dbPTM

FAS1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FAS1_SCHPO
UniProt AC	Q9UUG0
Protein Name	Fatty acid synthase subunit beta
Gene Name	fas1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	2073
Subcellular Localization
Protein Description	Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase..
Protein Sequence	MVEAEQVHQSLRSLVLSYAHFSPSILIPASQYLLAAQLRDEFLSLHPAPSAESVEKEGAELEFEHELHLLAGFLGLIAAKEEETPGQYTQLLRIITLEFERTFLAGNEVHAVVHSLGLNIPAQKDVVRFYYHSCALIGQTTKFHGSALLDESSVKLAAIFGGQGYEDYFDELIELYEVYAPFAAELIQVLSKHLFTLSQNEQASKVYSKGLNVLDWLAGERPERDYLVSAPVSLPLVGLTQLVHFSVTAQILGLNPGELASRFSAASGHSQGIVVAAAVSASTDSASFMENAKVALTTLFWIGVRSQQTFPTTTLPPSVVADSLASSEGNPTPMLAVRDLPIETLNKHIETTNTHLPEDRKVSLSLVNGPRSFVVSGPARSLYGLNLSLRKEKADGQNQSRIPHSKRKLRFINRFLSISVPFHSPYLAPVRSLLEKDLQGLQFSALKVPVYSTDDAGDLRFEQPSKLLLALAVMITEKVVHWEEACGFPDVTHIIDFGPGGISGVGSLTRANKDGQGVRVIVADSFESLDMGAKFEIFDRDAKSIEFAPNWVKLYSPKLVKNKLGRVYVDTRLSRMLGLPPLWVAGMTPTSVPWQFCSAIAKAGFTYELAGGGYFDPKMMREAIHKLSLNIPPGAGICVNVIYINPRTYAWQIPLIRDMVAEGYPIRGVTIAAGIPSLEVANELISTLGVQYLCLKPGSVEAVNAVISIAKANPTFPIVLQWTGGRAGGHHSFEDFHSPILLTYSAIRRCDNIVLIAGSGFGGADDTEPYLTGEWSAAFKLPPMPFDGILFGSRLMVAKEAHTSLAAKEAIVAAKGVDDSEWEKTYDGPTGGIVTVLSELGEPIHKLATRGIMFWKELDDTIFSLPRPKRLPALLAKKQYIIKRLNDDFQKVYFPAHIVEQVSPEKFKFEAVDSVEDMTYAELLYRAIDLMYVTKEKRWIDVTLRTFTGKLMRRIEERFTQDVGKTTLIENFEDLNDPYPVAARFLDAYPEASTQDLNTQDAQFFYSLCSNPFQKPVPFIPAIDDTFEFYFKKDSLWQSEDLAAVVGEDVGRVAILQGPMAAKHSTKVNEPAKELLDGINETHIQHFIKKFYAGDEKKIPIVEYFGGVPPVNVSHKSLESVSVTEEAGSKVYKLPEIGSNSALPSKKLWFELLAGPEYTWFRAIFTTQRVAKGWKLEHNPVRRIFAPRYGQRAVVKGKDNDTVVELYETQSGNYVLAARLSYDGETIVVSMFENRNALKKEVHLDFLFKYEPSAGYSPVSEILDGRNDRIKHFYWALWFGEEPYPENASITDTFTGPEVTVTGNMIEDFCRTVGNHNEAYTKRAIRKRMAPMDFAIVVGWQAITKAIFPKAIDGDLLRLVHLSNSFRMVGSHSLMEGDKVTTSASIIAILNNDSGKTVTVKGTVYRDGKEVIEVISRFLYRGTFTDFENTFEHTQETPMQLTLATPKDVAVLQSKSWFQLLDPSQDLSGSILTFRLNSYVRFKDQKVKSSVETKGIVLSELPSKAIIQVASVDFQSVDCHGNPVIEFLKRNGKPIEQPVEFENGGYSVIQVMDEGYSPVFVTPPTNSPYAEVSGDYNPIHVSPTFAAFVELPGTHGITHGMYTSAAARRFVETYAAQNVPERVKHYEVTFVNMVLPNTELITKLSHTGMINGRKIIKVEVLNQETSEPVLVGTAEVEQPVSAYVFTGQGSQEQGMGMDLYASSPVARKIWDSADKHFLTNYGFSIIDIVKHNPHSITIHFGGSKGKKIRDNYMAMAYEKLMEDGTSKVVPVFETITKDSTSFSFTHPSGLLSATQFTQPALTLMEKSAFEDMRSKGLVQNDCAFAGHSLGEYSALSAMGDVLSIEALVDLVFLRGLTMQNAVHRDELGRSDYGMVAANPSRVSASFTDAALRFIVDHIGQQTNLLLEIVNYNVENQQYVVSGNLLSLSTLGHVLNFLKVQKIDFEKLKETLTIEQLKEQLTDIVEACHAKTLEQQKKTGRIELERGYATIPLKIDVPFHSSFLRGGVRMFREYLVKKIFPHQINVAKLRGKYIPNLTAKPFEISKEYFQNVYDLTGSQRIKKILQNWDEYESS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
363	Phosphorylation	LPEDRKVSLSLVNGP CCCCCCEEEEEECCC	18.44	28889911
365	Phosphorylation	EDRKVSLSLVNGPRS CCCCEEEEEECCCCE	23.82	25720772
381	Phosphorylation	VVSGPARSLYGLNLS EEECCHHHHHCCCCC	28.22	25720772
383	Phosphorylation	SGPARSLYGLNLSLR ECCHHHHHCCCCCHH	22.33	25720772
417	Phosphorylation	RFINRFLSISVPFHS HHHHHHHCCCCCCCC	15.31	25720772
419	Phosphorylation	INRFLSISVPFHSPY HHHHHCCCCCCCCCC	21.99	29996109
432	Phosphorylation	PYLAPVRSLLEKDLQ CCHHHHHHHHHHHCC	37.22	25720772
544	Phosphorylation	IFDRDAKSIEFAPNW EECCCCCCCCCCCCC	29.13	25720772
723	Phosphorylation	FPIVLQWTGGRAGGH CCEEEEECCCCCCCC	19.46	25720772
1122	Phosphorylation	HKSLESVSVTEEAGS HHCCCCCEEECCCCC	32.38	28889911
1870	Phosphorylation	HRDELGRSDYGMVAA CHHCCCCCCCCEEEC	33.13	25720772
2072	Phosphorylation	QNWDEYESS------ HCHHHHCCC------	40.21	24763107
2073	Phosphorylation	NWDEYESS------- CHHHHCCC-------	32.09	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 FAS1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FAS1_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 FAS1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of FAS1_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of FAS1_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-1122 AND SER-2073, ANDMASS SPECTROMETRY.	18257517 [Abstract]