dbPTM

PTN22_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN22_HUMAN
UniProt AC	Q9Y2R2
Protein Name	Tyrosine-protein phosphatase non-receptor type 22
Gene Name	PTPN22
Organism	Homo sapiens (Human).
Sequence Length	807
Subcellular Localization	Cytoplasm.
Protein Description	Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. [PubMed: 16461343]
Protein Sequence	MDQREILQKFLDEAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFKRQMDVIRDKHSGTESQAKHCIPEKNHTLQADSYSPNLPKSTTKAAKMMNQQRTKMEIKESSSFDFRTSEISAKEELVLHPAKSSTSFDFLELNYSFDKNADTTMKWQTKAFPIVGEPLQKHQSLDLGSLLFEGCSNSKPVNAAGRYFNSKVPITRTKSTPFELIQQRETKEVDSKENFSYLESQPHDSCFVEMQAQKVMHVSSAELNYSLPYDSKHQIRNASNVKHHDSSALGVYSYIPLVENPYFSSWPPSGTSSKMSLDLPEKQDGTVFPSSLLPTSSTSLFSYYNSHDSLSLNSPTNISSLLNQESAVLATAPRIDDEIPPPLPVRTPESFIVVEEAGEFSPNVPKSLSSAVKVKIGTSLEWGGTSEPKKFDDSVILRPSKSVKLRSPKSELHQDRSSPPPPLPERTLESFFLADEDCMQAQSIETYSTSYPDTMENSTSSKQTLKTPGKSFTRSKSLKILRNMKKSICNSCPPNKPAESVQSNNSSSFLNFGFANRFSKPKGPRNPPPTWNI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Ubiquitination	DQREILQKFLDEAQS CHHHHHHHHHHHHHH	44.44	-
17	Ubiquitination	FLDEAQSKKITKEEF HHHHHHHCCCCHHHH	35.79	-
17	Ubiquitination	FLDEAQSKKITKEEF HHHHHHHCCCCHHHH	35.79	-
18	Ubiquitination	LDEAQSKKITKEEFA HHHHHHCCCCHHHHH	61.94	-
18	Ubiquitination	LDEAQSKKITKEEFA HHHHHHCCCCHHHHH	61.94	-
21	Ubiquitination	AQSKKITKEEFANEF HHHCCCCHHHHHHHH	59.73	-
21	Ubiquitination	AQSKKITKEEFANEF HHHCCCCHHHHHHHH	59.73	-
30	Ubiquitination	EFANEFLKLKRQSTK HHHHHHHHHHHCCCC	58.23	-
32	Ubiquitination	ANEFLKLKRQSTKYK HHHHHHHHHCCCCCC	46.97	-
32	Ubiquitination	ANEFLKLKRQSTKYK HHHHHHHHHCCCCCC	46.97	-
35	Phosphorylation	FLKLKRQSTKYKADK HHHHHHCCCCCCCCC	30.79	18056643
43	Phosphorylation	TKYKADKTYPTTVAE CCCCCCCCCCCCHHC	34.97	30242111
44	Phosphorylation	KYKADKTYPTTVAEK CCCCCCCCCCCHHCC	12.34	30242111
46	Phosphorylation	KADKTYPTTVAEKPK CCCCCCCCCHHCCCC	24.40	30242111
47	Phosphorylation	ADKTYPTTVAEKPKN CCCCCCCCHHCCCCC	17.14	30242111
51	Ubiquitination	YPTTVAEKPKNIKKN CCCCHHCCCCCCCCC	52.10	-
61	Ubiquitination	NIKKNRYKDILPYDY CCCCCCCCCCCCCCC	34.75	-
61	Ubiquitination	NIKKNRYKDILPYDY CCCCCCCCCCCCCCC	34.75	-
84	Phosphorylation	TSDEDSSYINANFIK ECCCCCCCCCCCEEC	11.35	-
142	Phosphorylation	GKKKCERYWAEPGEM CHHHHHHHCCCCCEE	6.15	29116813
166	Ubiquitination	SCEAEKRKSDYIIRT EEEEHHHCCCEEEEE	59.76	-
166	Ubiquitination	SCEAEKRKSDYIIRT EEEEHHHCCCEEEEE	59.76	-
167	Phosphorylation	CEAEKRKSDYIIRTL EEEHHHCCCEEEEEE	39.41	23532336
169	Phosphorylation	AEKRKSDYIIRTLKV EHHHCCCEEEEEEEE	12.82	29457462
173	Phosphorylation	KSDYIIRTLKVKFNS CCCEEEEEEEEEECC	22.11	-
260	Ubiquitination	PENFSVFSLIREMRT CCCCCHHHHHHHHHH	22.26	-
300	Ubiquitination	QMDVIRDKHSGTESQ HHHHHHCCCCCCHHH	29.80	-
309	Ubiquitination	SGTESQAKHCIPEKN CCCHHHHHHCCCCCC	31.22	-
309	Ubiquitination	SGTESQAKHCIPEKN CCCHHHHHHCCCCCC	31.22	-
315	Ubiquitination	AKHCIPEKNHTLQAD HHHCCCCCCCEECCC	48.99	-
318	Phosphorylation	CIPEKNHTLQADSYS CCCCCCCEECCCCCC	29.93	27080861
323	Phosphorylation	NHTLQADSYSPNLPK CCEECCCCCCCCCCH	30.44	23401153
324	Phosphorylation	HTLQADSYSPNLPKS CEECCCCCCCCCCHH	28.79	28450419
325	Phosphorylation	TLQADSYSPNLPKST EECCCCCCCCCCHHH	15.97	23401153
330	Ubiquitination	SYSPNLPKSTTKAAK CCCCCCCHHHHHHHH	64.70	-
337	Acetylation	KSTTKAAKMMNQQRT HHHHHHHHHHHHHHH	43.47	25953088
337	Ubiquitination	KSTTKAAKMMNQQRT HHHHHHHHHHHHHHH	43.47	-
341	Ubiquitination	KAAKMMNQQRTKMEI HHHHHHHHHHHCHHH	19.08	-
345	Ubiquitination	MMNQQRTKMEIKESS HHHHHHHCHHHHHCC	36.40	-
351	Phosphorylation	TKMEIKESSSFDFRT HCHHHHHCCCCCCCC	26.70	27251275
352	Phosphorylation	KMEIKESSSFDFRTS CHHHHHCCCCCCCCC	35.80	27251275
353	Phosphorylation	MEIKESSSFDFRTSE HHHHHCCCCCCCCCC	37.81	27251275
356	Ubiquitination	KESSSFDFRTSEISA HHCCCCCCCCCCCCC	9.64	-
364	Acetylation	RTSEISAKEELVLHP CCCCCCCCEEEEECC	44.95	19822837
364	Ubiquitination	RTSEISAKEELVLHP CCCCCCCCEEEEECC	44.95	-
373	Acetylation	ELVLHPAKSSTSFDF EEEECCCCCCCCCEE	49.76	19822847
374	Ubiquitination	LVLHPAKSSTSFDFL EEECCCCCCCCCEEE	40.74	-
374	Phosphorylation	LVLHPAKSSTSFDFL EEECCCCCCCCCEEE	40.74	26074081
375	Phosphorylation	VLHPAKSSTSFDFLE EECCCCCCCCCEEEE	27.62	26074081
376	Phosphorylation	LHPAKSSTSFDFLEL ECCCCCCCCCEEEEE	40.27	26074081
377	Phosphorylation	HPAKSSTSFDFLELN CCCCCCCCCEEEEEE	25.43	26074081
386	Ubiquitination	DFLELNYSFDKNADT EEEEEEEEECCCCCC	26.37	-
393	Ubiquitination	SFDKNADTTMKWQTK EECCCCCCCCEEECC	26.78	-
396	Ubiquitination	KNADTTMKWQTKAFP CCCCCCCEEECCCCC	33.77	-
400	Ubiquitination	TTMKWQTKAFPIVGE CCCEEECCCCCCCCC	32.69	-
406	Ubiquitination	TKAFPIVGEPLQKHQ CCCCCCCCCCCHHCC	31.37	-
411	Ubiquitination	IVGEPLQKHQSLDLG CCCCCCHHCCCCCHH	51.82	-
411	Ubiquitination	IVGEPLQKHQSLDLG CCCCCCHHCCCCCHH	51.82	-
414	Phosphorylation	EPLQKHQSLDLGSLL CCCHHCCCCCHHHHH	24.46	20058876
419	Phosphorylation	HQSLDLGSLLFEGCS CCCCCHHHHHHCCCC	29.24	28450419
429	Ubiquitination	FEGCSNSKPVNAAGR HCCCCCCCCCCCHHH	58.18	-
441	Ubiquitination	AGRYFNSKVPITRTK HHHHCCCCCCCCCCC	53.81	-
447	Phosphorylation	SKVPITRTKSTPFEL CCCCCCCCCCCHHHH	22.24	23401153
448	Ubiquitination	KVPITRTKSTPFELI CCCCCCCCCCHHHHH	49.38	-
449	Phosphorylation	VPITRTKSTPFELIQ CCCCCCCCCHHHHHH	40.47	23401153
450	Phosphorylation	PITRTKSTPFELIQQ CCCCCCCCHHHHHHC	33.29	28122231
451	Ubiquitination	ITRTKSTPFELIQQR CCCCCCCHHHHHHCC	28.01	-
461	Ubiquitination	LIQQRETKEVDSKEN HHHCCCCCCCCCHHC	51.49	-
466	Ubiquitination	ETKEVDSKENFSYLE CCCCCCCHHCCHHHH	52.81	-
493	Phosphorylation	AQKVMHVSSAELNYS CCEEEEECHHHCCCC	14.78	26434552
494	Phosphorylation	QKVMHVSSAELNYSL CEEEEECHHHCCCCC	25.36	26434552
499	Phosphorylation	VSSAELNYSLPYDSK ECHHHCCCCCCCCCH	24.98	28796482
500	Phosphorylation	SSAELNYSLPYDSKH CHHHCCCCCCCCCHH	23.07	28796482
503	Phosphorylation	ELNYSLPYDSKHQIR HCCCCCCCCCHHHHC	37.84	27080861
505	Phosphorylation	NYSLPYDSKHQIRNA CCCCCCCCHHHHCCC	26.62	27080861
506	Ubiquitination	YSLPYDSKHQIRNAS CCCCCCCHHHHCCCH	36.31	-
526	Phosphorylation	DSSALGVYSYIPLVE CCCCCCEEEECCCCC	8.24	-
527	Phosphorylation	SSALGVYSYIPLVEN CCCCCEEEECCCCCC	17.74	-
528	Phosphorylation	SALGVYSYIPLVENP CCCCEEEECCCCCCC	6.72	-
536	Phosphorylation	IPLVENPYFSSWPPS CCCCCCCCCCCCCCC	27.89	-
550	Phosphorylation	SGTSSKMSLDLPEKQ CCCCCCEECCCCCCC	23.59	28348404
585	Ubiquitination	YNSHDSLSLNSPTNI CCCCCCCCCCCCCCH	29.47	-
592	Ubiquitination	SLNSPTNISSLLNQE CCCCCCCHHHHHCHH	3.05	-
594	Ubiquitination	NSPTNISSLLNQESA CCCCCHHHHHCHHCH	32.83	-
609	Ubiquitination	VLATAPRIDDEIPPP HHHCCCCCCCCCCCC	8.35	-
635	Phosphorylation	VEEAGEFSPNVPKSL EEECCCCCCCCCCCH	15.97	28348404
640	Ubiquitination	EFSPNVPKSLSSAVK CCCCCCCCCHHCCEE	60.80	-
647	Ubiquitination	KSLSSAVKVKIGTSL CCHHCCEEEEECCCC	37.21	-
649	Ubiquitination	LSSAVKVKIGTSLEW HHCCEEEEECCCCCC	29.69	-
653	Phosphorylation	VKVKIGTSLEWGGTS EEEEECCCCCCCCCC	21.05	-
663	Ubiquitination	WGGTSEPKKFDDSVI CCCCCCCCCCCCCEE	63.12	-
664	Ubiquitination	GGTSEPKKFDDSVIL CCCCCCCCCCCCEEE	65.82	-
675	Ubiquitination	SVILRPSKSVKLRSP CEEECCCCCEECCCC	63.05	-
684	Phosphorylation	VKLRSPKSELHQDRS EECCCCCHHHCCCCC	49.10	28464451
691	Phosphorylation	SELHQDRSSPPPPLP HHHCCCCCCCCCCCC	56.33	23401153
692	Phosphorylation	ELHQDRSSPPPPLPE HHCCCCCCCCCCCCH	42.17	23911959
715	Ubiquitination	ADEDCMQAQSIETYS CCHHHHHCCCCEEEC	4.35	-
741	Phosphorylation	SSKQTLKTPGKSFTR CCCCCCCCCCCCCCH	40.15	23532336
744	Ubiquitination	QTLKTPGKSFTRSKS CCCCCCCCCCCHHHH	43.53	-
745	Phosphorylation	TLKTPGKSFTRSKSL CCCCCCCCCCHHHHH	37.45	30622161
747	Phosphorylation	KTPGKSFTRSKSLKI CCCCCCCCHHHHHHH	40.92	30622161
749	Phosphorylation	PGKSFTRSKSLKILR CCCCCCHHHHHHHHH	24.44	30622161
751	Phosphorylation	KSFTRSKSLKILRNM CCCCHHHHHHHHHHC	35.82	30622161
770	Ubiquitination	CNSCPPNKPAESVQS HHCCCCCCCCHHHCC	51.91	-
793	Phosphorylation	FGFANRFSKPKGPRN CCCCCCCCCCCCCCC	44.82	24719451

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
35	S	Phosphorylation	Kinase	PKCD	Q05655	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
35	S	Phosphorylation		18056643
Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability to dephosphorylate and inactivate the SRC family kinases.

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 PTN22_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRB2_HUMAN	GRB2	physical	11882361
SPTA1_HUMAN	SPTA1	physical	16461343
TERA_HUMAN	VCP	physical	16461343
VAV_HUMAN	VAV1	physical	16461343
ZAP70_HUMAN	ZAP70	physical	16461343
LCK_HUMAN	LCK	physical	16461343
ACTS_HUMAN	ACTA1	physical	16461343
CD3E_HUMAN	CD3E	physical	16461343
CD3Z_HUMAN	CD247	physical	16461343
PTN22_HUMAN	PTPN22	physical	10068674
CBL_HUMAN	CBL	physical	10068674
PPIP2_HUMAN	PSTPIP2	physical	27880917
TBC31_HUMAN	TBC1D31	physical	27880917
KIF7_HUMAN	KIF7	physical	27880917
CSK_HUMAN	CSK	physical	27880917
LZTS2_HUMAN	LZTS2	physical	27880917
CP131_HUMAN	CEP131	physical	27880917
PIBF1_HUMAN	PIBF1	physical	27880917
MOONR_HUMAN	KIAA0753	physical	27880917
MIB1_HUMAN	MIB1	physical	27880917
MED4_HUMAN	MED4	physical	27880917
ADIP_HUMAN	SSX2IP	physical	27880917
CC138_HUMAN	CCDC138	physical	27880917
PTN22_HUMAN	PTPN22	physical	27432908
PPIP2_HUMAN	PSTPIP2	physical	27432908
CSK_HUMAN	CSK	physical	27432908
MD2BP_HUMAN	MAD2L1BP	physical	27432908
NDUBA_HUMAN	NDUFB10	physical	27432908
KAP2_HUMAN	PRKAR2A	physical	27432908
ARK72_HUMAN	AKR7A2	physical	27432908
NDUA9_HUMAN	NDUFA9	physical	27432908
CALR_HUMAN	CALR	physical	27432908
CALU_HUMAN	CALU	physical	27432908
TPC_HUMAN	SLC25A19	physical	27432908
CAB45_HUMAN	SDF4	physical	27432908
MAIP1_HUMAN	C2orf47	physical	27432908
AROS_HUMAN	RPS19BP1	physical	27432908
SFXN4_HUMAN	SFXN4	physical	27432908
EIF3E_HUMAN	EIF3E	physical	27432908
HSPB1_HUMAN	HSPB1	physical	27432908
RCN1_HUMAN	RCN1	physical	27432908
ACAD8_HUMAN	ACAD8	physical	27432908
DHE3_HUMAN	GLUD1	physical	27432908
HAX1_HUMAN	HAX1	physical	27432908
SCO2_HUMAN	SCO2	physical	27432908

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
152700	Systemic lupus erythematosus (SLE)
222100	Diabetes mellitus, insulin-dependent (IDDM)
180300	Rheumatoid arthritis (RA)
193200	Vitiligo (VTLG)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PTN22_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases."; Yu X., Sun J.P., He Y., Guo X., Liu S., Zhou B., Hudmon A.,Zhang Z.Y.; Proc. Natl. Acad. Sci. U.S.A. 104:19767-19772(2007). Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-294 IN COMPLEX WITHINHIBITOR, FUNCTION, PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OFSER-35 AND THR-36.	18056643 [Abstract]

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