTP CCCCCCCCCCCCCCC	27.48	29255136
111	Phosphorylation	ETESRESYDAPPTPS CCCCCCCCCCCCCCC	16.03	29255136
116	Phosphorylation	ESYDAPPTPSGARLI CCCCCCCCCCCCCCC	29.09	29255136
118	Phosphorylation	YDAPPTPSGARLIPD CCCCCCCCCCCCCCC	47.79	30266825
124 (in isoform 4)	Ubiquitination	-	41.61	21890473
131	Phosphorylation	PDFPVARSSSPGRKG CCCCCCCCCCCCCCC	25.98	22199227
132	Phosphorylation	DFPVARSSSPGRKGS CCCCCCCCCCCCCCC	34.69	22199227
133	Phosphorylation	FPVARSSSPGRKGSG CCCCCCCCCCCCCCC	32.40	22199227
137	Ubiquitination	RSSSPGRKGSGKRPA CCCCCCCCCCCCCCH	64.44	22817900
139	Phosphorylation	SSPGRKGSGKRPAAA CCCCCCCCCCCCHHH	44.14	23403867
141	Acetylation	PGRKGSGKRPAAAAA CCCCCCCCCCHHHHH	57.83	25953088
141	Ubiquitination	PGRKGSGKRPAAAAA CCCCCCCCCCHHHHH	57.83	17550899
151	Phosphorylation	AAAAAAGSASPRSWD HHHHHCCCCCCCCCC	22.35	29255136
153	Phosphorylation	AAAAGSASPRSWDEA HHHCCCCCCCCCCHH	23.65	29255136
156	Phosphorylation	AGSASPRSWDEAEAQ CCCCCCCCCCHHHHH	42.11	28348404
203	Phosphorylation	AATAFGASGGGRPHP HHHHHCCCCCCCCCH	38.05	24275569
217 (in isoform 4)	Ubiquitination	-	38.45	21890473
225	Ubiquitination	IRQMLQGKPLADTMR HHHHHCCCCCHHHCC	24.73	21890473
225	Ubiquitination	IRQMLQGKPLADTMR HHHHHCCCCCHHHCC	24.73	23000965
225 (in isoform 1)	Ubiquitination	-	24.73	21890473
225 (in isoform 2)	Ubiquitination	-	24.73	21890473
239	Phosphorylation	RPDTLQDYFGQSKAV CCCHHHHHHCCCCCC	9.17	-
243 (in isoform 4)	Ubiquitination	-	23.98	21890473
244	Ubiquitination	QDYFGQSKAVGQDTL HHHHCCCCCCCHHHH	38.92	21963094
244 (in isoform 2)	Ubiquitination	-	38.92	-
249 (in isoform 4)	Ubiquitination	-	33.13	21890473
250	Phosphorylation	SKAVGQDTLLRSLLE CCCCCHHHHHHHHHH	21.58	27067055
252 (in isoform 4)	Ubiquitination	-	3.67	21890473
262 (in isoform 3)	Ubiquitination	-	19.53	21890473
272	Glutathionylation	ILWGPPGCGKTTLAH EEECCCCCCHHHHHH	6.61	22555962
277 (in isoform 4)	Ubiquitination	-	3.85	21890473
286	Ubiquitination	HIIASNSKKHSIRFV HHHHCCCCCCEEEEE	59.77	21890473
286	Neddylation	HIIASNSKKHSIRFV HHHHCCCCCCEEEEE	59.77	32015554
286	Ubiquitination	HIIASNSKKHSIRFV HHHHCCCCCCEEEEE	59.77	21906983
286 (in isoform 1)	Ubiquitination	-	59.77	21890473
286 (in isoform 2)	Ubiquitination	-	59.77	21890473
287	Ubiquitination	IIASNSKKHSIRFVT HHHCCCCCCEEEEEE	42.26	22817900
288 (in isoform 3)	Ubiquitination	-	31.99	21890473
301	Ubiquitination	TLSATNAKTNDVRDV EEECCCCCCCCHHHH	50.35	21890473
301	2-Hydroxyisobutyrylation	TLSATNAKTNDVRDV EEECCCCCCCCHHHH	50.35	-
301	Ubiquitination	TLSATNAKTNDVRDV EEECCCCCCCCHHHH	50.35	27667366
301 (in isoform 1)	Ubiquitination	-	50.35	21890473
301 (in isoform 2)	Ubiquitination	-	50.35	21890473
310	Ubiquitination	NDVRDVIKQAQNEKS CCHHHHHHHHHCHHC	39.15	21890473
310	Neddylation	NDVRDVIKQAQNEKS CCHHHHHHHHHCHHC	39.15	32015554
310	Ubiquitination	NDVRDVIKQAQNEKS CCHHHHHHHHHCHHC	39.15	27667366
310 (in isoform 1)	Ubiquitination	-	39.15	21890473
310 (in isoform 2)	Ubiquitination	-	39.15	21890473
316	Ubiquitination	IKQAQNEKSFFKRKT HHHHHCHHCHHHHHE	61.18	21890473
316	Acetylation	IKQAQNEKSFFKRKT HHHHHCHHCHHHHHE	61.18	25953088
316	Ubiquitination	IKQAQNEKSFFKRKT HHHHHCHHCHHHHHE	61.18	27667366
316 (in isoform 1)	Ubiquitination	-	61.18	21890473
316 (in isoform 2)	Ubiquitination	-	61.18	21890473
320	Ubiquitination	QNEKSFFKRKTILFI HCHHCHHHHHEEEEH	51.48	22817900
322	Ubiquitination	EKSFFKRKTILFIDE HHCHHHHHEEEEHHH	40.27	17550899
335	Ubiquitination	DEIHRFNKSQQDTFL HHHHHCCHHHCCCCC	47.10	17550899
336 (in isoform 2)	Phosphorylation	-	33.89	21406692
345 (in isoform 2)	Phosphorylation	-	6.51	21406692
370	Phosphorylation	QVNAALLSRCRVIVL HHHHHHHHCCEEEEE	30.13	-
381 (in isoform 3)	Ubiquitination	-	32.73	21890473
387	Phosphorylation	LPVEAMVTILMRAIN CCHHHHHHHHHHHHH	8.70	24043423
395	Phosphorylation	ILMRAINSLGIHVLD HHHHHHHHCCCEECC	23.12	24043423
403	Phosphorylation	LGIHVLDSSRPTDPL CCCEECCCCCCCCCC	24.88	24043423
404	Phosphorylation	GIHVLDSSRPTDPLS CCEECCCCCCCCCCC	41.78	24043423
407 (in isoform 3)	Ubiquitination	-	49.49	21890473
413	Phosphorylation	PTDPLSHSSNSSSEP CCCCCCCCCCCCCCC	28.04	24247654
413 (in isoform 3)	Ubiquitination	-	28.04	21890473
416 (in isoform 3)	Ubiquitination	-	36.87	21890473
434	Phosphorylation	KAVDTLAYLSDGDAR CHHHEEECCCCCCHH	15.17	29449344
436	Phosphorylation	VDTLAYLSDGDARAG HHEEECCCCCCHHCC	27.20	29449344
439	Ubiquitination	LAYLSDGDARAGLNG EECCCCCCHHCCCCH	37.56	22505724
441 (in isoform 3)	Ubiquitination	-	33.65	21890473
457	Ubiquitination	AVLARLSSRKMFCKK HHHHHHHCCCCCCCC	40.28	21890473
457	Ubiquitination	AVLARLSSRKMFCKK HHHHHHHCCCCCCCC	40.28	23000965
457 (in isoform 2)	Ubiquitination	-	40.28	21890473
464	Ubiquitination	SRKMFCKKSGQSYSP CCCCCCCCCCCCCCC	62.08	22505724
465	Phosphorylation	RKMFCKKSGQSYSPS CCCCCCCCCCCCCCC	27.79	29396449
468	Phosphorylation	FCKKSGQSYSPSRVL CCCCCCCCCCCCCEE	30.97	25159151
469	Phosphorylation	CKKSGQSYSPSRVLI CCCCCCCCCCCCEEE	19.40	29396449
470	Phosphorylation	KKSGQSYSPSRVLIT CCCCCCCCCCCEEEE	22.96	21815630
472	Phosphorylation	SGQSYSPSRVLITEN CCCCCCCCCEEEECC	29.13	28985074
477	Phosphorylation	SPSRVLITENDVKEG CCCCEEEECCHHHHH	25.28	26074081
482	Sumoylation	LITENDVKEGLQRSH EEECCHHHHHHHHHC	49.26	-
482	Sumoylation	LITENDVKEGLQRSH EEECCHHHHHHHHHC	49.26	28112733
482	Ubiquitination	LITENDVKEGLQRSH EEECCHHHHHHHHHC	49.26	23000965
482 (in isoform 1)	Ubiquitination	-	49.26	21890473
483	Ubiquitination	ITENDVKEGLQRSHI EECCHHHHHHHHHCC	66.05	21890473
483	Ubiquitination	ITENDVKEGLQRSHI EECCHHHHHHHHHCC	66.05	23000965
483 (in isoform 2)	Ubiquitination	-	66.05	21890473
500	Phosphorylation	DRAGEEHYNCISALH CCCCHHHHHHHHHHH	18.27	25884760
504	Phosphorylation	EEHYNCISALHKSMR HHHHHHHHHHHHHHC	27.29	28152594
508	Ubiquitination	NCISALHKSMRGSDQ HHHHHHHHHHCCCCH	46.96	23000965
508 (in isoform 1)	Ubiquitination	-	46.96	21890473
511	Methylation	SALHKSMRGSDQNAS HHHHHHHCCCCHHHH	48.86	115920089
534	Phosphorylation	EGGEDPLYVARRLVR HCCCCHHHHHHHHHH	9.46	20090780
562	Phosphorylation	LTQAVAAYQGCHFIG HHHHHHHHCCCCCCC	8.83	22817900
576	Ubiquitination	GMPECEVLLAQCVVY CCCHHHHHHHHHHHH	1.21	21890473
576	Ubiquitination	GMPECEVLLAQCVVY CCCHHHHHHHHHHHH	1.21	23000965
576 (in isoform 2)	Ubiquitination	-	1.21	21890473
594	Phosphorylation	APKSIEVYSAYNNVK CCCCEEHHHHHCCHH	3.77	28152594
595	Phosphorylation	PKSIEVYSAYNNVKA CCCEEHHHHHCCHHH	29.47	28152594
597	Phosphorylation	SIEVYSAYNNVKACL CEEHHHHHCCHHHHH	11.00	28152594
601	Ubiquitination	YSAYNNVKACLRNHQ HHHHCCHHHHHHHCC	35.19	23000965
601 (in isoform 1)	Ubiquitination	-	35.19	21890473
602	Ubiquitination	SAYNNVKACLRNHQG HHHCCHHHHHHHCCC	8.03	21890473
602	Ubiquitination	SAYNNVKACLRNHQG HHHCCHHHHHHHCCC	8.03	23000965
602 (in isoform 2)	Ubiquitination	-	8.03	21890473
608	Ubiquitination	KACLRNHQGPLPPVP HHHHHHCCCCCCCCC	59.76	21890473
608	Acetylation	KACLRNHQGPLPPVP HHHHHHCCCCCCCCC	59.76	19608861
608	Ubiquitination	KACLRNHQGPLPPVP HHHHHHCCCCCCCCC	59.76	23000965
608 (in isoform 2)	Ubiquitination	-	59.76	21890473
611	Ubiquitination	LRNHQGPLPPVPLHL HHHCCCCCCCCCCHH	10.81	21890473
611	Ubiquitination	LRNHQGPLPPVPLHL HHHCCCCCCCCCCHH	10.81	23000965
611 (in isoform 2)	Ubiquitination	-	10.81	21890473
627	Ubiquitination	NAPTRLMKDLGYGKG CCCCHHHHHHCCCCC	55.16	23000965
627 (in isoform 1)	Ubiquitination	-	55.16	21890473
631	Phosphorylation	RLMKDLGYGKGYKYN HHHHHHCCCCCCCCC	23.98	22817900
633	Acetylation	MKDLGYGKGYKYNPM HHHHCCCCCCCCCCC	51.05	19608861
633	Ubiquitination	MKDLGYGKGYKYNPM HHHHCCCCCCCCCCC	51.05	23000965
633 (in isoform 1)	Ubiquitination	-	51.05	21890473
635	Phosphorylation	DLGYGKGYKYNPMYS HHCCCCCCCCCCCCC	17.49	22817900
636	Ubiquitination	LGYGKGYKYNPMYSE HCCCCCCCCCCCCCC	47.41	21890473
636	Acetylation	LGYGKGYKYNPMYSE HCCCCCCCCCCCCCC	47.41	25953088
636	Neddylation	LGYGKGYKYNPMYSE HCCCCCCCCCCCCCC	47.41	32015554
636	Ubiquitination	LGYGKGYKYNPMYSE HCCCCCCCCCCCCCC	47.41	23000965
636 (in isoform 1)	Ubiquitination	-	47.41	21890473
636 (in isoform 2)	Ubiquitination	-	47.41	21890473
637	Phosphorylation	GYGKGYKYNPMYSEP CCCCCCCCCCCCCCC	18.93	27642862
641	Phosphorylation	GYKYNPMYSEPVDQE CCCCCCCCCCCCCHH	15.90	27642862
655	Methylation	EYLPEELRGVDFFKQ HHCCHHHCCCCCHHH	46.50	115920093
661	Neddylation	LRGVDFFKQRRC--- HCCCCCHHHCCC---	42.78	32015554
661	Ubiquitination	LRGVDFFKQRRC--- HCCCCCHHHCCC---	42.78	23000965
661 (in isoform 1)	Ubiquitination	-	42.78	21890473

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 WRIP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of WRIP1_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 WRIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WRN_HUMAN	WRN	physical	11301316
UBP11_HUMAN	USP11	physical	19615732
NU107_HUMAN	NUP107	physical	20676042
RAD18_HUMAN	RAD18	physical	19556710
WRIP1_HUMAN	WRNIP1	physical	15670210
DPOD1_HUMAN	POLD1	physical	15670210
TIF1B_HUMAN	TRIM28	physical	22863883
UBC_HUMAN	UBC	physical	17550899
UBC_HUMAN	UBC	physical	25872870

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 WRIP1_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-633, 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 THR-85; SER-91; SER-92;THR-116 AND TYR-534, 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-151 AND SER-153, ANDMASS SPECTROMETRY.	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-91 AND SER-92, AND MASSSPECTROMETRY.	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-75; THR-85; SER-91;SER-92 AND THR-116, AND MASS SPECTROMETRY.	18669648 [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-153, AND MASSSPECTROMETRY.	18220336 [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-75, AND MASSSPECTROMETRY.	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-65, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534 AND TYR-562, ANDMASS SPECTROMETRY.	15592455 [Abstract]
Ubiquitylation
Reference	PubMed
"Werner helicase-interacting protein 1 binds polyubiquitin via itszinc finger domain."; Bish R.A., Myers M.P.; J. Biol. Chem. 282:23184-23193(2007). Cited for: SUMOYLATION, UBIQUITINATION AT LYS-81; LYS-141; LYS-225; LYS-301;LYS-310; LYS-316; LYS-322; LYS-335; LYS-482; LYS-627; LYS-633 ANDLYS-636, AND DOMAIN UBZ-TYPE ZINC FINGER.	17550899 [Abstract]