wanglab/gogpt-training-data huggingface dataset:
Protein: Phenolphthiocerol/phthiocerol polyketide synthase subunit B (EC 2.3.1.292) ((Phenol)carboxyphthiodiolenone synthase subunit B) (Beta-ketoacyl-acyl-carrier-protein synthase I) (Phthiocerol synthesis polyketide synthase type I PpsB) (P9WQE5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the PpsABCDE complex involved in the biosynthesis of the lipid core common to phthiocerols and phenolphthiocerols by successive additions of malonyl-CoA or methylmalonyl-CoA extender units. PpsA can accept as substrate the activated forms of either icosanoyl (C20), docosanoyl (C22) or lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-hydroxyphenyl)-C19 fatty acyl from FadD29. PpsA initiates the biosynthesis and extends its substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins add the second and third malonyl-CoA extender units. PpsD adds an (R)-methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product.
Interaction partners:
- Probable fatty acid synthase Fas
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Phenolphthiocerol/phthiocerol polyketide synthase subunit A
- Long-chain-fatty-acid--AMP ligase FadD26
- Phenyloxazoline synthase MbtB
- Phenolphthiocerol/phthiocerol polyketide synthase subunit E
- Phenolphthiocerol/phthiocerol polyketide synthase subunit D
- Isonitrile lipopeptide synthase
- Malonyl CoA-acyl carrier protein transacylase
- Polyketide synthase Pks13
Sequence:
MMRTAFSRISGMTAQQRTSLADEFDRVSRIAVAEPVAVVGIGCRFPGDVDGPESFWDFLVAGRNAISTVPADRWDAEAFYHPDPLTPGRMTTKWGGFVPDVAGFDAEFFGITPREAAAMDPQQRMLLEVAWEALEHAGIPPDSLGGTRTAVMMGVYFNEYQSMLAASPQNVDAYSGTGNAHSITVGRISYLLGLRGPAVAVDTACSSSLVAVHLACQSLRLRETDLALAGGVSITLRPETQIAISAWGLLSPQGRCAAFDAAADGFVRGEGAGVVVLKRLTDAVRDGDQVLAVVRGSAVNQDGRSNGVTAPNTAAQCDVIADALRSGDVAPDSVNYVEAHGTGTVLGDPIEFEALAATYGHGGDACALGAVKTNIGHLEAAAGIAGFIKATLAVQRATIPPNLHFSQWNPAIDAASTRFFVPTQNSPWPTAEGPRRAAVSSFGLGGTNAHVIIEQGSELAPVSEGGEDTGVSTLVVTGKTAQRMAATAQVLADWMEGPGAEVAVADVAHTVNHHRARQATFGTVVARDRAQAIAGLRALAAGQHAPGVVSHQDGSPGPGTVFVYSGRGSQWAGMGRQLLADEPAFAAAVAELEPVFVEQAGFSLRDVIATGKELVGIEQIQLGLIGMQLTLTELWRSYGVQPDLVIGHSMGEVAAAVVAGALTPAEGLRVTATRARLMAPLSGQGGMALLGLDAAATEALIADYPQVTVGIYNSPRQTVIAGPTEQIDELIARVRAQNRFASRVNIEVAPHNPAMDALQPAMRSELADLTPRTPTIGIISTTYADLHTQPIFDAEHWATNMRNPVRFQQAIASAGSGADGAYHTFIEISAHPLLTQAIADTLEDAHRPTKSAAKYLSIGTLQRDADDTVTFRTNLYTADIAHPPHTCHPPEPHPTIPTTPWQHTHHWIATTHPSTAAPEDPGSNKVVVNGQSTSESRALEDWCHQLAWPIRPAVSADPPSTAAWLVVADNELCHELARAADSRVDSLSPPALAAGSDPAALLDALRGVDNVLYAPPVPGELLDIESAYQVFHATRRLAAAMVASSATAISPPKLFIMTRNAQPISEGDRANPGHAVLWGLGRSLALEHPEIWGGIIDLDDSMPAELAVRHVLTAAHGTDGEDQVVYRSGARHVPRLQRRTLPGKPVTLNADASQLVIGATGNIGPHLIRQLARMGAKTIVAMARKPGALDELTQCLAATGTDLIAVAADATDPAAMQTLFDRFGTELPPLEGIYLAAFAGRPALLSEMTDDDVTTMFRPKLDALALLHRRSLKSPVRHFVLFSSVSGLLGSRWLAHYTATSAFLDSFAGARRTMGLPATVVDWGLWKSLADVQKDATQISAESGLQPMADEVAIGALPLVMNPDAAVATVVVAADWPLLAAAYRTRGALRIVDDLLPAPEDVGKGESEFRTSLRSCPAEKRRDMLFDHVGALAATVMGMPPTEPLDPSAGFFQLGMDSLMSVTLQRALSESLGEFLPASVVFDYPTVYSLTDYLATVLPELLEIGATAVATQQATDSYHELTEAELLEQLSERLRGTQ
Protein: Kinesin-related protein 12 (Kinesin family member 12) (Kinesin-6) (Q6S000)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end (By similarity). Required for cytokinesis. May be involved in a vesicle-mediated transport of myosin II, the Aurora kinase (aurK) and other proteins along mitotic extracellular microtubules toward the center of the cell and the cleavage furrow in order to ensure cell division coupled to mitosis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15546981}. Nucleus {ECO:0000269|PubMed:15546981}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15546981}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15546981}. Note=Concentrates in the nucleus in interphase cells, translocates to the cytoplasm at the onset of mitosis, appears in the centrosomes and spindle, and later is concentrated in the spindle midbody.
Interaction partners:
- Aurora kinase
- SAP domain-containing protein
- Uncharacterized protein
- Probable serine/threonine-protein kinase PLK
- Kinesin-related protein 13
- Kinesin-related protein 8
- Inner centromere protein A
- DH domain-containing protein
- Kinesin-related protein 2
- Kinesin-related protein 1
Sequence:
MKDYISSPLSPSNKKMPDNQKISPTNTPIRKKLFENTQSPIHFISNNNNNNITTPAKGLASVIKFNSSNYGNHHHQHHHQHHNNNNNSTVSGSAIKQHLNKSTFSTSGTTLTSSSDAILLPEDKVPMSVYLRIRPLSKKEIESKESNCFTVLNTTSVSIKSSRSDSDSNKFSFSSVLPPNTTQPQLFKTITHPLIQSFLTGHNVLLLAYGVTNAGKTYTVSGSKRNPGIIPRSLDLIFKSIPNNCLKKTENLTLSNNNNNSTNNNSKDSKDILADSSDDEYTKVDNIDSSDEDDSNAKINSNLLESFSTTNTTATTNAAAAASSTTATSNGDVIQISDQFNYSIWISYYEIYKKNIYDLLDDSPSSKKKQSLKIESDNSVVNIKGLKEILVSSVEDARDIVEQGESNRKVGGTKLNATSSRSHAVLTIKLFTSPRHIPKSDIHPSQIRCSKLCIIDLAGSERASRTETTGETFKEGSSINTSLFTLGKCIEGLKQQALQQQQQQQQHSSKRQSIHHSNPIPWRESDLTRICQEYFCGNGKASMIVNVSPSSCDSEETLNVLRFSASAKEITTLSKIKPMVFLPPPPTTPSISLKKRKSMEQPINNNNNNNNNNNNNAYYNITQLQNSVNEIKKKIHLDNLLAVGQLPISNNNNNNNGKFDYISMEKDQLLDQIQIYQKKLSNYEIKFVESEVTLREEFNNELIKNYIELENQYKERLVKESQLIHDRVQSKLSLIKNVNINQTNKLNCKIEKLELQLEQQQQKTMEANNKALVIVPQTNKRTDDEWIIEITEVQTERDNIQNKLNSILFELDEQRQHNQFSLERIQQFTLQTEQLEIERENLLTEIESMQSKGQELIKLRELEMMQLKESMNSDAQKDRENLEIQHNFETSNLNNQLQMERQEKLQIIEEMRMLKLELQQFKSNQSIEQQRNNNLIKNQYYNHNHPTAATAMTTTTPPIMSTPPIMSTPIKISSVGKFKATPSKSLIKNILGAHSNSPFKNANIESSVGGGFKVQLNIPGSPIQLAPGTPNSIQSQTPDRPILDPNQYSDSGLLMQEIDDDDYLNITGGGSANDGNWTDINVNDDSASEYDDLNSSSKSFTKKPKKTKSFGTIKRIKAVAMIPANIASSALNSSTTNIDEKEKLEKLEKLEKEKERLEKERLEKEKEKERLEKEREKEKERLEKERERLEKEKEKERERLEKEREKEKESKPKVVKKTTSSSSIISKKPSSKTTSSLTNNNNNNNNNNNNNNNNNNNNNNNNNNKSISPIKTVQSPNSPSPTKLQPHSSPNTNAKEYFNLMNPQVIIHFREPETNFVPSVTANTTTSTSTSTSKSSKKTLDSLKDTPKKIANIFSSKSSKEKEASTSSKSSSKISSSTSTTSTAPKLKRFAAITASHSIENGSESSPIEVDTPPRITKKPPVPIVSKVSSKKVSSSSSSTSSSSSSAATIKRVRKIVNEKKNYLEDDDDDVITKMATETPRKTLGLRPRNLISQPIQFR
Protein: Glucose-1-phosphate adenylyltransferase small subunit 2, chloroplastic/amyloplastic/cytosolic (OsAGPS2) (OsAPS2) (EC 2.7.7.27) (ADP-glucose pyrophosphorylase AGPS2) (ADP-glucose synthase AGPS2) (AGPase B) (Alpha-D-glucose-1-phosphate adenyl transferase) (OsAGPS2a) (OsAGPS2b) (P15280)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. The chloroplastic isoform 1 is essential for starch synthesis in leaf chloroplasts and the cytosolic isoform 2 for synthesis in seed endosperm.
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000269|PubMed:17406793}. Plastid, amyloplast {ECO:0000305|PubMed:17406793}. Note=Found in the chloroplast in leaf. Found in the plastid in the developing endosperm. {ECO:0000305|PubMed:17406793}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:17406793}.
Interaction partners:
- Starch synthase, chloroplastic/amyloplastic
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Soluble starch synthase 3a, chloroplastic/amyloplastic
- Starch synthase, chloroplastic/amyloplastic
- ADP-glucose pyrophosphorylase
- Soluble starch synthase 1, chloroplastic/amyloplastic
- Sucrose synthase 4
- phosphoglucomutase
- Starch synthase, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
Sequence:
MAMAAAMGVASPYHAAHAAASTSCDSLRLLVAEGRPRRPRGVASSSSSSSSAGRRRRPLVFSPRAVSDSKSSQTCLDPDASTSVLGIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYGNNIGGYKNEGFVEVLAAQQSPDNPNWFQGTADAVRQYLWLFEEHNVMEFLILAGDHLYRMDYEKFIQAHRETDSDITVAALPMDEKRATAFGLMKIDEEGRIVEFAEKPKGEQLKAMMVDTTILGLDDVRAKEMPYIASMGIYVISKNVMLQLLREQFPGANDFGSEVIPGATNIGMRVQAYLYDGYWEDIGTIEAFYNANLGITKKPVPDFSFYDRSAPIYTQPRHLPPSKVLDADVTDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDSLLMGADYYETEADKKLLGEKGGIPIGIGKNCHIRRAIIDKNARIGDNVKIINVDNVQEAARETDGYFIKSGIVTVIKDALLPSGTVI
Protein: RuvB-like protein 1 (RUVBL1) (EC 3.6.4.12) (TIP49-homology protein 1) (TIP49a homolog) (Q03940)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to 'Ser-129' phosphorylated H2A histones as a response to DNA damage. RVB1 recruits ARP5 to the INO80 complex. During transcription may recruit SPT15/TBP to the TATA-boxes of involved genes. Required for box C/D and box H/ACA snoRNA accumulation and involved in pre-rRNA processing.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Actin-related protein 4
- Vacuolar protein sorting-associated protein 71
- Chromatin-remodeling ATPase INO80
- Chromatin-remodeling complex subunit IES6
- Actin-related protein 5
- TEL2-interacting protein 1
- Actin-like protein ARP6
- Protein AF-9 homolog
- RuvB-like protein 2
- Helicase SWR1
Sequence:
MVAISEVKENPGVNSSNSGAVTRTAAHTHIKGLGLDESGVAKRVEGGFVGQIEAREACGVIVDLIKAKKMSGRAILLAGGPSTGKTALALAISQELGPKVPFCPLVGSELYSVEVKKTETLMENFRRAIGLRIKETKEVYEGEVTELTPEDAENPLGGYGKTISHVIVGLKSAKGTKTLRLDPTIYESIQREKVSIGDVIYIEANTGAVKRVGRSDAYATEFDLETEEYVPLPKGEVHKKKEIVQDVTLHDLDVANARPQGGQDVISMMGQLLKPKKTEITEKLRQEVNKVVAKYIDQGVAELIPGVLFIDEVNMLDIEIFTYLNKALESNIAPVVVLASNRGMTTVRGTEDVISPHGVPPDLIDRLLIVRTLPYDKDEIRTIIERRATVERLQVESSALDLLATMGTETSLRYALQLLAPCGILAQTSNRKEIVVNDVNEAKLLFLDAKRSTKILETSANYL
Protein: Protein retinal degeneration B (Probable calcium transporter rdgB) (P43125)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidic acid (PA) between membranes. May control phosphatidylinositol concentration in transport vesicles from the subrhabdomeric cisternae (SRC) to the rhabdomere. May function as a calcium transporter.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Eye-specific diacylglycerol kinase
- Diacylglycerol kinase
- Serine/threonine-protein phosphatase rdgC
- LD30122p
- Phosphatidylinositol 4-phosphate 5-kinase 59B, isoform E
Sequence:
MLIKEYRIPLPLTVEEYRIAQLYMIAKKSREESHGEGSGVEIIINEPYKDGPGGNGQYTKKIYHVGNHLPGWIKSLLPKSALTVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYYPDNGYQDNVFQLSGSDLRNRIVDVIDIVKDQLWGGDYVKEEDPKHFVSDKTGRGPLAEDWLEEYWREVKGKKQPTPRNMSLMTAYKICRVEFRYWGMQTKLEKFIHDVALRKMMLRAHRQAWAWQDEWFGLTIEDIRELERQTQLALAKKMGGGEECSDDSVSEPYVSTAATAASTTGSERKKSAPAVPPIVTQQPPSAEASSDEEGEEEEDDDEDENDAIGTGVDLSANQGGSAQRSRSQSIQMAQKGKFGSKGALHSPVGSAHSFDLQVANWRMERLEVDSKSNSDEEFFDCLDTNETNSLAKWSSLELLGEGDDSPPPHGGPSSAASVGGRGNSRQEDSIFNQDFLMRVASERGNKRQLRSSASVDRSHDSSPPGSPSTPSCPTTILILVVHAGSVLDAASELTAKKSDVTTFRGSFEAVMRQHYPSLLTHVTIKMVPCPSICTDALGILSSLSPYSFDASPSAADIPNIADVPIGAIPLLSVASPEFHETVNKTVAAANIVYHEFLKSEEGHGFSGQIVMLGDSMGSLLAYEALCRSNGSQPGTASGASNSGGDAATNINTHNPLSPRNSRLDDDERFIEADLDAKRLLVAPSPRRRRSSSSSDSRATKLDFEVCDFFMFGSPLSVVLAARKLHDAKAALPRPNCHQVYNLFHPTDPIASRLEPLLSARFSILAPVNVPRYAKYPLGNGQPLHLLEVIQSHPQHFNDGNNLLAGRRLSDASMQSTISGLIENVSLSTIHALQNKWWGTKRLDYALYCPEGLSNFPAHALPHLFHASYWESPDVIAFILRQIGKFEGIPFVGSNDDKDNASFHPGQPREKWIKKRTSVKLKNVAANHRANDVIVQEGREQRLNARFMYGPLDMITLHGEKVDVHIMKDPPAGEWTFLSTEVTDKNGRISYSIPDQVSLGYGIYPVKMVVRGDHTSVDCYMAVVPPLTECVVFSIDGSFTASMSVTGRDPKVRAGAVDVCRHWQELGYLLIYITGRPDMQQQRVVSWLSQHNFPHGLISFADGLSTDPLGHKTAYLNNLVQNHGISITAAYGSSKDISVYTNVGMRTDQIFIVGKVGKKLQSNATVLSDGYAAHLAGLQAVGGSRPAKGNARMVIPRGCFNLPGQTANPRRRRYLERKTVSSCCLMVFQTT
Protein: Epididymis secretory sperm binding protein (J-type co-chaperone HSC20, isoform CRA_a) (A0A384NYJ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWRGRAGALLRVWGFWPTGVPRRRPLSCDAASQAGSNYPRCWNCGGPWGPGREDRFFCPQCRALQAPDPTRDYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLLKLHGIEIPERTDYEMDRQFLIEIMEINEKLAEAESEAAMKEIESIVKAKQKEFTDNVSSAFEQDDFEEAKEILTKMRYFSNIEEKIKLKKIPL
Protein: RE18302p (Q8MT55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKPISSYKLQQQQIQLGKQLVVDKLINVAAYVELTSDTDDSSRRSDTPAKISAMFIDEERKASFKGDPNQQAKVKVEQVKPMVLPMLLPSAKREPLKQQTTAELREKFERSAAAQAQTQNHSPVIHKVTQKPHHERFSSLDSLASSSSGVSSTTQNVSTTQETATEFGSFSSLGSNQSLITAQDVQQIVEEADPPLKTPEAFIIVLQRENPESSIGITLAGGSDYEAKEITIHKILSNTPAAKDGRLKKGDRILAVNGMSMRGLTHRESISVLKTPRPEVVLVVTRSESLVVKALTKKRSSLGSLSSLNEKPTELDYERKRNYHKASRSLDLDLDLVSNEAGESPVATTPSTGSVSPPQPASLHDEDAEATIAGIRARRQLSRGDAAKLSTSELLERAAEARNAIAAEIRAQAEDAAASGGGARCVEIVKDSCGLGFSIEGGFDSPLGNRPLIVKKVFMGGAAQKTNQVRNGDEILSINGASTSRMTRVDAWNYMKQLPLGPVKICFA
Protein: Multifunctional methyltransferase subunit TRM112-like protein (tRNA methyltransferase 112 homolog) (tRNA methyltransferase subunit 11-2) (Q9VP65)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as an activator of both RNA and protein methyltransferases (By similarity). Together with methyltransferase Mettl5, specifically methylates the 6th position of adenine in 18S rRNA.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UI30}.
Interaction partners:
- Methyltransferase N6AMT1
- Fe2OG dioxygenase domain-containing protein
- 18S rRNA
- rRNA N
- tRNA
- Fire dancer
- peptide chain release factor N
- RNA-binding protein NOB1
- Protein HGH1 homolog
- GH26392p
Sequence:
MKLSTYNFLTSVAIKGVKVGFPLKLTINKKEVVESEFNPTFVERILPKLDWSAVYGAAQVAELTEDIPAVQPENIVENELLLQKLHHLLFEIDVLEGQLECPETGRVFPISDGIPNMLLNEDEV
Protein: SH3-domain GRB2-like 3, isoform CRA_a (SH3GL3 protein) (Q8IVP1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVAGLKKQFHKASQLFSEKISGAEGTKLDDEFLDMERKIDVTNKVVAEILSKTTEYLQPNPAYRAKLGMLNTVSKIRGQVKTTGYPQTEGLLGDCMLKYGKELGEDSTFGNALIEVGESMKLMAEVKDSLDINVKQTFIDPLQLLQDKDLKEIGHHLKKLEGRRLDYDYKKKRVGKIPDEEVRQAVEKFEESKELAERSMFNFLENDVEQVSQLAVFIEAALDYHRQSTEILQELQSKLQMRISAASSVPRREYKPRPVKRSSSELNGVSTTSVVKTTAYSRLEPAD
Protein: Transporter (Q9WTR4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MVTRTRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQFNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFASFTLNLPWTNCGHAWNSPNCTDPKLLNASVLGDHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVIVVLYVSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVKIEDVATEGAGLVFVLYPEAISTLSGSTFWAVLFFLMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTCAVTLGTFLLAMFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYVYPPWANWVGWGIALSSMILVPAYVIYKFFSIRGSLWERVAYGITPENEHHLLALEIELSSLQSFVITSCPIDPLLSSFLFISCQKTLVFKKSGPAPLI
Protein: FA complementation group M (Fanconi anemia, complementation group M, isoform CRA_c) (H0YJS3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGRQRTLFQTWGSSISRSSGTPGCSSGTERPQSPGSSKAPLPAAAEAQLESDDDVLLVAAYEAERQLCLENGGFCTSAGALWIYPTNCPVRDYQLHISRAALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQIEACYQVMGIPQSHMAEMTGSTQASTRKEIWCSKRVLFLTPQVMVNDLSRGACPAAEIKCLVIDEAHKALGNYAYCQVVRELVKYTNHFRILALSATPGSDIKAVQQVITNLLIGQIELRSEDSPDILTYSHERKVEKLIVPLGEELAAIQKTYIQILESFARSLIQRNVLMRRDIPNLTKYQIILARDQFRKNPSPNIVGIQQGIIEGEFAICISLYHGYELLQQMGMRSLYFFLCGIMDGTKGMTRSKNELGRNEDFMKLYNHLECMFARTRSTSANGISAIQQGDKNKKFVYSHPKLKKLEEVVIEHFKSWNAENTTEKKRDETRVMIFSSFRDSVQEIAEMLSQHQPIIRVMTFVGHASGKSTKGFTQKEQLEIYNQSQSNKRSIYKAISSNRQVLHFYQRSPRMVPDGINPKLHKMFITHGVYEPEKPSRNLQRKSSIFSYRDGMRQSSLKKDWFLSEEEFKLWNRLYRLRDSDEIKEITLPQVQFSSLQNEENKPAQESTTGIHQLSLSEWRLWQDHPLPTHQVDHSDRCRHFIGLMQMIEGMRHEEGECSYELEVESYLQMEDVTSTFIAPRNESNNLASDTFITHKKSSFIKNINQGSSSSVIESDEECAEIVKQTHIKPTKIVSLKKKVSKEIKKDQLKKENNHGIIDSVDNDRNSTVENIFQEDLPNDKRTSDTDEIAATCTINENVIKEPCVLLTECQFTNKSTSSLAGNVLDSGYNSFNDEKSVSSNLFLPFEEELYIVRTDDQFYNCHSLTKEVLANVERFLSYSPPPLSGLSDLEYEIAKGTALENLLFLPCAEHLRSDKCTCLLSHSAVNSQQNLELNSLKCINYPSEKSCLYDIPNDNISDEPSLCDCDVHKHNQNENLVPNNRVQIHRSPAQNLVGENNHDVDNSDLPVLSTDQDESLLLFEDVNTEFDDVSLSPLNSKSESLPVSDKTAISETPLVSQFLISDELLLDNNSELQDQITRDANSFKSRDQRGVQEEKVKNHEDIFDCSRDLFSVTFDLGFCSPDSDDEILEHTSDSNRPLDDLYGRYLEIKEISDANYVSNQALIPRDHSKNFTSGTVIIPSNEDMQNPNYVHLPLSAAKNEELLSPGYSQFSLPVQKKVMSTPLSKSNTLNSFSKIRKEILKTPDSSKEKVNLQRFKEALNSTFDYSEFSLEKSKSSGPMYLHKSCHSVEDGQLLTSNESEDDEIFRRKVKRAKGNVLNSPEDQKNSEVDSPLHAVKKRRFPINRSELSSSDESENFPKPCSQLEDFKVCNGNARRGIKVPKRQSHLKHVARKFLDDEAELSEEDAEYVSSDENDESENEQDSSLLDFLNDETQLSQAINDSEMRAIYMKSLRSPMMNNKYKMIHKTHKNINIFSQIPEQDETYLEDSFCVDEEESCKGQSSEEEVCVDFNLITDDCFANSKKYKTRRAVMLKEMMEQNCAHSKKKLSRIILPDDSSEEENNVNDKRESNIAVNPSTVKKNKQQDHCLNSVPSGSSAQSKVRSTPRVNPLAKQSKQTSLNLKDTISEVSDFKPQNHNEVQSTTPPFTTVDSQKDCRKFPVPQKDGSALEDSSTSGASCSKSRPHLAGTHTSLRLPQEGKGTCILVGGHEITSGLEVISSLRAIHGLQVEVCPLNGCDYIVSNRMVVERRSQSEMLNSVNKNKFIEQIQHLQSMFERICVIVEKDREKTGDTSRMFRRTKSYDSLLTTLIGAGIRILFSSCQEETADLLKELSLVEQRKNVGIHVPTVVNSNKSEALQFYLSIPNISYITALNMCHQFSSVKRMANSSLQEISMYAQVTHQKAEEIYRYIHYVFDIQMLPNDLNQDRLKSDI
Protein: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1) (O88483)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9651365}.
Interaction partners:
- Pyruvate dehydrogenase phosphatase regulatory subunit
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
Sequence:
MPAPTQLFFPLVRNCELSRIYGTACYCHHKHLCCSPPYIPQNRLRYTPHPAYATFCRPRENWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSILGFDSNQLPANAPIEDRRSAATCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNSLRTYWQELIDLNTGESADIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNERELERLKLEHPKNEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYHTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRAKMSSVFEDQNAATHLIRHAVGNNEFGAVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQEQ
Protein: Transcription initiation factor TFIID subunit 14b (GAS 41-like protein) (Protein AF-9 homolog a) (TBP-associated factor 14b) (AtTAF14b) (Q9FH40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of flowering controlling the H4K5 acetylation levels in the FLC and FT chromatin. Positively regulates FLC expression. Component of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of a NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000305}.
Interaction partners:
- SWR1-complex protein 4
- SWR1 complex subunit 2
- RuvB-like protein 1
- SWR1 complex subunit 6
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- Actin-related protein 4
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Methyl-CpG-binding domain-containing protein 9
- Actin-related protein 6
Sequence:
MTNSSSSKKQAQDQPETSEPTLKSLKTKMTKSDEKQKKLKDIEISVPIVYGNVAFWLGKKASEYQSHKWAVYVRGATNEDISVVVKKVVFQLHSSFNSPTRVIEEPPFEVSESGWGEFEIAMTLHFHSDVCDKPLSLYHHLKLYPEDESGPLTMKKPVVVESYDEIVFPDPSESFLARVQNHPALTFPRLPSGYNLPAPMQVEDTGKKKRGDTKDHSLGQWFMSFSEADELLQLAAARQQVQAHIAKLRRQISLLEGQNQTVKTGSDL
Protein: MIP26555p1 (Q9VM12)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH18858p
- GH05923p
- GEO07291p1
Sequence:
MAATDIAEEAFHLRLGYLKPETVEIARVELRETEEVKAEAIIKLRELLKATPELNYKDDDAFLTVFLRACHFYPEGALEKMKTTASFRKEYASLVRGLLVEQVKEKFVKGSVINVLKNCDQKGRRVLIVNCGKLWDPSDITSDEMFRMLYMVHLAAQLEEETQVRGVVCIMDFEGLSMKQVKALSPSFSKRLLTFIQEAMPLRMKEVHFVKQPFIFNMVWSLFKPFVKQKLNNRMHFHGSDMKSLQKFLDPSVLPANYKGTLPAIDYGGVEWFPALEQQAQYVEEWSQLGPAQW
Protein: Alcohol acyl transferase 2 (MdAAT2) (EC 2.3.1.-) (Q6R311)
Organism: Malus domestica (Apple) (Pyrus malus)
Function: Involved in the biosynthesis of volatile esters which confer ripe apple fruit flavor (Ref.2). Alcohol acyl transferase that can use a wide range of alcohols as substrate to produce esters (By similarity).
Interaction partners:
Sequence:
MMPFSVLQVKRLQLELITPAKPTLQEAKFLSDIDDQEGLRFQVPVIMCYKDNPSLNKNCNPVKVIREALSRALVYYYPLAGRLKEGPNRKLMVDCNGEGILFVEASADVTLEQLGDKILPPCPLLEEFLFNFPGSDGIIGCPLLLVQVTCLTCGGFILALRVNHTMCDAPGLLLFLTAIAEMARGAHAPSILPVWERELLFSRDPPRITCAHHEYEDVIDHSDGLYASSNQSNMVQRSFYFGAKEMRVLRKQIPPHLISTCSTFDLITACLWKCRTLALNINPKEAVRVSCIVNARGKHNNVRLPLGYYGNAFAFPAAISKAEPLCKNPLGYALELVKKAKATMNEEYLRSVADLLVLRGRPQYSSTGSYLIVSDNTRAGFGDVNFGWGQPVFAGPAKALDLISFYVQHKNNTEDGILVPMCLPSSAMERFQQELERITQEPKEDICNNLRSTRIMSMM
Protein: Magnetosome protein MamS (Q2W8P6)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: May play a role in magnetite crystal growth and size.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:16303747}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Magnetosome protein MamT
- Magnetosome protein MamR
- Multi-heme protein MamP
- Magnetosome protein MamB
- Probable membrane transporter protein MamO
- Magnetosome protein MamM
- Magnetosome protein MamN
- Magnetosome protein MamQ 1
- Magnetosome protein MamA
Sequence:
MDIRPERMLSRIRQMAEGAVSPQLVLGLGVVLILGLVVSAMLPDRFTGGGKTGGGVTAQSQALSLPAALPGLSPFTPATPLQFSGRVTQVASIGNDVGWGQVHIWIDNGTGALQEISVAPQAYLTQIGCPSFDGARVSGVGFIFDPGRPNAELYVKSIQVGGRTCKLRDDEGLALWMVVQ