dbPTM

TSYL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TSYL2_HUMAN
UniProt AC	Q9H2G4
Protein Name	Testis-specific Y-encoded-like protein 2
Gene Name	TSPYL2
Organism	Homo sapiens (Human).
Sequence Length	693
Subcellular Localization	Nucleus . Cytoplasm. Enriched in transcriptionally active regions of chromatin in neurons..
Protein Description	Part of the CASK/TBR1/TSPYL2 transcriptional complex which modulates gene expression in response to neuronal synaptic activity, probably by facilitating nucleosome assembly. May inhibit cell proliferation by inducing p53-dependent CDKN1A expression..
Protein Sequence	MDRPDEGPPAKTRRLSSSESPQRDPPPPPPPPPLLRLPLPPPQQRPRLQEETEAAQVLADMRGVGLGPALPPPPPYVILEEGGIRAYFTLGAECPGWDSTIESGYGEAPPPTESLEALPTPEASGGSLEIDFQVVQSSSFGGEGALETCSAVGWAPQRLVDPKSKEEAIIIVEDEDEDERESMRSSRRRRRRRRRKQRKVKRESRERNAERMESILQALEDIQLDLEAVNIKAGKAFLRLKRKFIQMRRPFLERRDLIIQHIPGFWVKAFLNHPRISILINRRDEDIFRYLTNLQVQDLRHISMGYKMKLYFQTNPYFTNMVIVKEFQRNRSGRLVSHSTPIRWHRGQEPQARRHGNQDASHSFFSWFSNHSLPEADRIAEIIKNDLWVNPLRYYLRERGSRIKRKKQEMKKRKTRGRCEVVIMEDAPDYYAVEDIFSEISDIDETIHDIKISDFMETTDYFETTDNEITDINENICDSENPDHNEVPNNETTDNNESADDHETTDNNESADDNNENPEDNNKNTDDNEENPNNNENTYGNNFFKGGFWGSHGNNQDSSDSDNEADEASDDEDNDGNEGDNEGSDDDGNEGDNEGSDDDDRDIEYYEKVIEDFDKDQADYEDVIEIISDESVEEEGIEEGIQQDEDIYEEGNYEEEGSEDVWEEGEDSDDSDLEDVLQVPNGWANPGKRGKTG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Sumoylation	PDEGPPAKTRRLSSS CCCCCCCCCCCCCCC	48.62	28112733
11	Ubiquitination	PDEGPPAKTRRLSSS CCCCCCCCCCCCCCC	48.62	-
16	Phosphorylation	PAKTRRLSSSESPQR CCCCCCCCCCCCCCC	29.97	22167270
17	Phosphorylation	AKTRRLSSSESPQRD CCCCCCCCCCCCCCC	42.59	23401153
18	Phosphorylation	KTRRLSSSESPQRDP CCCCCCCCCCCCCCC	38.42	30266825
20	Phosphorylation	RRLSSSESPQRDPPP CCCCCCCCCCCCCCC	28.42	29255136
163	Sumoylation	PQRLVDPKSKEEAII CHHCCCCCCCCCEEE	70.47	28112733
165	Sumoylation	RLVDPKSKEEAIIIV HCCCCCCCCCEEEEE	66.74	28112733
182	Phosphorylation	EDEDERESMRSSRRR CCHHHHHHHHHHHHH	26.22	28102081
185	Phosphorylation	DERESMRSSRRRRRR HHHHHHHHHHHHHHH	21.39	27251275
186	Phosphorylation	ERESMRSSRRRRRRR HHHHHHHHHHHHHHH	21.31	24719451
235	Ubiquitination	AVNIKAGKAFLRLKR HHCHHHHHHHHHHHH	40.60	-
303	Phosphorylation	VQDLRHISMGYKMKL HHHHCHHHHCCCEEE	10.46	-
306	Phosphorylation	LRHISMGYKMKLYFQ HCHHHHCCCEEEEEE	10.16	-
311	Phosphorylation	MGYKMKLYFQTNPYF HCCCEEEEEECCCCC	6.52	-
339	Phosphorylation	SGRLVSHSTPIRWHR CCCCEECCCCCCCCC	28.51	17494752
340	Phosphorylation	GRLVSHSTPIRWHRG CCCEECCCCCCCCCC	19.81	22817900
384	Ubiquitination	DRIAEIIKNDLWVNP HHHHHHHHCCCCCCH	50.50	23000965
406	Ubiquitination	RGSRIKRKKQEMKKR HCHHHHHHHHHHHHH	54.53	30230243
407	Methylation	GSRIKRKKQEMKKRK CHHHHHHHHHHHHHC	56.37	23644510
407	Trimethylation	GSRIKRKKQEMKKRK CHHHHHHHHHHHHHC	56.37	-
414	Acetylation	KQEMKKRKTRGRCEV HHHHHHHCCCCCEEE	51.99	30593129
428	Ubiquitination	VVIMEDAPDYYAVED EEEECCCCCCCHHHH	42.32	21890473
498	Phosphorylation	ETTDNNESADDHETT CCCCCCCCCCCCCCC	38.84	22468782
504	Phosphorylation	ESADDHETTDNNESA CCCCCCCCCCCCCCC	35.71	22468782
525	Phosphorylation	PEDNNKNTDDNEENP CCCCCCCCCCCCCCC	46.47	21815630
658	Phosphorylation	GNYEEEGSEDVWEEG CCCCCCCCCCHHHCC	33.62	-
668	Phosphorylation	VWEEGEDSDDSDLED HHHCCCCCCCCCHHH	38.73	-
671	Phosphorylation	EGEDSDDSDLEDVLQ CCCCCCCCCHHHHHC	49.43	-

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
20	S	Phosphorylation	Kinase	CDK2	P24941	PSP
340	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
20	S	Phosphorylation	11395479
Phosphorylation at Ser-20 and/or Thr-340 impairs function on cell proliferation.
340	T	Phosphorylation	11395479
Phosphorylation at Ser-20 and/or Thr-340 impairs function on cell proliferation.

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 TSYL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PSMD3_HUMAN	PSMD3	physical	21829568

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 TSYL2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-18 AND SER-20, AND MASSSPECTROMETRY.	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-16 AND SER-17, AND MASSSPECTROMETRY.	17081983 [Abstract]
"SET-related cell division autoantigen-1 (CDA1) arrests cell growth."; Chai Z., Sarcevic B., Mawson A., Toh B.-H.; J. Biol. Chem. 276:33665-33674(2001). Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION ATSER-20 AND THR-340, MUTAGENESIS OF SER-20 AND THR-340, AND FUNCTION.	11395479 [Abstract]

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