wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A140VJW1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKYHVLEMIGEGSFGRVYKGRRKYSAQVVALKFIPKLGRSEKELRNLQREIEIMRGLRHPNIVHMLDSFETDKEVVVVTDYAEGELFQILEDDGKLPEDQVQAIAAQLVSALYYLHSHRILHRDMKPQNILLAKGGGIKLCDFGFARAMSTNTMVLTSIKGTPLYMSPELVEERPYDHTADLWSVGCILYELAVGTPPFYATSIFQLVSLILKDPVRWPSTISPCFKNFLQGLLTKDPRQRLSWPDLLYHPFIAGHVTIITEPAGPDLGTPFTSRLPPELQVLKDEQAHRLAPKGNQSRILTQAYKRMAEEAMQKKHQNTGPALEQEDKTSKVAPGTAPLPRLGATPQESSLLAGILASELKSSWAKSGTGEVPSAPRENRTTPDCERAFPEERPEVLGQRSTDVVDLENEEPDSDNEWQHLLETTEPVPIQLKAPLTLLCNPDFCQRIQSQLHEAGGQILKGILEGASHILPAFRVLSSLLSSCSDSVALYSFCREAGLPGLLLSLLRHSQESNSLQQQSWYGTFLQDLMAVIQAYFACTFNLERSQTSDSLQVFQEAANLFLDLLGKLLAQPDDSEQTLRRDSLMCFTVLCEAMDGNSRAISKAFYSSLLTTQQVVLDGLLHGLTVPQLPVHTPQGAPQVSQPLREQSEDIPGAISSALAAICTAPVGLPDCWDAKEQVCWHLANQLTEDSSQLRPSLISGLQHPILCLHLLKVLYSCCLVSEGLCRLLGQEPLALESLFMLIQGKVKVVDWEESTEVTLYFLSLLVFRLQNLPCGMEKLGSDVATLFTHSHVVSLVSAAACLLGQLGQQGVTFDLQPMEWMAAATHALSAPAEVRLTPPGSCGFYDGLLILLLQLLTEQGKASLIRDMSSSEMWTVLWHRFSMVLRLPEEASAQEGELSLSSPPSPEPDWTLISPQGMAALLSLAMATFTQEPQLCLSCLSQHGSILMSILKHLLCPSFLNQLRQAPHGSEFLPVVVLSVCQLLCFPFALDMDADLLIGVLADLRDSEVAAHLLQVCCYHLPLMQVELPISLLTRLALMDPTSLNQFVNTVSASPRTIVSFLSVALLSDQPLLTSDLLSLLAHTARVLSPSHLSFIQELLAGSDESYRPLRSLLGHPENSVRAHTYRLLGHLLQHSMALRGALQSQSGLLSLLLLGLGDKDPVVRCSASFAVGNAAYQAGPLGPALAAAVPSMTQLLGDPQAGIRRNVASALGNLGPEGLGEELLQCEVPQRLLEMACGDPQPNVKEAALIALRSLQQEPGIHQVLVSLGASEKLSLLSLGNQSLPHSSPRPASAKHCRKLIHLLRPAHSM
Protein: Cingulin-like protein 1 (Junction-associated coiled-coil protein) (Q6AW69)
Organism: Mus musculus (Mouse)
Function: May be involved in anchoring the apical junctional complex, especially tight junctions, to actin-based cytoskeletons.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:15292197}. Note=Localizes to the apical junction complex composed of tight and adherens junctions. In the liver and kidney, it is also found along non-junctional actin filament bundles in addition to the apical junction. {ECO:0000269|PubMed:15292197}.
Interaction partners:
- Tight junction protein 1
- Rho guanine nucleotide exchange factor 2
Sequence:
MELYFGEYQHVQQEYGVHLRLASGDTPKPRNSQPSKAGSYGVSIRVQGIDGHPYIVLNNTERCLAGTPFPENAPSFPSSVINNLSLHPSNGTVLKENTPEELQLPENPYLQTSPLRGQKQFSLHEGRNGVLERKDGPTKLPHVLNFQRHPELLQPYDPEKNEVNAKKHHPPESPWLRNATEDGTNCKKSRNCFPKSYGSQPNSPTSEDLAKTNMTAIRLCSSVVIEDPQKQTSVCVNVQRCAKEGVGEETLSPRRKSPTAPSPQAYSETKKNRPDVLPFRRQDSAGPILDGARSRRSSSSSTTPTSATSLYKFLLDDQECAIHADSVNRHENRRYIPFLPGTGRDIDTCSIPGVDQLIEKFDQKPGLQRRGRSGKRNRINPDDRKRSRSVDSAFPFGLQGNTEYLTEFSRNLGKSSEHLLRPSQVFPQRSVAQEHRGKHSPSSPPAKLQGAQGAHPKPPLQNKDGKVLNKGRQESTGACAPSLPAPNKKEEEIKIATATLMLQNRAVAATSDSGAKKISVKTFPSDSSTQATPDLLKGQQELTQQTNEETAKQILYNYLKEGGTDNEDATKRKVNLVFEKIQTLKSRAAGSAQGSNQAPNSPSEGNSLLDQKNKLILEVSELQQQLQLEMKNQQNIKEERERMREDLEELRVRHQSQVEETATLQRRLEESEGELRKSLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSTKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNSSEQSQAEADLREKVLKEENEKLQGRIAELERRAAQLQRQMEDVKGDEAQAKETLRKCESEVQQLEEALVHARKEEKEATCARRALEKELEQARRELSQVSQEQKELLEKLRDEAEQKEQLRKLKNEMESERWHLDKTIEKLQKEMADIAEASRTSSLELQKQLGEYKEKNRRELAEMQTQLKEKCLEVEKARLAASKMQDELRLKEEELQDYQRAEEEALTKRQLLEQSLKDLEYELEAKSHLKDDRSRLIKQMEDKVSQLEIELEEERTNADLLSERITWSREQMEQMRSELLQEKAAKQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLENEERDRANLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMGVNEQLQGQLNSLKKGLRLKTLSSKVLDDSDDDDLSSDAGSLYEAPLSYAFPKDSTIASQI
Protein: ATP-binding cassette sub-family C member 3 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (Canalicular multispecific organic anion transporter 2) (MRP-like protein 2) (MLP-2) (Multidrug resistance-associated protein 3) (O88563)
Organism: Rattus norvegicus (Rat)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (By similarity). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate). Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (By similarity). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:11897632}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:O15438}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hepatic sodium/bile acid cotransporter
- Solute carrier organic anion transporter family member 1A4
- Solute carrier organic anion transporter family member 1A1
- Solute carrier organic anion transporter family member 2B1
- Solute carrier organic anion transporter family member 1B2
- UDP-glucuronosyltransferase 1A1
Sequence:
MDRLCGSGELGSKFWDSNLTVYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHRLGYIVLSCLSRLKTALGVLLWCISWVDLFYSFHGLVHGSSPAPVFFITPLLVGITMLLATLLIQYERLRGVRSSGVLIIFWLLCVICAIIPFRSKILLALAEGKILDPFRFTTFYIYFALVLCAFILSCFQEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTKLAILGYRRPLEDSDLWSLSEEDCSHKVVQRLLEAWQKQQTQASGPQTAALEPKIAGEDEVLLKARPKTKKPSFLRALVRTFTSSLLMGACFKLIQDLSPSSTHSCSASSSGLFRPHGPYWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQGELQLLRKGAYLQAISTFIWVCTPFMVTLITLGVYVCVDKNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRIQDFLNQDELDPQCVERKTISPGRAITIHNGTFSWSKDLPPTLHSINIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLRNYAPDENQEANEGVLQHANEEVLLLEDTLSTHTDLTDTEPAIYEVRKQFMREMSSLSSEGEGQNRPVLKRYTSSLEKEVPATQTKETGALIKEEIAETGNVKLSVYWDYAKSVGLCTTLFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIHEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPWVLESNRAPEGWPRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA
Protein: LUC7 related protein (F4IZU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDAIRKQLDVLMGANRNGDVQEVNRKYYDRDVCRLYLSGLCPHDLFQLTKMDMGPCPKVHSLQLRKEYREARAKGVDNYDRELEDAIDRLIVECDRKIGRALKRLQEEDAKAAIAISVSEVTQSPEILELSEKIKEKMKEADIHDLEGKMDLKIRALELVEEMRTKRADQQAVLLLEAFNKDRASLPQPVPAQPPSSELPPPDPRTQEMINEKLKKAEDLGEQGMVDEAQKALEEAEALKKLTVRREPPADSTKYTAVDVRITDQKLRLCDICGAFLSVYDSDRRLADHFGGKLHLGYMLVRDKLTELLDEKANIRKERSKERNSKERESSKDREKEQETSREHRRDYDRRSRDRDRHHDRDREQDRDYDRSHSRSRRRSRSRSRSRDRPRDYDRHRRHNRY
Protein: Flagellar biosynthetic protein FlhB (Q0PBH4)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Flagellar biosynthetic protein FliR
- Flagellar biosynthesis protein FlhA
- Flagellar biosynthetic protein FliQ
- Flagellar biosynthetic protein FliP
- Flagellum-specific ATP synthase
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliG
- Flagellar M-ring protein
- Flagellar motor switch protein FliN
- Flagellar basal-body rod protein FlgC
Sequence:
MAGEDQEKTEEPTSKKIEDARKEGNVPKSQDAAAIVTLIIGVTITLFMMSFMGERIVNLYRYYQSFIGVEFDLRIIQAIMIKSIFEVLIILAPIVLSIMIAGVLGNIMQFGFIFTTKPIMPNLGKINPLKGLKNLFSLKKIVESIKIILKVGIVFTIAFIVLLKFMQELPRVELYTMVAQLTWLRDRAIVLAAIVIVAFLIIAVLDVFLVRFQYFKGLRMSKQEIKDEYKQMEGDPQVKGRIRRLQMEAARRRMVQDVAGADVVITNPTHYAVAIRYDTGKEQAPRVVAKGVDFLALRIKQVAYENNVVVYENPPLARELYKACDVNDLIPREMFKAVAEVLGFVYNTNNKSRLAGQVKKGN
Protein: Heat shock 70 kDa protein (HSP70) (P08106)
Organism: Gallus gallus (Chicken)
Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.
Interaction partners:
Sequence:
MSGKGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKYDDPTVQSDMKHWPFRVVNEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGKKVETAVITVPAYFNDSQRQATKDAGTITGLNVMRIINEPTAAAIAYGLDKKGTRAGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNRFVEEFKGKHKRDNAGNKRAVRRLRTACERARRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVTPLSLGIETAGGVMTALIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKDDIDRMVQEAEKYKAEDEANRDRVGAKNSLESYTYNMKQTVEDEKLKGKISDQDKQKVLDKCQEVISSLDRNQMAEKEEYEHKQKELEKLCNPIVTKLYQGAGGAGAGGSGGPTIEEVD
Protein: FAD-dependent monooxygenase afoD (EC 1.-.-.-) (Asperfuranone biosynthesis protein D) (Q5BEJ7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent. The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation. AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2. After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination. AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone. Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood. Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Asperfuranone cluster transcription factor afoA
Sequence:
MADHEQEQEPLSIAIIGGGIIGLMTALGLLHRNIGKVTIYERASAWPDIGAAFAFTGIARECMQRLDPAILSALSKVAQRNPHDKVRYWDGFHPKSKEEAQDPEKSVLFEIEEKNMAYWACLRGVFHAEMARLLPERVVRFGKRLVAYEDGGDQKVVLRFEDGEVEEADIVIACDGVHSTARRVLLGAEHPAANARYSRKAVYRALVPMPAAIDALGTEKAHVQIAHCGPDAHIVSFPVNNAQIYNVFLFTHDSNEWTHGHTMTVPSSKEEILSAVENWGPHIKELASLFPEQLSKYAIFDQADHPLPYYAAGRVALAGDAAHASSPFHGAGACMGVEDALVLAELLEKVQNGSAFKEKKSNIELALKTYSDVRIERSQWLVKSSREMGDLYEWRYEDIGGDGVKCKAEWERRSRVIWDFDVQGMVDQAREAYERAVVKV
Protein: Inhibitor of growth protein 2 (Inhibitor of growth 1-like protein) (ING1Lp) (p32) (p33ING2) (Q9H160)
Organism: Homo sapiens (Human)
Function: Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs).
Subcellular location: Nucleus {ECO:0000269|PubMed:12859901}. Note=Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns(5)P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Histone H3.3
- Histone H3.1t
- Histone H3.3C
- Histone deacetylase complex subunit SAP30
- Histone H3.1
- Histone H3.2
- Histone H3-7
- Histone deacetylase 1
- Histone deacetylase 2
Sequence:
MLGQQQQQLYSSAALLTGERSRLLTCYVQDYLECVESLPHDMQRNVSVLRELDNKYQETLKEIDDVYEKYKKEDDLNQKKRLQQLLQRALINSQELGDEKIQIVTQMLELVENRARQMELHSQCFQDPAESERASDKAKMDSSQPERSSRRPRRQRTSESRDLCHMANGIEDCDDQPPKEKKSKSAKKKKRSKAKQEREASPVEFAIDPNEPTYCLCNQVSYGEMIGCDNEQCPIEWFHFSCVSLTYKPKGKWYCPKCRGDNEKTMDKSTEKTKKDRRSR
Protein: Endonuclease V, putative (Q38AS1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGVGEMSEVTATKLDMWASMQKRLAAEVCVPNTNGMVELYEEGTECVKAPRDSFLLPHHLVEEFASSAIGPQLERDERRRGRHSPPILRHVGGVDISFIQGGDTAVACLAVMEYPSMKVCRTFVQRCEVKEPYITSYLAFREAGPLVQLIESVRDELFEEACFPQLLLVDGCGVHHPLRCGLASHLGVVLDIPTVGCAKKFLSIDGITRDSMDARFAEEHTVASRRFEGTYLSSSSGVCEACFVPIIGESGRLWGYAATPNRRVKNPIFISPGNRVGYAEAAALAVSMCKYRVPEPIRAADLHSREFIRRIQLNEC
Protein: Probable proton-coupled zinc antiporter SLC30A3 (Solute carrier family 30 member 3) (Zinc transporter 3) (ZnT-3) (Q99726)
Organism: Homo sapiens (Human)
Function: Probable proton-coupled zinc ion antiporter mediating the import of zinc from cytoplasm into synaptic vesicles and participating to cellular zinc ion homeostasis in the brain.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:26647834}; Multi-pass membrane protein {ECO:0000255}. Synapse, synaptosome {ECO:0000250|UniProtKB:P97441}. Late endosome membrane {ECO:0000269|PubMed:17349999}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17349999}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- AP-3 complex subunit delta-1
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter SLC39A7
- Zinc transporter ZIP1
Sequence:
MEPSPAAGGLETTRLVSPRDRGGAGGSLRLKSLFTEPSEPLPEESKPVEMPFHHCHRDPLPPPGLTPERLHARRQLYAACAVCFVFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFVRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPPHSHGSRGAEYAPLEEGPEEPLPLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQYKAADPISTFLFSICALGSTAPTLRDVLRILMEGTPRNVGFEPVRDTLLSVPGVRATHELHLWALTLTYHVASAHLAIDSTADPEAVLAEASSRLYSRFGFSSCTLQVEQYQPEMAQCLRCQEPPQA
Protein: Uncharacterized protein (Q38E33)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MTTATELKQKGNEAYAAKRFEEALKYYEEGLALDGGNIDLLNNAAAASFSLGRCEAAISFARRSLGVRDNFKAHKRVGEAFWKMGNLREAAAEYEKALALEPTDSSSRENLQKLRQEMNRGQAQFGGSPVVMPQITPHGTVGLLVDTLVLVLSFAALASSLIGVNGSSAWFLLLIAAAARHAVIAHSRHMLVPDLSILKSWFDVRCTLDLILCLVALISGVRAQLPLVVVQGLYSALSLATNFSRVQQVAPAAYQAGLRYAQSITSNAQRLIMHAVSLEAIMLLTVIFSGGAIFTLFYIQYAKNLYRIDGNVRLAFYGIRENLTQLARKGFMPAFVDSTLQRVCDTLYQFSQQPF
Protein: Uncharacterized protein, isoform D (EC 3.1.4.2) (Q86BI9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Myosin 10A, isoform D
- GEO12033p1
Sequence:
MIFSRAPVQHVILFAPLKVTSGSGATKDACLSRELVFDSKSRNRRFRRAGGGIGSTGARELGSRDSRQSTPRLEKLYQAETESARGHRLISLAQQESCRAFNSGLRRSIDFQSARDLHSNPMAMSRTVLILAVALSLQCAAFVDGASITYGTGNELESGSGSSAACKPTLREFNVRLEVPLAAEERLGLTGDVKALGEWQLSRSVALESLDELNWQATVALQSCRQLEYRYFVYVEDLSGYKQIRRWETHFKPRSLGPCTELQCSQLDVFGITSDNSDLKPQVHRGWLNHEAILQLKFNGEKMFQVHDIETFDPQHVQLKIVPVEKTAGLHVEYSKQEYGKSQLELQPTFGVPYTKGDIVIFHITLPLERMMEQHFRLECYSMSNELLGSATLVTSDLTGSEGVLHLPIKSAKNADETLARLRLPYVAVQPYRYSPLDFKNTYAHYWPKSWPNLDVGHRGNGKSYIADAPAERENTIASFLSAHEHHADMIELDVHLTADGVPVIYHDFGLRTAPPGKQISRPDQLEYVLIKDINYELLKRLRIFSVIAGQVREYPSHNAEPRMEHRIFPTLVEVLEKLPKSLGIDVEIKWPQRRQGGGSEAEQTIDKNFFADKVIHQVIQKGCGRPIIFSSFDADMCTMLRFKQNVFPVMFLTQGETKKWQPFLDLRTRTFIAAVNNAQAFELAGTAPHAEDFLGENASEMLRKAKDLGQIAVIWGDDCNSKERVQYFTRIGATATCYDRSDLFMPEGKREAFFKSPALMAEFAAQCRI
Protein: Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1) (Q9NYF8)
Organism: Homo sapiens (Human)
Function: Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA.
Subcellular location: Cytoplasm. Nucleus. Nucleus speckle {ECO:0000269|PubMed:24100041}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24100041}.
Interaction partners:
- Thyroid hormone receptor-associated protein 3
- Emerin
- Apoptosis regulator Bcl-2
- G2/mitotic-specific cyclin-B1
- Histone H2AX
- Pinin
- Smad nuclear-interacting protein 1
- SNW domain-containing protein 1
- Eukaryotic initiation factor 4A-III
- Dual specificity protein kinase CLK2
Sequence:
MGRSNSRSHSSRSKSRSQSSSRSRSRSHSRKKRYSSRSRSRTYSRSRSRDRMYSRDYRRDYRNNRGMRRPYGYRGRGRGYYQGGGGRYHRGGYRPVWNRRHSRSPRRGRSRSRSPKRRSVSSQRSRSRSRRSYRSSRSPRSSSSRSSSPYSKSPVSKRRGSQEKQTKKAEGEPQEESPLKSKSQEEPKDTFEHDPSESIDEFNKSSATSGDIWPGLSAYDNSPRSPHSPSPIATPPSQSSSCSDAPMLSTVHSAKNTPSQHSHSIQHSPERSGSGSVGNGSSRYSPSQNSPIHHIPSRRSPAKTIAPQNAPRDESRGRSSFYPDGGDQETAKTGKFLKRFTDEESRVFLLDRGNTRDKEASKEKGSEKGRAEGEWEDQEALDYFSDKESGKQKFNDSEGDDTEETEDYRQFRKSVLADQGKSFATASHRNTEEEGLKYKSKVSLKGNRESDGFREEKNYKLKETGYVVERPSTTKDKHKEEDKNSERITVKKETQSPEQVKSEKLKDLFDYSPPLHKNLDAREKSTFREESPLRIKMIASDSHRPEVKLKMAPVPLDDSNRPASLTKDRLLASTLVHSVKKEQEFRSIFDHIKLPQASKSTSESFIQHIVSLVHHVKEQYFKSAAMTLNERFTSYQKATEEHSTRQKSPEIHRRIDISPSTLRKHTRLAGEERVFKEENQKGDKKLRCDSADLRHDIDRRRKERSKERGDSKGSRESSGSRKQEKTPKDYKEYKSYKDDSKHKREQDHSRSSSSSASPSSPSSREEKESKKEREEEFKTHHEMKEYSGFAGVSRPRGTFFRIRGRGRARGVFAGTNTGPNNSNTTFQKRPKEEEWDPEYTPKSKKYFLHDDRDDGVDYWAKRGRGRGTFQRGRGRFNFKKSGSSPKWTHDKYQGDGIVEDEEETMENNEEKKDRRKEEKE
Protein: Gelsolin (Actin-depolymerizing factor) (ADF) (Brevin) (Q68FP1)
Organism: Rattus norvegicus (Rat)
Function: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role in ciliogenesis (By similarity).
Subcellular location: [Isoform 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton {ECO:0000250}. Note=A cytoplasmic form may also exist. {ECO:0000250}.
Interaction partners:
- Actin nucleation-promoting factor WASL
- Hematopoietic lineage cell-specific protein
- Src substrate cortactin
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Scinderin
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
- Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
Sequence:
MAPYCSSLRSALLVLALCALSPSHAATASRGRAQERAPQSRVSETRPSTMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESSTFQGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWDSFNNGDCFILDLGNNIYQWCGSGSNKFERLKATQVSKGIRDNERSGRAQVHVSEEGSEPEAMLQVLGPKPDLPQGTEDTAKEDAANRRLAKLYKVSNSGGSMSVSLVADENPFAQSALRSEDCFILDHGRDGKIFVWKGKQANMDERKAALKTASDFISKMQYPRQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGPGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVLVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSRDGGQTTPASTRLFQVRASSSGATRAVEVMPKAGALNSNDAFVLKTPSAAYLWVGTGASDAEKTGALELLKVLRAQHVQVEEGSEPDGFWEALGGKTAYRTSPRLKDKKMDAHPPRLFACSNRIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVRQGFEPPSFVGWFLGWDDDYWSVDPLDRALAELAA
Protein: Exchange protein directly activated by cAMP, isoform F (A0A0B4KF54)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLFRRSCTYNVEQSTRHYAKSAVTLCNLGVGATFGESVLHDLPRDSTVVTKTTCELLRVEQQDFRLIWEKNKELMNDIFTNCKLKNGFGPSVQATAAATSPTKRPLSPDHPNPALPITETPSPAMNRMGWALRTLLVADNSSCLKDRKVSGKLIRKCAPGTELVDWLVNLSPIVHTRAQAAGMWQALLEEGVLAHVNKEQPFKDKCFLYRFRIDEEGGTAAAGVPQAEDLGAANEHIREALSALFQRGPDATLRMILRKPSHERTSEELELVFEELVHIAALSHLSTSIKRELSSIFVFEAHAQAGTILFNQGDEGRSWYILLKGSVDVVIHGKGTVATLKTGDDFGKLALINDAPRAATIVLKENNCHLLRVDKEHFNRILRDVEANTLRLQEHGKDVLVLERVAKQRGQHSAFKYTVMSGTPAKMLEHLLETRLGQSVGGMDPFLDDFLLTHIVFMPVVQLVDELANYFHCDAHEDAQTPEDREYIINFKKRVIQFMQKWVMAVRHAAFEEPSVCDFIEDLAAEVEADPDLNEETSIVHNVLTQMARYQEDRNQNAGQKWKLPPNGQPICLFSGNATPSKTVIRPDDDIIFRVYCADHTYCTLRFPMHTTAELIKACAADKLQLNRGPEDLVLVEVKSNGERSVFKDNDVSIPTGLSLNGRLFVSVKDHLDALTQLQEQECPTEGVDIDLEILSTKELAYHITLFEWDLFWAVHEYELLYHTFGRHHFGKITANLDVFLRRFNEVQYWIVTELVSTPSLSKRVGLVRKFIKLAAYCKEYQNLNAFFAVVMGLSNMAVSRLQQTWEKIPSKFRKIFQEFEALIDPSRNHRAYRVFVGKLQPPLIPFMPLLLKDMTFAHEGNKTSLDGLVNFEKMHMMAQTMRTIRFCRSRSLGLEPPSPKSEGEVRSYISSFRVIDNQRVLTAMSQKVEPTRKL
Protein: NAD(P)H-quinone oxidoreductase subunit O, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit O) (NDH subunit O) (NDH-O) (NADH-plastoquinone oxidoreductase subunit O) (Q9S829)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:Q9CAC5}; Peripheral membrane protein {ECO:0000305}; Stromal side {ECO:0000305}.
Interaction partners:
- NAD
- NAD
- NAD
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
- NAD
- Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
- NAD
- Photosynthetic NDH subunit of subcomplex B 5, chloroplastic
Sequence:
MAFSATVSQLSSLSTISSSLPISSRRLPHRSLPQFTVKAEAEKEKQSTQGKSDGEASPAATKTPKTLPKKPVYSMKKGQIVRVEKEKYLNSINYLSVGHPPFYKGLDYIYEDRGEVLDLRVFETGEYALVGWVGIPTAPAWLPTDMLIKCEKLVYERM
Protein: small monomeric GTPase (EC 3.6.5.2) (B5X2X6)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- CRK SH3-binding GNRP
- CRK SH3-binding GNRP
- CRK SH3-binding GNRP
- CRK SH3-binding GNRP
- Afadin
- Afadin-like
- Rap guanine nucleotide exchange factor 6-like isoform X6
- Rap guanine nucleotide exchange factor 4
- Rap guanine nucleotide exchange factor 4
- Intersectin-2-like
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWNHCAFLESSAKSKINVLDIFYDLVRQINSKTPVEKKKAKKKSNCVLL