dbPTM

NIPA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NIPA_HUMAN
UniProt AC	Q86WB0
Protein Name	Nuclear-interacting partner of ALK
Gene Name	ZC3HC1
Organism	Homo sapiens (Human).
Sequence Length	502
Subcellular Localization	Nucleus .
Protein Description	Essential component of a SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry. May have an antiapoptotic role in NPM-ALK-mediated signaling events..
Protein Sequence	MAAPCEGQAFAVGVEKNWGAVVRSPEGTPQKIRQLIDEGIAPEEGGVDAKDTSATSQSVNGSPQAEQPSLESTSKEAFFSRVETFSSLKWAGKPFELSPLVCAKYGWVTVECDMLKCSSCQAFLCASLQPAFDFDRYKQRCAELKKALCTAHEKFCFWPDSPSPDRFGMLPLDEPAILVSEFLDRFQSLCHLDLQLPSLRPEDLKTMCLTEDKISLLLHLLEDELDHRTDERKTTIKLGSDIQVHVTACILSVCGWACSSSLESMQLSLITCSQCMRKVGLWGFQQIESSMTDLDASFGLTSSPIPGLEGRPERLPLVPESPRRMMTRSQDATFSPGSEQAEKSPGPIVSRTRSWDSSSPVDRPEPEAASPTTRTRPVTRSMGTGDTPGLEVPSSPLRKAKRARLCSSSSSDTSSRSFFDPTSQHRDWCPWVNITLGKESRENGGTEPDASAPAEPGWKAVLTILLAHKQSSQPAETDSMSLSEKSRKVFRIFRQWESLCSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAPCEGQA ------CCCCCCCCC	21.80	22223895
12 (in isoform 2)	Phosphorylation	-	7.73	20068231
21 (in isoform 2)	Phosphorylation	-	3.03	20068231
23 (in isoform 2)	Phosphorylation	-	39.64	20068231
24	Phosphorylation	NWGAVVRSPEGTPQK CCEEEEECCCCCHHH	18.72	22167270
28	Phosphorylation	VVRSPEGTPQKIRQL EEECCCCCHHHHHHH	22.38	22167270
31	Acetylation	SPEGTPQKIRQLIDE CCCCCHHHHHHHHHC	40.85	25953088
31	Ubiquitination	SPEGTPQKIRQLIDE CCCCCHHHHHHHHHC	40.85	29967540
52	Phosphorylation	GGVDAKDTSATSQSV CCCCCCCCCCCCCCC	21.39	30278072
53	Phosphorylation	GVDAKDTSATSQSVN CCCCCCCCCCCCCCC	39.42	23401153
53 (in isoform 2)	Phosphorylation	-	39.42	22468782
54	Ubiquitination	VDAKDTSATSQSVNG CCCCCCCCCCCCCCC	17.23	22817900
54 (in isoform 2)	Ubiquitination	-	17.23	21906983
55	Phosphorylation	DAKDTSATSQSVNGS CCCCCCCCCCCCCCC	27.37	30278072
56	Phosphorylation	AKDTSATSQSVNGSP CCCCCCCCCCCCCCC	21.85	23401153
58	Phosphorylation	DTSATSQSVNGSPQA CCCCCCCCCCCCCCC	19.81	25159151
62	Phosphorylation	TSQSVNGSPQAEQPS CCCCCCCCCCCCCCC	14.50	19664994
68	Ubiquitination	GSPQAEQPSLESTSK CCCCCCCCCCCCCCH	32.18	29967540
69	Phosphorylation	SPQAEQPSLESTSKE CCCCCCCCCCCCCHH	44.45	30266825
72	Phosphorylation	AEQPSLESTSKEAFF CCCCCCCCCCHHHHH	43.18	23403867
72	Ubiquitination	AEQPSLESTSKEAFF CCCCCCCCCCHHHHH	43.18	29967540
73	Phosphorylation	EQPSLESTSKEAFFS CCCCCCCCCHHHHHH	34.15	23403867
74	Phosphorylation	QPSLESTSKEAFFSR CCCCCCCCHHHHHHH	37.47	23403867
75	Ubiquitination	PSLESTSKEAFFSRV CCCCCCCHHHHHHHH	53.82	21906983
75 (in isoform 1)	Ubiquitination	-	53.82	21906983
75 (in isoform 3)	Ubiquitination	-	53.82	21906983
84	Phosphorylation	AFFSRVETFSSLKWA HHHHHHHHHHCCCCC	26.43	29255136
86	Phosphorylation	FSRVETFSSLKWAGK HHHHHHHHCCCCCCC	42.03	29255136
87	Phosphorylation	SRVETFSSLKWAGKP HHHHHHHCCCCCCCC	29.76	29255136
89	Ubiquitination	VETFSSLKWAGKPFE HHHHHCCCCCCCCCC	36.62	29967540
93	Ubiquitination	SSLKWAGKPFELSPL HCCCCCCCCCCCCCE	38.49	29967540
98	Phosphorylation	AGKPFELSPLVCAKY CCCCCCCCCEEHHHH	14.69	27050516
105	Phosphorylation	SPLVCAKYGWVTVEC CCEEHHHHCCEEEEE	9.55	23898821
109	Phosphorylation	CAKYGWVTVECDMLK HHHHCCEEEEECEEE	12.22	23898821
125	Ubiquitination	SSCQAFLCASLQPAF CCCCHHHHHHCCCCC	1.63	29967540
133	Ubiquitination	ASLQPAFDFDRYKQR HHCCCCCCHHHHHHH	46.79	33845483
137	Phosphorylation	PAFDFDRYKQRCAEL CCCCHHHHHHHHHHH	17.20	12748172
146	Ubiquitination	QRCAELKKALCTAHE HHHHHHHHHHHHHHH	60.25	29967540
154	Ubiquitination	ALCTAHEKFCFWPDS HHHHHHHHHCCCCCC	37.25	33845483
161	Phosphorylation	KFCFWPDSPSPDRFG HHCCCCCCCCCCCCC	24.17	25159151
163	Phosphorylation	CFWPDSPSPDRFGML CCCCCCCCCCCCCCC	43.30	25159151
175	Ubiquitination	GMLPLDEPAILVSEF CCCCCCCCHHHHHHH	25.02	24816145
198	Phosphorylation	HLDLQLPSLRPEDLK CCCCCCCCCCHHHHH	45.67	24719451
219	Ubiquitination	DKISLLLHLLEDELD HHHHHHHHHHHHHHC	28.47	24816145
253	Ubiquitination	VTACILSVCGWACSS HHHHHHHHHHHHHHC	2.91	24816145
276	Ubiquitination	LITCSQCMRKVGLWG HHHHHHHHHHHCCCC	3.44	24816145
278	Phosphorylation	TCSQCMRKVGLWGFQ HHHHHHHHHCCCCHH	17.48	32142685
292	Phosphorylation	QQIESSMTDLDASFG HHHHHHCCHHHHHCC	35.04	32142685
297	Phosphorylation	SMTDLDASFGLTSSP HCCHHHHHCCCCCCC	21.36	24275569
300	Phosphorylation	DLDASFGLTSSPIPG HHHHHCCCCCCCCCC	3.85	32142685
300	Ubiquitination	DLDASFGLTSSPIPG HHHHHCCCCCCCCCC	3.85	24816145
301	Phosphorylation	LDASFGLTSSPIPGL HHHHCCCCCCCCCCC	27.77	25850435
302	Phosphorylation	DASFGLTSSPIPGLE HHHCCCCCCCCCCCC	38.88	26074081
303	Phosphorylation	ASFGLTSSPIPGLEG HHCCCCCCCCCCCCC	22.93	26074081
314	Phosphorylation	GLEGRPERLPLVPES CCCCCCCCCCCCCCC	44.26	32142685
317	Ubiquitination	GRPERLPLVPESPRR CCCCCCCCCCCCCCC	13.70	22817900
320	Ubiquitination	ERLPLVPESPRRMMT CCCCCCCCCCCCCCC	66.93	22817900
321	Phosphorylation	RLPLVPESPRRMMTR CCCCCCCCCCCCCCC	20.03	19664994
322	Ubiquitination	LPLVPESPRRMMTRS CCCCCCCCCCCCCCC	26.66	24816145
323	Phosphorylation	PLVPESPRRMMTRSQ CCCCCCCCCCCCCCC	48.70	32142685
329	Phosphorylation	PRRMMTRSQDATFSP CCCCCCCCCCCCCCC	24.20	23927012
333	Phosphorylation	MTRSQDATFSPGSEQ CCCCCCCCCCCCCHH	32.70	25159151
335	Phosphorylation	RSQDATFSPGSEQAE CCCCCCCCCCCHHHH	24.81	19664994
338	Phosphorylation	DATFSPGSEQAEKSP CCCCCCCCHHHHCCC	29.89	29255136
343	Ubiquitination	PGSEQAEKSPGPIVS CCCHHHHCCCCCCEE	66.03	24816145
344	Phosphorylation	GSEQAEKSPGPIVSR CCHHHHCCCCCCEEC	26.96	29255136
350	Phosphorylation	KSPGPIVSRTRSWDS CCCCCCEECCCCCCC	28.75	22167270
352	Phosphorylation	PGPIVSRTRSWDSSS CCCCEECCCCCCCCC	22.88	23927012
354	Phosphorylation	PIVSRTRSWDSSSPV CCEECCCCCCCCCCC	34.32	20201521
357	Phosphorylation	SRTRSWDSSSPVDRP ECCCCCCCCCCCCCC	26.85	22167270
358	Phosphorylation	RTRSWDSSSPVDRPE CCCCCCCCCCCCCCC	35.87	22167270
359	Phosphorylation	TRSWDSSSPVDRPEP CCCCCCCCCCCCCCC	32.66	22167270
361	Ubiquitination	SWDSSSPVDRPEPEA CCCCCCCCCCCCCCC	12.01	22817900
363	Methylation	DSSSPVDRPEPEAAS CCCCCCCCCCCCCCC	37.40	115485017
364	Ubiquitination	SSSPVDRPEPEAASP CCCCCCCCCCCCCCC	57.96	22817900
366	Phosphorylation	SPVDRPEPEAASPTT CCCCCCCCCCCCCCC	38.93	32645325
367	Ubiquitination	PVDRPEPEAASPTTR CCCCCCCCCCCCCCC	56.03	29967540
370	Phosphorylation	RPEPEAASPTTRTRP CCCCCCCCCCCCCCC	29.81	19664994
372	Phosphorylation	EPEAASPTTRTRPVT CCCCCCCCCCCCCCC	26.81	22167270
373	Phosphorylation	PEAASPTTRTRPVTR CCCCCCCCCCCCCCC	33.17	22167270
374	Phosphorylation	EAASPTTRTRPVTRS CCCCCCCCCCCCCCC	31.08	32142685
375	Phosphorylation	AASPTTRTRPVTRSM CCCCCCCCCCCCCCC	36.91	26074081
379	Phosphorylation	TTRTRPVTRSMGTGD CCCCCCCCCCCCCCC	21.51	26074081
381	Phosphorylation	RTRPVTRSMGTGDTP CCCCCCCCCCCCCCC	16.52	29255136
384	Phosphorylation	PVTRSMGTGDTPGLE CCCCCCCCCCCCCCC	24.20	29255136
387	Phosphorylation	RSMGTGDTPGLEVPS CCCCCCCCCCCCCCC	22.17	29255136
388	Phosphorylation	SMGTGDTPGLEVPSS CCCCCCCCCCCCCCC	50.54	33259812
394	Phosphorylation	TPGLEVPSSPLRKAK CCCCCCCCCHHHHHH	50.17	29255136
395	Phosphorylation	PGLEVPSSPLRKAKR CCCCCCCCHHHHHHH	23.14	29255136
395	Ubiquitination	PGLEVPSSPLRKAKR CCCCCCCCHHHHHHH	23.14	22817900
398	Ubiquitination	EVPSSPLRKAKRARL CCCCCHHHHHHHHHH	40.03	22817900
407	Phosphorylation	AKRARLCSSSSSDTS HHHHHHCCCCCCCCC	37.54	29255136
408	Phosphorylation	KRARLCSSSSSDTSS HHHHHCCCCCCCCCC	32.99	27273156
409	Phosphorylation	RARLCSSSSSDTSSR HHHHCCCCCCCCCCC	19.98	29255136
410	Phosphorylation	ARLCSSSSSDTSSRS HHHCCCCCCCCCCCC	33.89	27273156
411	Phosphorylation	RLCSSSSSDTSSRSF HHCCCCCCCCCCCCC	47.02	27273156
413	Phosphorylation	CSSSSSDTSSRSFFD CCCCCCCCCCCCCCC	30.46	29255136
414	Phosphorylation	SSSSSDTSSRSFFDP CCCCCCCCCCCCCCC	28.83	27273156
414	Ubiquitination	SSSSSDTSSRSFFDP CCCCCCCCCCCCCCC	28.83	22817900
414 (in isoform 3)	Ubiquitination	-	28.83	21906983
415	Phosphorylation	SSSSDTSSRSFFDPT CCCCCCCCCCCCCCC	33.75	29255136
417	Phosphorylation	SSDTSSRSFFDPTSQ CCCCCCCCCCCCCCC	32.01	27273156
417	Ubiquitination	SSDTSSRSFFDPTSQ CCCCCCCCCCCCCCC	32.01	22817900
418	Ubiquitination	SDTSSRSFFDPTSQH CCCCCCCCCCCCCCC	8.60	22817900
421	Ubiquitination	SSRSFFDPTSQHRDW CCCCCCCCCCCCCCC	28.88	22817900
438	Ubiquitination	WVNITLGKESRENGG EEEEEECHHHHHCCC	56.48	29967540
442	Ubiquitination	TLGKESRENGGTEPD EECHHHHHCCCCCCC	70.30	22817900
445	Ubiquitination	KESRENGGTEPDASA HHHHHCCCCCCCCCC	38.19	22817900
464	Ubiquitination	GWKAVLTILLAHKQS HHHHHHHHHHHHHCC	2.31	22817900
464 (in isoform 2)	Ubiquitination	-	2.31	21906983
467	Ubiquitination	AVLTILLAHKQSSQP HHHHHHHHHHCCCCC	12.37	22817900
471	Phosphorylation	ILLAHKQSSQPAETD HHHHHHCCCCCCCCC	35.43	20068231
472	Phosphorylation	LLAHKQSSQPAETDS HHHHHCCCCCCCCCC	37.38	20068231
477	Phosphorylation	QSSQPAETDSMSLSE CCCCCCCCCCCCHHH	35.17	20068231
479	Phosphorylation	SQPAETDSMSLSEKS CCCCCCCCCCHHHHH	20.07	21815630
480	Sulfoxidation	QPAETDSMSLSEKSR CCCCCCCCCHHHHHH	5.34	21406390
481	Phosphorylation	PAETDSMSLSEKSRK CCCCCCCCHHHHHHH	32.47	25159151
483	Phosphorylation	ETDSMSLSEKSRKVF CCCCCCHHHHHHHHH	35.35	25159151
485	Ubiquitination	DSMSLSEKSRKVFRI CCCCHHHHHHHHHHH	52.78	22817900
485 (in isoform 1)	Ubiquitination	-	52.78	21906983
486	Phosphorylation	SMSLSEKSRKVFRIF CCCHHHHHHHHHHHH	33.03	20044836
488	Ubiquitination	SLSEKSRKVFRIFRQ CHHHHHHHHHHHHHH	53.46	22817900

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
84	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
105	Y	Phosphorylation	Kinase	ALK	Q9UM73	PhosphoELM
137	Y	Phosphorylation	Kinase	ALK	Q9UM73	PhosphoELM
354	S	Phosphorylation	Kinase	ALK	Q9UM73	GPS
395	S	Phosphorylation	Kinase	CDK1	P06493	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:22205987

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
354	S	Phosphorylation		12748172
Ser-354 phosphorylation, a major site during the course of cell-cycle-dependent phosphorylation, results in its dissociation from the SCF(NIPA) complex, thereby preventing CCNB1 degradation leading to mitotic entry.

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 NIPA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCNB1_HUMAN	CCNB1	physical	17389604
SKP1_HUMAN	SKP1	physical	17389604
CUL1_HUMAN	CUL1	physical	17389604
RBX1_HUMAN	RBX1	physical	16009132
CUL1_HUMAN	CUL1	physical	16009132
SKP1_HUMAN	SKP1	physical	16009132
CCNB1_HUMAN	CCNB1	physical	16009132
SKP1_HUMAN	SKP1	physical	22205987
A4_HUMAN	APP	physical	21832049
EHD4_HUMAN	EHD4	physical	22863883
TF3C4_HUMAN	GTF3C4	physical	22863883
FZR1_HUMAN	FZR1	physical	22205987
CUL1_MOUSE	Cul1	physical	22955283
SKP1_HUMAN	SKP1	physical	26474281
CCNB1_HUMAN	CCNB1	physical	26474281
PLK1_HUMAN	PLK1	physical	28514442
TPR_HUMAN	TPR	physical	28514442
SRBD1_HUMAN	SRBD1	physical	28514442
SALL2_HUMAN	SALL2	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 NIPA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-58; SER-62; SER-321; SER-335; SER-338; SER-344;THR-387 AND SER-395, AND MASS SPECTROMETRY.	19413330 [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-58; SER-62; SER-321;SER-335; SER-338; SER-344; SER-354; SER-359; SER-370; THR-387 ANDSER-395, 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-338, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-58; SER-62; SER-321; SER-335; SER-338; SER-344;THR-387 AND SER-395, 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-24; THR-28; SER-321;THR-333; SER-335; SER-338; SER-344; SER-354; SER-357; SER-370;THR-384; THR-387; SER-394 AND SER-395, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-395, ANDMASS SPECTROMETRY.	18691976 [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-321 AND SER-395, ANDMASS SPECTROMETRY.	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-24 AND THR-84, 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-370, AND MASSSPECTROMETRY.	19007248 [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 SER-24; THR-28 AND SER-321,AND MASS SPECTROMETRY.	16964243 [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-24; THR-28; SER-321 ANDSER-354, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Identification and characterization of a nuclear interacting partnerof anaplastic lymphoma kinase (NIPA)."; Ouyang T., Bai R.-Y., Bassermann F., von Klitzing C., Klumpen S.,Miething C., Morris S.W., Peschel C., Duyster J.; J. Biol. Chem. 278:30028-30036(2003). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUESPECIFICITY, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH NPM-ALKFUSION PROTEIN, PHOSPHORYLATION AT SER-354, AND MUTAGENESIS OFTYR-105; TYR-137; SER-354; LYS-399 AND 398-ARG--LYS-401.	12748172 [Abstract]

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