GCN1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GCN1_SCHPO
• UniProt AC: Q10105
• Protein Name: eIF-2-alpha kinase activator gcn1 {ECO:0000250|UniProtKB:P33892}
• Gene Name: gcn1 {ECO:0000312|PomBase:SPAC18G6.05c}
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 2670
• Subcellular Localization: Cytoplasm .
• Protein Description: Acts as a positive activator of the gcn2 protein kinase activity in response to amino acid starvation. Component of the gcn1-gcn20 complex that forms a complex with gcn2 on translating ribosomes; during this process, gcn1 seems to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of gcn2, and hence stimulating gcn2 kinase activity. Participates in the repression of global protein synthesis and in gene-specific mRNA translation activation, such as the transcriptional activator gcn4, by promoting the gcn2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/tif211) on 'Ser-52', and hence allowing gcn4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion..
• Protein Sequence: MSVEEPGIEAHGHKDRMLYAMLLSKDTSLAFLGSKKIMIDILQHICRTQDIDEESAIAALEDIFETLPRNLSRDARKQIEITINHLVSRLPSIVLPFLVRRLTTIAGRLDRFRSTVSVSFDCLNWVNSMIPNLPEKELQYWILELLPLQSSFLSYALRDGKPSVADSAIKSTRRCYRSLFCKKMDSLKKLVSFLLTETENAILPPKSLPLYGVIISTCYYFHQSPNPRNEISQQAELFSKIMAQNVLMAKPALEKYLYHEFCYSLGLLLSVDQLKLYLLPSIEKALLRSPEIIFSGILSSLAHGFADSKVDASSLILSSVLTSFVNGLKSSNAEVRRNCFQTFKDLSANASDNESLSRVASELITSLRTGKVTASDQRVLFVDALSSLSLKHIDASMLLNELLPLFTKAKESDFNSLASLIVKTLKFLLMNGRNPGDKIYDFLSKSLQRPVAHESMFWLTSLATMAWDLPASDDVQIEFINFFLNNLSILTEKALMSVSGATQNGTYLAPIIYLSFGVNKLSVWNSERISHTLELQDILVKLSTPKNNDVFIFSSKITNKLNDDQSKLWYFQGLCDFAKVSDNLLFSNFVERWFQSVIGVFSFASRENSNRALKILKSAILYRPHLRMSICSQLWNYHADFEKSKSVGKFDSAKYDEISSLFQSLILSSMSADTSNFSNQELVDFDKYLVELLFLSFAFKDKFDWIRFCQVSKRDPATLVSERIHSIIEEIELLLSSAIKDSKETAAIASISMIVFVAPEESIPLFVNVFRNQLLHLNISSVSSTDLEIWKTPEGVLWDNVLEKKSSKKLDKNTKDYETKRWEAEVRAKQSAKKPAKLSKDQQALVDAQLDAEAKIRSRVNLIALSLERGLGIIRSLGEAVQLAPALWVEDAIDVLLFHNVLKYSEPFLKNLAYDTFLLTLKASGFSERLGDRSYSSSLASILAHTFSVNSSENIKELTKSILYKLRFAIEQNYFEPQMFACIFPLLYDLTFNITNSDEEDEAELQLLVTEILEFQALYSASLRRMRSKLIKSLLHLLEIAPTQYQENKNSLLSLCEGLHSTYTDEELNLLLSNLFHPESSIRSAVLQALQAFDLSRFEFIKEIFLELYDDNETNASIAHQISTQNGLDATETSFFELQIFFTQDSDYLQQIIGKSLIDLLDEFEELGQFIPKELMRTYRENALPSAPEYDEYGIIKKETIGRDLGRIARESVAVSFFHISKYLSSNLLLPFLEFLLTASEAEAQIPVTDASQKVSSKMLEAGKLAIFQSGAHQVEALMELFEQKLNVDSLPTDANDRLREATVVLFGTVAQHLPSNDPRLAVVMDSLLSVLSTPSESVQLAVAVCLPPLVKKSLGKSKEYYELLSNKLMNSTSLADQKGAAYGLAGLVKGYGIKAFQDFNILDSLSELISNRQNATHRQVALFAVEAFSRILGIYFEPYLPDLLPLLLTSFGDNANEVREATMDAVKQIMSQLSAFGVKLLLPTLLDGLNEYNWRSKKASVEILGLMSYMAPKQLSVFLPTIIPKLSEVLTDSHSQVRNTANKSLLRFGDVISNPEIQTLVPTLLKALSDCTRYTDDALEALLKTSFVHYLDPPSLALVIPILKYGLRERNAGTKRQSAKIFGLMASLTEPENLAVYLESLMPRLREVLIDPVPDTRATAAKALGSLIEKLGEKKFPTLIPELFNVLRSECSEVDRQGAAQGLSEILAGLGLARLEDVLPEILKNTSSPVPHIRESFISLLIYLPATFGSRFQPYLARAIPPILSGLADDSELVQTASLRAAKMIVNNYATKSVDLLLPELEKGLFDNAWRIRLSSVQLVGDLVFKLAGINRKALQEDEEEEGTHSDVSRKALLDIIGQERHDRILSTLYIVRQDIAAVVRTPAIQIWKAIVVNTPRTVREILPTLTSIIVSNLNSSSNDRRTMCVKSLGDLLKKAGFDVLPQLLPVLKQGLESANSGDRIGVCIALEELINSATPEQLEIYSDDFVYAVRRALMDGDLEVRETAAEAFDSLQSILGDRAVDDVLPQLLKLLESENQSEQALSALREIISRRSSTIFPVLIPTLIKKPVSAFNARALSSLAQVAGVTLNKRLPSILNALMESSLASTGDDLVALNGAIDKVNLSVKDQEGLQILMAHFYSFSESEDFRKRLFAAEHMLVFFQNCKLDYYRYVGDWVRHFITLFEDKSQDVVVAAVAAQNTLVSALRKDQLDSLVSIAYHSLRDVGSQGVNLPAFEVAQGVNSILPIFLYGLMHGTMDQREQSALGIADIVLKTEPSKLRPFVTQITGPLIRIIGERFPVEVKCAILYTLNIILSKISTFLRPFLPQLQRTFAKCLGDPSSEVIRSRAATALGTLITLQTRLAPIITELVSGARTPDAGVRKAMLNALFAVVSKSGQNMNEASAEAIEQLLDEISAESSEHMVICAKLYGALFSHLPDAQAKQLLESKVLSLEIQSEFSVLILNAAVKFGSQKIIELKLSDIVCSIISTASLQKEVTIAENGILALGKALLADIPQSFGNAKNLVEALKVNIEAPPSTSQDSRRLALLIIRVVSKENYSLIKPHISILAPAIFGCVRAIVIPVKLAAEAAFLALFQLVEDDSVLNKYIETLEGPRARSFVDYSRRVAVKLAAAERDRINSGSERVKLEEVEDLAEINAVGRDNEVSTNDP

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
2	Phosphorylation	------MSVEEPGIE ------CCCCCCCCC	49.92	24763107
1794	Phosphorylation	VNNYATKSVDLLLPE HHHHHHHCHHHHHHH	19.26	25720772
2055	Phosphorylation	EIISRRSSTIFPVLI HHHHHCCCCHHHCHH	24.58	25720772
2056	Phosphorylation	IISRRSSTIFPVLIP HHHHCCCCHHHCHHH	28.08	25720772

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

Oops, there are no upstream regulatory protein records of GCN1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GCN1_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 GCN1_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of GCN1_SCHPO !!

Drug and Disease Associations

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