wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor 7-like 2 (HMG box transcription factor 4) (T-cell-specific transcription factor 4) (T-cell factor 4) (TCF-4) (mTCF-4) (Q924A0)
Organism: Mus musculus (Mouse)
Function: Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif CCTTTGATC in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1 (By similarity). Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine.
Subcellular location: Nucleus, PML body {ECO:0000250|UniProtKB:Q9NQB0}. Nucleus {ECO:0000250|UniProtKB:Q9NQB0}. Note=Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies (By similarity). {ECO:0000250|UniProtKB:Q9NQB0}.
Interaction partners:
- Catenin beta-1
- Serine/threonine-protein kinase NLK
- Histone acetyltransferase p300
- Junction plakoglobin
- Transcription factor 7-like 1
- Histone lysine acetyltransferase CREBBP
- Histone deacetylase 1
- Mothers against decapentaplegic homolog 4
- Transcription factor 7
- C-terminal-binding protein 1
Sequence:
MPQLNGGGGDDLGANDELISFKDEGEQEEKNSENSSAERDLADVKSSLVNESETNQDSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTYLQMKWPLLDVQAGSLQSRQTLKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCSL
Protein: Epithelial calcium channel (Q7ZZQ8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAPALARSAPGELNHWWSQFRFRLQNRKGWKEMLDETFLLQNKRTNGVPLFFAAKESSAGCIKKLLDCASTNIFERRALGETALHVAVMNDNMEAALALMDGAPELINEPMTSELFLGMKPLHIAVVNQNFNLVRSLIGKGADVATPRVTGLYFRKRRGGLLYYGEHILAFAACVGNQDIISMVINVGASTRAQDSIGNTVLHILVLQPNKTIACLVLDLLLARDIELDQAVPLDMVPNYHGLTPFKLAAKEGNLVAFQHLVNRRRINQWNLGPLTSNLYDLTGIDSLVADDDCSVLEHIVGSKRREAKRILEVTPVRQLVSFKWNLYGKHYFRLLLLLYLLYIGTFTLCCVYRPLKDAPENYTVSDMDKTIRVQKTLKESYVTYGDNLRLAGEMISVLGALVILLLEVPDMLRVGAKHYFGQTALGGPFHVILIAYAFLVVLLCVFRVSGVQGETVVMAVCLVLGWSNVMFFARGFQMLGPYVIMIQKIIFGDLTKFMWLSFIVLIGFSTSLWVVYMTQDPDSLPAYRSFPITLFSQFELSVGLIDLPVDHTITTPPIVHVLHCTFSVVSYILLLNLLTAMMSDTQWRVAQERDELWRTQVVATTLMLERRLPRCLWPRLGVCGLLYGLGERWYLRVEDRNDPLVQKMRRYVQAFSKDEDQSKEREEMENTDMSKGPGSPLIRTKHRGGIDGNRKSLACWQMIRHSALGLDVEQEEPEDDQEVRYV
Protein: Isochorismate synthase EntC (EC 5.4.4.2) (Isochorismate mutase) (P0AEJ2)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the siderophore enterobactin (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate.
Interaction partners:
- Enterobactin synthase component B
- Enterobactin synthase component E
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- Enterobactin synthase component F
- Iron
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- Ferric enterobactin-binding periplasmic protein FepB
- Proofreading thioesterase EntH
- Ferrienterobactin receptor
- Enterobactin synthase component D
Sequence:
MDTSLAEEVQQTMATLAPNRFFFMSPYRSFTTSGCFARFDEPAVNGDSPDSPFQQKLAALFADAKAQGIKNPVMVGAIPFDPRQPSSLYIPESWQSFSRQEKQASARRFTRSQSLNVVERQAIPEQTTFEQMVARAAALTATPQVDKVVLSRLIDITTDAAIDSGVLLERLIAQNPVSYNFHVPLADGGVLLGASPELLLRKDGERFSSIPLAGSARRQPDEVLDREAGNRLLASEKDRHEHELVTQAMKEVLRERSSELHVPSSPQLITTPTLWHLATPFEGKANSQENALTLACLLHPTPALSGFPHQAATQVIAELEPFDRELFGGIVGWCDSEGNGEWVVTIRCAKLRENQVRLFAGAGIVPASSPLGEWRETGVKLSTMLNVFGLH
Protein: Coniferyl aldehyde dehydrogenase (CALDH) (EC 1.2.1.68) (O86447)
Organism: Pseudomonas sp. (strain HR199 / DSM 7063)
Function: Catalyzes the NAD(+)-dependent oxidation of coniferyl aldehyde to ferulic acid and which is induced during growth with eugenol as the carbon source.
Interaction partners:
Sequence:
MSILGLNGAPVGAEQLGSALDRMKKAHLEQGPANLELRLSRLDRAIAMLLENREAIADAVSADFGNRSREQTLLCDIAGSVASLKDSREHVAKWMEPEHHKAMFPGAEARVEFQPLGVVGVISPWNFPIVLAFGPLAGIFAAGNRAMLKPSELTPRTSALLAELIARYFDETELTTVLGDAEVGALFSAQPFDHLIFTGGTAVAKHIMRAAADNLVPVTLELGGKSPVIVSRSADMADVAQRVLTVKTFNAGQICLAPDYVLLPEESLDSFVAEATRFVAAMYPSLLDNPDYTSIINARNFDRLHRYLTDAQAKGGRVIEINPAAEELGDSGIRKIAPTLIVNVSDEMLVLNEEIFGPLLPIKTYRDFDSAIDYVNSKQRPLASYFFGEDAVEREQVLKRTVSGAVVVNDVMSHVMMDTLPFGGVGHSGMGAYHGIYGFRTFSHAKPVLVQSPVGESNLAMRAPYGEAIHGLLSVLLSTEC
Protein: HL01538p (Q95S15)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRVRRLLVFINPYGGRKAGAQTYERHVRPIFQLAGVDATCITTQRANQVKDILLSHDLGVYDAVCCVGGDGTVAEVINGLIFRQMRELGLDEQRPPYIPRPALPVGVIPAGSTDTIAYSMHGTADVRTAAIHVILGQHRGLDVCSVSNGQSLLRFCASVLSYGYLGDVAAQSENYRWMGPRRYEYSGVKAFLNNRGYDAELRMLEEPDLLLTTPLEDIPQSPDSVCSLGESVPSVCYANCQRCSFASSIQEQRSSLFIQEESKEAERNQQVETEDSHLAASEAALLRPRPRPGNLRLPTGSISSMRNLGNDQWKVVRGNFFMICGANITCACARSPNGISRYSHLGDGCLDLILVKKTSLLNNVRFLLNTAGRSGDIRNLPFVEVYRTREFRFRTFSASEEDYSLAGSCQPITPPEEMTAHSSSTEFSSWNCDGEVVTDLDITMRSHCQLIEVFMRGPHSYSKPLKGGTTPTTPASSSDNVYCCCKD
Protein: Probable ATP-dependent RNA helicase DDX27 (EC 3.6.4.13) (DEAD box protein 27) (Q96GQ7)
Organism: Homo sapiens (Human)
Function: Probable ATP-dependent RNA helicase. Component of the nucleolar ribosomal RNA (rRNA) processing machinery that regulates 3' end formation of ribosomal 47S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:25825154}. Chromosome {ECO:0000269|PubMed:20813266}. Note=Associates with 60S and 90S pre-ribosomal particles (PubMed:25825154). {ECO:0000269|PubMed:25825154}.
Interaction partners:
- RNA-binding protein 28
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Pescadillo homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- Ribosome biogenesis protein BOP1
- RNA-binding protein 34
- Ribosome biogenesis protein WDR12
- Nucleolar complex protein 2 homolog
- U3 small nucleolar RNA-associated protein 18 homolog
- Ribosome production factor 2 homolog
Sequence:
MVLAQRRRGGCEKLRAGPQAVLASGSGFCDNMLADLGLIGTIGEDDEVPVEPESDSGDEEEEGPIVLGRRQKALGKNRSADFNPDFVFTEKEGTYDGSWALADVMSQLKKKRAATTLDEKIEKVRKKRKTEDKEAKSGKLEKEKEAKEGSEPKEQEDLQENDEEGSEDEASETDYSSADENILTKADTLKVKDRKKKKKKGQEAGGFFEDASQYDENLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREGDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQLEAEEKEMQQSEAQINTAKRLLEKGKEAVVQEPERSWFQTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILKAQMFAERLAKRNRRAKRARAMPEEEPVRGPAKKQKQGKKSVFDEELTNTSKKALKQYRAGPSFEERKQLGLPHQRRGGNFKSKSRYKRRK
Protein: Sulfotransferase (EC 2.8.2.-) (V9HVX9)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
Sequence:
MSRSPQRALPPGALPRLLQAAPAAAPRALLPQWPRRPGRRWPASPLGMKVFRRKALVLCAGYALLLVLTMLNLLDYKWHKEPLQQCNPDGPLGAAAGAAGGSWGRPGPPPAGPPRAHARLDLRTPYRPPAAAVGAAPAAAAGMAGVAAPPGNGTRGTGGVGDKRQLVYVFTTWRSGSSFFGELFNQNPEVFFLYEPVWHVWQKLYPGDAVSLQGAARDMLSALYRCDLSVFQLYSPAGSGGRNLTTLGIFGAATNKVVCSSPLCPAYRKEVVGLVDDRVCKKCPPQRLARFEEECRKYRTLVIKGVRVFDVAVLAPLLRDPALDLKVIHLVRDPRAVASSRIRSRHGLIRESLQVVRSRDPRAHRMPFLEAAGHKLGAKKEGVGGPADYHALGAMEVICNSMAKTLQTALQPPDWLQGHYLVVRYEDLVGDPVKTLRRVYDFVGLLVSPEMEQFALNMTSGSGSSSKPFVVSARNATQAANAWRTALTFQQIKQVEEFCYQPMAVLGYERVNSPEEVKDLSKTLLRKPRL
Protein: N-(5'-phosphoribosyl)anthranilate isomerase (PRAI) (EC 5.3.1.24) (P50857)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Tryptophan synthase
- Anthranilate phosphoribosyltransferase
- Multifunctional tryptophan biosynthesis protein
- anthranilate synthase
- aminodeoxychorismate synthase
- Imidazoleglycerol-phosphate dehydratase
- 3-isopropylmalate dehydrogenase
- 1-
- Histidine biosynthesis trifunctional protein
- L-2-aminoadipate reductase large subunit
Sequence:
MSFDSLLDKNDKLVKVCGIQTVEAAETALQAGADLIGIICVPNRKRTIESAVAREISKLIHKSGTTKLVGVFRNQSVEDVHRLSEEYDLDIIQLHGDESWPEYYNVIKKPIIKRVIFPRDVDVVTQVCQRKPLVCLPLFDSEAGGTGEKLDWSSISSWASEQNNVFYILAGGLTAENVMEAVGLPGVIGVDVSGGVETDGVKDNDKIIKYVQNAKKQ
Protein: Bone morphogenetic protein 5 (BMP-5) (P22003)
Organism: Homo sapiens (Human)
Function: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cartilage and bone formation or neurogenesis. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathway such as MAPK p38 signaling cascade to promote chondrogenic differentiation.
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein receptor type-2
- Noggin
- Chordin
- Activin receptor type-2A
- Activin receptor type-2B
- Bone morphogenetic protein receptor type-1B
- Activin receptor type-1
- Neuroblastoma suppressor of tumorigenicity 1
- Gremlin-2
Sequence:
MHLTVFLLKGIVGFLWSCWVLVGYAKGGLGDNHVHSSFIYRRLRNHERREIQREILSILGLPHRPRPFSPGKQASSAPLFMLDLYNAMTNEENPEESEYSVRASLAEETRGARKGYPASPNGYPRRIQLSRTTPLTTQSPPLASLHDTNFLNDADMVMSFVNLVERDKDFSHQRRHYKEFRFDLTQIPHGEAVTAAEFRIYKDRSNNRFENETIKISIYQIIKEYTNRDADLFLLDTRKAQALDVGWLVFDITVTSNHWVINPQNNLGLQLCAETGDGRSINVKSAGLVGRQGPQSKQPFMVAFFKASEVLLRSVRAANKRKNQNRNKSSSHQDSSRMSSVGDYNTSEQKQACKKHELYVSFRDLGWQDWIIAPEGYAAFYCDGECSFPLNAHMNATNHAIVQTLVHLMFPDHVPKPCCAPTKLNAISVLYFDDSSNVILKKYRNMVVRSCGCH
Protein: Transcription factor (A7LHG5)
Organism: Glycine max (Soybean) (Glycine hispida)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESDLSWERNTLINELIQGMEVARKLKADLKLPYSVDTRDLLLQRILSSYEKALLILRCSNASTSELQGMNQATPTLLPESPLSVHGSPLREDVHGAIMDHHDSKKRKITRRWMDRVRVSCESGLEGPHEDGYNWRKYGQKDILGAKYPRSYYRCTFRSTQGCWATKQVQRSDEDPTVFDITYRGKHTCSQGNNAVLPPKSPEKQEKPTHSHNIDIHRAQASQESLTKFRNILSVNTDNLNNGDMAYPFTFPSTSFGCMKQDNHSLIP
Protein: Zinc finger MYND-type containing 8 (A0A087WVZ6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHPQSLAEEEIKTEQEVVEGMDISTRSKDPGSAERTAQKRKFPSPPHSSNGHSPQDTSTSPIKKKKKPGLLNSNNKEQDGRNDFYCWVCHREGQVLCCELCPRVYHAKCLRLTSEPEGDWFCPECEKITVAECIETQSKAMTMLTIEQLSYLLKFAIQKMKQPGTDAFQKPVPLEQHPDYAEYIFHPMDLCTLEKNAKKKMYGCTEAFLADAKWILHNCIIYNGGNHKLTQIAKVVIKICEHEMNEIEVCPECYLAACQKRDNWFCEPCSNPHPLVWAKLKGFPFWPAKALRDKDGQVDARFFGQHDRAWVPINNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRRKFGVFNYSPFRTPYTPNSQYQMLLDPTNPSAGTAKIDKQEKVKLNFDMTASPKILMSKPVLSGGTGRRISLSDMPRSPMSTNSSVHTGSDVEQDAEKKATSSHFSASEESMDFLDKSTASPASTKTGQAGSLSGSPKPFSPQLSAPITTKTDKTSTTGSILNLNLDRSKAEMDLKELSESVQQQSTPVPLISPKRQIRSRFQLNLDKTIESCKAQLGINEISEDVYTAVEHSDSEDSEKSDSSDSEYISDDEQKSKNEPEDTEDKEGCQMDKEPSAVKKKPKPTNPVEIKEELKSTSPASEKADPGAVKDKASPEPEKDFSEKAKPSPHPIKDKLKGKDETDSPTVHLGLDSDSESELVIDLGEDHSGREGRKNKKEPKEPSPKQDVVGKTPPSTTVGSHSPPETPVLTRSSAQTSAAGATATTSTSSTVTVTAPAPAATGSPVKKQRPLLPKETAPAVQRVVWNSSTVQQKEITQSPSTSTITLVTSTQSSPLVTSSGSMSTLVSSVNADLPIATASADVAADIAKYTSKIRRLRIEIEKLQWLHQQELSEMKHNLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKKKQWCANCKKEAIFYCCWNTSYCDYPCQQAHWPEHMKSCTQSATAPQQEADAEVNTETLNKSSQGSSSSTQSAPSETASASKEKETSAEKSKESGSTLDLSGSRETPSSILLGSNQGSVSKRCDKQPAYAPTTTDHQPHPNYPAQKYHSRSNKSSWSSSDEKRGSTRSDHNTSTSTKSLLPKESRLDTFWD
Protein: Mitochondrial import inner membrane translocase subunit TIM23 (Membrane import machinery protein MIM23) (Mitochondrial protein import protein 3) (Mitochondrial protein import protein MAS6) (P32897)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18418384}; Multi-pass membrane protein {ECO:0000269|PubMed:18418384}. Note=Around 20 amino acids of the N-terminus are believed to span the mitochondrial outer membrane. This association is dynamic and depends on the translocation activity of the TIM23 complex. However, this topology seems not to be critical for formation of a TOM-TIM supercomplex and preprotein import.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit TIM17
- Cytochrome c oxidase subunit 4, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM44
- Import motor subunit, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM21
- Mitochondrial import inner membrane translocase subunit TIM16
- Mitochondrial import inner membrane translocase subunit TIM14
- Presequence translocated-associated motor subunit PAM17
- Mitochondrial import inner membrane translocase subunit TIM22
Sequence:
MSWLFGDKTPTDDANAAVGGQDTTKPKELSLKQSLGFEPNINNIISGPGGMHVDTARLHPLAGLDKGVEYLDLEEEQLSSLEGSQGLIPSRGWTDDLCYGTGAVYLLGLGIGGFSGMMQGLQNIPPNSPGKLQLNTVLNHITKRGPFLGNNAGILALSYNIINSTIDALRGKHDTAGSIGAGALTGALFKSSKGLKPMGYSSAMVAAACAVWCSVKKRLLEK
Protein: Transcription factor bHLH94 (Basic helix-loop-helix protein 94) (AtbHLH94) (bHLH 94) (Transcription factor EN 16) (bHLH transcription factor bHLH094) (Q9SK91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Plant self-incompatibility protein S1 family
- F14J9.2 protein
- Putative purine permease 19
- Pentatricopeptide repeat-containing protein At5g12100
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Regulator of Vps4 activity in the MVB pathway protein
- Transcription factor bHLH111
- Putative transcription factor bHLH041
- Auxin-responsive protein SAUR77
- Transcription factor EMB1444
Sequence:
MPLEAVVYPQDPFGYLSNCKDFMFHDLYSQEEFVAQDTKNNIDKLGHEQSFVEQGKEDDHQWRDYHQYPLLIPSLGEELGLTAIDVESHPPPQHRRKRRRTRNCKNKEEIENQRMTHIAVERNRRKQMNEYLAVLRSLMPSSYAQRGDQASIVGGAINYVKELEHILQSMEPKRTRTHDPKGDKTSTSSLVGPFTDFFSFPQYSTKSSSDVPESSSSPAEIEVTVAESHANIKIMTKKKPRQLLKLITSLQSLRLTLLHLNVTTLHNSILYSISVRVEEGSQLNTVDDIATALNQTIRRIQEET
Protein: G1/S-specific cyclin CLN3 (P13365)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the control of the cell cycle at the G1/S (start) transition. CLN3 may be an upstream activator of the G1 cyclins which directly catalyze start.
Interaction partners:
- G1-specific transcriptional repressor WHI5
- Transcription factor MBP1
- Protein BCK2
- Regulatory protein SWI4
- Cyclin-dependent kinase 1
- G1/S-specific cyclin CLN2
- G1/S-specific cyclin CLN1
- Regulatory protein SWI6
- Protein WHI3
- Zinc finger protein RME1
Sequence:
MAILKDTIIRYANARYATASGTSTATAASVSAASCPNLPLLLQKRRAIASAKSKNPNLVKRELQAHHSAISEYNNDQLDHYFRLSHTERPLYNLTNFNSQPQVNPKMRFLIFDFIMYCHTRLNLSTSTLFLTFTILDKYSSRFIIKSYNYQLLSLTALWISSKFWDSKNRMATLKVLQNLCCNQYSIKQFTTMEMHLFKSLDWSICQSATFDSYIDIFLFQSTSPLSPGVVLSAPLEAFIQQKLALLNNAAGTAINKSSSSQGPSLNINEIKLGAIMLCELASFNLELSFKYDRSLIALGAINLIKLSLNYYNSNLWENINLALEENCQDLDIKLSEISNTLLDIAMDQNSFPSSFKSKYLNSNKTSLAKSLLDALQNYCIQLKLEEFYRSQELETMYNTIFAQSFDSDSLTCVYSNATTPKSATVSSAATDYFSDHTHLRRLTKDSISPPFAFTPTSSSSSPSPFNSPYKTSSSMTTPDSASHHSHSGSFSSTQNSFKRSLSIPQNSSIFWPSPLTPTTPSLMSNRKLLQNLSVRSKRLFPVRPMATAHPCSAPTQLKKRSTSSVDCDFNDSSNLKKTR
Protein: Phosphatidylinositol 4-kinase STT4 (PI4-kinase) (PtdIns-4-kinase) (EC 2.7.1.67) (P37297)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate. STT4 functions in PKC1 protein kinase pathway.
Interaction partners:
- Phosphatidylinositol 4-kinase LSB6
- Phosphatidylinositol 4-phosphate 5-kinase MSS4
- Phosphatidylinositol-3-phosphatase SAC1
- Cargo-transport protein YPP1
- Phosphatidylinositol 4-kinase PIK1
- Protein EFR3
- Protein SFK1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Polyphosphatidylinositol phosphatase INP53
- 1-phosphatidylinositol 3-phosphate 5-kinase FAB1
Sequence:
MRFTRGLKASSSLRAKAIGRLTKLSTGAPNDQNSNGTTLDLITHTLPIFYSTNTSKIYTIPLTLSEWEVLTSLCVAIPTTLDLVETMLKEIIAPYFLETPRQRISDVLSSKFKLEQMRNPIELLTFQLTKFMIQACEQYPVLYENIGGIISTYFERVLKIFTIKQSGLLSLVGFINAFIQFPNSTELTKFTWKKLAKLVLRGSFLNEVDKILNSSATFTNDSIVQYYDAGNELSSAYLLELISRLQVSLISHLLNTSHVGANLSEFLLNQQYQFYKFDQEVADENDDTKCIDDFFFNVRSNKQFFTDMCKISLQFCSESHILDLSTDNRARFSFDTRAHYLQTLCLIPFIEDTESELFESFTNVVSESIDKFFLSDVVTPSLIKAIVASASLLNFFTEKLSLTLIRMFPLLVASPHITTETVNDVAKIFTTGLYPLNEDAIVSTIYSMNNLLAVSEDGSPVPVLRERQLTITSGKNIEKDYFPLRNSSASLDGTGALLGNTTVGQLSSHDVNSGATMTYHASLISNCVAATTTIASYYNTQSITALTISILTQKVNSMSKELDGVILNSLARLAPNTSLTEFSLLLKFFKSRTVIATKIDDSALLKNIIKAKCVISKELLARHFSSDLYFMYLHDLLDSIIASGEVERLEHHRPQTEISRVADQIATYLEPLAALLPVPGDTPLDINKDEVTTNKFRNAWFNFVIHGYHLGGPIVKRNFSFLLTIAYNSPPLASEFPANNKELSLEMNTILRRGSSNENIKQQKQQITEYFNTNIVQYRTTSSSKIMFLAAAVLLETIRCEAGDCSKTLLYFSDPSILSGSIEKCIAVLSVSMIRKYARLIQKGNDAIFNSKMIAQQLNNLLLCLSHREPTLQDAAFHACEIFIRSIPSSLCHHLSLYTLLDMLTALFDSILDSEAHKFEPRYEFKLKHSKTTILVPSSSSWRATTLSRLHKSAKEWVRILLNRSNQDTKILLQSYISDLGEYSRLNSVEFGVSFAMDMAGLILPADKELSRLTYYGPEKPNTISGFISLHSWRSKYLFDTAITSSPEDIKRQIGISTQNIRKNLTLGNKIITKDVTDFLDMATALLILGNGAPASLIYDIVHIPFEVFTSASLKIATNVWLTIITEKPEVAHLLLVEVCYCWMRSIDDNIGLYSRDHDLKGEEYQKMEYSPYDKAGINRDAKNASQAMQPHLHVIKFFASHFEGTLFQSDFLLKIFTKCALYGIKNLYKASLHPFARMIRHELLLFATLVLNASYKQGSKYMGRLSQEITNGALSWFKRPVAWPFGSNELKIKADLSVTRDLFLQLNKLSSLMSRHCGKDYKILNYFLASEIQQIQTWLTPTEKIEGADSNELTSDIVEATFAKDPTLAINLLQRCYSKKAEDVLVGLVAKHALMCVGSPSALDLFIKGSHLSSKKDLHATLYWAPVSPLKSINLFLPEWQGNSFILQFSIYSLESQDVNLAFFYVPQIVQCLRYDKTGYVERLILDTAKISVLFSHQIIWNMLANCYKDDEGIQEDEIKPTLDRIRERMVSSFSQSHRDFYEREFEFFDEVTGISGKLKPYIKKSKAEKKHKIDEEMSKIEVKPDVYLPSNPDGVVIDIDRKSGKPLQSHAKAPFMATFKIKKDVKDPLTGKNKEVEKWQAAIFKVGDDCRQDVLALQLISLFRTIWSSIGLDVYVFPYRVTATAPGCGVIDVLPNSVSRDMLGREAVNGLYEYFTSKFGNESTIEFQNARNNFVKSLAGYSVISYLLQFKDRHNGNIMYDDQGHCLHIDFGFIFDIVPGGIKFEAVPFKLTKEMVKVMGGSPQTPAYLDFEELCIKAYLAARPHVEAIIECVNPMLGSGLPCFKGHKTIRNLRARFQPQKTDHEAALYMKALIRKSYESIFTKGYDEFQRLTNGIPY
Protein: Ethylene-responsive transcription factor ERF035 (Q9M210)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Chaperone protein dnaJ 72
- Heavy metal-associated isoprenylated plant protein 4
- 2-oxoglutarate
Sequence:
MGKQINIESSATHHQDNIVSVITATISSSSVVTSSSDSWSTSKRSLVQDNDSGGKRRKSNVSDDNKNPTSYRGVRMRSWGKWVSEIREPRKKSRIWLGTYPTAEMAARAHDVAALAIKGNSGFLNFPELSGLLPRPVSCSPKDIQAAATKAAEATTWHKPVIDKKLADELSHSELLSTAQSSTSSSFVFSSDTSETSSTDKESNEETVFDLPDLFTDGLMNPNDAFCLCNGTFTWQLYGEEDVGFRFEEPFNWQND
Protein: Dematin (Dematin actin-binding protein) (Erythrocyte membrane protein band 4.9) (Q9WV69)
Organism: Mus musculus (Mouse)
Function: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:18505823}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18505823}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000269|PubMed:18505823}. Endomembrane system {ECO:0000250}. Cell projection {ECO:0000269|PubMed:18505823}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Beta-adducin
- Alpha-adducin
- Gamma-adducin
- Protein 4.1
- Tropomodulin-1
- Tropomodulin-2
- Tropomodulin-4
- Tropomodulin-3
- Glycophorin-C
- Band 3 anion transport protein
Sequence:
MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRECSLSPKSTSPPPSPEVWAESRTLGIISQASTPRTTGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRESVGGSPQSKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRKGAEEEEEEEDDDSEEEIKAIRERQKEELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHSGTSKSSSLPSYGRTTLSRLQSTEFSPSGSEAGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF
Protein: Ferric/cupric reductase transmembrane component 1 (EC 1.16.1.9) (Ferric-chelate reductase 1) (Q5A446)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Ferric reductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity). Involved in maintenance of cell wall integrity (CWI), mitochondrial function, and interaction between the pathogen and the host.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P32791}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32791}.
Interaction partners:
- High-affinity iron permease
- Ferroxidase
- Fth1p
- Siderophore transporter
- Cu
- Fre9p
- Copper transport protein
Sequence:
MKIQQLIVFLFAVVLIDARTPKRYSELDIVMSTCTTFIGKYGTVCTSTGKRSTNWNCYCKTDAGFGTISDCLVRGFNNNTNIISKFTESCNMTESKFHAKYDKIQAEFKTNGTEYAKMTTKSSSGSKTSASASKSSKSTGSSNASKSSTNAHGSNSSTSSTSSSSSKSGKGNSGTSTTETITTPLLIDYKKFTPYKDAYQMSNNNFNLSINYGSGLLGYWAGILAIAIFANMIKKMFPSLTNYLSGSISNLFRKHLFLPATFRKKKAQEFSIGVYGFFDGLIPTRLETIIVVIFVVLTGLFSALHIHHVKDNPQYATKNAELGHLIADRTGILGTFLIPLLILFGGRNNFLQWLTGWDFATFIMYHRWISRVDVLLIIVHAITFSVSDKATGKYNTRMKRDFMIWGTVSTICGGFILFQAMLFFRRKCYEVFFLIHIVLVVFFVVGGYYHLESQGYGDFMWAAIAVWAFDRVVRLGRIFFFGARKATVSIKGDDTLKIEVPKPKYWKSVAGGHAFIHFLKPTLFLQSHPFTFTTTESNDKIVLYAKIKNGITSNIAKYLSPLPGNTATIRVLVEGPYGEPSSAGRNCKNVVFVAGGNGIPGIYSECVDLAKKSKNQSIKLIWIIRHWKSLSWFTEELEYLKKTNVQSTIYVTQPQDCSGLECFEHDVSFEKKSDEKDSVESSQYSLISNIKQGLSHVEFIEGRPDISTQVEQEVKQADGAIGFVTCGHPAMVDELRFAVTQNLNVSKHRVEYHEQLQTWA