dbPTM

YF2E_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YF2E_SCHPO
UniProt AC	O13779
Protein Name	Putative metal ion transporter C17A12.14
Gene Name	SPAC17A2.14, SPAC17G6.01
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	617
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description
Protein Sequence	MPSNTSRSVPTGFYYKQNARMQNRPRFSDRKHSSKSKHRFPVDPSLQPDEADEGTRLLGNSDSDLLEPPSEHSSNGEDDKDINNPPSMPSSVCSSPKSPHRHYESDEDIENISLPESHPEDIQRKEFETENGKNTRDQPSPLAEVSDFAISSPHVYPKSANSHDSHYEQFANNDVTESAVDDHPATRKLSRDELYLPISPNNAQEPKFSVLDEWTKKMVANFEEYSVEDVDKRRERNRKLSEPLLVNGRYRVRDRWAQFRKSEIEKPYRFTFFTDELPSTIHSHEMWELVHDGQSFEDLFHSGGTWWLDVSCPKEEEIRVLAKAFGIHPLTVEDITLEEDREKVELFRTYYFVTFRSFNQLPSNSEYLKPLNFYLVVFRDGIITFHMNPTPHPANVRRRIRQLNGYLTVNADWIAYALLDDTTDAFAPFIEQIEDEVDTIDSMILSIHYDHVMEVKPQERMLQRVGECRKLIMSLLRLLANKADVVRGLSKRCNESWQVAPRGEIALYLGDVQDHIVTMVQNLNHYEKILSRSHSNYLAQISINMTLVSNETNEVLSRLTILGTILIPLNLVTGLWGMNVKVPGQDVPGLGWFFSILGSLMIFAISSFILCKWYKVI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MPSNTSRSVPTGFYY CCCCCCCCCCCCHHH	32.01	29996109
105	Phosphorylation	SPHRHYESDEDIENI CCCCCCCCHHHHHCC	38.85	28889911
113	Phosphorylation	DEDIENISLPESHPE HHHHHCCCCCCCCHH	49.83	28889911
117	Phosphorylation	ENISLPESHPEDIQR HCCCCCCCCHHHHHH	42.26	25720772
135	Phosphorylation	ETENGKNTRDQPSPL CCCCCCCCCCCCCCC	38.82	21712547
140	Phosphorylation	KNTRDQPSPLAEVSD CCCCCCCCCCCCCCC	27.23	21712547
146	Phosphorylation	PSPLAEVSDFAISSP CCCCCCCCCEEECCC	20.65	21712547
151	Phosphorylation	EVSDFAISSPHVYPK CCCCEEECCCCCCCC	34.09	24763107
152	Phosphorylation	VSDFAISSPHVYPKS CCCEEECCCCCCCCC	16.95	28889911
156	Phosphorylation	AISSPHVYPKSANSH EECCCCCCCCCCCCC	11.25	25720772
159	Phosphorylation	SPHVYPKSANSHDSH CCCCCCCCCCCCCHH	28.33	25720772
162	Phosphorylation	VYPKSANSHDSHYEQ CCCCCCCCCCHHHHH	28.52	28889911
165	Phosphorylation	KSANSHDSHYEQFAN CCCCCCCHHHHHHCC	23.65	21712547
167	Phosphorylation	ANSHDSHYEQFANND CCCCCHHHHHHCCCC	18.51	29996109
190	Phosphorylation	HPATRKLSRDELYLP CHHHCCCCCCEEECC	40.49	28889911
195	Phosphorylation	KLSRDELYLPISPNN CCCCCEEECCCCCCC	14.37	25720772
199	Phosphorylation	DELYLPISPNNAQEP CEEECCCCCCCCCCC	21.45	28889911
226	Phosphorylation	VANFEEYSVEDVDKR HHHCHHCCHHHHHHH	23.47	28889911
241	Phosphorylation	RERNRKLSEPLLVNG HHHHHCCCCCCEECC	39.96	28889911

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 YF2E_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YF2E_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 YF2E_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of YF2E_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of YF2E_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-105; SER-152; SER-162;SER-226 AND SER-241, AND MASS SPECTROMETRY.	18257517 [Abstract]