dbPTM

KRI1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KRI1_SCHPO
UniProt AC	Q09799
Protein Name	Protein kri1
Gene Name	kri1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	598
Subcellular Localization	Nucleus, nucleolus.
Protein Description	Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA (By similarity)..
Protein Sequence	MPRKKSAAKKAREALVQKKVINSNVPTDKKSIDQLQENVTSKSHLLEESSSEDEEINSFQINEEYAKRFEHNKKREELQKLEAKYGEQMANGVDGEGSDESSSEEEEDSDGELVTPEVDAAILRMIVKIRNKDPDLYDSQQKYFDEVEKDVQGSLKSKDGFRSVTLKDYHRQKLLSGEILDAEEDEPMPNDANPTHVEEQERLRKETIAAFHDVNGNKDAVSNESDEDGDFLVKKEKTKKQLEEEEHGYERFLLESAQSKEARKVLEDLSSSYVKQRPSVLVNTEDDENGIKPSDEDFLLKYMMNRGWRTSNTKQPSYEEIIDEVDAENRFDEDAEEFENKFNFRFEEEAGSQIVSHPRNVADSLRRKDDSRKRARDRKKERLEEASQKRLEEVNRLKNLKRKELEEKLNQVIEIAGSKNIDVSKLDLDEDFDPEKWESKMSEIFNENYYEEDSAKKPEFGDDIDIDDIAQVDNGSEDLGSIENKTVEDTGNREKSKKSLRKDIREKKRKIDEYVEEKYGVPEAVIVKNSKFRYQQVAPETFGLDILDILNASDADLNNYVGLKKMTPYRTPEEIARDKKKYGKKKRLREWKKQVFGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	VQKKVINSNVPTDKK HHHHHHCCCCCCCHH	28.25	28889911
27	Phosphorylation	VINSNVPTDKKSIDQ HHCCCCCCCHHHHHH	57.05	28889911
43	Phosphorylation	QENVTSKSHLLEESS HHHCCCHHHHHHCCC	21.09	25720772
49	Phosphorylation	KSHLLEESSSEDEEI HHHHHHCCCCCCCHH	29.77	24763107
50	Phosphorylation	SHLLEESSSEDEEIN HHHHHCCCCCCCHHH	40.81	24763107
51	Phosphorylation	HLLEESSSEDEEINS HHHHCCCCCCCHHHH	59.34	24763107
207	Phosphorylation	QERLRKETIAAFHDV HHHHHHHHHHHHHCC	20.96	27738172
222	Phosphorylation	NGNKDAVSNESDEDG CCCCCCCCCCCCCCC	36.28	28889911
225	Phosphorylation	KDAVSNESDEDGDFL CCCCCCCCCCCCCEE	51.02	28889911
476	Phosphorylation	IAQVDNGSEDLGSIE HHCCCCCCCCCCCCC	33.90	28889911
481	Phosphorylation	NGSEDLGSIENKTVE CCCCCCCCCCCCCHH	33.74	21712547

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 KRI1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KRI1_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 KRI1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KRI1_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of KRI1_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-222; SER-225 ANDSER-476, AND MASS SPECTROMETRY.	18257517 [Abstract]