wanglab/gogpt-training-data huggingface dataset:
Protein: BCL-6 corepressor-like protein 1 (BCoR-L1) (BCoR-like protein 1) (Q5H9F3)
Organism: Homo sapiens (Human)
Function: Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence-specific DNA-binding proteins such as BCL6. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:17379597, ECO:0000269|PubMed:38342987}.
Interaction partners:
- Polycomb group RING finger protein 1
- Lysine-specific demethylase 2B
- S-phase kinase-associated protein 1
- RING1 and YY1-binding protein
- YY1-associated factor 2
- C-terminal-binding protein 1
- Polycomb group RING finger protein 3
- E3 ubiquitin-protein ligase RING1
- Polycomb group RING finger protein 2
- E3 ubiquitin-protein ligase RING2
Sequence:
MISTAPLYSGVHNWTSSDRIRMCGINEERRAPLSDEESTTGDCQHFGSQEFCVSSSFSKVELTAVGSGSNARGADPDGSATEKLGHKSEDKPDDPQPKMDYAGNVAEAEGLLVPLSSPGDGLKLPASDSAEASNSRADCSWTPLNTQMSKQVDCSPAGVKALDSRQGVGEKNTFILATLGTGVPVEGTLPLVTTNFSPLPAPICPPAPGSASVPHSVPDAFQVPLSVPAPVPHSGLVPVQVATSVPAPSPPLAPVPALAPAPPSVPTLISDSNPLSVSASVLVPVPASAPPSGPVPLSAPAPAPLSVPVSAPPLALIQAPVPPSAPTLVLAPVPTPVLAPMPASTPPAAPAPPSVPMPTPTPSSGPPSTPTLIPAFAPTPVPAPTPAPIFTPAPTPMPAATPAAIPTSAPIPASFSLSRVCFPAAQAPAMQKVPLSFQPGTVLTPSQPLVYIPPPSCGQPLSVATLPTTLGVSSTLTLPVLPSYLQDRCLPGVLASPELRSYPYAFSVARPLTSDSKLVSLEVNRLPCTSPSGSTTTQPAPDGVPGPLADTSLVTASAKVLPTPQPLLPAPSGSSAPPHPAKMPSGTEQQTEGTSVTFSPLKSPPQLEREMASPPECSEMPLDLSSKSNRQKLPLPNQRKTPPMPVLTPVHTSSKALLSTVLSRSQRTTQAAGGNVTSCLGSTSSPFVIFPEIVRNGDPSTWVKNSTALISTIPGTYVGVANPVPASLLLNKDPNLGLNRDPRHLPKQEPISIIDQGEPKGTGATCGKKGSQAGAEGQPSTVKRYTPARIAPGLPGCQTKELSLWKPTGPANIYPRCSVNGKPTSTQVLPVGWSPYHQASLLSIGISSAGQLTPSQGAPIRPTSVVSEFSGVPSLSSSEAVHGLPEGQPRPGGSFVPEQDPVTKNKTCRIAAKPYEEQVNPVLLTLSPQTGTLALSVQPSGGDIRMNQGPEESESHLCSDSTPKMEGPQGACGLKLAGDTKPKNQVLATYMSHELVLATPQNLPKMPELPLLPHDSHPKELILDVVPSSRRGSSTERPQLGSQVDLGRVKMEKVDGDVVFNLATCFRADGLPVAPQRGQAEVRAKAGQARVKQESVGVFACKNKWQPDDVTESLPPKKMKCGKEKDSEEQQLQPQAKAVVRSSHRPKCRKLPSDPQESTKKSPRGASDSGKEHNGVRGKHKHRKPTKPESQSPGKRADSHEEGSLEKKAKSSFRDFIPVVLSTRTRSQSGSICSSFAGMADSDMGSQEVFPTEEEEEVTPTPAKRRKVRKTQRDTQYRSHHAQDKSLLSQGRRHLWRAREMPWRTEAARQMWDTNEEEEEEEEEGLLKRKKRRRQKSRKYQTGEYLTEQEDEQRRKGRADLKARKQKTSSSQSLEHRLRNRNLLLPNKVQGISDSPNGFLPNNLEEPACLENSEKPSGKRKCKTKHMATVSEEAKGKGRWSQQKTRSPKSPTPVKPTEPCTPSKSRSASSEEASESPTARQIPPEARRLIVNKNAGETLLQRAARLGYKDVVLYCLQKDSEDVNHRDNAGYTALHEACSRGWTDILNILLEHGANVNCSAQDGTRPVHDAVVNDNLETIWLLLSYGADPTLATYSGQTAMKLASSDTMKRFLSDHLSDLQGRAEGDPGVSWDFYSSSVLEEKDGFACDLLHNPPGSSDQEGDDPMEEDDFMFELSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEITTMPKAEFYRQVASSQLLTPAERPGGLDDRSPPGSSETVELVRYEPDLLRLLGSEVEFQSCNS
Protein: HTH-type transcriptional regulator YodB (O34844)
Organism: Bacillus subtilis (strain 168)
Function: Negatively regulates yodC and azoR1 which may contribute to the degradation of aromatic compounds. Probably positively regulates the catechol-specific transcription of mhqNOP, mhqED, and mhqA.
Interaction partners:
- Putative NAD
- FMN-dependent NADH:quinone oxidoreductase 1
- Peroxide operon regulator
- Organic hydroperoxide resistance transcriptional regulator
- Catechol-2,3-dioxygenase
- General stress protein 14
Sequence:
MGNTMCPKMESAFSLLGKRWNGLIIHVLMDGPKRFKEITETIPMISQKMLAERLKELEQNEIVERQVLPETPVKVIYTLTEKGTALQAVFQEMQAWADQFCEPGDTVCEEEK
Protein: Probable phospholipid-transporting ATPase DNF3 (EC 7.6.2.1) (Aminophospholipid translocase) (APT) (Phospholipid translocase) (PLT) (Q12674)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Probable). Forms a heteromeric phospholipid translocase (PLT) DNF3-CRF1, implicated in the translocation of phospholipids from the outer to the inner leaflet of membrane bilayers. Shares an essential function for cell growth with PLTs DRS2-CDC50 and DNF1/2-LEM3. May be involved in transport from early endosomes to the trans-Golgi network (TGN) (Probable).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12631737, ECO:0000269|PubMed:17093059}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:12631737, ECO:0000269|PubMed:16452632}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholipid-transporting ATPase accessory subunit CDC50
- Phospholipid-transporting ATPase accessory subunit CRF1
- Phospholipid-transporting ATPase accessory subunit LEM3
- Flippase kinase 1
- Serine/threonine-protein kinase KIN82
- Phospholipid-transporting ATPase DNF1
- Phospholipid-transporting ATPase NEO1
- Scramblase ANY1
Sequence:
MGIADGQRRRSSSLRTQMFNKHLYDKYRGRTDDEIELEDINESKTFSGSDNNDKDDRDETSGNYAAEEDYEMEEYGSPDVSYSIITKILDTILDRRRTFHSKDGRHIPIILDHNAIEYKQAATKRDGHLIDERFNKPYCDNRITSSRYTFYSFLPRQLYAQFSKLANTYFFIVAVLQMIPGWSTTGTYTTIIPLCVFMGISMTREAWDDFRRHRLDKEENNKPVGVLVKDGNNDAQEVYTLPSSVVSSTAYLTKSAAAENNPPLNDDRNSSQGHFLDTHFNNFELLKNKYNVHIHQKKWEKLRVGDFVLLTQDDWVPADLLLLTCDGENSECFVETMALDGETNLKSKQPHPELNKLTKAASGLANINAQVTVEDPNIDLYNFEGNLELKNHRNDTIMKYPLGPDNVIYRGSILRNTQNVVGMVIFSGEETKIRMNALKNPRTKAPKLQRKINMIIVFMVFVVATISLFSYLGHVLHKKKYIDQNKAWYLFQADAGVAPTIMSFIIMYNTVIPLSLYVTMEIIKVVQSKMMEWDIDMYHAETNTPCESRTATILEELGQVSYIFSDKTGTLTDNKMIFRKFSLCGSSWLHNVDLGNSEDNFEDNRDNTNSLRLPPKAHNGSSIDVVSIGDQNVLDRLGFSDAPIEKGHRPSLDNFPKSRNSIEYKGNSSAIYTGRPSMRSLFGKDNSHLSKQASVISPSETFSENIKSSFDLIQFIQRYPTALFSQKAKFFFLSLALCHSCLPKKTHNESIGEDSIEYQSSSPDELALVTAARDLGYIVLNRNAQILTIKTFPDGFDGEAKLENYEILNYIDFNSQRKRMSVLVRMPNQPNQVLLICKGADNVIMERLHDRELAAKKMADICTSTKERKDAEAELVLQQRKSLERMVDEEAMARTSLRNSLSSVPRASLSLQAVRKSLSMKNSRTRDPEKQIDSIDQFLETVKKSDQEIGSVVNKSRKSLHKQQIEKYGPRISIDGTHFPNNNVPIDTRKEGLQHDYDTEILEHIGSDELILNEEYVIERTLQAIDEFSTEGLRTLVYAYKWIDIGQYENWNKRYHQAKTSLTDRKIKVDEAGAEIEDGLNLLGVTAIEDKLQDGVSEAIEKIRRAGIKMWMLTGDKRETAINIGYSCMLIKDYSTVVILTTTDENIISKMNAVSQEVDSGNIAHCVVVIDGATMAMFEGNPTYMSVFVELCTKTDSVICCRASPSQKALMVSNIRNTDPNLVTLAIGDGANDIAMIQSADIGVGIAGKEGLQASRVSDYSIGQFRFLLKLLFVHGRYNYIRTSKFMLCTFYKEITFYFTQLIYQRYTMFSGSSLYEPWSLSMFNTLFTSLPVLCIGMFEKDLKPMTLLTVPELYSYGRLSQGFNWLIFMEWVILATTNSLIITFLNVVMWGMSSLSDNTMYPLGLINFTAIVALINVKSQFVEMHNRNWLAFTSVVLSCGGWLVWCCALPILNNTDQIYDVAYGFYNHFGKDITFWCTSLVLALLPITLDIVYKTFKVMIWPSDSDIFAELEQKSDIRKKLELGAYSEMRQGWTWDKDPSTFTRYTDKVLSRPRTNSRASAKTHNSSIYSMSNGNVDHSSKKNFFGNSSKKSSERYEVLPSGKLIKRPSLKTQSSKDSIGGNITTKLTKKLKLPSRNVEDEDVNQIIQARLKDLE
Protein: Collagen triple helix repeat-containing protein 1 (Q96CG8)
Organism: Homo sapiens (Human)
Function: May act as a negative regulator of collagen matrix deposition.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-1
- Frizzled-3
- Frizzled-9
- Periostin
Sequence:
MRPQGPAASPQRLRGLLLLLLLQLPAPSSASEIPKGKQKAQLRQREVVDLYNGMCLQGPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKGECLRESFEESWTPNYKQCSWSSLNYGIDLGKIAECTFTKMRSNSALRVLFSGSLRLKCRNACCQRWYFTFNGAECSGPLPIEAIIYLDQGSPEMNSTINIHRTSSVEGLCEGIGAGLVDVAIWVGTCSDYPKGDASTGWNSVSRIIIEELPK
Protein: Ankyrin repeat domain 17 (H0YM23)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEEEEDDDDEEEEVSEVESFILDQDDLENPMLETASKLLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGADIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLSAPPPDVTQLTPPSHDLNRAPRVPVQALPMVVPPQEPDKPPANVATTLPIRNKAASKQKSSSHLPANSQDVQGYITNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLLTPVGVGEQLSEGDYARLQQVDPVLLKDEPQQTAAQMGFAPIQPLAMPQALPLAAGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQGLMVASPAQTLNDTLDDIMAVSGRASAMSNTPTHSIAASISQPQTPTPSPIISPSAMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSSRDTALTIAADKGHYKFCELLIGRGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQFPSDSECMRYIATITDKEMLKKCHLCMESIVQAKDRQAAEANKNASILLEELDLEKLREESRRLALAAKREKRKEKRRKKKEEQRRKLEEIEAKNKENFELQAAQEKEKLKVEDEPEVLTEPPSATTTTTIGISATWTTLAGSHGKRNNTITTTSSKRKNRKNKITPENVQIIFDDPLPISYSQPEKVNGESKSSSTSESGDSDNMRISSCSDESSNSNSSRKSDNHSPAVVTTTVSSKKQPSVLVTFPKEERKSVSGKASIKLSETISEGTSNSLSTCTKSGPSPLSSPNGKLTVASPKRGQKREEGWKEVVRRSKKVSVPSTVISRVIGRGGCNINAIREFTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDKEIDELIPKNRLKSSSANSKIGSSAPTTTAANTSLMGIKMTTVALSSTSQTATALTVPAISSASTHKTIKNPVNNVRPGFPVSLPLAYPPPQFAHALLAAQTFQQIRPPRLPMTHFGGTFPPAQSTWGPFPVRPLSPARATNSPKPHMVPRHSNQNSSGSQVNSAGSLTSSPTTTTSSSASTVPGTSTNGSPSSPSVRRQLFVTVVKTSNATTTTVTTTASNNNTAPTNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDCGSASPNKVASSSEQEAGSPPVVETTNTRPPNSSSSSGSSSAHSNQQQPPGSVSQEPRPPLQQSQVPPPEVRMTVPPLATSSAPVAVPSTAPVTYPMPQTPMGCPQPTPKMETPAIRPPPHGTTAPHKNSASVQNSSVAVLSVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPIAPNFSAPLPFGPFSTLFENSPTSAHAFWGGSVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDSPYGSVTPSSTHLGNFASNISGGQMYGPGAPLGGAPAAANFNRQHFSPLSLLTPCSSASNDSSAQSVSSGVRAPSPAPSSVPLGSEKPSNVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHSGIWSFEGIGGNQDKVDWCNPGMGNPMIHRPMSDPGVFSQHQAMERDSTGIVTPSGTFHQHVPAGYMDFPKVGGMPFSVYGNAMIPPVAPIPDGAGGPIFNGPHAADPSWNSLIKMVSSSTENNGPQTVWTGPWAPHMNSVHMNQLG
Protein: Lethal(2) giant larvae protein homolog 1 (LLGL) (Mgl-1) (Mlgl) (Q80Y17)
Organism: Mus musculus (Mouse)
Function: Cortical cytoskeleton protein found in a complex involved in maintaining cell polarity and epithelial integrity. Involved in the regulation of mitotic spindle orientation, proliferation, differentiation and tissue organization of neuroepithelial cells. Involved in axonogenesis through RAB10 activation thereby regulating vesicular membrane trafficking toward the axonal plasma membrane.
Subcellular location: Early endosome membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to the lateral membrane during the polarization and formation cell-cell contacts. Enriched in developing axons (By similarity). {ECO:0000250}.
Interaction partners:
- LLGL scribble cell polarity complex component 2
- Protein kinase C iota type
- Protein kinase C zeta type
- Protein scribble homolog
- Disks large homolog 4
- Disks large homolog 1
- Disks large homolog 3
- Ubiquitin-protein ligase E3A
- Disks large homolog 2
- Partitioning defective 6 homolog alpha
Sequence:
MMKFRFRRQGADPQREKLKQELFAFHKTVEHGFPNQPSALAFDPELRIMAIGTRSGAVKIYGAPGVEFTGLHRDAATVTQMHFLPGQGRLLTLLDDSSLHLWEIIHHNGCAHLEEGLSFHPPSRPSFDNASFPASLTRVTVVLLVAGNTAALGTESGSIFFLDVATLALLEGQTLSPDVVLRSVPDDYRCGKALGPVESLQGHLQDPSKILIGYSRGLLVIWSQATQSVDNVFLGNQQLESLCWGRDGSSIISSHSDGSYAIWSTDTGSPPTLQPTVVTTPYGPFPCKAINKILWRSCESGDHFIIFSGGMPRASYGDRHCVSVLRAETLVTLDFTSRVIDFFTVHSTQPEDECDNPQALAVLLEEELVVLDLQTPGWPAVPAPYLAPLHSSAITCSAHVANVPSKLWARIVSAGEQQSPQPASSALSWPITGGRNLAQEPSQRGLLLTGHEDGTVRFWDASGVALRPLYKLSTAGLFQTDCEHADSLAQAVEDDWPPFRKVGCFDPYSDDPRLGIQKVALCKYTAQMVVAGTAGQVLVLELSEVPAEHAVSVANVDLLQDREGFTWKGHERLNPHTGLLPWPAGFQPRMLIQCLPPAAVTAVTLHAEWSLVAFGTSHGFGLFDYQRKSPVLARCTLHPNDSLAMEGPLSRVKSLKKSLRQSFRRIRKSRVSGKKRTPAASSKLQEANAQLAEQTCPHDLEMTPVQRRIEPRSADDSLSGVVRCLYFADTFLRDATHHGPTMWAGTNSGSVFAYALEVPAATAGGEKRPEQAVEAVLGKEVQLMHRAPVVAIAVLDGRGRPLPEPYEASRDLAQAPDMQGGHAVLIASEEQFKVFTLPKVSAKTKFKLTAHEGCRVRKVALATFASVMSEDYAETCLACLTNLGDVHVFSVPGLRPQVHYSCIRKEDISGIASCVFTRHGQGFYLISPSEFERFSLSARNITEPLCSLDISWPQNATQPRLQESPKLSQANGTRDIILAPESCEGSPSSAHSKRADTMEPPEAALSPVSIDSAASGDTMLDTTGDVTVEYVKDFLG
Protein: G protein subunit alpha transducin 1 (Rod-type transducin alpha subunit) (Q9DG28)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYSNTLQSMLAIVRAMTTLNIQYGDSARQDDARKLLHLSDTIEEGTMPKEMSDIIGRLWKDAGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFLEKIKKAHLSICFPDYDGPNTYDDAGNYIKLQFLELNMRRDVKEIYSHMTCATDTENVKFVFDAVTDIIIKENLKDCGLF
Protein: Emp24/gp25L/p24 family protein (Q769F7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}.
Interaction partners:
- Emp24/gp25L/p24 family protein
- Transmembrane emp24 domain-containing protein B
- Transmembrane emp24 domain-containing protein A
- Vesicle-trafficking protein SEC22b
- Probable serine/threonine-protein kinase ndrA
Sequence:
MMIKLSLLFIIAIIFNVGSAVYFELNGGQTKCFIEENPKDTTVLGKYILEDITPQQGGYGNQLSLTVKVTDPEKREVLSKTMPSNGRFAFSTQVGGEHKICFSTNTSKWFGPSVKTRLHLEIEGGAGANDYEEIAKVEHLTGIEISLRRLNDRVNQIRKEQSYQKGREIVFRNTSESTNARVMWWSIIQLVVLVLTGVWQMKHLKSFFKAKKLV
Protein: Spermidine transporter DUR3 (A0A1D8PDB5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Urea amidolyase
Sequence:
MADSYVPLPQSAGYAVVVGLGFVFAFGMMLTTYILRRYNKEVMTAEEFATAGRSVKTGLIAACIVSSWTWSATLNGSTSQVYNNGVCGSIFYAMGATVQITLFACLAIKARERAPAAHTYLEIVKGRYGTTTHFVYIFWGIVTNILVTSMLLSGGSATVNDLTGMNIVAAILLLPLGVVIYTLFGGIKATFLTDYAHTVVLIVIIFIFAFTTWATSSKLGSPQAVWEIVTKLAESNPREGNAGGSYFTMHSRSGGMFFVINIIGNFGTVFLDNGYFNKAFAANPSSTYKGYIFGSLAWCAIPALCSLTMGFAALALEHTEYWPLGRPMTAAEVASGLVLPNAASALLGKAGAVLALLMVFMAVTSAMSAELIAVSTIATYDIYRTYINPNASGKKLIWVSHLSTVIFAYTMAGFAIGLYYAKVSMGYLYEMMGVIIGGAVLSSALTILSKRQNWHAATFSPIISTALAIMAWLVCTKKKFGSVTYLKTFEDDAMLTGNCVALLTPFIIVPILTFIFKPQNFDWKLLDQRITRVDEEEELAEALGGTVSSDPERLHPIKSQISVIASQLVEGEREQYQKEKEILNKSFKICCIVCCTLAICLVVLFPMPLYGTKYIFSKKFFTGWVVVFIIWLFYSAFQVIIFPIWESRTDLYHTFRGIYWDLTGQTYKLKAWQNEHPEEMHAVRSQLQAQLSRTAVTHEIVDGKAFGDGYVTPANIDDALEEKKG
Protein: Exopolyphosphatase PRUNE1 (EC 3.6.1.1) (Drosophila-related expressed sequence 17) (DRES-17) (DRES17) (HTcD37) (Protein prune homolog 1) (hPrune) (Q86TP1)
Organism: Homo sapiens (Human)
Function: Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, migration and differentiation, and acts as a negative regulator of NME1. Plays a role in the regulation of neurogenesis. Involved in the regulation of microtubule polymerization.
Subcellular location: Cytoplasm. Nucleus. Cell junction, focal adhesion. Note=In some transfected cells a nuclear staining is also observed.
Interaction partners:
- Nucleoside diphosphate kinase A
- Guanosine-3',5'-bis
- Glycogen synthase kinase-3 beta
- Adenine phosphoribosyltransferase
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
Sequence:
MEDYLQGCRAALQESRPLHVVLGNEACDLDSTVSALALAFYLAKTTEAEEVFVPVLNIKRSELPLRGDIVFFLQKVHIPESILIFRDEIDLHALYQAGQLTLILVDHHILSKSDTALEEAVAEVLDHRPIEPKHCPPCHVSVELVGSCATLVTERILQGAPEILDRQTAALLHGTIILDCVNMDLKIGKATPKDSKYVEKLEALFPDLPKRNDIFDSLQKAKFDVSGLTTEQMLRKDQKTIYRQGVKVAISAIYMDLEAFLQRSNLLADLHAFCQAHSYDVLVAMTIFFNTHNEPVRQLAIFCPHVALQTTICEVLERSHSPPLKLTPASSTHPNLHAYLQGNTQVSRKKLLPLLQEALSAYFDSMKIPSGQPETADVSREQVDKELDRASNSLISGLSQDEEDPPLPPTPMNSLVDECPLDQGLPKLSAEAVFEKCSQISLSQSTTASLSKK
Protein: Fucose kinase (D3ZDZ7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDQPKGVNWTVIILTCQYKDSVQVFQRELEVRQKREQIPAGTMLLAVEDPQTRVGSGGATLNALLVAAEHLSARAGFTVVTSDVLHSAWILILHMGRDFPFDDCGRAFTCLPVENPQAPVEALVCNLDCLLDIMTHRLGPGSPPGVWVCSTDMLLSVPPNPGISWDGFRGTRVIAFPGSLAYALNHGVYLTDSQGVVLDIYYQGTKAEIQRCVRPDGLVPLVSGVVFFSVETAEHLLATHVSPPLDACTYMGLDSGAQPVQLSLFFDILLCMARNMSRENFVAGRPPEMGQGDPDVARYLKGARAQLWRELRDQPLTMVYVPDGGYSYMTTDATEFLHRLTMPGVAVAQIVHSQVEEPQLLEATCSVVSCLLEGPVHLGPRSVLQHCHLRGPIHIGAGCFVSGLDTAHSEALHGLELHDLILQGHHIRLHGSQSRVFTLAGRLDSWERQGAGMYLNMSWNEFFKKTGIRDWDLWDPDTPLSDRCLLSARLFPVLHPTRALGPQDVLWMLHPHKDRGEALRAWRASWRLSWEQLQPRLDRAATLDFRRDLFFRQALQKARHVLEARQDLCLHPLIRAAVGEGCSGPLLATLDKVAAGAEDPGVAARALACVADVLGCMAEGQGGLRSGPAANPEWIQPFSYLERGDLMRGVEALAQEREKWLTRPALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVDGRRPIGAKARRILEPELWLAVGPRQDEMTVKIVCRSLDDLQDYCQPHAPGALLKAAFICADIVHVNSEVPLHEQLLRSFNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRTVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKVGRSRAQLPLKVEVEEITVPENFQKKLMAPGCEPLAVHRMMDVLAPYAFGQSLAGAGGGGFLYLLTKEPRQKEVLEAVLAKVEGLGNYSVHLVQVDTQGLSLQLLGHDAHLCGAGPSEVGNT
Protein: 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6 (EC 2.4.1.152) (Fucosyltransferase 6) (Fucosyltransferase VI) (Fuc-TVI) (FucT-VI) (Galactoside 3-L-fucosyltransferase) (P51993)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein- or a glycolipid-linked sialopolylactosamines chain or of a distal or internal lactosamine unit of a neutral glycoprotein- or a glycolipid-linked polylactosamines chain through an alpha-1,3 glycosidic linkage and participates in surface expression of the sialyl Lewis X (sLe(x)), Lewis X (Le(x)) and non sialylated VIM2 determinants. Moreover transfers fucose to H-type 2 (Fucalpha1-2Galbeta1-4GlcNAc) chain acceptor substrates and participates in difucosylated sialyl Lewis x determinants. Also fucosylates a polylactosamine substrate having a 6 sulfate modification at the GlcNAc moiety and gives rise to sialyl and non-sialyl 6-sulfo lewis X. Does not have activity towards type 1 ((Galbeta1-3GlcNAc)) and H-type 1 chain (Fucalpha1-2Galbeta1-3GlcNAc) acceptors substrates.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Golgi apparatus {ECO:0000269|PubMed:9451035}. Secreted {ECO:0000269|PubMed:9451035}. Note=Membrane-bound form in trans cisternae of Golgi.
Interaction partners:
- Galactoside alpha-
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 1
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- Type 2 lactosamine alpha-2,3-sialyltransferase
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- Beta-1,4-galactosyltransferase 2
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- Beta-1,4-galactosyltransferase 4
- N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
Sequence:
MDPLGPAKPQWSWRCCLTTLLFQLLMAVCFFSYLRVSQDDPTVYPNGSRFPDSTGTPAHSIPLILLWTWPFNKPIALPRCSEMVPGTADCNITADRKVYPQADAVIVHHREVMYNPSAQLPRSPRRQGQRWIWFSMESPSHCWQLKAMDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWGPNSARVRYYQSLQAHLKVDVYGRSHKPLPQGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALAFCKACWKLQEESRYQTRGIAAWFT
Protein: mRNA-capping enzyme [Includes: mRNA 5'-triphosphate monophosphatase (EC 3.6.1.74) (mRNA 5'-phosphatase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase)] (Q9VY44)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR036958}.
Interaction partners:
- mRNA cap guanine-N
- Transcription elongation factor SPT5
- DNA-directed RNA polymerase II subunit RPB1
- Nuclear cap-binding protein subunit 2
- Smrter, isoform G
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MALTNRDRERGSGPLPNRWLYCPRKSDTIIAERFLAFKTPLSNNFHDKMPIECTFQPEMLFEYCKTLKVKLGLWVDLTNTKRFYDRSAVEELGAKYIKLQCRGHGETPSPEQTHSFIEIVDNFINERPFDVIAVHCTHGFNRTGFLIVCYLVERLDCSVSAALAIFASARPPGIYKQDYINELYKRYEDTNAAPAAPEQPNWCLDYDDGNGDGFVQDNSSSTSQQAGEQDDDAEEVEGEDAGGDCDASTSDGQPRKKRRREMIIKNATFMAGVPGVRQVSDQPRLGDLQRKVQDWCDWKKNGFPGAQPVSMDRENIKRLSEIPYRVSWKADGTRYMMLIDGRDEVYFFDRNHSCFQVENVTFVESRNLNEHLDGTLVDGEMVLDKIGETVTPRYLIYDIVRLSNRDVRDEPFYPNRLDYIKTEVIGPRILGMKHGIINQRLQAFSVRGKDFWDIWMSARLLGEKFSRTLAHEPDGLIFQPSKQPYTAGTCSDVFKWKPHELNSVDFRLKIITERGEGLLTKKVGFLYVGGHDAPYGRMQRLTKETRELDNRIVECTMNQFGNWDFMRERTDKKNPNSYNTARSVVDSIKHPVTKEYLLNFIASSGYRNDHVMMPPPINSHNQNHNHNHFYPHGHGQHQRRPCVNPTLGN
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FNN0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- glutamate--tRNA ligase
- methionine--tRNA ligase
- glutamine--tRNA ligase
- Tyrosine--tRNA ligase
- leucine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- proline--tRNA ligase
- Lysine--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- leucine--tRNA ligase
Sequence:
MSDLVAKFKGLSVADSTAQLSREQSALVAQWESILKTGQLQANLNNLNLQLRDNSFIAATSQPTVHDVELFEATLPVIKELVSSSKDIKGTLGSYRHIIRWVDYLQALLQLSKDQTLEFDRNIELPREVIEKPKKKDDAKKDDGKKDDKKDDKKKANDGDKKQRGKPDEETLKKLREEAKAKKAAKKAAQAQQQKETKAPEKVLPSVIDFRVGFIQKAIKHPDADSLYVSTIDVGDEEGPRTVCSGLVKHFPLEAMQERYVVAVCNLKPVNMRGVKSTAMVLCGSNAEDKVEFVEPPKGSKAGDKVFFEGFGAEDPLKQLNPKKKLWEQLQPHFSTNENLEVIFKDEEDKEHPVRKLTNAKGEEFKVATIVNANVR
Protein: Bromo domain-containing protein (A0A1D8PG88)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex protein RSC58
- RSC chromatin remodeling complex ATPase subunit
- Npl6p
- RFX-type winged-helix domain-containing protein
- Chromatin structure-remodeling complex subunit SFH1
- Arp9p
- Uncharacterized protein
- Chromatin structure-remodeling complex subunit RSC1
- Uncharacterized protein
Sequence:
MPPKRKLSQSSAESSPVKKSTEESQNVAVTHSPQEYLDFFTSTLDMVFNLRDGDEELAPPFIKLPSKKFYPDYYHLIKQPISLNEIGKRIKTRYSGTSSREFLNDFELLLENASTYNSPDSWIVESARKIVNFVEGQVEEFESTSSTNLSTNKAADDTKKPRIKLKLKSIKKQTETETGPEFGSLVKVRKEEPLITFGRLAEFCINILNDVINHKFPNQGVLSGPFLEEVDTGVYTDYLDYVTKPMSFNTILSNLEKKKLLSPKFPLLDNLKKFHDTTTLIFSNAKAYNNEDSQIYQDAVILEEYFNEQYNKLKSRIESEADKLHPSTPKLKLNLGRIGPSVAEPQLKKKRKRSIKQEFPEEQIHEEEEDIDITQSEPTNADTQDIDEPADSKELDTSKSREVVTERNAPNTMGKTLPLLPEQNSIIQESVIFSSPAVSTNITKFVQQKSSQPATILSRDQEIKKSLFPTQPGNPIATLFSYKVPANGYTDQAHTIALPNGASPFVSFKVSLHNLLYQLKEPELIDDHGILSHLGNDDFQCKLSVNEEEVSNVADCFKEEKGEDVVLGVQYDVKLSYGLNVLSFNCKVAPALSKKIKNTFIEEEEVAGRHTRHQLQQMQKTWDVETITFYVVCTSG
Protein: Synaptic vesicle glycoprotein 2C (Synaptic vesicle protein 2C) (Q69ZS6)
Organism: Mus musculus (Mouse)
Function: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9Z2I6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z2I6}. Note=Enriched in small synaptic vesicles and adrenal microsomes, not present in chromaffin granules. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas. {ECO:0000250|UniProtKB:Q9Z2I6}.
Interaction partners:
- Synaptic vesicle glycoprotein 2B
- Synaptic vesicle glycoprotein 2A
- Laminin subunit gamma-2
- Laminin subunit gamma-1
Sequence:
MEDSYKDRTSLMKGAKDIAKEVKKQTVKKVNQAVDRAQDEYTQRSYSRFQDEEDDDDYYPPGETYSGEVNDDEGSSEATEGHDEEDEIYEGEYQGIPSTNQGKDSIVSVGQPKGDEYKDRRELESERRADEEELAQQYELIIQECGHGRFQWALFFVLGMALMADGVEVFVVGFVLPSAETDLCIPNSGSGWLGSIVYLGMMVGAFFWGGLADKVGRKQSLLICMSVNGFFAFLSSFVQGYGFFLVCRLLSGFGIGGAIPTVFSYFAEVLAREKRGEHLSWLCMFWMIGGIYASAMAWAIIPHYGWSFSMGSAYQFHSWRVFVIVCALPCVSSVVALTFMPESPRFLLEVGKHDEAWMILKLIHDTNMRARGQPEKVFTVNKIKTPKQIDELIEIESDTGTWYRRCFVRIRTELYGIWLTFMRCFNYPVRENTIKLTIVWFTLSFGYYGLSVWFPDVIKHLQSDEYALLTRNVQKDKYANFSINFTMENQIHTGMEYENGRFLGVKFKSVTFKDSVFKSCTFDDVTSVNTYFKNCTFIDTLFDNTDFEPYKFIDSEFQNCSFLHNKTGCQITFDDDYSAYWIYFVNFLGTLAVLPGNIVSALLMDRIGRLTMLGGSMVLSGISCFFLWFGTSESMMIGMLCLYNGLTISAWNSLDVVTVELYPTDRRATGFGFLNALCKAAAVLGNLIFGSLVSITKAIPILLASTVLVCGGLVGLRLPDTRTQVLM