wanglab/gogpt-training-data huggingface dataset:
Protein: Dehydrogenase pkfF (EC 1.1.-.-) (Q5B8A1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone. The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA. Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E. The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Interaction partners:
- Short-chain dehydrogenase/reductase pkfC
- Mediator of RNA polymerase II transcription subunit 17
- FAD-dependent monooxygenase pkfD
Sequence:
MRHTALLPLVSSFIVPALAQIPGQTTVNATVNQGRFGNATYDYVIVGGGTSGLAIAARLAEDPSLSVAVIEAGGYYELDGTVASIIPGLAAGANVGTDATEYSTVDWNFQAQPLTSANDRSLRYNRGKTLGGSSARHYMVYQRGTRGSYDQWAELTGDESWGWDSVFPYFQRSVNVTPANMTGRFPNTTVTYDPSGFNKAGGPLHVTWPNYGSPWSTWIEQGLEAIGILPDTDFNTGTLNGSSWAPITINPLSQKRDSSETSFLQQSLKTTNLTVYLHTMALKIGFDGTTASSVDVRSPVGRFTLSARREIIVSAGALQSPQLLMVSGIGPRETLERHGIPVVKELAGVGQKMWEHPFFGITHQVNLVTATELAINQQALLQALNQYKSQQGPLTSAGFGVLGWEKLPNSTLSDSTNEALATFPSDWPTIEYLSIDGYLNGWHSAADQATGNGQQWGTIAVALVAPLSRGNVTISSSDMDDPPVFDLGFLTHPADREIAVAAMRRIRQAFAAISEITIGDEVVPGADVSTDEELLDFIRESIVPVYHVAGTCAMGREDDPEAVVDPQARVIGVNNLRVVDASIFPTLPPGHPQSTCYMVAEKIADLIKKGN
Protein: Zinc finger protein 503 (NocA-like zinc finger protein 2) (Q6UFS5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for segmental gene expression during hindbrain development. May function as a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:14709556}.
Interaction partners:
Sequence:
MITSPSASRNSDTDLVWESSSSSSRNNSSAVASKPFLHSVPPSDPLRQANRLPIKILKMLTARTGHILHPEYLQPLPSTPVSPIELDAKKSPLALLAQTCSQIGKPDPPPSSKLSSVTSNGSSEKESKSGPLKLSDIGVEDKSSFKPYSKPADKKDSSSGVSSGEKSGFRVPSATCQPFTPRTGSPNSSTSASPMPSDGKGERDEKKDSDCNKNCSSDGSAPTSVSHSRISVSCAGINVEVNQHQETTSGSKASATSDSVSCVTSSSSASVLGSGLVAPVSPYKPGQTVFPLPPAGMTYPGSLAGAYAGYPQHFLPHGGSLVNAQLASSLGCSKAGSSPLAGASPPSIMSASLCRDPYCLSYHCASHLAGAAGASCTHDSAAAAAASALKSGYPLMYPTHPLHGVHSSPPSFGGHPLYPYGFMLPNDPLPHVCNWVSANGPCDKRFSSSEELLNHLRTHTAFTGTEKLISGYPSSSSLASAAAAAMACHMHMPPSGAPGSPGTLALRSPHHALGLSSRYHPYSKSPLPTPGAPVPVPAATGPYYSPYALYGQRLTTASALGYQ
Protein: Acyltransferase helD1 (EC 2.3.1.-) (Helvolic acid biosynthesis cluster protein D1) (Q4WR21)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Interaction partners:
- Cytochrome P450 monooxygenase helB3
- Cytochrome P450 monooxygenase helB1
Sequence:
MESIPLSPFDLQGSFSNIPYAFFYENTQSENDFMPFDFLKGSLWASLQRFPILTGRLRARSTGHIVVEVDAGNPNQPDIRETLCDSVHWSQLKESSFAWDAWPAGVATVGPVATAAADGEIKLLNIHVMRLAQNSGVILFINIPHYVVDGVGYFAFINHWAETMRMQQQQQEQENEARSRFSFDRGIIQRYLPTERAPLDPLTASIYGQRNLLVDWLAWLSPTTLGGLLSKTAAMARGEAHLFRIPRASLDQVHKDVQPYIPASARLSDNDLLVALISKTYIQSQPQPKPPTGFLSWLRPGQGQPESHCTVRIPCDVRRHLKVRERYTGNLLLGMMVRTPLAELARPTSSETLAAAALNVRQSIERVQPGLVAAYHDLIQANPTSHMRPLAFTATRTTTSLVTTSQVRFPMYEADFGSGKPCFVCLTPVFAGSYTMAAILPTPEGREGGVYVLLTSNVEAMQGIKKNQYWNGLVEIIW
Protein: Vacuolar protein sorting-associated protein 20 (O94318)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole.
Subcellular location: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein sorting-associated protein 24
- Vacuolar protein-sorting-associated protein 36
- ESCRT-III complex subunit did4
- Suppressor protein of bem1/bed5 double mutants
- Vacuolar protein-sorting-associated protein 46
- Vacuolar-sorting protein snf7
- Vacuolar-sorting protein dot2
- Vacuolar protein sorting-associated protein 28 homolog
- Uncharacterized protein C162.06c
Sequence:
MGVNSSKINDKDRSILSIKEQRDKLLRYSKRLEKIEQLEIDIARKCLRDSDKRGALRALKAKKLYSGLITQTYGQLGNIEQLLSTIEFTLIQKDVMFGLQEGTNLIRQLQADMPLERVGRICNDRDEAMSYVDEVNDMLQGRMSRDQEDEIQEELDSLIREQEDEKVKDLEKPGFTPSTGVDVLPSVPLKNAIPSLDESFPKAASVSNTSSAVVIDEELRKDPVLG
Protein: SREBP regulating gene protein (SREBF pathway regulator in Golgi 1) (Q8BTG6)
Organism: Mus musculus (Mouse)
Function: Positively regulates hepatic SREBP signaling pathway by modulating the proper localization of SCAP (SREBP cleavage-activating protein) to the endoplasmic reticulum, thereby controlling the level of functional SCAP. Plays a crucial role during embyrogenesis.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H741}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLNLAALLWRRLLRKRWVLALVFGLSLVYFLSSTFKQEERAVRDRNLLQVQDREQPIPWKVQFNLGNSSRPSNQCRNSVQGKHLLTDELGYVCERKDLLANGCCDVSVPSTKQYCCDGCLANGCCEAYEYCVSCCLQPSKQLLLERFLNRAAVAFQNLFMAVEDHFELCLAKCRTSSQSVQHENTYRDPIAKYCYGESPPELFPA
Protein: 78 kDa glucose-regulated protein (Binding-immunoglobulin protein) (Heat shock protein 70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Q7SZD3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MRLLCLFLLVAGSVFAEEDDKKESVGTVIGIDLGTTYSCVGVYKNGRVEIIANDQGNRITPSYVAFTTEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWGDSSVQQDIKYFPFKVIEKKNKPHIQLDIGSGQMKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKRDGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSAQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDPKKPDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGEEETGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEDIERMVNEAERFADEDKKLKERIDSRNELESYAYSLKNQIGDKEKLGGKLSSEDKEAIEKAVEEKIEWLEAHQDADLEEFQAKKKELEEVVQPIVSKLYGSAGGPPPEEAEEKDEL
Protein: Phytoene synthase 1, chloroplastic (EC 2.5.1.32) (P37271)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reaction from prephytoene diphosphate to phytoene.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:25675505, ECO:0000269|PubMed:26224804}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- Prolycopene isomerase, chloroplastic
- Zeta-carotene desaturase, chloroplastic/chromoplastic
- Violaxanthin de-epoxidase, chloroplastic
- Lycopene beta cyclase, chloroplastic
- Zeaxanthin epoxidase, chloroplastic
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2
- Lycopene epsilon cyclase, chloroplastic
- Protein ORANGE, chloroplastic
Sequence:
MSSSVAVLWVATSSLNPDPMNNCGLVRVLESSRLFSPCQNQRLNKGKKKQIPTWSSSFVRNRSRRIGVVSSSLVASPSGEIALSSEEKVYNVVLKQAALVNKQLRSSSYDLDVKKPQDVVLPGSLSLLGEAYDRCGEVCAEYAKTFYLGTLLMTPERRKAIWAIYVWCRRTDELVDGPNASHITPMALDRWEARLEDLFRGRPFDMLDAALADTVARYPVDIQPFRDMIEGMRMDLKKSRYQNFDDLYLYCYYVAGTVGLMSVPVMGIDPKSKATTESVYNAALALGIANQLTNILRDVGEDARRGRVYLPQDELAQAGLSDEDIFAGKVTDKWRNFMKMQLKRARMFFDEAEKGVTELSAASRWPVWASLLLYRRILDEIEANDYNNFTKRAYVGKVKKIAALPLAYAKSVLKTSSSRLSI
Protein: TEA domain transcription factor 1 (E9PKB7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRYVLSWCVTVTFKDQTAKDKALQHMAAMSSAQIVSATAIHNKLGLPGIPRPTFPGAPGFWPGMIQTGQPGSSQDVKPFVQQAYPIQPAVTAPIPGFEPASAPAPSVPAWQGRSIGTTKLRLVEFSAFLEQQRDPDSYNKHLFVHIGHANHSYSDPLLESVDIRQIYDKFPEKKGGLKELFGKGPQNAFFLVKFWADLNCNIQDDAGAFYGVTSQYESSENMTVTCSTKVCSFGKQVVEKVETEYARFENGRFVYRINRSPMCEYMINFIHKLKHLPEKYMMNSVLENFTILLVVTNRDTQETLLCMACVFEVSNSEHGAQHHIYRLVKD
Protein: XPC (Xeroderma Pigmentosum group C) DNA repair gene homolog (Q9N4C3)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- UV excision repair protein RAD23
- XPA C-terminal domain-containing protein
- Uncharacterized calcium-binding protein R08D7.5
- DNA repair and recombination protein RAD54-like
- DNA repair endonuclease XPF
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- BSD domain-containing protein
- ERCC1-like central domain-containing protein
- General transcription and DNA repair factor IIH helicase subunit XPD
- XPG
Sequence:
METRRRSSRLQQQTTSDLNAREEPQPSEPPVKRARGAKKNEAPSTAPMPPKTTKKSTKPSRKQGSPIEAELDEMGFELENEEEAEIVVQKSKKNGRKLVKIDENLRISAENGSKSSNFLEENRMEIDEKPGNLAKKSSKNGSRVVKSDEKSENLVQSVPKSTTNGSKVAIIEDDPEIRAENGVKSSKSDEKPDFSAQNGSKLAQNAPNRISRPRRSVTTAKKVSYVPSDDQLELSSSSSELESSSEDEDTEIRPKTGSKIAKKREKSFKISESESSSESPDDESEASEASEDPSIPGPSEPRKRRKIQRKSTLSSGGATTKDLHWPKCSKASIARKTGNPGSKNAAKKPAKSSLRMAQKQKPDQPWKKNLKDYETDRKLAKGERRMLEYRHVAHAYVARGKIEEITYDEAYKLHEMMKKAYFAGRSLLDAAVLDPVEFEKSQKNVKKSEKNDEKNTAGDSSSSEDEWEEMEHFQPPIIDDNIEVSIDHEGGGGDDGEEVVKDWWAIYLRQEINRKIREMWENTHKVHLLCFMAHLKFVVKIALDESLVPSLMMSQLPNGYLKFIGEPVVPIDIMKNLVKWFADAFRPLNGVVSVASIEQDSLLEGHEARYPETRRLTALVDAKCFETDLDRATLLFCLLRGLELTTRLVVNVRAIPRRWDKTQQKELQNELSKFRELSRSRSTTPGEKSLEIQEKSGEKSQKPAKKGQKSEKKAAKKVVVEERNYWVEYWQPREKRWICVDPLHKSVDEPLSIHEHSASPISYVFAIDNKQGICEVSQRYAMDCVKQDFRRRRTNPKWVAWTLFLPPFAANSERKKWEMMQMREDLVKRPLPTVMSEYKNHPLYALEKDLLKFEAIYPPPATQKPLGQIRGHNVYPRSTVFTLQGENNWLKLARSVKIGEKPYKIVKARPDPRIPVEDREDKFLDVYGYWQTEKYRRPPLKNGKIPHNEYGNVYMFNENMCPLDCTYLKLSGLVQISRKLGKQCIPAVVGWAFDGGFTHPVIDGAIVLEKDAIDFINAWEKLESGRAEKEEKQRVEKIHENWKKLIKGMLRLAYVRKQFGHPAAEKPTKRQKIGGKTEEIEENEGGAGPPSSVDHITDNTEQITPMHGFSLDDFINKKK
Protein: Acyltransferase 3 domain-containing protein (Q9HTB2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glycosyltransferase
- Class I SAM-dependent methyltransferase
- Glycosyltransferase
- Methyltransferase type 11 domain-containing protein
- DUF1127 domain-containing protein
- Glycosyltransferase WbpX
- GDP-6-deoxy-D-mannose reductase
- Alginate biosynthesis protein AlgA
- Glycosyltransferase WbpY
- Spore protein YkvP/CgeB glycosyl transferase-like domain-containing protein
Sequence:
MSGKRILDIELLRGLAVLGVVFHHLHGNLFSGSPALLDGINQRVQFWWGVDLFFAISGFVIARTLIPQLREAPTRQAFWEQARYFWIRRAFRLLPSAWLWLALILACCLLLNRSGAFGSLSANLAASLAGFLQVANFRFADSFYRYEYGASFVYWSLSLEEQFYLLLPLLILCLRRYLGWALLALVLVQFFSLRTPLLMVLRTDALAIGVLLALASLQPGYARWNPTLLGRAWSGPLLLAAVAAALGVLASEAYSLVAVRIGAIALLCGLLVWIASYDRDYLLSNGPLKRLLVWVGARSYAIYLIHIPAFYLSRELCFRLGWDAGERPLSLLGTSLVLIVVLSELNYRFVESPCRDLGSRLVKRLSAARRVATTSGATSC
Protein: Kinesin-like protein KIFC1 (Q9QWT9)
Organism: Mus musculus (Mouse)
Function: Minus end-directed microtubule-dependent motor required for bipolar spindle formation. May contribute to movement of early endocytic vesicles. Regulates cilium formation and structure.
Subcellular location: Nucleus {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972, ECO:0000269|PubMed:23807208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. Early endosome {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}. Note=Associated with nucleus during interphase, centrosomes in early and spindle in later mitosis. {ECO:0000269|PubMed:16638812, ECO:0000269|PubMed:17360972}.
Interaction partners:
- Kinesin-like protein
- Kinesin-like protein KIF11
- Kinesin-like protein KIF2C
- Kinesin-like protein KIF20A
- Kinesin-like protein KIF18B
- Disks large-associated protein 5
- Kinesin-like protein KIF22
- Kinesin-like protein KIF15
- Kinesin-like protein KIF18A
- Cell division cycle protein 20 homolog
Sequence:
MDVQAQRPPLLEVKRNVELKAALVKSSSRVPLSASRLKRGPDQMEDALEPAKKRTRVMGAVTKVDTSRPRGPLLSTVSQTQGHTAAQKGPKKTGPRGCSAIGTVLRSQKPVPAAPAQKPGTSTAPVVVGKRAGKRPAWDLKGQLCDLNEELKRYREKTQTLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQERRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNIRVFCRVRPVLEGESTPSPGFLVFPPGPAGPSDPPTGLSLSRSDDRRSTLTGAPAPTVRHDFSFDRVFPPGSKQEEVFEEIAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDPQLEGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYNETVRDLLATGPRKGQGGECEIRRASPGSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISGEHAARGLQCGAPLNLVDLAGSERLDPGLHLGPGERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIGTAQANKK
Protein: Rab-related protein 4 (O18337)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADRAIKLLVIGESGVGKSSLIRRFVENKFDQNHDVTIGMDFKSKVMQVDGIDYKVALWDTAGAERFRSLTASFYRKALGAILVYDITSRDSLVKLETWLAELDSYSDNPNIAIIVVGNKIDEERVVDREEGRKFARKHRALFIETSAKCDQFVSDVFKDVVEKIVSSEYFNNGNASAGLDIASDRDLEASASTCYC
Protein: Uncharacterized WD repeat-containing protein C2E1P5.05 (Q9P7C0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Probable U3 small nucleolar RNA-associated protein 7
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 6
- Uncharacterized protein C1604.06c
- Nucleolar protein 56
- KRR1 small subunit processome component homolog
- Nucleolar protein 58
- 13 kDa ribonucleoprotein-associated protein
- U3 small nucleolar RNA-associated protein 10
- U3 small nucleolar RNA-associated protein 22
Sequence:
MSDPFFTRPEHRKRKARSATSKREKENQKLERNGPANEDLASISSESEFNGFEDEIDEENEDTYETAAEKRLRLAREYLDEVKNELVEDGGFDAKEVDRELLASRLKEDVLEKKGQMYLDYTSKINPDVKIETAQLRGRHMRPLVGVVAYENFVYSADKSGLIQKWEALQEKDTENRENDDHEIGKAIKLHFRPIKFSRSRRGENDHVKEITCLAISNDGRWIVTGGLDHRIVIRDSVTLEPQHCWKHHRDAVMGLAMRRGTNEMFSCSADRSIKVWSLDQMSYIETLFGHQDVIFGVDALARERCVSVGGRDRTSRLWKIVEESQLVFRSGGTSMKATAGYMEGSVDCVAMIDEDHFVTGSDNGVIALWSVQRKKPLFTYPLAHGLDPILAPGRHSAETSPDPVTIPPQPRWITSLAAIPYSNLFASGSWDGNIRLWKIAEGLRSFEPLTIATPLSVYGCINSLSLSLQGKGKQSEVRVFAACGRETRVGRWKTLRGIPNSGFVFNIPLTVIPSVTDGDEIDE
Protein: Jonah 99Fi (EC 3.4.21.-) (TA01126p1) (Q9VA66)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Jonah 25Biii
- Jonah 99Fii
- Peptidase S1 domain-containing protein
- trypsin
- Jonah 65Aii
- Jonah 44E, isoform A
- Zinc carboxypeptidase A 1
- Peptidase S1 domain-containing protein
- Serine protease 3
- Jonah 25Bii, isoform A
Sequence:
MKLLVFLALAVAAATAIPTPEQKLVPTPVKDVKIQGRITNGYPAYEGKVPYIVGLLFSGNGNWWCGGSIIGNTWVLTAAHCTNGASGVTINYGASLRNQPQYTHWVGSGNFVQHHHYNSGNLHNDISLIRTPHVDFWHLVNKVELPSYNDRYQDYAGWWAVASGWGGTYDGSPLPDWLQAVDVQIMSQSDCSRTWSLHDNMICINTNGGKSTCGGDSGGPLVTHEGNRLVGVTSFVSSAGCQSGAPAVFSRVTGYLDWIRDNTGISY
Protein: Cyclic nucleotide-binding protein, putative (Q381G5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSYEYPDYAMGDHDWLLTRTDVPSCDDILQGTEPVQPFTVPPLPPQRQGSRRYAQIVENINMNSVFTDWEKRAIVSRLRRCEPLNEENFLRRLSNVKARNEVEYLENVRMRGAELKARAQNELRAAYEHERPRREYIFRRHLNLKNVLIEEVRQHRAARWYTIITSHVFLTVLIKERRDYEAMEKIKFRLLPIIKRRLAVQRKRMLAAELTRDNLDKIPFPTPSIIHRMQGTFFDGWPNKLLEQLGHKARPLYLKEGSYLMHEGDVDRCMYMITAGTISVIMNDREKGKRRIKENSKACFTLSPPCYVGEFALVCKEPRSASIICETDVGVWSVPPEGFEEVAQQLSQEIKSKQREATDVRRRANLQRFFPLRVEFLRSFPYFVQFSNAALENIISKAEPIVLHNNDHLFSKSELDPSAYFIQDGVAVLLEASGNQRLVPRGSCVGIFECACSVNERKKCTIISQNYCDIWRISREALMDVGMSEPAAFLYCRGAAKSHRAMEVEKPCAVPRSLSKDPFIQFCLTRQLMMRMWEMSVPTIFLNDEKLVIQGQKFQRFVIIHSGVCETTISTEEGEYATVRITVSGDASPGGDVVSPYESISRRRSLADKLFISRILGAYEYASLKTHYTYTVTSYGLTEAFLVDVAAFEKSVPPELKAIMHNNKKSQELISLCQTEHNASYLTNSVNQSFVHLYRKSKEFMAKR
Protein: Cell division suppressor protein YneA (Q8Y7H6)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: Inhibits cell division during the SOS response. Affects a later stage of the cell division protein assembly, after the assembly of the Z ring, by probably suppressing recruitment of FtsL and/or DivIC to the division machinery.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02014}.
Interaction partners:
- UPF0291 protein lmo1304
- Protein RecA
- LexA repressor
- GMP synthase
Sequence:
MTLKLIWDKFYVSIIFVLTCIVLGIILMCTVVGGGSDYSEVNVNEGDSLWALADQYAGKSDMAKADFVSWVEKENNLSDGHVEAGDSVVIPVHKTKLLKSDSTIQLANQ
Protein: Mical-like 2b (Protein-methionine sulfoxide oxidase mical2b (EC 1.14.13.225)) (F1QAZ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Ras-related protein Rab-13
- small monomeric GTPase
- small monomeric GTPase
- MICAL-like protein 2a
- Actinin, alpha 1
- Actinin, alpha 4.
Sequence:
MAAVKALQQWCKIQCEGYRDVSITNMTTSFRDGLAFCALIHKHRPDLIDFDSLSKENIYENNQRAFEVAEKELGIPALLDAEDMVALKVPDRLSILTYVSQYYNYFHGRSPIGGMGGIKRPAEESNEAPSGKKNPPVIAKVLPSPKPATENKTPKPANENKREVLTERANKSSTPSSNCSVCNQHVHLVQRHLVDGKLYHRNCFKCKECSTILLSGTYKAGKEPGTFICKTHTSIEKPLTTRFTAPSKTQSTFINKPDQSALGGSTGKASLNTNTSKLGWLANKSDRIPMRGFTDTPTPAVQLTPTAKATPTPDTTTAKSPSGPRSATESLKPVSNTVQKNQEARMRFFESSSSSPSSVVPASKSTSSYTSTTSVSTAGVKTTAPETTTPRVPAGAGKGRVLLRVGDWAKSQDTEKEKENEKEKEKAKAVIGKMVKVDKDSNSSSASPAGLKANSSNVPPLESNAKAPFGRVRLKALEASGETTAPATTVPSWMKEKSLSRNVNTPSSNSKENDTVPSDWRSMLKPVSKPVSNLESKGLPARRTEAVSSPKTSVPASSTTTISISISSSKTPLTTPLKNGSKPNDSSSVFPVSPSGTETHKSHKPGYIPKEDIQKELKEIEMNMNELEKKGVELEKQLRQCDEDGEEDALMNDLMVDWFTLIRNKQVYMRRESELVYIARTQDLEEEQPSVDAELRRLMEKPDHLKTLWDRKREEELMAKLVEIVNDRNAIVEGLDEDRLREEEEDEQLNKMMQSFDMKKEKVKKMSPVTRWFSMRKRRSSED
Protein: Large ribosomal subunit protein eL42A (60S ribosomal protein L42-A) (L41) (YL27) (YP44) (P0CX27)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MVNVPKTRKTYCKGKTCRKHTQHKVTQYKAGKASLFAQGKRRYDRKQSGFGGQTKPVFHKKAKTTKKVVLRLECVKCKTRAQLTLKRCKHFELGGEKKQKGQALQF
Protein: Presenilin-associated rhomboid-like protein, mitochondrial (EC 3.4.21.105) (Mitochondrial intramembrane cleaving protease PARL) [Cleaved into: P-beta (Pbeta)] (Q9H300)
Organism: Homo sapiens (Human)
Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals (By similarity). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain. Required for processing of CLPB into a form with higher protein disaggregase activity by removing an autoinhibitory N-terminal peptide.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17116872, ECO:0000269|PubMed:22354088}; Multi-pass membrane protein {ECO:0000269|PubMed:17116872}.; SUBCELLULAR LOCATION: [P-beta]: Nucleus {ECO:0000269|PubMed:17116872}. Note=Translocated into the nucleus by an unknown mechanism (PubMed:17116872). {ECO:0000269|PubMed:17116872}.
Interaction partners:
- ATP-dependent zinc metalloprotease YME1L1
- Serine/threonine-protein kinase PINK1, mitochondrial
- Serine protease HTRA2, mitochondrial
- Dynamin-like GTPase OPA1, mitochondrial
- Prohibitin-2
- Stomatin-like protein 2, mitochondrial
- HCLS1-associated protein X-1
- Metalloendopeptidase OMA1, mitochondrial
- Mitofusin-1
- Serine/threonine-protein phosphatase PGAM5, mitochondrial
Sequence:
MAWRGWAQRGWGCGQAWGASVGGRSCEELTAVLTPPQLLGRRFNFFIQQKCGFRKAPRKVEPRRSDPGTSGEAYKRSALIPPVEETVFYPSPYPIRSLIKPLFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVLVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYVGKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK