wanglab/gogpt-training-data huggingface dataset:
Protein: Unconventional myosin-XVI (Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3) (Unconventional myosin-16) (Q9Y6X6)
Organism: Homo sapiens (Human)
Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. May be involved in targeting of the catalytic subunit of protein phosphatase 1 during brain development. Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9ERC1}. Note=Found in puncta in soma and processes of astrocytes and dissociated cerebellar cells with the morphology of migrating granule cells. {ECO:0000250|UniProtKB:Q9ERC1}.
Interaction partners:
Sequence:
MEIDQCLLESLPLGQRQRLVKRMRCEQIKAYYEREKAFQKQEGFLKRLKHAKNPKVHFNLTDMLQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIAASEFIEEMLLKAEIAWEEKMKEPLSASTLAQEEPYEEIIHDLPVLSSKLSPLVLPIAKQDSLLEKDIMFKDATKGLCKQQSQDSIPENPMMSGSTKPEQVKLMPPAPNDDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAVYSPMKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSALLSKKMTASSIIGENKNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKLQGWQMGVRKVFLKYWHADQLNDLCLQLQRKIITCQKVIRGFLARQHLLQRISIRQQEVTSINSFLQNTEDMGLKTYDALVIQNASDIARENDRLRSEMNAPYHKEKLEVRNMQEEGSKRTDDKSGPRHFHPSSMSVCAAVDGLGQCLVGPSIWSPSLHSVFSMDDSSSLPSPRKQPPPKPKRDPNTRLSASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPAGAPGAAARVLTPGTPQCALPPAAPPGDEDDSEPVYIEMLGHAARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLLHGASPPLLHRAPEDEAAGPPGDACDIPPPFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQPEGSSPLSPQYSKSQKGDGDRPASPGLALFNGSGRASPPSTPPPPPPPPGPPPAPYRPCAHLAFPPEPAPVNAGKAGPSAEAPKVHPKPNSAPVAGPCSSFPKIPYSPVKATRADARKAGSSASPPAPYSPPSSRPLSSPLDELASLFNSGRSVLRKSAAGRKIREAEGFETNMNISSRDDPSTSEITSETQDRNANNHGIQLSNSLSSAITAENGNSISNGLPEEDGYSRLSISGTGTSTFQRHRDSHTTQVIHQLRLSENESVALQELLDWRRKLCEEGQDWQQILHHAEPRVPPPPPCKKPSLLKKPEGASCNRLPSELWDTTI
Protein: Guanosine nucleotide diphosphate dissociation inhibitor 1 (AtGDI1) (Q96254)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the GDP/GTP exchange reaction of most RAB proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP.
Interaction partners:
- Ras-related protein RABH1c
- Ras-related protein RABF2a
- Ras-related protein RABF1
- Ras-related protein RABF2b
- Ras-related protein RABA5c
- Ras-related protein RABG3f
- Ras-related protein RABH1b
- Ras-related protein RABH1d
- Ras-related protein RABH1a
- Ras-related protein RABH1e
Sequence:
MDEEYEVIVLGTGLKECILSGLLSVDGLKVLHMDRNDYYGGESTSLNLNQLWKKFRGEEKAPAHLGSSRDYNVDMMPKFMMANGKLVRVLIHTDVTKYLSFKAVDGSYVFVQGKVQKVPATPMEALKSPLMGIFEKRRAGKFFSYVQEYDEKDPKTHDGMDLRRVTTKDLIAKFGLKEDTIDFIGHAVALHCNDNHLHQPAYDTVMRMKLYAESLARFQGGSPYIYPLYGLGELPQAFARLSAVYGGTYMLNKPECKVEFDEEGKVSGVTSEGETAKCKKVVCDPSYLTNKVRKIGRVARAIAIMSHPIPNTNDSQSVQVILPQKQLGRKSDMYVFCCSYSHNVAPKGKFIAFVSTDAETDNPQTELQPGIDLLGPVDELFFDIYDRYEPVNEPTLDNCFISTSYDATTHFDTTVVDVLNMYKLITGKELDLSVDLNAASAAEEE
Protein: Tetraspanin (Q6DH58)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
Interaction partners:
Sequence:
MEGDCLSCIKYLMFVFNFLIFLGGSFLLGVGVWVVVDPTGFREIVAANPLLFTGVYIILAMGGMLFLLGFLGCCRAIRENKCLLLFFFMLILIIFLAELAAAILAFIFREHLTREYFTKELKKHYQGYNNTDVFTSTWNAIMNTFDCCGVNSPEDFEESIFRIINPSEMVPEACCRRNNHVGESGFSNREECLSGSMLYRNNKGCYSAVVDYFEMYIYVAGALAIVVLTIELFAMVFAMCLFRGIQ
Protein: Anion exchange protein (H2L0C4)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSNGSPGRHSNKAFSIGSDDGENENVFVEETSTPPKTPLGTLLTNCTEQSPLILPMPTRPRLEDSPVAEHDHHIVVDVFTVNNDDGTWKQASRFARYEEDCEGFDNHLGRPHVPCIPMGTYDALKMVTAKSILFPKVQYESLDEFVNFLETKIVDPDVPKLGEKIAKLINDRIAEIEKMRPLHQRNSSSTQSLDASNPQTISTVGIFPRSLLSAPNNLGSLAHHPMRRLPTSHSGLRFGSSFLPQQPVVSQLEPVIWDEDNEISMLVAGEIPHVNVCRFIAIRFVETTAMEKIFPNMTNVRHLFFLIGPALENVTYLDLGRALASVVSNPPATTTFDQLKSPDSITKAIERFLAGTVVIAPGRIDNKNLVRSDLIRKLVNMQGEKTETKIVHPKDVDVERNATKKAEEAEDKPFRLFSGVTSDLRNRAKHYFSDYRDGFNISIFTVVFYMFCVTVVPTLTFGAIMGAGTSGLLAVKECLVSQALSGLIWSVLSCQPLLVMSPTGPFLVFEKALFKFTDQNDMDFLEVRFYTGIFLFFISIVGAATNCAHLIHYVTIYTEDIFCALISLIFFSEVVEFIHLQEEHNSIENLKYYIENAANCTVTEVKDCALSRPNTFLLQLIMVVVSIAIFHYLRQVSRSTFFGRTFRNLCKNFGGIFAVIAVSIAYRILFQNVGVAVVDIPVAVGQSRPFDGIFVIPSAPPTASTLTIALISSILLFVLIFVETEIPEQMALREGRKLKKGGGLHWDLIVVGFCTLVSSVLGLPWMCPAAVQSLAHITSLTEYKKSAPGVPSRISHVIEQRVSGMVTYLLLGTFAILGHFLAIPAATIFGVFFYLGVRNLEGSKMILRLKLCFLPSKYRGSHKFLEIVSSLKICSLIFNLH
Protein: Urocortin (Corticotensin) (P55090)
Organism: Rattus norvegicus (Rat)
Function: Acts in vitro to stimulate the secretion of adrenocorticotropic hormone (ACTH). Binds with high affinity to CRF receptor types 1, 2-alpha, and 2-beta (By similarity). Plays a role in the establishment of normal hearing thresholds (By similarity). Reduces food intake and regulates ghrelin levels in gastric body and plasma.
Subcellular location: Secreted.
Interaction partners:
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor receptor 2
- Urocortin-2
- Corticoliberin
- Urocortin 3.
- Corticotropin-releasing factor-binding protein
- Guanine nucleotide-binding protein subunit gamma
- Pro-opiomelanocortin
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
Sequence:
MRQRGRATLLVALLLLVQLRPESSQWSPAAAAANVVQDPNLRWNPGVRNQGGGVRALLLLLAERFPRRAGSEPAGERQRRDDPPLSIDLTFHLLRTLLELARTQSQRERAEQNRIIFDSVGK
Protein: Torsin-1A-interacting protein 2, isoform IFRG15 (15 kDa interferon-responsive protein) (IFRG15) (Q9ER81)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFSDNSHCPDCGQQWFPSLELGHWLYQTELVENECYQVFLDRINRADYCPECYPDNPANRSLVLPWSFPLEWAPQNLTRWTFEKACHPFLLGPPLVRKKIHDSRVAGFNPALQLILSRTDKTLNKKLGQSK
Protein: Methyl-accepting/DNA response regulator (A0A6L8P7A9)
Organism: Bacillus anthracis
Interaction partners:
Sequence:
MEDKTLGLLLDVVGELFSDEISIAVSNTKEYIYYRPSKRIDLKISAGDPIKEGTIAHKAMVTNQKTSEFINRDVFGIPYHGMAVPFSNNGKLEGCVTAIYPALTDGKSVVTLKTTDGWVPVPFSKVMYLEAKDKKTYVNAEELTGTHKYSLQEFEYLLPKDSFIRCHRSFIVNVNHIKAIYPDTHSTFVLSMDNGERVPVSQSYASYFRKLLGF
Protein: PIN domain-containing protein (Q1T6W7)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNGDTDASSSRTGAPRKPRPEIQIYRPGMLRQGGSTKSLSSTNEEARPPRPEKLNTTTTTMSGNSRRRSNDTDSVTSRGGSGSTTPDANVINAMNERGGGRNRFEKGYRQQQRTDGPSNYNSTQSLYDTRQHGGYMEYQGNHRSNHRNNGRYSNQQHQQHRQPFERPGGNHYTRGFNERASMRGDGAIARRPQGSRRQRNDSINSTQSEMPPQTGAQLHIDTSFDSASQCGASSNFSMNSLGEAFSFEEMCQNLQNFASMDWSKEVENEFAMQKEQEEEEERRMEQKLQEAAAQEAQKAASPRRNNRRNNRRGGGNSRYHPDESDRESSFGGSIAEEKEEEEAEEELKSGERTPTSVRSGNSYNPRVLYQRTRGANDENHPKRRDAAVEKKPKEPRRYRGEHDDRDDDASEYHGTLENHMSSGRLAGRIQIVQRSQNGTEAGGNRNRQSSEEKPRTYQKRSQNQSEMANRAEINRRRQEDIDRNEGKQIREISEKIEKLSAPVKKRDLKSAEKMAEISMELANIYSQVIIHDVIYSFTAGLEQKLFRQAFYKCIESLRTGSNSAAPDARLIRAVTQKLLLNGIVYYENLIATYETQFHVALTDALTWQSGSPSDEELCEQYIELPIGIQKFDSATQKTAIKSLSRHLISLGDLHRYKSLIDGSENYEISKSCYQKSSQLWPSTGHPYNQLGIVVYYSKRVIDEFFCLTRALACSHPYEVAKDRLKQRIDAMRTKVAKYQPVLDKESGIVKEQGNVLRRLQRIRQIWIHPITETSQDGTGERIVDDVLVHFMEHSKAKLHRRAVSYLCDTFGMLVTKIGMDHFESVSERAFGLLYASLSKSETDFSADQLVKFSAMFIYAAQVNFDKSTPSTSKSQLHTAVRTIFTYFLVLLEHISTHTTLLLPAANVIATWILHADTEELLSYLEHLEPLSSTIISSFSNFPPNLESEAENPENVTTPEAILLASFFKIYEPNPTPVRCSRSTNISQAVEKLKILGFSAEKSEKSGENGKQKLGDGLEEPKSREQMIDEQRGLGKTTIVIHPEYLIPDTNVLIGDLQLMKNLLETAQKNKKFQILVPTTVLDELQYIAKLSPLDSKSNSEAHDPERISKAKIAVAWLKEQAKQKTGHLYTLTTTGKRLPTLSIVSEDLEGHEMTTNDDMILNSALRWSESLPGSTAPSATEISQKCVLITGDRGLTIKAIGNNFPCRGISNFTKWIINV
Protein: 60S ribosomal protein L7, putative (Q388M6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- 60S ribosomal protein L17, putative
- GST N-terminal domain-containing protein
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L19, putative
- 60S ribosomal protein L27, putative
- 60S acidic ribosomal protein P0
- Ribosomal protein
- 60S ribosomal protein L6, putative
Sequence:
MGKNPPKWLPGERVKETILLQRKSVEQLRVDRVLRRDKLQERRERHKAKIDAKRKRKLSTKKFISAQTILKRAQLREKQGRLFQKIGEKATGKKGRMGEEEYGKSLEDSRVVLIVRARGKLIPHEVALAFGRLGLRKLYSARLLCLNPFTDPLVKQLGPFSVVGHPEPAQLNELLRTRGALWNEETKTKRLINGNLMLEKALGEYNVLCIEDLCDVIINKTEHVRDVLKHIAPFDFHPPRQLFMERHRNVYQKMEVMNKESFAAYLAQELKASARREKRAVGKRKAVEESSQSSQKTS
Protein: Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (Formylglycinamide ribotide amidotransferase) (Phosphoribosylformylglycineamide amidotransferase) (O15067)
Organism: Homo sapiens (Human)
Function: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Amidophosphoribosyltransferase
- Receptor expression-enhancing protein 5
- Adenylosuccinate lyase
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Bifunctional purine biosynthesis protein ATIC
- RNA-binding protein 8A
Sequence:
MSPVLHFYVRPSGHEGAAPGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKLMWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVETTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEGRLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLHVDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQGLRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREWIKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTSRFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVLVDDRECPVRRNGQGDAPPTPLPTPVDLELEWVLGKMPRKEFFLQRKPPMLQPLALPPGLSVHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIGAATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAALADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTPDLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLKDRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPDLAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDRLQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAGAELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLRHNLSGRYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWADDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTSPWLQLFINARNWTLEGSC
Protein: Bardet-Biedl syndrome 4 isoform 3 (A0A0S2Z328)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEERVATAILAAGSMMQTHGDFDVALTKYRVVACAVPESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPFDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDIENAKRAYAEAVHLDKCNPLVNLNYAVLLYNQGEKKNALAQYQEMEKKVSLLKDNSSLEFDSEMVEMAQKLGAALQVGEALVWTKPVKDPKSKHQTTSTSKPASFQQPLGSNQALGQAMSSAAAYRTLPSGAGGTSQFTKPPSLPLEPEPAVESSPTETSEQIREK
Protein: Phox domain-containing protein (Q86IF6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Vacuolar protein sorting-associated protein 26
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
Sequence:
MSDYNSNLLFGTQVTYEDNGENTFVGFSNEPIESSNPFLAPPQQQEQQEQPSYPQVQQQYSKERIPASQPPSYNPPQPTQQQQQQTNNNGTTVQQKQRTSQNYQQPPPQQQQQVSNNSNFQSNFKPTFTTPVNQFISNSRTSMDITVNFPDMVGEGMGAYAIYKIVTKSALNENPDYKKEVSVNRRYSDFLWLRNALKETRKGCIIPQLPEKAVLNNRNKDFLEQRRRDLEKFLNRVVESNSLAQSNEILTFLEGSDEQLNAAKQSRPDQSNMESSTMSPPPSQEGGKMGKISSFFGNSISTLTQGVHSVKEIDGWFGDKKSYILQLDSTLHRLEDTINNVIRKRRELAAAMGELTSAGLSFSSCEIPVRQDIANGYQRLTEVENNIRQGMEDLSNNEQGYFEEGIRDYLRAISSVKELLNDRLDALMSMQNNERNVAAKKEKAAKTTGAKAANMQKEVDDAVRKLTEATTEYEKISASARLELTKFDEKRAYEMKRILNYVIRLNLDHFLKSSDCWRELLTEQHSNGDPNFDSKNKASWGSTSI
Protein: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase) (GFAT) (Glucosamine-6-phosphate synthase) (Hexosephosphate aminotransferase) (L-glutamine--D-fructose-6-phosphate amidotransferase) (Q6LWM9)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glutamine synthetase
- Carbamoyl phosphate synthase large chain
- Phosphoglucosamine mutase
- Probable glucose-6-phosphate isomerase
- Amidophosphoribosyltransferase
- Carbamoyl phosphate synthase small chain
- Phosphoribosylformylglycinamidine synthase subunit PurQ
- Uncharacterized metallohydrolase MMP1398
- Bifunctional protein GlmU
- Conserved hypothetical Archael protein
Sequence:
MCGIIGYIGNEKASKILLKGLKRLEYRGYDSCGIATIDDTIKLKKNTGKVLEVSKKENFEDMTGFIGIGHSRWATHGGITKNNAHPHYDCSEKICIAHNGIISNYKELKELLISKGHIFKSETDTEVIPHLIEEEIKDFKEITEKTYINAIQNTIKKLNGTYALLILNQDFPEMLVGVRNESPLILGIKKDECFIGSDISAFLEYTKLAMPLNDRDIVILRKENDEIDIEVLNYGKQVQRDTIELQWDMESAEKEGYEHFMLKEIMEEPVILKNSMKISKLEIENLGKEIEKCDKIYITAMGTSLHAAMVAEYWFSGLNKLVIPIDSSEFLTKGIVDEKTLVIAITQSGETYDTMKAVKYAKEKGAKTATIVNVLGSTATREADITIMMGSGLEIAVCATKTFMSQLVILYRLFIEYGKIIGKNMDIFEKELLNIPNYISKVLDEKENISKIAEELTAKNYLFISKGINLANALEGALKFKEITYLHAEGMSSGFLKHGTISLIDENMDTVALIPPSKSELLNSVLSNVEEIKARNGKIIGISPVEDNLKYSIKVPDVIEEVSPFVYATACQLLAYYKAVDLKRDVDKPRGLAKSVTVE
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 2 (Q86IL5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable regulatory subunit of serine/threonine-protein phosphatase 4 (PP4).
Interaction partners:
- Suppressor of Mek1
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 2A catalytic subunit A
- Protein phosphatase 2A catalytic subunit B
- Probable serine/threonine-protein phosphatase 2A activator 1
- Probable serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase 2B catalytic subunit
- RNA methyltransferase
- Cleavage and polyadenylation specificity factor FIP1
- Large ribosomal subunit protein eL18
Sequence:
MTLVEYSETLKKSLEEFCKQDKKVVTPELNSIIENISKTGITCYPWNILKELFYFKLNEILDIFEKEYIATSSTTTTSTTTTTTNTSSSSTNSPQSPQSPQSPQLNVNIKDEEMQKIKNQVNLSGLIKMKKEFLDSFKESKLSPFTVQRLCELIINYKMYTSFSKYLCAVEKMLNVSTLPHLTPEEVIEFNKNQNSGSRLNSSTNTTTTTTTTTTTTTPTEKGNNDQPNLDSFAFSSSFTTSFPSDTTSSTSTSLSTDQEMKDLDVEQQKDDTDNTANENESK
Protein: Outer segment 6 (A1ZBM3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport 43
- WD repeat-containing protein 35
- Reduced mechanoreceptor potential A, isoform B
- Outer segment 5
- No mechanoreceptor potential B, isoform D
- Intraflagellar transport 52
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
Sequence:
MSFEKILYKYEEPHGIGDVYFIWQKALLATTGTDGSVALYNRQGQLVQRIILSGLCSGFAWDQEGDLLGIITSGSPNITLWDYNSQEKISVETGLRDPLTCILWSKQQQLLAVGTGRGNLAIYNHSSGKRPTPVLGKHSKRITCGAWSAQNLLALGSEDKSFSLSNEDGDTVRVVQLRDAPTDMYFAEMANDERIAGDNAISMIIGKRTLFLYYLPEPENPTELGFQSRYGSLMQHKWFGDGYILLGFSNGHVVAISTHPKDVGQELWQVKNHKDSLTGLAYCPTLDIVASCGDDSIKIHSITNLQETERIITVPDHAGVQMIDWSPDGQLLAVTTNHGTVYIYVTKLPHLFAVSAPRIVLLSSLAEVSIYVYAPDKTKSLPFRLPLEGEPTFMAVGPYNFATGIEKHVWFYDLGKSLGEEPRPLSERDFPRSVESMKLNADYCAALCPPQLILQAIAADNPNCKDKLQAVFPTALPNMPSDAVITCFALSQELLIFATDIGHLVFYSLEKWDSCTIYRHSMGIRQLFMDIEGTKVIFIDDHSQGYVFLPVVEEALLIPDIPKQCLGCLWDLTQPNIFISYDARIVNTHVFVRHSVQGTHTLMVGESKLNPGQFPLLLCGGEMALHIDGGQYATQSLSTHVVNPSNSQAANLQMLLKLRNYDEAYKLCKQMNQSSAWREFGEQAISDLEPDIAIRAYRQLGDAALVNALSELRYVEDLDMLIGCCCTLLAQYDQAKEHMLKGVYTRAALDLCRDLLQWDQALLLAHKNDPQEVPYIAREYAQQLEFNGNYTDALYHYEKGYKEDLINSKETETDALMDSSPEYEEHVRLCKMGIARTSIRAGDFRRGIQYAVELEDQQLLFDCAELLATVGHLTEAAGLYERGGFYDEACGHYIALKMWNKANNILPKVKSTKLHAAYAKAKENDGHYEEAIRSYRIAGDLDACVRIYLDHLCDPHAASEIVLESRSMDSAKLLAKFYQKIGDVEQALQFLVICGCVEEAFALAQRHNKLRRHGELLERYENAKSSDYLALAHYFEGEKYTLLAGKYYFLAREFTKALRFLLKASAFNNEEQVSLSLAIDCVATSNNEQLATQLIEFLLGEVDGVPKDPRYLFRLYMARKHYKDAAKTAVIIANQEQIAGNYKSARDLLYSMYQELRRNNLSVTAEMRHQFILLHRYTLVRIHVKLGNHLLAAKLLVQVAACISQFPEHIIPILTSTVIECHRAGLKKSAFTYASTLMRPDYRNQLDPRYAKKIESIVRKAPKGIKQLRDEIDGETMECPICDSNLANMEVTCYSCKTTLPICIATGQHIIKQLMTSCPQCDFLCFRAEMENILSENGECPMCGENVAPEQLLDVEDIRPYILAAS
Protein: B double prime 1, isoform A (FI12401p) (Q9VJZ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- B-related factor 1
- TATA-box-binding protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC6
- FI04119p
- LD32951p
- TBP-related factor
- LD44919p
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC2
Sequence:
MSMRRQRIKAPANLSLIKRKPRREELPTAKKEDEEEEAVVVEAEAESPPVASTPAAELELEADAIAFKMPASSAGQLEEVFHSDLEDNVIQMDLQKTTNGFPMSPSKAQARQRVRPTPVFGQRRNSFVGSPMASDYEGDYQSPATPTRRERYLSGSSSGTPLQQQVHSPMPPSPYKYLPPASPGMGRIRTESTCSTYSEGGSKQRKGDDRSQSQIGQRLNARRDFETRFNKGVPDKSTFKMMDMIFYNPENNPMVPKQSVTTIKDESGGDDSKPAVSQLLEPKGESTSAMLVPQLKLDANGEMIIDEKTLEIETTAEVEARKVLANSSLILMDETTGDNGFYKRHKRTPYWTSDETVRFYRSLQIIGTDFSLMCQMFPTRSRRDLKLKYKKEERTNGQLINKALLYPKAFNIQELKDQLEEEDREREENDRKWREIARALPGNPKKRSRVQQQSKASRALNDGDVVYENEHVTSTKLGKHAWAKRRKELETDENDGSAPAKRKPKAKRRSPKVSVPAATESLSDVAAIKQEKTIKTEQTSSHLPTGGELQAELNGLLMDDPVEYDVDVNKPRDKTIINMDDGTLSYVSDVEPAPETPNRKAETYLINFIEDQDHELITPDDPIPPSTTEPDIEQILAELAEGSLALVSSLDPEHEDRVLNEIYMLDKKTGELCETPLKIPEHIVQCIMNVMQPED
Protein: Cytochrome P450 3A (EC 1.14.14.-) (Q8HZK1)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
Interaction partners:
Sequence:
MDLIPSFSTETWLLLAISLVLLYLYGTYTHGIFRKLGIPGPTPLPFVGTALGYRNGFYVFDMKCFSKYGRMWGFYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRTLGPVGFMKSAISLSEDEEWKRIRTLLSPTFTTGKLKEMFPIIGQYGDVLVNNLRKEAEKGKAINLKDVFGAYSMDVITSISFGVNIDSLNHPQDPFVENTKNLLKFDFLDPFLFSILLFPFLTPVFEILNIWLFPKKVTDFFRKSVERMKESRLKDKQKHRVDFLQLMINSQNSKEMDTHKALSDLELVAQSIVFIFAGYETTSSCLSFLMYELATHRDVQQKLQEEIDATFPNKAAPTYEALVQMEYLDMVLNETLRLYSVAGRLERVCKKDVEISGVFIPKGTVVMVPTFILHRDQNLWPEPEEFRPERFSRKNKDSINPYTYLPFGTGPRNCIGMRFAIMNMKLALVRVLQNFSFKSCKETQISLRINTRGIIQPEKPVVLKVEPRDGSVSGA
Protein: Lipid phosphate phosphatase delta (AtLPPD) (EC 3.1.3.-) (Phosphatidic acid phosphatase delta) (Sphingoid phosphate phosphatase 1) (AtSSP1) (Sphingosine-1-phosphate phosphatase) (AtSPPASE) (Q9M2G7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as sphingoid long-chain base phosphate (LCBP) phosphatase. May play a role in the regulation of LCBP levels and be involved in stomatal responses through LCBP-mediated ABA signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:21910031}; Multi-pass membrane protein {ECO:0000305|PubMed:21910031}.
Interaction partners:
- Sphingosine-1-phosphate lyase
- Sphingosine kinase 2
- Sphingosine kinase 1
- Putative lipid phosphate phosphatase 3, chloroplastic
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 31
- Sphinganine C4-monooxygenase 1
- Sphinganine C4-monooxygenase 2
- Mediator of RNA polymerase II transcription subunit 23
Sequence:
MKKILERSMEGSGTWQGLVLVGIVTWICASSYLKFTHKFRSLLQPWVARQVVGGVPLILRIQKCQNGVLDAFFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDNAMEYGLPSSHTLNTVCLSGYLLHYVLSSLEYESVSIQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLWLTVNEKLDDFITSKQNVSSFWTALSFLLLFAYPTPEHPTPSYEYHTAFNGVTLGIVTGVQQTYSQFHHEAAPRIFSPELPISSYLGRVMVGIPTILLVKFCSKSLAKWTLPMVSNALGIPIRSSMYIPKLKGYASGKKTDEPKNSVGYLQKLCEFLSHDSFDIDTGIRFFQYAGLAWSVVDLVPSLFSYVNL
Protein: Core histone macro-H2A.1 (Histone macroH2A1) (mH2A1) (H2A.y) (H2A/y) (Q9QZQ8)
Organism: Mus musculus (Mouse)
Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription (By similarity). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (By similarity). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (By similarity). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). Involved in stable X chromosome inactivation (By similarity). Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (By similarity). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15564378, ECO:0000269|PubMed:9634239}. Chromosome {ECO:0000269|PubMed:15564378, ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin (PubMed:9634239). In quiescent lymphocytes, associated with centromeric constitutive heterochromatin (PubMed:15564378). Recruited to DNA damage sites in an APLF-dependent manner (By similarity). {ECO:0000250|UniProtKB:O75367, ECO:0000269|PubMed:15564378, ECO:0000269|PubMed:9634239}.
Interaction partners:
- Histone deacetylase 1
- Histone H4
- Histone H3.3
- Histone H3.2
- Histone H3.1
- Histone deacetylase 4
- Histone deacetylase 2
- Lysine-specific demethylase 6A
- Histone H2B type 1-A
- Poly [ADP-ribose] polymerase 1
Sequence:
MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVAKKTGGKKGARKSKKKQGEVSKAASADSTTEGTPTDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYTGGEVGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAISAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDRKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFMLFDSESIGIYVQEMAKLDAN