wanglab/gogpt-training-data huggingface dataset:
Protein: Somatostatin receptor type 3 (SS-3-R) (SS3-R) (SS3R) (SST3) (SSR-28) (P32745)
Organism: Homo sapiens (Human)
Function: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Internalized into endoplasmic vesicles upon somatostatin-stimulation. {ECO:0000250}.
Interaction partners:
- Somatostatin
- Cortistatin
- Guanine nucleotide-binding protein G
- BBSome complex member BBS1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- BBSome complex member BBS2
- BBSome complex member BBS4
- BBSome complex member BBS7
- Protein PTHB1
Sequence:
MDMLHPSSVSTTSEPENASSAWPPDATLGNVSAGPSPAGLAVSGVLIPLVYLVVCVVGLLGNSLVIYVVLRHTASPSVTNVYILNLALADELFMLGLPFLAAQNALSYWPFGSLMCRLVMAVDGINQFTSIFCLTVMSVDRYLAVVHPTRSARWRTAPVARTVSAAVWVASAVVVLPVVVFSGVPRGMSTCHMQWPEPAAAWRAGFIIYTAALGFFGPLLVICLCYLLIVVKVRSAGRRVWAPSCQRRRRSERRVTRMVVAVVALFVLCWMPFYVLNIVNVVCPLPEEPAFFGLYFLVVALPYANSCANPILYGFLSYRFKQGFRRVLLRPSRRVRSQEPTVGPPEKTEEEDEEEEDGEESREGGKGKEMNGRVSQITQPGTSGQERPPSRVASKEQQLLPQEASTGEKSSTMRISYL
Protein: Phenylalanine ammonia-lyase 1 (PhPAL1) (EC 4.3.1.24) (Q50EX7)
Organism: Petunia hybrida (Petunia)
Function: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P24481}.
Interaction partners:
Sequence:
MEYANENCNGHASQDICVKGHDQQLDPLNWNMAADALKGSHLDEVKRMVKEFRKPVVRLGGETLTVAQVAAIASQSGTDVTVQLSEASRAGVKASSDWVLQGMINGTDSYGVTTGFGATSHRRTKEGAALQKELIRFLNAGIFGNGTESSHTLPHSATRAAMLVRINTLLQGYSGIRFEILEAITKLLNNNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKATGPNGELLDAVKAFQRAGIDTGFFELQPKEGLALVNGTAVGSGLASMVLFDANILAVLSEVLSAIFAEVMQGKPEFTDYLTHKLKHHPGQIEAAAIMEHILDGSSYVKEAKIVHEMDPLQKPKQDRYALRTSPQWLGPQIEVIRAATKMIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLALASIGKLMFAQFSELVNDYYNNGLPSNLTGGRNPSLDYGFKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISSRKTAEAVDILKLMSSTYLVALCQAIDLRHLEENLKATVKNSVSLVAKKVLTIGEKGELHHSRFCEKDMLKVVDREYIFAYADDACSATYPLMQKLRQVLVDRALLNVDGEKDSSTSIFQKIKAFEEELKVVLPKEIERARSDLEQGKPAIPNRIQECRSYPLYKFVREELKANYLTGEKVQSPGEEFDKVFTAMNEGKLVDPLLNCLKEWNGAPLPLC
Protein: Uncharacterized protein (Q38DW1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
- BRCT domain-containing protein
- DNA polymerase eta
- Uncharacterized protein
- Replication protein A subunit
- DNA primase
- Proliferating cell nuclear antigen
- DNA primase large subunit
- DNA polymerase alpha subunit B
- SAM-dependent MTase RsmB/NOP-type domain-containing protein
- Cilia- and flagella-associated protein 58 central coiled coil domain-containing protein
Sequence:
MSRSVDTSALRDVTSWRDPNRSLNPEFSALNEPTHTLTGCSSDKTALLEVLLPVHAKLEDREEVCRDLGVSIQTGKGGSNGLSRRVCMRLTDPGDPFFLFELDLLEDDYGVFKQKLELLVDFSGFPKYLVTMLDNVCSGIVPYVVSFVVDNRDTTRGTLRVLERTEFRTVEHISLILLRQGDSGQKRYLAERFRHFERAYTTAIEEHRKEATEAAANIEALKREVATLEETSTALRDRLDSTTSECKRNQLTSIGQLREEHASQLSQLRATLEADLRHTAQRAEETQKRLREELQVKEMELNEARKRIASLDSEVIKMRSELRVSEDTRKVQAKDLEELRSANGELQAFRSQATSSLSENELNCVKLQERLRGLEHVLESREKEHKMLRDQYKKQDNYVRILASQNEQLTEQKAKEEASLSKAHHIISTQLKNIKSLKTRSRMMRSQIHSQDGLIQEKENTIMQLRGELSSSTEKLQALQSKVTELRDQLEKTDDARSKLANELRCANDALISLQRGTSISGRRWNSGLIPSLSNGSNDVRTGDPMAAGFNGNYAPPSFGVYKELNKNASTTYRQFNAHASRGIVENNDGVLSMNATKGPSGYGEERKPDGRLGEVEKQFEAQQSVKSFGNGTANGTSSNSTLLAGSSVSAVLSEQNKAEHKRSNGQLARAPLDSKVANGMSSSTMQPFATKSFFSDDTHKTGVNDAPTVRNEYNVPIDNVRSSYF
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (EC 2.4.1.109) (P33775)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. Required for incorporation of proteins in the cell wall.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000303|PubMed:10085156}; Multi-pass membrane protein {ECO:0000269|PubMed:10085156}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Dolichyl-phosphate-mannose--protein mannosyltransferase 3
- Dolichyl-phosphate-mannose--protein mannosyltransferase 4
- Putative glycosyltransferase HOC1
- Mannan polymerase I complex VAN1 subunit
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Mannan polymerase II complex ANP1 subunit
- Mannan polymerase complexes subunit MNN9
- Dolichyl-phosphate-mannose--protein mannosyltransferase 5
- Probable alpha-1,6-mannosyltransferase MNN10
Sequence:
MSEEKTYKRVEQDDPVPELDIKQGPVRPFIVTDPSAELASLRTMVTLKEKLLVACLAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFDFENIGDSFPSTTPYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSFKKYEMYPANSLNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIHFQSLTLDGDGASFFSPEFRSTLKNNKIPQNVVADVGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGESLTTFQNLTDGTKVRLFHTVTRCRLHSHDHKPPVSESSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFEQQEVTCASSGRHDLTLWYVENNSNPLLPEDTKRISYKPASFISKFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRNVYLLGNAIVWWAVTAFIGIFGLIVITELFSWQLGKPILKDSKVVNFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAYYFGILALGHALDIIVSYVFRSKRQMGYAVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLSGWDYNCNTYFSSLEEYKNQTLTKRESQPAATSTVEEITIEGDGPSYEDLMNEDGKKIFKDTEGNELDPEVVKKMLEEEGANILKVEKRAVLE
Protein: Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Microtubule-destabilizing protein moe1) (O94236)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003, ECO:0000269|PubMed:9892665}.
Interaction partners:
- Probable eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit M
Sequence:
MATGFKLPELAPVKSAWGPPETEQIGGDIPYAPFSKGDRLGKIADWSVDQPKDGREQRGRQGAFAGRFRDQYQTYGYGASSIFGYQHSEDESSFSVIDRGSVNRTRTSARNGGTLLKVRGRGQNVQRGGRGGRYGSSGGRGAGDTVVSRSSGAGGARGRRFGWKDYDKHQRLRNASVTVGDDWQLLDEVEFSHLSKLNLAAAAPVTVDSYGYIYPYDKSFDKIHVKSEKPLQALDRVHYNPTTTEDPVIQKLALNSDANIFITDSILSLLMCSTRSVYPWDIVITHQSGKLFFDKREGGPFDYLTVNENAYDSPMDADNREGVNSPGALSVEATYINQNFCVQALRETEEEKYKLPHPNPFYNSKEQSEPLAAHGYIYRDVDLSLETDEKPVKLMVRTEVDGYVKNPANDVQYISIKALNEYDPKFTNVTGSVDWRSKLESQRGAVFATEMKNNSCKLARWTVEALLAGVDSMKVGFVSRSNARDAQHHGILGVVAYKPADLASQMNLSLSNGWGIVRTIADVCLKMPDGKYVLVKDPNRPILRLYSVPPNTFEEAAGPSLEASSTA
Protein: NS3 protease (Q91RS4)
Organism: Hepacivirus hominis
Subcellular location: Host cell {ECO:0000256|ARBA:ARBA00004340}. Host membrane {ECO:0000256|ARBA:ARBA00004551}. Virion membrane {ECO:0000256|ARBA:ARBA00004182}.
Interaction partners:
Sequence:
APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGARSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETTMRS
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1) (Q6PH57)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity).
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein
- Cone transducin alpha subunit, alpha transducing activity polypeptide 2) subunit alpha-2)
- Regulator of G-protein signaling 9
- Regulator of G-protein signaling 9a
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Gnb1l protein, beta polypeptide 1, like), beta polypeptide 1b isoform X1), beta polypeptide 1b)
Sequence:
MSELDQLRQEAEQLKNQIRDARKACADATLSQITANIDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFAGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMVYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Protein: Epididymis secretory sperm binding protein (A0A384N5Z8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
Protein: Protein TIC 62, chloroplastic (Translocon at the inner envelope membrane of chloroplasts 62) (OsTIC62) (Q10A77)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in protein precursor import into chloroplasts. Part of the redox regulon consisting of TIC32, TIC 55 and TIC62. Acts as a membrane anchor of LFNR1 and LFNR2. Has a NADPH-dependent dehydrogenase activity, but only after preincubation with lipids.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000250|UniProtKB:Q8H0U5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8H0U5}. Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q8H0U5}. Plastid, chloroplast thylakoid {ECO:0000250|UniProtKB:Q8H0U5}. Note=Shuttles between the membranes and the stroma, depending on the redox state of the plastidic NADP(+)/NADPH pool. {ECO:0000250|UniProtKB:Q8H0U5}.
Interaction partners:
- Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- NADH dehydrogenase flavoprotein 1, mitochondrial
- CHCH domain containing protein, expressed
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- Os07g0585800 protein.
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- Os06g0714100 protein
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Os07g0640100 protein
Sequence:
MEQAAKATISLSPPSYAGCCMAACPYRSTRHLRRGGGCSARSISSLRHAPSARVYAAAAAAATPESKSTKENDLVFIAGATGKVGSRAVREFIKLGFRVRAGVRSAQRASSLVQSVEQLKVDDDATSPAERLEIVECDLEKQAQSDIVSAIGNAAIVVCSIGASEKDILDVTGPYRIDYMATNNLVQAATAAKVEHFILVTSLGTNRIGFPAFLLNLFWGVLCWKRRAEEALIGSGLPYTIVRPGGMERPTDAFKETHNLVVAVEDTYVGGLVSNLQVAELIACIASNRRTAYCKVVEAIAETTAPLLPTEDQLANIPSKRQPPPEPEVVQQGETPPKPIQQSQRPLSPYTAFVDLKPPSSPSPCPPSAAAPAPTSTDTAAAGSSSTLNSSATGTPISVDQPKQQQRPLSPYTRYEELKPPSSPSPTPPSAASSASVSASPDTPPAAAASSAALDSSANGTPITGDQLNQQQSPLSPYTRYEELKPPSSPTPSTPKL
Protein: Small ribosomal subunit protein mS27 (28S ribosomal protein S27, mitochondrial) (MRP-S27) (S27mt) (Mitochondrial ribosomal protein S27) (Q92552)
Organism: Homo sapiens (Human)
Function: RNA-binding component of the mitochondrial small ribosomal subunit (mt-SSU) that plays a role in mitochondrial protein synthesis. Stimulates mitochondrial mRNA translation of subunit components of the mitochondrial electron transport chain. Binds to the mitochondrial 12S rRNA (12S mt-rRNA) and tRNA(Glu). Involved also in positive regulation of cell proliferation and tumor cell growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28714366}. Mitochondrion {ECO:0000269|PubMed:22841715, ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS34
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS16m
Sequence:
MAASIVRRGMLLARQVVLPQLSPAGKRYLLSSAYVDSHKWEAREKEHYCLADLASLMDKTFERKLPVSSLTISRLIDNISSREEIDHAEYYLYKFRHSPNCWYLRNWTIHTWIRQCLKYDAQDKALYTLVNKVQYGIFPDNFTFNLLMDSFIKKENYKDALSVVFEVMMQEAFEVPSTQLLSLYVLFHCLAKKTDFSWEEERNFGASLLLPGLKQKNSVGFSSQLYGYALLGKVELQQGLRAVYHNMPLIWKPGYLDRALQVMEKVAASPEDIKLCREALDVLGAVLKALTSADGASEEQSQNDEDNQGSEKLVEQLDIEETEQSKLPQYLERFKALHSKLQALGKIESEGLLSLTTQLVKEKLSTCEAEDIATYEQNLQQWHLDLVQLIQREQQQREQAKQEYQAQKAAKASA
Protein: Protein SRN2 (ESCRT-I complex subunit VPS37) (Vacuolar protein sorting-associated protein 37) (Q99176)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for normal endocytic and biosynthetic traffic to the yeast vacuole.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9790597}. Endosome {ECO:0000305|PubMed:9790597}. Late endosome membrane {ECO:0000305|PubMed:9790597}; Peripheral membrane protein {ECO:0000305|PubMed:9790597}.
Interaction partners:
- Vacuolar protein sorting-associated protein 28
- Multivesicular body sorting factor 12
- Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein-sorting-associated protein 24
- DOA4-independent degradation protein 4
- Vacuolar-sorting protein SNF7
- Vacuolar-sorting protein SNF8
Sequence:
MKVKATKLRIKQRRKNKGLNISRLDIIRAEMDVVPSPGLPEKVNEKSKNIPLPEGINLLSSKEIIDLIQTHRHQLELYVTKFNPLTDFAGKIHAFRDQFKQLEENFEDLHEQKDKVQALLENCRILESKYVASWQDYHSEFSKKYGDIALKKKLEQNTKKLDEESSQLETTTRSIDSADDLDQFIKNYLDIRTQYHLRREKLATWDKQGNLKY
Protein: Sodium/proline symporter (Proline permease) (Q9I5F5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|RuleBase:RU366012}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU366012}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Bifunctional protein PutA
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- CstA N-terminal domain-containing protein
- Lysine-specific permease
Sequence:
MSVNTPTLITFVIYIAAMVLIGLAAYRSTNNFSDYILGGRSLGSFVTALSAGASDMSGWLLMGLPGAVYLSGLSESWIAIGLIVGAYLNWLFVAGRLRVQTEHNGNALTLPDYFTNRFEDNSRLLRIFSALVILVFFTIYCASGIVAGARLFESTFGLSYETALWAGAAATIAYTFIGGFLAVSWTDTVQASLMIFALILTPVIVMLATGGVEPTFTAIELKDATSFDMLKGASFIGVISLMAWGLGYFGQPHILARFMAADSVKSIPAARRISMTWMILCLGGAVAVGFFGIAYFQAHPEQAGAVSENPERVFIELAKILFNPWIAGVLLSAILAAVMSTLSCQLLVCSSALTEDFYKAFLRKGASQLELVWVGRAMVLLVAVIAIWLASNPENRVLGLVSYAWAGFGAAFGPLVLFSLLWKRMTRNGALAGMIVGAATVILWKNLLGWTGLYEIIPGFLFASVAIVVFSLLGKAPSTSMLKRFDDAEQEYREAHQGSAAPVTQR
Protein: Malate dehydrogenase (EC 1.1.1.37) (Vegetative protein 69) (VEG69) (P49814)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Interaction partners:
- Isocitrate dehydrogenase
- Citrate synthase 2
- Fumarate hydratase class II
- Citrate/2-methylcitrate synthase
- Citrate synthase 1
- Pyruvate carboxylase
- Bifunctional malic/malolactic enzyme
- Phosphoenolpyruvate carboxykinase
- NAD-dependent malic enzyme 1
- NAD-dependent malic enzyme 2
Sequence:
MGNTRKKVSVIGAGFTGATTAFLIAQKELADVVLVDIPQLENPTKGKALDMLEASPVQGFDAKITGTSNYEDTAGSDIVVITAGIARKPGMSRDDLVSTNEKIMRSVTQEIVKYSPDSIIVVLTNPVDAMTYAVYKESGFPKERVIGQSGVLDTARFRTFVAEELNLSVKDVTGFVLGGHGDDMVPLVRYSYAGGIPLETLIPKERIDAIVERTRKGGGEIVNLLGNGSAYYAPAASLTEMVEAILKDQRRVLPTIAYLEGEYGYEGIYLGVPTIVGGNGLEQIIELELTDYERAQLNKSVESVKNVMKVLS
Protein: N-syb protein (Q26335)
Organism: Drosophila sp. (Fruit fly)
Interaction partners:
Sequence:
MADAAPAGDAPPNAGAPAGEGGDGEIVGGPHNPQQIAAQKRLQQTQAQVDEVVDIMRTNVEKVLERDTKLSELDDRADALQQGASQFEQQAGKLKRKFWLQNLKMMIIMGVIGLVVVGIIANKLGLIGGEQPPQYQYPPQYMQPPPPPPQQPAGGQSSLVDGAGAGDGAGGSAGAGDHGGV
Protein: adenylate cyclase (EC 4.6.1.1) (Q966F9)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit
- cAMP-dependent protein kinase regulatory subunit
Sequence:
MVERAYNSIRAHKQTRVAQRPVSKKTSSTMRETFGSQVLRELEMKNRMECPSLDEILSFYHFPWEKLRYRKNSQKKKRSTLYSFYFEQVNSGRIQFSFVILLSICISEAAFSAFGAEWLKSLILCILTLVISILSFFHAKRTELVCIASIISCVIISACTSMRTSVTYLLIFSTYSLLPMSFMLMIFSTFALTFLVAFIGVLMDYNVGFDIILTRVMMVILVNVVGSLVYYPTEFVQRKTFHETRKCVQSRMLLDKEMHRQEKILLAVLPKNIAFEVKKDMQETHEERMFHKIYIRKYEDISILFADICGFTNLASEYNPKDLVLMLNELFARFDKVASIHQCMRIKILGDCYYCVCGVPEYQKNHAINTVEMGRDMIEAIRLVREMTLVNVNMRVGIHTGKAHCGVLGLKKWQFDVWSNDVTLANQMESGGLAGRVHITDATRSYLKGAYILEEGNGGSRSKFLEKEKIKTWLVVDRSPDYDNICQEATNHPVMVPWKSTRGISKQERLTGMSTRTRGASTRNGLSEEEVLVENVDSHLRQGIQAIHQENWKTMHCKNWSLKYKQVRVENKFVRLKYKDIPFQVTLYVAIVAICIGIKFGLMNLVSFSFVPQMFIVLTSVMIFILTRALIKHARLVSLVIGVLFILLSIQIVILMGMYESKFTCDVEKCFKNNYTDFFEIFEICTLATCVILSVDFMTKLLMSMIYFSSFTVLITAKLIRINQYEALLSTYANFCVLSCLTLLLVVFSTRRSELISRYDFIWKLQALDEQLQMKRKHEQNRSVLENILPSHVAKHFVEDATSVSKLYHESRDNACIMFATLTEFDKFYIECDGNNEGVECLRLLNEIISDFDQILDQILDREEFKKIEKIKTISTTYMVASGLAGRECGDNSHVEAIALFARELLVKLESTNIHSFNNFNLRIGINVGPVVAGVIGSDKPHYDIWGNSVNVASRMDSGGVAGRIQVTEEVKSILEPLGYNFECRGQINVKGKGMMETFFLLPPEDFDCQLYH
Protein: Candida glabrata strain CBS138 chromosome C complete sequence (Q6FWQ0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MAYNKVALILSAAIAATKVAAISNNEISEFNVILSDVMGHLTDYISYAENDPNFTLPDHVLDLYMAMTTATDDSYTTMYDQINFSQVTDAMTRLPWYSSRILPNVSPFLEDNAASAAASSAASSASSSAASSVSSEASEASSSVSSASSASVSSSSAASSSASSASSAASSEASSASSEASSRASSVSSAASSAASSISASASRAASSASSSASSASAARNGTSTSSHKNAAGKEYGSAAAGMGAMFVGAAALLL
Protein: Geranylgeranyl diphosphate synthase 1 (C9J6G3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQV
Protein: Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.360) (DOT1-like protein) (Histone H3-K79 methyltransferase) (H3-K79-HMTase) (Lysine N-methyltransferase 4) (Q8TEK3)
Organism: Homo sapiens (Human)
Function: Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:15851025}.
Interaction partners:
- Protein AF-10
- Protein AF-9
- Histone H3.2
- Histone H3.1
- Protein ENL
- Histone H4
- Protein AF-17
- Histone H2B type 1-J
- Histone H2B type 1-K
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPTPPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGYELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIVLRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSPLQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGGGLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLSGPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSSVPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGN
Protein: Translin-associated protein X (Translin-associated factor X) (Q9QZE7)
Organism: Mus musculus (Mouse)
Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:15314092}. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN (By similarity). Accumulate in the Golgi complex of mid-late pachytene spermatocytes. {ECO:0000250}.
Interaction partners:
- Translin
- Protein argonaute-2
- Endoribonuclease Dicer
- Protein argonaute-1
- Protein argonaute-4
- Ribonuclease 3
- Protein argonaute-3
- RISC-loading complex subunit TARBP2
- Ribonuclease P protein subunit p30
- tRNA methyltransferase 10 homolog C
Sequence:
MNGKEGPGGFRKRKHDTFPHNQRREGKDASLSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSAPDMEEILTESESKLDGVRQKILQVAQELSGEDMHQFHRAVTTGLQEYVEAVSFQHFIKTRSLISMEEINKQLTFTAEDSGKESKTPPAEGQEKQLVTWRLKLTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVSKKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVFSVKTDMIDQEESIS
Protein: Autophagy-related protein 8a (Autophagy-related ubiquitin-like modifier ATG8a) (AtAPG8a) (Protein autophagy 8a) (Q8LEM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like modifier involved in autophagosomes formation. May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15178341}.
Interaction partners:
- Protein NBR1 homolog
- Autophagy-related protein 3
- Ubiquitin-like modifier-activating enzyme atg7
- Cysteine protease ATG4b
- Cysteine protease ATG4a
- Autophagy protein 5
- Serine/threonine-protein kinase ATG1b
- Ubiquitin-like protein ATG12A
- Serine/threonine-protein kinase ATG1c
- Serine/threonine-protein kinase ATG1a
Sequence:
MAKSSFKISNPLEARMSESSRIREKYPDRIPVIVEKAGQSDVPDIDKKKYLVPADLTVGQFVYVVRKRIKLGAEKAIFVFVKNTLPPTAALMSAIYEEHKDEDGFLYMTYSGENTFGSLTVA