PIF1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIF1_SCHPO
• UniProt AC: Q9UUA2
• Protein Name: ATP-dependent DNA helicase pfh1
• Gene Name: pfh1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 805
• Subcellular Localization: Isoform Nuclear: Nucleus, nucleolus . Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair.; Isoform Mitochondrial: Mitochondrion .
• Protein Description: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Involved in the maintenance of mitochondrial (mtDNA). Required for both repair of mitochondrial DNA and recognition of a recombinogenic signal characterized by a 26-bp palindromic at sequence in the ery region of mitochondrial DNA. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. Required for the completion of S-phase..
• Protein Sequence: MFSCQSLYKFSHSFRKRIPVMFQRAQQKSSLLHTQNESSHQPSLNKLGGFSSASLNFNSSRSSTNDDQQTFSSQSDNLPSSPITLPAKRGRSAASLKQLDNTVGFDVSKPSLPVFENSGLGSKYSTEIANGVYIDENDFDDDLLLENDIDQKPIPWSSSPIEHTKLTKSMLSSEKRSKNHLSKIYEDHTSEKGASSVISSNITRQGIKRSRTLPWAVDPYRYGDPDPKRTSTSADISQHTVSNDSSNKLSNGRSSSLDSLAKKRMSKSKSTPQISKKFSVPLNSASKSPIGSSLFKTSDSRKKSVPSIFLSDEQKRILDMVVEQQHSIFFTGSAGTGKSVLLRKIIEVLKSKYRKQSDRVAVTASTGLAACNIGGVTLHSFAGVGLARESVDLLVSKIKKNKKCVNRWLRTRVLIIDEVSMVDAELMDKLEEVARVIRKDSKPFGGIQLVLTGDFFQLPPVPENGKESKFCFESQTWKSALDFTIGLTHVFRQKDEEFVKMLNELRLGKLSDESVRKFKVLNRTIEYEDGLLPTELFPTRYEVERSNDMRMQQINQNPVTFTAIDSGTVRDKEFRDRLLQGCMAPATLVLKVNAQVMLIKNIDDQLVNGSLGKVIGFIDDETYQMEKKDAEMQGRNAFEYDSLDISPFDLPDVKQKKYKLIAMRKASSTAIKWPLVRFKLPNGGERTIVVQRETWNIELPNGEVQASRSQIPLILAYAISIHKAQGQTLDRVKVDLGRVFEKGQAYVALSRATTQEGLQVLNFSPAKVMAHPKVVQFYKQLASVNGLPIRNENKAPVQMRGVKNK

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
62	Phosphorylation	LNFNSSRSSTNDDQQ EECCCCCCCCCCCCH	43.38	29996109
63	Phosphorylation	NFNSSRSSTNDDQQT ECCCCCCCCCCCCHH	30.07	29996109
80	Phosphorylation	SQSDNLPSSPITLPA CCCCCCCCCCCCCCC	52.49	28889911
81	Phosphorylation	QSDNLPSSPITLPAK CCCCCCCCCCCCCCC	20.55	28889911
84	Phosphorylation	NLPSSPITLPAKRGR CCCCCCCCCCCCCCC	30.03	29996109
254	Phosphorylation	NKLSNGRSSSLDSLA CCCCCCCCCHHHHHH	26.19	24763107
255	Phosphorylation	KLSNGRSSSLDSLAK CCCCCCCCHHHHHHH	33.29	21712547
256	Phosphorylation	LSNGRSSSLDSLAKK CCCCCCCHHHHHHHH	37.13	28889911
259	Phosphorylation	GRSSSLDSLAKKRMS CCCCHHHHHHHHHHH	35.20	21712547
288	Phosphorylation	PLNSASKSPIGSSLF CCCCCCCCCCCCCCC	21.18	24763107
292	Phosphorylation	ASKSPIGSSLFKTSD CCCCCCCCCCCCCCC	25.29	21712547
764	Phosphorylation	GLQVLNFSPAKVMAH CCEECCCCHHHHHCC	23.91	28889911

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PIF1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIF1_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 PIF1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPOD_SCHPO	cdc6	genetic	15302919
DPOD3_SCHPO	cdc27	genetic	15302919
SWI1_SCHPO	swi1	genetic	22426534
PCNA_SCHPO	pcn1	physical	22308326
RAD22_SCHPO	rad52	genetic	22426535
MUS81_SCHPO	mus81	genetic	22426535

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-80 AND SER-81, AND MASSSPECTROMETRY.
PubMed: 18257517