dbPTM

PIAS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PIAS1_HUMAN
UniProt AC	O75925
Protein Name	E3 SUMO-protein ligase PIAS1
Gene Name	PIAS1
Organism	Homo sapiens (Human).
Sequence Length	651
Subcellular Localization	Nucleus speckle . Nucleus, PML body. Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton.
Protein Description	Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity)..
Protein Sequence	MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGTWAPMRSKKEVQEVSASYNGVDGCLSSTLEHQVASHHQSSNKNKKVEVIDLTIDSSSDEEEEEPSAKRTCPSLSPTSPLNNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPTTNGSSSGSNSSLVSSNSLRESHSHTVTNRSSTDTASIFGIIPDIISLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSAELKQ ------CCCHHHHHH	21.33	22814378
4	Phosphorylation	----MADSAELKQMV ----CCCHHHHHHHH	17.69	20860994
8	Ubiquitination	MADSAELKQMVMSLR CCCHHHHHHHHHHHC	28.05	-
8	Sumoylation	MADSAELKQMVMSLR CCCHHHHHHHHHHHC	28.05	-
8	Sumoylation	MADSAELKQMVMSLR CCCHHHHHHHHHHHC	28.05	-
8	Ubiquitination	MADSAELKQMVMSLR CCCHHHHHHHHHHHC	28.05	-
13	Phosphorylation	ELKQMVMSLRVSELQ HHHHHHHHHCHHHHH	11.12	-
17	Phosphorylation	MVMSLRVSELQVLLG HHHHHCHHHHHHHHH	26.59	-
30	Ubiquitination	LGYAGRNKHGRKHEL HHHCCCCCCCCHHHH	46.18	-
34	Ubiquitination	GRNKHGRKHELLTKA CCCCCCCHHHHHHHH	46.13	-
40	Sumoylation	RKHELLTKALHLLKA CHHHHHHHHHHHHHC	49.25	-
40	Sumoylation	RKHELLTKALHLLKA CHHHHHHHHHHHHHC	49.25	28112733
40	Ubiquitination	RKHELLTKALHLLKA CHHHHHHHHHHHHHC	49.25	-
46	Ubiquitination	TKALHLLKAGCSPAV HHHHHHHHCCCCHHH	49.44	-
46	Sumoylation	TKALHLLKAGCSPAV HHHHHHHHCCCCHHH	49.44	-
46	Sumoylation	TKALHLLKAGCSPAV HHHHHHHHCCCCHHH	49.44	28112733
46	Ubiquitination	TKALHLLKAGCSPAV HHHHHHHHCCCCHHH	49.44	-
48	Ubiquitination	ALHLLKAGCSPAVQM HHHHHHCCCCHHHHH	15.73	-
50	Phosphorylation	HLLKAGCSPAVQMKI HHHHCCCCHHHHHHH	18.25	21815630
56	Sumoylation	CSPAVQMKIKELYRR CCHHHHHHHHHHHHH	33.27	-
56	Sumoylation	CSPAVQMKIKELYRR CCHHHHHHHHHHHHH	33.27	-
56	Ubiquitination	CSPAVQMKIKELYRR CCHHHHHHHHHHHHH	33.27	-
58	Ubiquitination	PAVQMKIKELYRRRF HHHHHHHHHHHHHHC	35.83	-
58	Sumoylation	PAVQMKIKELYRRRF HHHHHHHHHHHHHHC	35.83	-
58	Sumoylation	PAVQMKIKELYRRRF HHHHHHHHHHHHHHC	35.83	-
58	Ubiquitination	PAVQMKIKELYRRRF HHHHHHHHHHHHHHC	35.83	-
60	Ubiquitination	VQMKIKELYRRRFPQ HHHHHHHHHHHHCCC	3.24	-
71	Phosphorylation	RFPQKIMTPADLSIP HCCCCCCCCCCCCCC	20.85	-
82	Phosphorylation	LSIPNVHSSPMPATL CCCCCCCCCCCCCCC	31.67	26074081
83	Phosphorylation	SIPNVHSSPMPATLS CCCCCCCCCCCCCCC	15.44	26074081
88	Phosphorylation	HSSPMPATLSPSTIP CCCCCCCCCCCCCCC	23.15	26074081
90	Phosphorylation	SPMPATLSPSTIPQL CCCCCCCCCCCCCCC	16.67	17540171
92	Phosphorylation	MPATLSPSTIPQLTY CCCCCCCCCCCCCCC	35.28	26074081
93	Phosphorylation	PATLSPSTIPQLTYD CCCCCCCCCCCCCCC	39.81	26074081
105	Phosphorylation	TYDGHPASSPLLPVS CCCCCCCCCCCCCHH	36.62	26074081
106	Phosphorylation	YDGHPASSPLLPVSL CCCCCCCCCCCCHHH	22.98	26074081
112	Phosphorylation	SSPLLPVSLLGPKHE CCCCCCHHHCCCCCC	18.88	26074081
117	Sumoylation	PVSLLGPKHELELPH CHHHCCCCCCCCCCC	48.16	-
137	Sumoylation	HPVHPDIKLQKLPFY CCCCCCCHHHCCCHH	52.85	-
137	Acetylation	HPVHPDIKLQKLPFY CCCCCCCHHHCCCHH	52.85	26051181
137	Sumoylation	HPVHPDIKLQKLPFY CCCCCCCHHHCCCHH	52.85	28112733
137	Ubiquitination	HPVHPDIKLQKLPFY CCCCCCCHHHCCCHH	52.85	-
140	Ubiquitination	HPDIKLQKLPFYDLL CCCCHHHCCCHHHHH	69.44	-
142	Ubiquitination	DIKLQKLPFYDLLDE CCHHHCCCHHHHHHH	32.55	-
152	Sumoylation	DLLDELIKPTSLASD HHHHHHHCCCCCCCC	55.67	-
152	Sumoylation	DLLDELIKPTSLASD HHHHHHHCCCCCCCC	55.67	-
152	Ubiquitination	DLLDELIKPTSLASD HHHHHHHCCCCCCCC	55.67	-
154	Phosphorylation	LDELIKPTSLASDNS HHHHHCCCCCCCCCH	31.22	25262027
155	Phosphorylation	DELIKPTSLASDNSQ HHHHCCCCCCCCCHH	30.39	25262027
158	Phosphorylation	IKPTSLASDNSQRFR HCCCCCCCCCHHHHH	42.49	25262027
226	Ubiquitination	LCVKVNTKPCSLPGY CEEEECCEECCCCCC	38.53	-
228	Ubiquitination	VKVNTKPCSLPGYLP EEECCEECCCCCCCC	7.51	-
238	Sumoylation	PGYLPPTKNGVEPKR CCCCCCCCCCCCCCC	58.43	-
238	Sumoylation	PGYLPPTKNGVEPKR CCCCCCCCCCCCCCC	58.43	28112733
238	Ubiquitination	PGYLPPTKNGVEPKR CCCCCCCCCCCCCCC	58.43	-
240	Ubiquitination	YLPPTKNGVEPKRPS CCCCCCCCCCCCCCC	27.07	-
254	Phosphorylation	SRPINITSLVRLSTT CCCCCHHEEEEECCC	22.52	20860994
261	Phosphorylation	SLVRLSTTVPNTIVV EEEEECCCCCCEEEE	30.50	25332170
289	Phosphorylation	VYLVKQLSSTVLLQR HHHHHHHCHHHHHHH	22.82	23898821
290	Phosphorylation	YLVKQLSSTVLLQRL HHHHHHCHHHHHHHH	31.00	-
291	Phosphorylation	LVKQLSSTVLLQRLR HHHHHCHHHHHHHHH	16.28	-
303	Asymmetric dimethylarginine	RLRAKGIRNPDHSRA HHHHCCCCCCHHHHH	58.24	-
303	Methylation	RLRAKGIRNPDHSRA HHHHCCCCCCHHHHH	58.24	19136629
308	Phosphorylation	GIRNPDHSRALIKEK CCCCCHHHHHHHHHH	26.99	22964224
313	Ubiquitination	DHSRALIKEKLTADP HHHHHHHHHHHCCCC	50.04	-
315	Ubiquitination	SRALIKEKLTADPDS HHHHHHHHHCCCCCC	46.25	-
315	Sumoylation	SRALIKEKLTADPDS HHHHHHHHHCCCCCC	46.25	-
315	Sumoylation	SRALIKEKLTADPDS HHHHHHHHHCCCCCC	46.25	-
315	Ubiquitination	SRALIKEKLTADPDS HHHHHHHHHCCCCCC	46.25	21906983
317	Ubiquitination	ALIKEKLTADPDSEI HHHHHHHCCCCCCHH	39.83	21906983
317	Phosphorylation	ALIKEKLTADPDSEI HHHHHHHCCCCCCHH	39.83	27251275
322	Phosphorylation	KLTADPDSEIATTSL HHCCCCCCHHHHHHH	35.97	27251275
326	Phosphorylation	DPDSEIATTSLRVSL CCCCHHHHHHHHHEE	23.68	27251275
327	Phosphorylation	PDSEIATTSLRVSLL CCCHHHHHHHHHEEE	19.42	27251275
328	Phosphorylation	DSEIATTSLRVSLLC CCHHHHHHHHHEEEC	15.15	27251275
332	Phosphorylation	ATTSLRVSLLCPLGK HHHHHHHEEECCCCC	14.80	27251275
339	Ubiquitination	SLLCPLGKMRLTIPC EEECCCCCCEEEEEE	28.64	-
341	Ubiquitination	LCPLGKMRLTIPCRA ECCCCCCEEEEEECE	31.97	-
369	Ubiquitination	YIQMNEKKPTWVCPV EEECCCCCCCEEECC	41.31	-
408	Ubiquitination	DCDEIQFKEDGTWAP CCCCEEECCCCCCCC	38.22	-
410	Ubiquitination	DEIQFKEDGTWAPMR CCEEECCCCCCCCCC	61.48	-
419	Ubiquitination	TWAPMRSKKEVQEVS CCCCCCCHHHHHHHH	42.46	-
420	Ubiquitination	WAPMRSKKEVQEVSA CCCCCCHHHHHHHHH	65.45	-
421	Ubiquitination	APMRSKKEVQEVSAS CCCCCHHHHHHHHHH	53.85	-
422	Ubiquitination	PMRSKKEVQEVSASY CCCCHHHHHHHHHHH	8.92	-
451	Phosphorylation	VASHHQSSNKNKKVE HHHHHHCCCCCCCEE	45.30	22817900
453	Sumoylation	SHHQSSNKNKKVEVI HHHHCCCCCCCEEEE	72.58	28112733
453	Ubiquitination	SHHQSSNKNKKVEVI HHHHCCCCCCCEEEE	72.58	-
455	Ubiquitination	HQSSNKNKKVEVIDL HHCCCCCCCEEEEEE	60.86	-
455	Ubiquitination	HQSSNKNKKVEVIDL HHCCCCCCCEEEEEE	60.86	-
456	Ubiquitination	QSSNKNKKVEVIDLT HCCCCCCCEEEEEEE	53.69	-
457	Ubiquitination	SSNKNKKVEVIDLTI CCCCCCCEEEEEEEE	8.30	-
458	Ubiquitination	SNKNKKVEVIDLTID CCCCCCEEEEEEEEC	42.51	-
463	Phosphorylation	KVEVIDLTIDSSSDE CEEEEEEEECCCCCC	20.99	20363803
466	Phosphorylation	VIDLTIDSSSDEEEE EEEEEECCCCCCCCC	28.08	30631047
467	Phosphorylation	IDLTIDSSSDEEEEE EEEEECCCCCCCCCC	37.75	30631047
468	Phosphorylation	DLTIDSSSDEEEEEP EEEECCCCCCCCCCC	53.66	30631047
476	Phosphorylation	DEEEEEPSAKRTCPS CCCCCCCCCCCCCCC	50.10	20363803
480	Phosphorylation	EEPSAKRTCPSLSPT CCCCCCCCCCCCCCC	28.23	23927012
483	Phosphorylation	SAKRTCPSLSPTSPL CCCCCCCCCCCCCCC	43.56	23927012
485	Phosphorylation	KRTCPSLSPTSPLNN CCCCCCCCCCCCCCC	30.39	23927012
487	Phosphorylation	TCPSLSPTSPLNNKG CCCCCCCCCCCCCCC	39.33	30266825
488	Phosphorylation	CPSLSPTSPLNNKGI CCCCCCCCCCCCCCC	30.67	25159151
493	Sumoylation	PTSPLNNKGILSLPH CCCCCCCCCCCCCCC	46.37	28112733
493	Ubiquitination	PTSPLNNKGILSLPH CCCCCCCCCCCCCCC	46.37	-
495	Ubiquitination	SPLNNKGILSLPHQA CCCCCCCCCCCCCCC	2.23	-
497	Phosphorylation	LNNKGILSLPHQASP CCCCCCCCCCCCCCC	37.62	23927012
503	Phosphorylation	LSLPHQASPVSRTPS CCCCCCCCCCCCCCC	21.18	29255136
506	Phosphorylation	PHQASPVSRTPSLPA CCCCCCCCCCCCCCC	33.54	29255136
508	Phosphorylation	QASPVSRTPSLPAVD CCCCCCCCCCCCCCC	15.10	28102081
510	Phosphorylation	SPVSRTPSLPAVDTS CCCCCCCCCCCCCCC	46.50	21082442
516	Phosphorylation	PSLPAVDTSYINTSL CCCCCCCCCCCCHHH	19.48	28450419
517	Phosphorylation	SLPAVDTSYINTSLI CCCCCCCCCCCHHHH	21.39	28464451
518	Phosphorylation	LPAVDTSYINTSLIQ CCCCCCCCCCHHHHC	10.57	28464451
521	Phosphorylation	VDTSYINTSLIQDYR CCCCCCCHHHHCCCC	18.49	28464451
522	Phosphorylation	DTSYINTSLIQDYRH CCCCCCHHHHCCCCC	20.98	25218447
527	Phosphorylation	NTSLIQDYRHPFHMT CHHHHCCCCCCCCCC	8.41	27251275
633	Phosphorylation	SHTVTNRSSTDTASI CCCCCCCCCCCHHHH	39.39	20068231
634	Phosphorylation	HTVTNRSSTDTASIF CCCCCCCCCCHHHHH	27.37	25159151
635	Phosphorylation	TVTNRSSTDTASIFG CCCCCCCCCHHHHHC	38.32	20068231
637	Phosphorylation	TNRSSTDTASIFGII CCCCCCCHHHHHCCC	23.53	20068231
639	Phosphorylation	RSSTDTASIFGIIPD CCCCCHHHHHCCCCC	22.12	20068231

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
17	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
466	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
467	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
468	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
510	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
522	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	HECTD2	Q5U5R9	PMID:26157031
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH2	O43255	PMID:17533377

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PIAS1_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 PIAS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAT1_HUMAN	STAT1	physical	10805787
DNM3A_HUMAN	DNMT3A	physical	14752048
STAB2_HUMAN	STAB2	physical	14701874
SP3_HUMAN	SP3	physical	12356736
SUMO1_HUMAN	SUMO1	physical	11583632
UBC9_HUMAN	UBE2I	physical	11583632
P53_HUMAN	TP53	physical	11583632
SIAH2_HUMAN	SIAH2	physical	17533377
ZMIZ2_HUMAN	ZMIZ2	physical	20159969
BRCA1_HUMAN	BRCA1	physical	20016594
NCOR1_HUMAN	NCOR1	physical	16421255
PPARG_HUMAN	PPARG	physical	16127449
JUN_HUMAN	JUN	physical	11867732
P53_HUMAN	TP53	physical	11867732
HIC1_HUMAN	HIC1	physical	17283066
DDX5_HUMAN	DDX5	physical	17369852
SATB1_HUMAN	SATB1	physical	20351170
MAML1_HUMAN	MAML1	physical	20203086
DCR1A_HUMAN	DCLRE1A	physical	15572677
DNM3A_HUMAN	DNMT3A	physical	20966256
DNM3B_HUMAN	DNMT3B	physical	20966256
MDC1_HUMAN	MDC1	physical	22661230
PRDM1_HUMAN	PRDM1	physical	22555612
MDM2_HUMAN	MDM2	physical	12393906
IKKA_HUMAN	CHUK	physical	17540171
DYN1_RAT	Dnm1	physical	15123615
PML_HUMAN	PML	physical	22406621
ATX7_HUMAN	ATXN7	physical	19843541
SRSF1_HUMAN	SRSF1	physical	20805487
P53_HUMAN	TP53	physical	20805487
CEBPE_HUMAN	CEBPE	physical	15588942
FLI1_HUMAN	FLI1	physical	16148010
SUMO1_HUMAN	SUMO1	physical	19217413
SATB1_HUMAN	SATB1	physical	18408014
C8AP2_HUMAN	CASP8AP2	physical	21338522
STAT1_HUMAN	STAT1	physical	17371985
PLAG1_HUMAN	PLAG1	physical	15208321
NR1H3_HUMAN	NR1H3	physical	22969086
NR1H2_HUMAN	NR1H2	physical	22969086
PRGC2_HUMAN	PPARGC1B	physical	22969086
PRGC1_HUMAN	PPARGC1A	physical	22969086
STAT1_HUMAN	STAT1	physical	18566411
STAT1_HUMAN	STAT1	physical	9724754
IKKA_HUMAN	CHUK	physical	23032264
SMAD4_HUMAN	SMAD4	physical	21988832
SGTA_HUMAN	SGTA	physical	21988832
1433Z_HUMAN	YWHAZ	physical	21988832
SPOP_HUMAN	SPOP	physical	21988832
LMBL2_HUMAN	L3MBTL2	physical	24369422
ZN451_HUMAN	ZNF451	physical	18656483
UBC9_HUMAN	UBE2I	physical	22661230
PIAS1_HUMAN	PIAS1	physical	15561718
UBC9_HUMAN	UBE2I	physical	15561718
SUMO1_HUMAN	SUMO1	physical	22578841
SUMO2_HUMAN	SUMO2	physical	22578841
UBC9_HUMAN	UBE2I	physical	16148010
UBC9_HUMAN	UBE2I	physical	11867732
ANDR_HUMAN	AR	physical	25552417
TERF2_HUMAN	TERF2	physical	26450775
TRIM5_HUMAN	TRIM5	physical	25880753
TRIM5_MACMU	TRIM5	physical	25880753
HECD2_HUMAN	HECTD2	physical	26157031
GSK3B_HUMAN	GSK3B	physical	26157031
NCOA3_HUMAN	NCOA3	physical	22283414
PSME3_HUMAN	PSME3	physical	21445096
NR0B2_HUMAN	NR0B2	physical	27485016
SIAH1_HUMAN	SIAH1	physical	27485016
SIAH2_HUMAN	SIAH2	physical	27485016
MYB_HUMAN	MYB	physical	27032383

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 PIAS1_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"PRMT1-mediated arginine methylation of PIAS1 regulates STAT1signaling."; Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.; Genes Dev. 23:118-132(2009). Cited for: FUNCTION, INTERACTION WITH STAT1, METHYLATION AT ARG-303 BY PRMT1,MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-303.	19136629 [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-503 AND SER-510, ANDMASS SPECTROMETRY.	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-503 AND SER-522, 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-466; SER-467 ANDSER-468, AND MASS SPECTROMETRY.	17081983 [Abstract]