dbPTM

PTN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN1_HUMAN
UniProt AC	P18031
Protein Name	Tyrosine-protein phosphatase non-receptor type 1
Gene Name	PTPN1
Organism	Homo sapiens (Human).
Sequence Length	435
Subcellular Localization	Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side . Interacts with EPHA3 at the cell membrane.
Protein Description	Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET..
Protein Sequence	MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYGIESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLTAGAYLCYRFLFNSNT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEMEKEFE -------CCHHHHHH	11.32	2546149
5	Ubiquitination	---MEMEKEFEQIDK ---CCHHHHHHHHCC	67.41	-
12	Ubiquitination	KEFEQIDKSGSWAAI HHHHHHCCCCCHHHH	59.34	-
13	Phosphorylation	EFEQIDKSGSWAAIY HHHHHCCCCCHHHHH	34.02	28796482
15	Phosphorylation	EQIDKSGSWAAIYQD HHHCCCCCHHHHHHH	22.19	28796482
20	Phosphorylation	SGSWAAIYQDIRHEA CCCHHHHHHHHHHHH	8.73	21082442
32	S-nitrosocysteine	HEASDFPCRVAKLPK HHHCCCCCCEECCCC	5.73	-
32	S-nitrosylation	HEASDFPCRVAKLPK HHHCCCCCCEECCCC	5.73	22178444
46	Phosphorylation	KNKNRNRYRDVSPFD CCCCCCCCCCCCCCC	18.08	23927012
50	Phosphorylation	RNRYRDVSPFDHSRI CCCCCCCCCCCCCCC	24.92	29255136
55	Phosphorylation	DVSPFDHSRIKLHQE CCCCCCCCCCEECCC	37.23	23927012
58	Ubiquitination	PFDHSRIKLHQEDND CCCCCCCEECCCCCC	38.51	-
66	Phosphorylation	LHQEDNDYINASLIK ECCCCCCCCCHHHEE	11.43	8999839
70	Phosphorylation	DNDYINASLIKMEEA CCCCCCHHHEEHHHH	26.58	28796482
73	2-Hydroxyisobutyrylation	YINASLIKMEEAQRS CCCHHHEEHHHHHHH	45.62	-
73	Ubiquitination	YINASLIKMEEAQRS CCCHHHEEHHHHHHH	45.62	-
80	Phosphorylation	KMEEAQRSYILTQGP EHHHHHHHHEECCCC	12.40	28796482
81	Phosphorylation	MEEAQRSYILTQGPL HHHHHHHHEECCCCC	11.35	28796482
84	Phosphorylation	AQRSYILTQGPLPNT HHHHHEECCCCCCCC	23.17	29978859
91	Phosphorylation	TQGPLPNTCGHFWEM CCCCCCCCCHHHHHH	20.23	29978859
92	S-nitrosylation	QGPLPNTCGHFWEMV CCCCCCCCHHHHHHH	5.18	22178444
92	S-nitrosocysteine	QGPLPNTCGHFWEMV CCCCCCCCHHHHHHH	5.18	-
104	Phosphorylation	EMVWEQKSRGVVMLN HHHHHHHCCCEEEEC	33.68	29978859
116	Ubiquitination	MLNRVMEKGSLKCAQ EECCHHHHCCCCCHH	35.39	-
116	2-Hydroxyisobutyrylation	MLNRVMEKGSLKCAQ EECCHHHHCCCCCHH	35.39	-
116	Acetylation	MLNRVMEKGSLKCAQ EECCHHHHCCCCCHH	35.39	25953088
118	Phosphorylation	NRVMEKGSLKCAQYW CCHHHHCCCCCHHCC	35.41	23401153
120	Malonylation	VMEKGSLKCAQYWPQ HHHHCCCCCHHCCCC	29.26	26320211
120	Ubiquitination	VMEKGSLKCAQYWPQ HHHHCCCCCHHCCCC	29.26	-
120	Acetylation	VMEKGSLKCAQYWPQ HHHHCCCCCHHCCCC	29.26	25953088
128	Ubiquitination	CAQYWPQKEEKEMIF CHHCCCCHHHHHEEE	64.86	-
131	Ubiquitination	YWPQKEEKEMIFEDT CCCCHHHHHEEECCC	54.39	-
131	2-Hydroxyisobutyrylation	YWPQKEEKEMIFEDT CCCCHHHHHEEECCC	54.39	-
131	Acetylation	YWPQKEEKEMIFEDT CCCCHHHHHEEECCC	54.39	8242811
133	Sulfoxidation	PQKEEKEMIFEDTNL CCHHHHHEEECCCCC	6.69	21406390
141	Acetylation	IFEDTNLKLTLISED EECCCCCEEEEECHH	41.31	8242823
141	2-Hydroxyisobutyrylation	IFEDTNLKLTLISED EECCCCCEEEEECHH	41.31	-
146	Phosphorylation	NLKLTLISEDIKSYY CCEEEEECHHHHHHE	32.12	21712546
150	Ubiquitination	TLISEDIKSYYTVRQ EEECHHHHHHEEEEE	44.73	-
152	Phosphorylation	ISEDIKSYYTVRQLE ECHHHHHHEEEEEHH	9.73	8999839
153	Phosphorylation	SEDIKSYYTVRQLEL CHHHHHHEEEEEHHH	13.07	8999839
201	Phosphorylation	FLFKVRESGSLSPEH HHHHHHCCCCCCCCC	24.10	30108239
203	Phosphorylation	FKVRESGSLSPEHGP HHHHCCCCCCCCCCC	34.65	30108239
205	Phosphorylation	VRESGSLSPEHGPVV HHCCCCCCCCCCCEE	29.91	30108239
215	S-nitrosylation	HGPVVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	22169477
215	Oxidation	HGPVVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	12802338
215	Sulfation	HGPVVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	12802338
215	Sulfhydration	HGPVVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	22169477
215	Glutathionylation	HGPVVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	12802338
215	Cysteine persulfide	HGPVVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	-
216	Phosphorylation	GPVVVHCSAGIGRSG CCEEEECCCCCCCCH	18.04	30108239
222	Phosphorylation	CSAGIGRSGTFCLAD CCCCCCCCHHEEEHH	36.65	27251275
224	Phosphorylation	AGIGRSGTFCLADTC CCCCCCHHEEEHHHH	16.66	27251275
239	Ubiquitination	LLLMDKRKDPSSVDI HHHHHCCCCCCCCCH	78.65	-
242	Phosphorylation	MDKRKDPSSVDIKKV HHCCCCCCCCCHHHH	53.80	20068231
243	Phosphorylation	DKRKDPSSVDIKKVL HCCCCCCCCCHHHHH	29.24	20068231
247	Ubiquitination	DPSSVDIKKVLLEMR CCCCCCHHHHHHHHH	32.16	-
248	Ubiquitination	PSSVDIKKVLLEMRK CCCCCHHHHHHHHHH	38.15	-
258	Sulfoxidation	LEMRKFRMGLIQTAD HHHHHHHHCCCHHHH	6.03	21406390
270	Phosphorylation	TADQLRFSYLAVIEG HHHHHHHHHHHHCCC	16.89	23663014
271	Phosphorylation	ADQLRFSYLAVIEGA HHHHHHHHHHHCCCC	8.93	23663014
285	Phosphorylation	AKFIMGDSSVQDQWK CEEECCCCCHHHHHH	27.04	25627689
286	Phosphorylation	KFIMGDSSVQDQWKE EEECCCCCHHHHHHH	28.65	25159151
295	Phosphorylation	QDQWKELSHEDLEPP HHHHHHCCCCCCCCC	26.39	29255136
314	Ubiquitination	PPPPRPPKRILEPHN CCCCCCCCCCCCCCC	55.54	-
323	Acetylation	ILEPHNGKCREFFPN CCCCCCCCCHHHCCC	35.12	25953088
323	Ubiquitination	ILEPHNGKCREFFPN CCCCCCCCCHHHCCC	35.12	-
335	Sumoylation	FPNHQWVKEETQEDK CCCCHHHHHHCCCCC	47.04	-
335	Ubiquitination	FPNHQWVKEETQEDK CCCCHHHHHHCCCCC	47.04	-
335	Sumoylation	FPNHQWVKEETQEDK CCCCHHHHHHCCCCC	47.04	-
338	Phosphorylation	HQWVKEETQEDKDCP CHHHHHHCCCCCCCC	38.05	30108239
347	Sumoylation	EDKDCPIKEEKGSPL CCCCCCCCCCCCCCC	44.99	-
347	Sumoylation	EDKDCPIKEEKGSPL CCCCCCCCCCCCCCC	44.99	-
350	Ubiquitination	DCPIKEEKGSPLNAA CCCCCCCCCCCCCCC	66.82	21906983
352	Phosphorylation	PIKEEKGSPLNAAPY CCCCCCCCCCCCCCC	36.96	29255136
359	Phosphorylation	SPLNAAPYGIESMSQ CCCCCCCCCHHHCCC	26.47	30266825
363	Phosphorylation	AAPYGIESMSQDTEV CCCCCHHHCCCCCCH	23.08	30266825
365	Phosphorylation	PYGIESMSQDTEVRS CCCHHHCCCCCCHHH	33.90	30266825
368	Phosphorylation	IESMSQDTEVRSRVV HHHCCCCCCHHHHHH	28.83	30266825
372	Phosphorylation	SQDTEVRSRVVGGSL CCCCCHHHHHHCCCC	34.30	26074081
378	Phosphorylation	RSRVVGGSLRGAQAA HHHHHCCCCCCHHCC	14.68	25159151
380	Methylation	RVVGGSLRGAQAASP HHHCCCCCCHHCCCC	39.85	115489601
386	Phosphorylation	LRGAQAASPAKGEPS CCCHHCCCCCCCCCC	28.53	25159151
393	Phosphorylation	SPAKGEPSLPEKDED CCCCCCCCCCCCCCC	52.86	25159151
417	Phosphorylation	LVNMCVATVLTAGAY HHHHHHHHHHHHHHH	8.82	24719451
424	Phosphorylation	TVLTAGAYLCYRFLF HHHHHHHHHHHHHHH	9.08	24719451
427	Phosphorylation	TAGAYLCYRFLFNSN HHHHHHHHHHHHCCC	11.21	26267517

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
50	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
50	S	Phosphorylation	Kinase	CLK1	P49759	Uniprot
50	S	Phosphorylation	Kinase	CLK2	P49760	Uniprot
50	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
50	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
66	Y	Phosphorylation	Kinase	EGFR	P00533	Uniprot
152	Y	Phosphorylation	Kinase	INSR	P06213	PhosphoELM
153	Y	Phosphorylation	Kinase	INSR	P06213	PhosphoELM
242	S	Phosphorylation	Kinase	CLK1	P49759	Uniprot
242	S	Phosphorylation	Kinase	CLK2	P49760	Uniprot
243	S	Phosphorylation	Kinase	CLK1	P49759	Uniprot
243	S	Phosphorylation	Kinase	CLK2	P49760	Uniprot
286	S	Phosphorylation	Kinase	PLK1	P53350	PSP
378	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
378	S	Phosphorylation	Kinase	PKC	-	Uniprot
378	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
378	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
386	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
386	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
386	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
393	S	Phosphorylation	Kinase	PLK1	P53350	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
50	S	Phosphorylation	11579209
Activated by phosphorylation at Ser-50.
50	S	Phosphorylation	11579209
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243.
215	C	S-nitrosylation	22169477
S-nitrosylation of Cys-215 inactivates the enzyme activity.
242	S	Phosphorylation	11579209
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243.
243	S	Phosphorylation	11579209
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243.

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 PTN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GSK3B_HUMAN	GSK3B	physical	7514173
GRB2_HUMAN	GRB2	physical	10660596
IRS1_HUMAN	IRS1	physical	10660596
CAV1_HUMAN	CAV1	physical	12176037
EGFR_HUMAN	EGFR	physical	10889023
BCAR1_HUMAN	BCAR1	physical	8940134
CTNB1_HUMAN	CTNNB1	physical	12377785
EGFR_HUMAN	EGFR	physical	8621392
STA5A_HUMAN	STAT5A	physical	12237455
STA5B_HUMAN	STAT5B	physical	12237455
NTRK1_HUMAN	NTRK1	physical	12237455
NTRK2_HUMAN	NTRK2	physical	12237455
NTRK3_HUMAN	NTRK3	physical	12237455
LTK_HUMAN	LTK	physical	12237455
TYK2_HUMAN	TYK2	physical	11694501
JAK2_HUMAN	JAK2	physical	11694501
INSR_HUMAN	INSR	physical	11726652
STAM2_HUMAN	STAM2	physical	20504764
STAT3_HUMAN	STAT3	physical	15821101
JAK2_HUMAN	JAK2	physical	15821101
RFWD2_HUMAN	RFWD2	physical	23439647
IL1B_HUMAN	IL1B	physical	23439647
AGR3_HUMAN	AGR3	physical	25640309
BCAS3_HUMAN	BCAS3	physical	25640309
CASC3_HUMAN	CASC3	physical	25640309
CASZ1_HUMAN	CASZ1	physical	25640309
CCL5_HUMAN	CCL5	physical	25640309
CAD13_HUMAN	CDH13	physical	25640309
DIRA3_HUMAN	DIRAS3	physical	25640309
FA84B_HUMAN	FAM84B	physical	25640309
KLK7_HUMAN	KLK7	physical	25640309
MRC2_HUMAN	MRC2	physical	25640309
RHBT2_HUMAN	RHOBTB2	physical	25640309
SNAI1_HUMAN	SNAI1	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
VPS45_HUMAN	VPS45	physical	25640309
VATB2_HUMAN	ATP6V1B2	physical	26496610
VPP1_HUMAN	ATP6V0A1	physical	26496610
CO5A1_HUMAN	COL5A1	physical	26496610
STOM_HUMAN	STOM	physical	26496610
FLOT2_HUMAN	FLOT2	physical	26496610
GALT2_HUMAN	GALNT2	physical	26496610
MOES_HUMAN	MSN	physical	26496610
PHB_HUMAN	PHB	physical	26496610
ABCD3_HUMAN	ABCD3	physical	26496610
SMRD2_HUMAN	SMARCD2	physical	26496610
VA0D1_HUMAN	ATP6V0D1	physical	26496610
GOSR1_HUMAN	GOSR1	physical	26496610
MVP_HUMAN	MVP	physical	26496610
FLOT1_HUMAN	FLOT1	physical	26496610
PHB2_HUMAN	PHB2	physical	26496610
LTN1_HUMAN	LTN1	physical	26496610
GOLI4_HUMAN	GOLIM4	physical	26496610
BCOR_HUMAN	BCOR	physical	26496610
WAP53_HUMAN	WRAP53	physical	26496610
MREG_HUMAN	MREG	physical	26496610
PCNP_HUMAN	PCNP	physical	26496610
KDIS_HUMAN	KIDINS220	physical	26496610
RN213_HUMAN	RNF213	physical	26496610
RHG39_HUMAN	ARHGAP39	physical	26496610
CAVN1_HUMAN	PTRF	physical	26496610
EGFR_HUMAN	EGFR	physical	7693694
ACTB_HUMAN	ACTB	physical	27880917
APLP2_HUMAN	APLP2	physical	27880917
CASC4_HUMAN	CASC4	physical	27880917
GOLI4_HUMAN	GOLIM4	physical	27880917
RN213_HUMAN	RNF213	physical	27880917
SMD2_HUMAN	SNRPD2	physical	27880917
TOM70_HUMAN	TOMM70A	physical	27880917
DUS1_HUMAN	DUSP1	physical	27432908
GRB2_HUMAN	GRB2	physical	27432908
DCNL5_HUMAN	DCUN1D5	physical	27432908
PISD_HUMAN	PISD	physical	27432908
COX11_HUMAN	COX11	physical	27432908
NDUF4_HUMAN	NDUFAF4	physical	27432908
SYNC_HUMAN	NARS	physical	27432908
PTH2_HUMAN	PTRH2	physical	27432908
TBC15_HUMAN	TBC1D15	physical	27432908
ANFC_HUMAN	NPPC	physical	27432908
PROF2_HUMAN	PFN2	physical	27432908
ARL1_HUMAN	ARL1	physical	27432908
DHC24_HUMAN	DHCR24	physical	27432908
AIP_HUMAN	AIP	physical	27432908
RAB5C_HUMAN	RAB5C	physical	27432908
PGRC1_HUMAN	PGRMC1	physical	27432908
S61A1_HUMAN	SEC61A1	physical	27432908
CDIPT_HUMAN	CDIPT	physical	27432908
S27A4_HUMAN	SLC27A4	physical	27432908
ILVBL_HUMAN	ILVBL	physical	27432908
DHCR7_HUMAN	DHCR7	physical	27432908
PCH2_HUMAN	TRIP13	physical	27432908
ABCD3_HUMAN	ABCD3	physical	27432908
ARF4_HUMAN	ARF4	physical	27432908
HEAT3_HUMAN	HEATR3	physical	27432908
PIMT_HUMAN	PCMT1	physical	27432908
ARF1_HUMAN	ARF1	physical	27432908
CCD47_HUMAN	CCDC47	physical	27432908
CDK4_HUMAN	CDK4	physical	27432908
FAD1_HUMAN	FLAD1	physical	27432908
LAT_HUMAN	LAT	physical	12857726
SRC_HUMAN	SRC	physical	12857726

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
D04050	Ertiprotafib (USAN/INN)
DrugBank
DB01133	Tiludronate

Regulatory Network of PTN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Human placenta protein-tyrosine-phosphatase: amino acid sequence andrelationship to a family of receptor-like proteins."; Charbonneau H., Tonks N.K., Kumar S., Diltz C.D., Harrylock M.,Cool D.E., Krebs E.G., Fischer E.H., Walsh K.A.; Proc. Natl. Acad. Sci. U.S.A. 86:5252-5256(1989). Cited for: PROTEIN SEQUENCE OF 1-321.	2546149 [Abstract]
Phosphorylation
Reference	PubMed
"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-50 AND SER-352, AND MASSSPECTROMETRY.	18691976 [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-50 AND SER-295, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability todephosphorylate the insulin receptor."; Ravichandran L.V., Chen H., Li Y., Quon M.J.; Mol. Endocrinol. 15:1768-1780(2001). Cited for: PHOSPHORYLATION AT SER-50, AND MUTAGENESIS OF SER-50.	11579209 [Abstract]
"The CLK family kinases, CLK1 and CLK2, phosphorylate and activate thetyrosine phosphatase, PTP-1B."; Moeslein F.M., Myers M.P., Landreth G.E.; J. Biol. Chem. 274:26697-26704(1999). Cited for: PHOSPHORYLATION AT SER-50; SER-242 AND SER-243, AND MUTAGENESIS OFSER-50.	10480872 [Abstract]
"Multi-site phosphorylation of the protein tyrosine phosphatase,PTP1B: identification of cell cycle regulated and phorbol esterstimulated sites of phosphorylation."; Flint A.J., Gebbink M.F.G.B., Franza B.R. Jr., Hill D.E., Tonks N.K.; EMBO J. 12:1937-1946(1993). Cited for: PHOSPHORYLATION AT SER-352; SER-378 AND SER-386.	8491187 [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-20, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Protein tyrosine phosphatase 1B interacts with and is tyrosinephosphorylated by the epidermal growth factor receptor."; Liu F., Chernoff J.; Biochem. J. 327:139-145(1997). Cited for: PHOSPHORYLATION AT TYR-66.	9355745 [Abstract]
S-nitrosylation
Reference	PubMed
"H2s-induced sulfhydration of the phosphatase PTP1B and its role inthe endoplasmic reticulum stress response."; Krishnan N., Fu C., Pappin D.J., Tonks N.K.; Sci. Signal. 4:RA86-RA86(2011). Cited for: FUNCTION, SULFHYDRATION AT CYS-215, S-NITROSYLATION AT CYS-215,MUTAGENESIS OF CYS-215, AND MUTAGENESIS OF ASP-181 AND CYS-215.	22169477 [Abstract]

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