dbPTM

IPK1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IPK1_SCHPO
UniProt AC	Q9USK0
Protein Name	Inositol-pentakisphosphate 2-kinase
Gene Name	ipk1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	640
Subcellular Localization	Nucleus.
Protein Description	Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate..
Protein Sequence	MPLKNYTKTTSKKEPKQLDIAASDQQIEQWSDQIHKLDKAIRSTIDNSRLFYDAWRCMVCIAPSVTASWISLYRQLPPEKQPAASVGTLVDWNKALERQRREVLLALQNFHVIVIAPCKEVKGYVKKAVEMIKRRDKKVKELEKIQKELLVVYELPDPETKKSKIKALQSQLVRVNGELDDLQKHLTLSFPTLIAKSRVFFGQLMKHFYCLQLQMFRKMHNIVRPWDCFQDDIPQTWLVEFSSVCQAAESISLIAVNNNRPPVELPKSGDVLSNREWEAGKIDAMNSLIAQNLHTSASQVSLSPMASTASSSVTNSPVDTHTPSTPIMSRPPSMKALSSGVESQDESVASSNFQVPIISNPLFKSPAPYSPTSVISNHSSTGKSLVISEWAYLASGSANVVFEYVGKNPYFQDKVIRLRRRGQVFTTEQVYEYYQNVIYPLFAGMESFLIEVFLQPVTRDFLLAAQNASGIYLNLNEQYCLVMKDLKDGIEMKPKWLTQSPAAPPDWVVCRTCALSRMRGRPVGFCPLQLDFNNWPKFLCCLQGFVSPDIAMRLFQSGILRKLRDLQEQYSRTDVALAMTLRDVTLYIGKDHITLLDLDPKDMNTKMSKWERDERNLIEGGWYYGRGMKSTDKACRSSIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
273	Phosphorylation	PKSGDVLSNREWEAG CCCCCCCCCCCCCCC	33.42	24763107
287	Phosphorylation	GKIDAMNSLIAQNLH CHHHHHHHHHHHHHC	14.20	27738172
295	Phosphorylation	LIAQNLHTSASQVSL HHHHHHCCCCHHEEC	29.20	27738172
298	Phosphorylation	QNLHTSASQVSLSPM HHHCCCCHHEECCCC	30.77	27738172
301	Phosphorylation	HTSASQVSLSPMAST CCCCHHEECCCCCCC	18.59	27738172
303	Phosphorylation	SASQVSLSPMASTAS CCHHEECCCCCCCCC	12.72	27738172
338	Phosphorylation	PPSMKALSSGVESQD CCCHHHHHCCCCCCC	29.88	25720772
343	Phosphorylation	ALSSGVESQDESVAS HHHCCCCCCCHHHHC	40.29	29996109
347	Phosphorylation	GVESQDESVASSNFQ CCCCCCHHHHCCCCC	31.13	25720772
365	Phosphorylation	ISNPLFKSPAPYSPT ECCCCCCCCCCCCCC	20.96	21712547
369	Phosphorylation	LFKSPAPYSPTSVIS CCCCCCCCCCCCEEE	29.41	21712547
370	Phosphorylation	FKSPAPYSPTSVISN CCCCCCCCCCCEEEC	22.20	28889911
372	Phosphorylation	SPAPYSPTSVISNHS CCCCCCCCCEEECCC	29.68	28889911
373	Phosphorylation	PAPYSPTSVISNHSS CCCCCCCCEEECCCC	22.34	29996109
376	Phosphorylation	YSPTSVISNHSSTGK CCCCCEEECCCCCCC	26.74	25720772
379	Phosphorylation	TSVISNHSSTGKSLV CCEEECCCCCCCEEE	33.57	25720772
380	Phosphorylation	SVISNHSSTGKSLVI CEEECCCCCCCEEEE	33.36	25720772
381	Phosphorylation	VISNHSSTGKSLVIS EEECCCCCCCEEEEE	52.20	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 IPK1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IPK1_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 IPK1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
IPK1_SCHPO	ipk1	physical	26771498

Drug and Disease Associations

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

Regulatory Network of IPK1_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 THR-372, AND MASSSPECTROMETRY.	18257517 [Abstract]