SLD2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SLD2_SCHPO
• UniProt AC: O14216
• Protein Name: DNA replication regulator sld2
• Gene Name: drc1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 337
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Has a role in the initiation of DNA replication. Required at S-phase checkpoint..
• Protein Sequence: MHDESRTKQISSIKALLKKWEHEYVHTNNCKPSKEDVKKQPEIALLYKQYYELKRESSITPKKAKTKVDFKFQTPTKQRAETEANESPKAPRNDYLQVTPKTVDKSLLGPTPQLSRRVLNLLEDMSPIADSHVDQISDIKHNTSEISSTMIPTTPSKNPEPVAQHTPTVLETPSSYRLQVYTSPNLLRVNAPCRKSLSEMLRELKDIEDDYGSNEEKILQEFESFSSSSSESLVDRDISQPMKKKIKRQNRLVKLPPSMNLSKSHLEGLPEIDEDAENGIDDNEDTTASKDSSPFLDLQSERQNKKIMRNGLVIGKQVSQNYSSYKLKKRKFRRHRS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
57	Phosphorylation	YYELKRESSITPKKA HHHHHHHCCCCCCCC	30.95	24763107
60	Phosphorylation	LKRESSITPKKAKTK HHHHCCCCCCCCCCC	30.88	28889911
74	Phosphorylation	KVDFKFQTPTKQRAE CEEEEECCCCHHHHH	35.74	28889911
82	Phosphorylation	PTKQRAETEANESPK CCHHHHHHHCCCCCC	39.14	21712547
87	Phosphorylation	AETEANESPKAPRND HHHHCCCCCCCCCCC	31.35	28889911
99	Phosphorylation	RNDYLQVTPKTVDKS CCCCCCCCCCCCCHH	13.20	28889911
102	Phosphorylation	YLQVTPKTVDKSLLG CCCCCCCCCCHHHHC	34.83	24763107
106	Phosphorylation	TPKTVDKSLLGPTPQ CCCCCCHHHHCCCHH	25.10	21712547
111	Phosphorylation	DKSLLGPTPQLSRRV CHHHHCCCHHHHHHH	23.13	29996109
115	Phosphorylation	LGPTPQLSRRVLNLL HCCCHHHHHHHHHHH	16.88	21712547
126	Phosphorylation	LNLLEDMSPIADSHV HHHHHHCCHHCHHCH	26.02	21712547
154	Phosphorylation	SSTMIPTTPSKNPEP CCCCCCCCCCCCCCC	21.88	28889911
156	Phosphorylation	TMIPTTPSKNPEPVA CCCCCCCCCCCCCCH	42.86	24763107
166	Phosphorylation	PEPVAQHTPTVLETP CCCCHHCCCCEEECC	14.47	29996109
172	Phosphorylation	HTPTVLETPSSYRLQ CCCCEEECCCCEEEE	25.06	29996109
181	Phosphorylation	SSYRLQVYTSPNLLR CCEEEEEECCCCEEE	6.63	29996109
182	Phosphorylation	SYRLQVYTSPNLLRV CEEEEEECCCCEEEC	38.56	29996109
183	Phosphorylation	YRLQVYTSPNLLRVN EEEEEECCCCEEECC	8.29	28889911
286	Phosphorylation	GIDDNEDTTASKDSS CCCCCCCCCCCCCCC	20.34	21712547
293	Phosphorylation	TTASKDSSPFLDLQS CCCCCCCCCCCCCCH	29.79	24763107

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
60	T	Phosphorylation	Kinase	CDK1	P04551	GPS
74	T	Phosphorylation	Kinase	CDK1	P04551	GPS
87	S	Phosphorylation	Kinase	CDK1	P04551	GPS
99	T	Phosphorylation	Kinase	CDK1	P04551	GPS
111	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
154	T	Phosphorylation	Kinase	CDK1	P04551	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SLD2_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SLD2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK1_SCHPO	cdc2	physical	11937031
RAD4_SCHPO	rad4	physical	21593208
RAD4_SCHPO	rad4	physical	21945095
GOS1_SCHPO	gos1	genetic	22681890
YF48_SCHPO	SPAC3H5.08c	genetic	22681890
VPS38_SCHPO	vps38	genetic	22681890

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-183, AND MASSSPECTROMETRY.
PubMed: 18257517

"CDK phosphorylation of Drc1 regulates DNA replication in fissionyeast.";
Noguchi E., Shanahan P., Noguchi C., Russell P.;
Curr. Biol. 12:599-605(2002).
Cited for: FUNCTION, INTERACTION WITH RAD4, SUBCELLULAR LOCATION, PHOSPHORYLATIONAT THR-60; THR-74; SER-87; THR-99 AND THR-154, AND MUTAGENESIS OFTHR-60; THR-74; SER-87; THR-99 AND THR-154.
PubMed: 11937031