dbPTM

CSX2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CSX2_SCHPO
UniProt AC	Q9UUE2
Protein Name	Protein csx2
Gene Name	csx2
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	870
Subcellular Localization
Protein Description
Protein Sequence	MTGHVDPVHFERLKIQSVTFGSANDNASLQVHNVSKSPEYSKYSYSRKNNEPIEFIQLREEEGPIVKVEEEDGLTLRFQLEFHAQEGKRDVTNLTCVYGTSPQQLDRLITREFSSDANFQNNHQVFLIGNIEFHSNENSKKIEWTWSNQSLHTLYFRNGGSPIYLCFAEYDKRLNCLVPLKTFQFYVTESDQDSTPATPFPMPMHLAEETATSPEISDAPPLSGNVDPLPINSPPLTNPVARDIDQTEPEDGPLFRATILNYERTTHDMRMVLKKLIKRIEHVAHSHGLLYMSYKELMSAFERVATINPPAFKPFLDHYYAAAAQSFDSFNIDRARLLRNFLIEPLRKIYDTDIKNVSTKKKDFEETSRDYYTSLSRYLSKSEKETSSDKTKESKFAAKKRDFELSRFDYYSYMQDINGGRKGQEVLSVLTSFAANDYNLIHSSLTDIDALRPSIIQLQDIVTEANKEFQLLRAEREERRRYIETSSRELEDKDAEIAAQAYKAKVDQDTSAKQGLLLAFSKSTSDLQVVGKSGWHKYWVVLDHGKICEYANWKQSLELHTEPIDLLMATVRPAQSVSRKFCFEVITPQTKRTYQATSKAEMHSWIEAIQYSISESIVQKGKGTSMNSEETSVKHGPTSTIGKALQRVASVTSPSRHNSDSKEKKQTKSPSLVKTLKEMHSSDQSCADCNTTARVEWCAINFPVVLCIDCSGIHRSLGTHITKIRSLTLDKFNPETVDLLYATGNSFVNEIYEGGITDWKIKNFENQERRVQFVKDKYLYKRFIKSSFSHDPNTGLLESIEHSNLKEAVLCLALGADVNYQRAVVKALLKNNYLIAELLTLNGASLNVDEVTMETLSARAQAFVMNRATP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
380	Phosphorylation	TSLSRYLSKSEKETS HHHHHHHCCCCCCCC	25.79	21712547
524	Phosphorylation	LLAFSKSTSDLQVVG HHEEECCCCCEEEEC	29.96	25720772
525	Phosphorylation	LAFSKSTSDLQVVGK HEEECCCCCEEEECC	43.33	28889911
624	Phosphorylation	IVQKGKGTSMNSEET HHHCCCCCCCCCCCC	28.43	21712547
625	Phosphorylation	VQKGKGTSMNSEETS HHCCCCCCCCCCCCC	25.32	28889911
628	Phosphorylation	GKGTSMNSEETSVKH CCCCCCCCCCCCCCC	28.33	24763107
631	Phosphorylation	TSMNSEETSVKHGPT CCCCCCCCCCCCCCC	34.47	21712547
632	Phosphorylation	SMNSEETSVKHGPTS CCCCCCCCCCCCCCC	32.23	21712547
638	Phosphorylation	TSVKHGPTSTIGKAL CCCCCCCCCHHHHHH	42.99	21712547
639	Phosphorylation	SVKHGPTSTIGKALQ CCCCCCCCHHHHHHH	22.59	24763107
640	Phosphorylation	VKHGPTSTIGKALQR CCCCCCCHHHHHHHH	35.91	24763107
650	Phosphorylation	KALQRVASVTSPSRH HHHHHHHHCCCCCCC	24.07	28889911
652	Phosphorylation	LQRVASVTSPSRHNS HHHHHHCCCCCCCCC	32.21	25720772
653	Phosphorylation	QRVASVTSPSRHNSD HHHHHCCCCCCCCCC	20.79	28889911
655	Phosphorylation	VASVTSPSRHNSDSK HHHCCCCCCCCCCCH	46.03	28889911
659	Phosphorylation	TSPSRHNSDSKEKKQ CCCCCCCCCCHHHHH	36.82	21712547
661	Phosphorylation	PSRHNSDSKEKKQTK CCCCCCCCHHHHHCC	42.40	21712547
789	Phosphorylation	RFIKSSFSHDPNTGL HHHHHHHCCCCCCCH	29.00	25720772

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
Oops, there are no upstream regulatory protein records of CSX2_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CSX2_SCHPO !!

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 CSX2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CSX2_SCHPO	cnt5	physical	26771498

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CSX2_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; SER-653 ANDSER-655, AND MASS SPECTROMETRY.	18257517 [Abstract]