wanglab/gogpt-training-data huggingface dataset:
Protein: BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 (O54940)
Organism: Mus musculus (Mouse)
Function: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}.
Interaction partners:
- Apoptosis regulator Bcl-2
- Cell division control protein 42 homolog
- Rho GTPase-activating protein 1
- Mitogen-activated protein kinase 14
Sequence:
MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEVDLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQEPPKSEQ
Protein: Defective proboscis extension response 7, isoform G (A8DZ28)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKTYNAFLNTKTKIIHVYLTNLERPFFDDISPRNVSAVVDEIAILRCRVKNKGNRTVSWMRKRDLHILTTNIYTYTGDQRFSVIHPPGSEDWDLKIDYAQPRDSGVYECQVNTEPKINLAICLQVIADNDFQDLKTKKRFYDTKSARAKILGSTEIHVKRDSTIALACSVNIHAPSVIWYHGSSVVDFDSLRGGISLETEKTDVGTTSRLMLTRASLRDSGNYTCVPNGAIPASVRVHVLTGEQPAAMQTSSAIRIRAFTAMITIISTKVLLYISSLMEHMYLRER
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (A0A0B4LHX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNGGGRTPALTRSCSSPAVYDIETHPASPVFPHLLLGNGRDADDPSSVGANCVLNVTCQSPNESHLQGLKYMQIPASDTPHQNIKQYFQEAYDFIEDARKTGSRVLLHCHAGISRSATIAIAYVMRYKSLSLLEAYKLVKVARPIISPNLNFMGQLLELEQNLRKSGVLAPATPHLNSPSNPSSSSVGLSTQSSQLVEQPEEEEKREQRERGKSKSDSEAMDEDGFDYDDVDSGSGSLAGSNCSSRLTSPPITPDDEAPSTSAAASSVSELDSPSSTSSSSGICSLLQSTSSSVSPRAISKPNLLSPTRQLALFKRNSPAKLRLDLESSYAPASPIPNTMPWLSVPSTPVCEEAPDSRINHVASNLTRD
Protein: CCAAT-binding factor domain-containing protein (Q38AX4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar complex protein 2
- Nucleolar protein, putative
- Nucleolar GTP-binding protein 1
- NLE domain-containing protein
- Ribosome biogenesis protein, putative
- Pescadillo homolog
- Ribosome biogenesis protein BOP1 homolog
- Protein MAK16 homolog
- RNA-binding protein, putative
- Eukaryotic translation initiation factor 6
Sequence:
MAAMQRYLMNTSYLSSQLKELHSLHNRTVSDYGELVENLTKECSILCDVIPNYKISATIEEEDGGQTGRKQKEVYQVQKLEHEVLVQYEHFLQLLRRLQRKPHPEQQALGSRLCARLVPRASEFNHADKLLSLAVTFANAKSTRVARPALTALAELLDGQMVSDATECIVSALLDIVRKQHYAMNPKLLNLLLHIRVAMVDMHRRDLTEEVAKNKRLKKEDKELARQLQKSKARRDRAEIVVKQSRILHRVFVIYLRVLEASKSCSQQHQTRILAPALEGLVKFAPLVNVELHQQLITALKDLVNDEATSVTTKLHALVSVASLAQRDATTTASDWRVDLSYFHEVLFRCLPEALTLPKCVESNKGTTGEGGDGDDDGDEVASQGSTSSAGSLSSQAFSITESMAQEKFVHSNASREWTFRVGLVLRAMDLLVLTQKHLPVPRVTAFVRRIMQAIPSCPPHIGLSLLALNHRLMLRYPAVSGIVIGGSDNFIAGRGVYTPGATQIASSNADCSFTWELSLLAKSFHPTMRNVAEVFCKHFYKVSKLTHGQAPVVTKQLDALGPYELLESHDPSSGEIRPPPPLPETMKRRKSGKLTAGVKRAHNDEASDPAGE
Protein: UPAR/Ly6 domain-containing protein crok (Protein crooked) (Q9VKA0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Vesicle {ECO:0000269|PubMed:20570942}. Membrane {ECO:0000269|PubMed:20570942}; Lipid-anchor, GPI-anchor {ECO:0000255}. Endomembrane system {ECO:0000269|PubMed:20570942}.
Interaction partners:
- FI02817p
- UPAR/Ly6 domain-containing protein crim
- LD32918p
- Kune-kune
- UPAR/Ly6 domain-containing protein bou
- LD29228p
- RE19849p
- Sinuous
Sequence:
MKTLEKYILFAIVLCCLLQLGQAIKCWDCRSDNDPKCGDPFDNSTLAITDCQQAPELEHLKGVRPTMCRKIRQKVHGEWRYFRSCAYMGEPGIEGDERFCLMRTGSYNIFMEFCTCNSKDGCNSAGIHRLGLMGVLTGTLLSVIVAHLLRQ
Protein: Steroid sulfatase (microsomal), isozyme S (Steryl-sulfatase isoform X1) (F1QB82)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Sulfotransferase
- Sulfotransferase
- Cytochrome P450, family 3, subfamily A, polypeptide 65
- Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2
- Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
- Cytochrome P450, family 17, subfamily A, polypeptide 1
- Cytochrome P450 1A
- Cytochrome P450, family 17, subfamily A, polypeptide 2
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Cholesterol side-chain cleavage enzyme
Sequence:
MKSFQWIPCTFCLLLYTADAGSGTKPNFVFMMVDDLGIGDLGCYGNTTLRTPNIDRLALEGVKLTQHIAAAPLCTPSRAAFLTGRYPIRSGMAAHGHMGVFLFSASSGGLPQEEITFAKAVKVQGYSTAVIGKWHLGLNCEDSSDHCHHPNSHGFDYFYGTIMTHLRDCQPGHGSVLYNVYSHIPFKPLSIGLVSLVVLHIRGMLTVSRRVFFSFLILVGLVLSLFRLLVYTFPNLNCFVMRGTEIVEQPYISENLTQRMTSEAIEFLERNSETPFLLFFSFIQVHTGVFASPLFRGRSQHGLYGDAVMEVDWSVGQIMQTLERLNLKDNTLVYMTSDQGPHLEEISVHGEMHGGYSGIYKAGKSTNWEGGIRIPGILSWPGVLPAGNIIDEPTSNMDIFPTVLNLAGASIPDDRVIDGHDLLPLLQGQVKRSEHELLFHYCNAELNAVRWRPPNSSAIWKAFFFTPDFYPKNSSACFHTHVCFCIKPFVTFHDPPLLYDLSKDPTESTPLSPDTEPQFHSVLEVIRAAVSRHTQSLKPVPVQVSPLKIVWKPWLQPCCSSLSQLCRCERDHQIEKVQDGLQKE
Protein: Transcriptional regulatory protein WalR (E0TZB5)
Organism: Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus subtilis subsp. spizizenii)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMDKKILVVDDEKPIADILEFNLRKEGYEVHCAHDGNEAVEMVEELQPDLILLDIMLPNKDGVEVCREVRKKYDMPIIMLTAKDSEIDKVIGLEIGADDYVTKPFSTRELLARVKANLRRQLTTAPAEEEPSSNEIHIGSLVIFPDAYVVSKRDETIELTHREFELLHYLAKHIGQVMTREHLLQTVWGYDYFGDVRTVDVTVRRLREKIEDNPSHPNWIVTRRGVGYYLRNPEQD
Protein: Protein stoned-A (Stn-A) (StonedA) (Q24211)
Organism: Drosophila melanogaster (Fruit fly)
Function: Adapter protein involved in endocytic recycling of synaptic vesicles membranes. May act by mediating the retrieval of synaptotagmin protein Syt from the plasma membrane, thereby facilitating the internalization of multiple synaptic vesicles from the plasma membrane.
Subcellular location: Cytoplasm. Synapse. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Colocalizes with synaptic vesicle pools. Colocalizes with the endocytic network within synaptic boutons.
Interaction partners:
- Protein stoned-B
- Synaptotagmin 1
- AP-2 complex subunit alpha
Sequence:
MLKLPKGLKKKKKKSKKDQELFTEEELEQYKRDLKAKQEAAATKSDAGESDGASSDVEAHHEPVAFNSGLGSGSSSSILNAQQQLSDQNQGAAGGDEEWAKFKALTSGVDSILHKTQDELDRIKKESFYQRLPSAAEKKKQKEEEAARLEAEQQEREKQRLGQIEAQRDKLAEAVVQLSESEEEAGDYEADDIFATDYIEAITSGELQLAVVPDSPVLAEDGPDPFDTAYAEKVIVGADRAKGNKKLVSLGAAVEVLSGRVDREHAVALANPKRKLRKGIQNLLLSESIELADSEAELLAATSNAEPQHNLLDDLDEELSESSVPIDLSVSLHLHLIKHKQPVEEEEELEQKGRENQLLNPDLSEFDSLKDEEDDEFAELAAESLTKKEEVTVVSQVVLPVAQLPTEAFEAGSWAEFEEQSGQEPGKPKRPPPPVRPPTGPHIVPGAIYVSEDEEENPEDDPFNTNYAEQVIKKTTVLEEDDDFDPRAEEHATEPPFLAAPQRDLLAGSATDLSQVVPAPLAPTLSVDQEAEDFDPFDTSAVSALVQPKSTELRFLERELLNYSGLDGVTLKHSLSDQDFDPRADQKEPAAPQVKLEQKETDFDTAQRKSSLSLNIQAKSVGFLVPASDLLGAGNELGASKKPLTPYYAPSDNRLQEREREAEDVDPFDTSHVPEAKLSDIELKHIEKDLISVPANLRHSLSDPDFDPRAPPTPVPAEVLLAVEENINIKVLTPAQDRKKLTNSGGSGKSEEDIDPFDTSIAANLQPGQTELKLLENELLPETKTLVTDVLDVQSDAQELGLGDKVLTPSTHSRPSLPAQDIDPFDTSIAENLAPGEAEIKLLESELIER
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8YCJ4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAGVDCGDGVGARQHVFLVSEYLKDASKKMKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKLGLPTGHFVMAAQRQKRGK
Protein: Retinoid X receptor beta isoform 3 (A0A0S2Z4M5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MSWAARPPFLPQRHAAGQCGPVGVRKEMHCGVASRWRRRRPWLDPAAAAAAAVAGGEQQTPEPEPGEAGRDGMGDSGRDSRSPDSSSPNPLPQGVPPPSPPGPPLPPSTAPSLGGSGAPPPPPMPPPPLGSPFPVISSSMGSPGLPPPAPPGFSGPVSSPQINSTVSLPGGGSGPPEDVKPPVLGVRGLHCPPPPGGPGAGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYSCRDNKDCTVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGEGAGGAPEEMPVDRILEAELAVEQKSDQGVEGPGGTGGSGSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSSLPLDDQVILLRAGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPSEVEVLREKVYASLETYCKQKYPEQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQLA
Protein: Minor curlin subunit (Fimbrin SEF17 minor subunit) (P0A1E9)
Organism: Salmonella enteritidis
Function: Curlin is the structural subunit of the curli. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. The minor subunit is the nucleation component of curlin monomers.
Subcellular location: Fimbrium {ECO:0000269|PubMed:17379722}. Note=Part of the curli surface structure.
Interaction partners:
Sequence:
MKNKLLFMMLTILGAPGIATATNYDLARSEYNFAVNELSKSSFNQAAIIGQVGTDNSARVRQEGSKLLSVISQEGGNNRAKVDQAGNYNFAYIEQTGNANDASISQSAYGNSAAIIQKGSGNKANITQYGTQKTAVVVQKQSHMAIRVTQR
Protein: Calcium/manganese antiporter SLC30A10 (Solute carrier family 30 member 10) (Zinc transporter 10) (ZnT-10) (Q6XR72)
Organism: Homo sapiens (Human)
Function: Plays a pivotal role in manganese transport. Manganese is an essential cation for the function of several enzymes, including some crucially important for the metabolism of neurotransmitters and other neuronal metabolic pathways. However, elevated levels of manganese are cytotoxic and induce oxidative stress, mitochondrial dysfunction and apoptosis. Acts as manganese efflux transporter and confers protection against manganese-induced cell death. Also acts as zinc transporter involved in zinc homeostasis. Seems to mediate zinc transport into early endosomes and recycling endosomes to prevent zinc toxicity; the function may be regulated by heterodimerization with other zinc transporters of the SLC30A subfamily. The SLC30A3:SLC30A10 heterodimer is involved in zinc transport-dependent regulation of the EGFR/ERK transduction pathway in endosomes. May be involved in regulation of zinc-dependent senescence of vascular smooth muscle cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22706290, ECO:0000269|PubMed:25319704, ECO:0000269|PubMed:26728129, ECO:0000269|PubMed:27226609, ECO:0000269|PubMed:27307044}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:22706290, ECO:0000269|PubMed:27226609}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:22427991, ECO:0000269|PubMed:26728129}. Early endosome membrane {ECO:0000269|PubMed:22427991, ECO:0000269|PubMed:26728129}; Multi-pass membrane protein {ECO:0000255}. Note=Localization to the Golgi and plasma membrane is regulated by zinc. {ECO:0000269|PubMed:22706290}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase-like N
- Glutamate decarboxylase 2
- Insulin
- Metal cation symporter ZIP14
- Zinc transporter 6
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Metal cation symporter ZIP8
- Insulinoma-associated protein 2
- Zinc transporter SLC39A7
- Zinc transporter ZIP1
Sequence:
MGRYSGKTCRLLFMLVLTVAFFVAELVSGYLGNSIALLSDSFNMLSDLISLCVGLSAGYIARRPTRGFSATYGYARAEVVGALSNAVFLTALCFTIFVEAVLRLARPERIDDPELVLIVGVLGLLVNVVGLLIFQDCAAWFACCLRGRSRRLQQRQQLAEGCVPGAFGGPQGAEDPRRAADPTAPGSDSAVTLRGTSVERKREKGATVFANVAGDSFNTQNEPEDMMKKEKKSEALNIRGVLLHVMGDALGSVVVVITAIIFYVLPLKSEDPCNWQCYIDPSLTVLMVIIILSSAFPLIKETAAILLQMVPKGVNMEELMSKLSAVPGISSVHEVHIWELVSGKIIATLHIKYPKDRGYQDASTKIREIFHHAGIHNVTIQFENVDLKEPLEQKDLLLLCNSPCISKGCAKQLCCPPGALPLAHVNGCAEHNGGPSLDTYGSDGLSRRDAREVAIEVSLDSCLSDHGQSLNKTQEDQCYVNRTHF
Protein: Dihydroflavonol 4-reductase (Dihydroflavonol-4-reductase-like) (A2IBG0)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Leucoanthocyanidin dioxygenase-like
- Leucoanthocyanidin dioxygenase-like
- Leucoanthocyanidin dioxygenase-like
- Leucoanthocyanidin reductase-like
- Leucoanthocyanidin reductase-like
- Leucoanthocyanidin reductase-like
- Flavonol synthase/flavanone 3-hydroxylase-like
- Flavonol synthase/flavanone 3-hydroxylase-like
- Flavonol synthase/flavanone 3-hydroxylase-like
- Flavonol synthase/flavanone 3-hydroxylase-like
Sequence:
MPTDNQMKDMKPNSIMGSSVTDGEIVCVTGGSGFIGSWLIKLLLERGYVVRATVRDPGNSKKVKHLLELPKAETHLTLWKADLAEEGSFDDAIQACTGVFHVATPMDFESEDPENEVIKPTINGVLSIMKACAKAKTVRRLVFTSSAGTIDVAEQQKPCYDETCWSDLEFIQAKKMTGWMYFVSKTMAEQAAWKFAKENNIDFVSIIPPLVVGPFIMQSMPPSLITALSPITGNEAHYSIIKQGQFIHLDDLCRAHIFLFENPKAEGRHICASHHATIIDLAKMLSEKYPEYNVPTKFKDVDENLKSVEFSSKKLLDLGFEFKYSLEDMFVGAVETCREKGLLPLSNEKKIKNID
Protein: THO complex subunit 2 (Tho2) (hTREX120) (Q8NI27)
Organism: Homo sapiens (Human)
Function: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. Required for NXF1 localization to the nuclear rim. Plays a role for proper neuronal development.
Subcellular location: Nucleus {ECO:0000269|PubMed:29851191}. Nucleus speckle {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:29851191}.
Interaction partners:
- THO complex subunit 6
- THO complex subunit 5
- THO complex subunit 7
- THO complex subunit 1
- Spliceosome RNA helicase DDX39B
- THO complex subunit 3
- THO complex subunit 4
- Ubiquitin carboxyl-terminal hydrolase CYLD
- Zinc finger protein GLI2
- Chromatin target of PRMT1 protein
Sequence:
MAAAAVVVPAEWIKNWEKSGRGEFLHLCRILSENKSHDSSTYRDFQQALYELSYHVIKGNLKHEQASNVLSDISEFREDMPSILADVFCILDIETNCLEEKSKRDYFTQLVLACLYLVSDTVLKERLDPETLESLGLIKQSQQFNQKSVKIKTKLFYKQQKFNLLREENEGYAKLIAELGQDLSGSITSDLILENIKSLIGCFNLDPNRVLDVILEVFECRPEHDDFFISLLESYMSMCEPQTLCHILGFKFKFYQEPNGETPSSLYRVAAVLLQFNLIDLDDLYVHLLPADNCIMDEHKREIAEAKQIVRKLTMVVLSSEKMDEREKEKEKEEEKVEKPPDNQKLGLLEALLKIGDWQHAQNIMDQMPPYYAASHKLIALAICKLIHITIEPLYRRVGVPKGAKGSPVNALQNKRAPKQAESFEDLRRDVFNMFCYLGPHLSHDPILFAKVVRIGKSFMKEFQSDGSKQEDKEKTEVILSCLLSITDQVLLPSLSLMDCNACMSEELWGMFKTFPYQHRYRLYGQWKNETYNSHPLLVKVKAQTIDRAKYIMKRLTKENVKPSGRQIGKLSHSNPTILFDYILSQIQKYDNLITPVVDSLKYLTSLNYDVLAYCIIEALANPEKERMKHDDTTISSWLQSLASFCGAVFRKYPIDLAGLLQYVANQLKAGKSFDLLILKEVVQKMAGIEITEEMTMEQLEAMTGGEQLKAEGGYFGQIRNTKKSSQRLKDALLDHDLALPLCLLMAQQRNGVIFQEGGEKHLKLVGKLYDQCHDTLVQFGGFLASNLSTEDYIKRVPSIDVLCNEFHTPHDAAFFLSRPMYAHHISSKYDELKKSEKGSKQQHKVHKYITSCEMVMAPVHEAVVSLHVSKVWDDISPQFYATFWSLTMYDLAVPHTSYEREVNKLKVQMKAIDDNQEMPPNKKKKEKERCTALQDKLLEEEKKQMEHVQRVLQRLKLEKDNWLLAKSTKNETITKFLQLCIFPRCIFSAIDAVYCARFVELVHQQKTPNFSTLLCYDRVFSDIIYTVASCTENEASRYGRFLCCMLETVTRWHSDRATYEKECGNYPGFLTILRATGFDGGNKADQLDYENFRHVVHKWHYKLTKASVHCLETGEYTHIRNILIVLTKILPWYPKVLNLGQALERRVHKICQEEKEKRPDLYALAMGYSGQLKSRKSYMIPENEFHHKDPPPRNAVASVQNGPGGGPSSSSIGSASKSDESSTEETDKSRERSQCGVKAVNKASSTTPKGNSSNGNSGSNSNKAVKENDKEKGKEKEKEKKEKTPATTPEARVLGKDGKEKPKEERPNKDEKARETKERTPKSDKEKEKFKKEEKAKDEKFKTTVPNAESKSTQEREREKEPSRERDIAKEMKSKENVKGGEKTPVSGSLKSPVPRSDIPEPEREQKRRKIDTHPSPSHSSTVKDSLIELKESSAKLYINHTPPPLSKSKEREMDKKDLDKSRERSREREKKDEKDRKERKRDHSNNDREVPPDLTKRRKEENGTMGVSKHKSESPCESPYPNEKDKEKNKSKSSGKEKGSDSFKSEKMDKISSGGKKESRHDKEKIEKKEKRDSSGGKEEKKHHKSSDKHR
Protein: Carboxypeptidase Y homolog A (EC 3.4.16.5) (Q96VC4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity).
Subcellular location: Vacuole {ECO:0000269|PubMed:11440134}.
Interaction partners:
- Vacuolar protein sorting/targeting protein 10
Sequence:
MRVLPATLLVGAATAATPAQQVLGGLQDFGNAVQDAMHENLPKINKPLEAFQEQLKSLYEAREFWEEVANAFPQNLDHNPVFSLPKKHTRRPDSHWDHIVRGADVQSVWVTGENGEKEREIEGKLEAYDLRIKKTDPSSLGIDPDVKQYTGYLDDNENDKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFMELGPSSIDENIKPVYNPYAWNSNASVIFLDQPVNVGYSYSGSTVSDTVAAGKDVYALLTLFFKQFPEYAEQDFHIAGESYAGHYIPVFTSEILSHQKRNINLKSVLIGNGLTDGLTQYEYYRPMACGEGGYPAVLDESSCRSMDNALGRCQSMIESCYNSESAWVCVPASIYCNNALLAPYQRTGQNVYDVRGKCEDESNLCYKGMGYVSEYLNKPEVRAAVGAEVDGYDSCNFDINRNFLFHGDWMKPYHRLVPGILEQIPVLIYAGDADFICNWLGNKAWTEALEWPGHKEFAAAPMEDLKIVDNEHTGKKIGQIKTHGNFTFMRLYGGGHMVPMDQPEASLEFFNRWLGGEWF
Protein: Auxin transporter protein 1 (Auxin influx carrier protein 1) (Polar auxin transport inhibitor-resistant protein 1) (Q96247)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carrier protein involved in proton-driven auxin influx. Mediates the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips by contributing to the loading of auxin in vascular tissues and facilitating acropetal (base to tip) auxin transport within inner tissues of the root apex, and basipetal (tip to base) auxin transport within outer tissues of the root apex. Unloads auxin from the mature phloem to deliver the hormone to the root meristem via the protophloem cell files. Coordinated subcellular localization of AUX1 is regulated by a brefeldin A-sensitive (BFA) vesicle trafficking process. Involved in lateral root formation, trichoblast polarization and root hair elongation. Required for gravitropism and thigmotropism, especially in roots, by modulating responses to auxin, ethylene and cytokinins such as benzyladenine (BA). Needed for ammonium-mediated root-growth inhibition. Confers sensitivity to the herbicide 2,4-dichlorophenoxyacetic acid (2,4-D, auxin analog), and to polar auxin transport inhibitors such as N-1-naphthylphthalamic acid (NPA) and 2,3,5-triiodobenzoic acid (TIBA).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11641271, ECO:0000269|PubMed:11864575, ECO:0000269|PubMed:15486104}; Multi-pass membrane protein {ECO:0000269|PubMed:11641271, ECO:0000269|PubMed:11864575, ECO:0000269|PubMed:15486104}. Note=In S2 columella cells, a dynamic cytoplasmic to membrane localization seems to occur during early stage of gravity signal transduction. In roots protophloem cells, asymmetric repartition in the upper plasma membrane.
Interaction partners:
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Protein TOPLESS
- Auxin response factor 19
- Toll/interleukin-1 receptor-like protein
- Auxin response factor 7
- Auxin response factor 5
- Auxin efflux carrier component 7
- Corepressor
- Auxin efflux carrier component 3
- Protein AUXIN SIGNALING F-BOX 3
Sequence:
MSEGVEAIVANDNGTDQVNGNRTGKDNEEHDGSTGSNLSNFLWHGGSVWDAWFSCASNQVAQVLLTLPYSFSQLGMLSGIVLQIFYGLLGSWTAYLISVLYVEYRARKEKEGKSFKNHVIQWFEVLDGLLGSYWKALGLAFNCTFLLFGSVIQLIACASNIYYINDHLDKRTWTYIFGACCATTVFIPSFHNYRIWSFLGLGMTTYTAWYLAIASIIHGQAEGVKHSGPTKLVLYFTGATNILYTFGGHAVTVEIMHAMWKPQKFKYIYLMATLYVFTLTIPSAAAVYWAFGDALLDHSNAFSLMPKNAWRDAAVILMLIHQFITFGFACTPLYFVWEKVIGMHDTKSICLRALARLPVVIPIWFLAIIFPFFGPINSAVGALLVSFTVYIIPSLAHMLTYRSASARQNAAEKPPFFMPSWTAMYVLNAFVVVWVLIVGFGFGGWASVTNFVRQVDTFGLFAKCYQCKPAAAAAHAPVSALHHRL
Protein: Cutinase cut1 (EC 3.1.1.74) (Poly(ethylene terephthalate) hydrolase) (PET hydrolase) (PETase) (EC 3.1.1.101) (G8GER6)
Organism: Thermobifida fusca (Thermomonospora fusca)
Function: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Probable). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world.
Subcellular location: Secreted {ECO:0000269|PubMed:23604968}. Periplasm {ECO:0000269|PubMed:23604968}.
Interaction partners:
Sequence:
MPPHAARPGPAQNRRGRAMAVITPRRERSSLLSRALRFTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF
Protein: Oxygen sensor histidine kinase response regulator DevS/DosS (EC 2.7.13.3) (P9WGK3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response. Regulates an approximately 48-member regulon. Required for full induction of the DevR (DosR) regulon; acts later than DosT to positively regulate expression of the DevR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Autophosphorylates under anaerobic but not aerobic conditions, binding of NO or CO does not dramatically change the level of autophosphorylation of Fe(2+) protein, binding of O(2) inactivates kinase activity. Binds O(2), NO, CO. It is probably reduced by flavin nucleotides such as FMN and FAD. May be the primary sensor for CO. Donates a phosphate group to transcriptional regulator DevR (DosR).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:16213520, ECO:0000305|PubMed:17600145}.
Interaction partners:
- DNA-binding transcriptional activator DevR/DosR
- Universal stress protein Rv3134c
- Uncharacterized protein Rv0569
- Universal stress protein Rv2028c
- Probable transcriptional regulatory protein NarL
- Nitrate reductase-like protein NarX
- Universal stress protein Rv2005c
- Universal stress protein Rv2624c
- ATP-dependent 6-phosphofructokinase isozyme 2
- Probable cation-transporting ATPase F
Sequence:
MTTGGLVDENDGAAMRPLRHTLSQLRLHELLVEVQDRVEQIVEGRDRLDGLVEAMLVVTAGLDLEATLRAIVHSATSLVDARYGAMEVHDRQHRVLHFVYEGIDEETVRRIGHLPKGLGVIGLLIEDPKPLRLDDVSAHPASIGFPPYHPPMRTFLGVPVRVRDESFGTLYLTDKTNGQPFSDDDEVLVQALAAAAGIAVANARLYQQAKARQSWIEATRDIATELLSGTEPATVFRLVAAEALKLTAADAALVAVPVDEDMPAADVGELLVIETVGSAVASIVGRTIPVAGAVLREVFVNGIPRRVDRVDLEGLDELADAGPALLLPLRARGTVAGVVVVLSQGGPGAFTDEQLEMMAAFADQAALAWQLATSQRRMRELDVLTDRDRIARDLHDHVIQRLFAIGLALQGAVPHERNPEVQQRLSDVVDDLQDVIQEIRTTIYDLHGASQGITRLRQRIDAAVAQFADSGLRTSVQFVGPLSVVDSALADQAEAVVREAVSNAVRHAKASTLTVRVKVDDDLCIEVTDNGRGLPDEFTGSGLTNLRQRAEQAGGEFTLASVPGASGTVLRWSAPLSQ
Protein: Mediator of RNA polymerase II transcription subunit 6 (Mediator complex subunit 6) (dMED6) (Q8MSX2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for activated transcription of the MtnA, MtnB and MtnD genes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 26
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 18
Sequence:
MASRQMTNDHLRLSWHDTQMMATLSPQTVMDYFCRKSNPFYDHMCNNETVRMQRLGPEHLHNMIGLEYILLHVAEPILYVIRKQHRHNPSEATPIADYYIIGGTVYKAPDLANVINSRILNTVVNLQSAFEEASSYARYHPNKGYTWDFSSNKVFSDRSKSDKKDANSAKDENSGTLFQKQRVDMLLAELLRKFPPPIPPMLQNLQQPPPAGDDLNTARNASEMNNATGPLDIKTEGVDMKPPPEKKSK