wanglab/gogpt-training-data huggingface dataset:
Protein: Branched-chain alpha-ketoacid dehydrogenase kinase (BCKDH kinase) (BCKDHKIN) (BDK) (EC 2.7.11.1) ([3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial) (EC 2.7.11.4) (Q00972)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex.
Subcellular location: Mitochondrion matrix. Mitochondrion {ECO:0000269|PubMed:29779826}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000269|PubMed:29779826}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit beta, mitochondrial
Sequence:
MILTSVLGSGPRSGSSLWPLLGSSLSLRVRSTSATDTHHVELARERSKTVTSFYNQSAIDVVAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
Protein: Major DNA-binding protein (P04296)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007, ECO:0000269|PubMed:26676794, ECO:0000269|PubMed:9151871}. Note=In the absence of DNA replication, found in the nuclear framework-associated structures (prereplicative sites). As viral DNA replication proceeds, it migrates to globular intranuclear structures (replication compartments). {ECO:0000255|HAMAP-Rule:MF_04007}.
Interaction partners:
Sequence:
METKPKTATTIKVPPGPLGYVYARACPSEGIELLALLSARSGDSDVAVAPLVVGLTVESGFEANVAVVVGSRTTGLGGTAVSLKLTPSHYSSSVYVFHGGRHLDPSTQAPNLTRLCERARRHFGFSDYTPRPGDLKHETTGEALCERLGLDPDRALLYLVVTEGFKEAVCINNTFLHLGGSDKVTIGGAEVHRIPVYPLQLFMPDFSRVIAEPFNANHRSIGEKFTYPLPFFNRPLNRLLFEAVVGPAAVALRCRNVDAVARAAAHLAFDENHEGAALPADITFTAFEASQGKTPRGGRDGGGKGAAGGFEQRLASVMAGDAALALESIVSMAVFDEPPTDISAWPLFEGQDTAAARANAVGAYLARAAGLVGAMVFSTNSALHLTEVDDAGPADPKDHSKPSFYRFFLVPGTHVAANPQVDREGHVVPGFEGRPTAPLVGGTQEFAGEHLAMLCGFSPALLAKMLFYLERCDGAVIVGRQEMDVFRYVADSNQTDVPCNLCTFDTRHACVHTTLMRLRARHPKFASAARGAIGVFGTMNSMYSDCDVLGNYAAFSALKRADGSETARTIMQETYRAATERVMAELETLQYVDQAVPTAMGRLETIITNREALHTVVNNVRQVVDREVEQLMRNLVEGRNFKFRDGLGEANHAMSLTLDPYACGPCPLLQLLGRRSNLAVYQDLALSQCHGVFAGQSVEGRNFRNQFQPVLRRRVMDMFNNGFLSAKTLTVALSEGAAICAPSLTAGQTAPAESSFEGDVARVTLGFPKELRVKSRVLFAGASANASEAAKARVASLQSAYQKPDKRVDILLGPLGFLLKQFHAAIFPNGKPPGSNQPNPQWFWTALQRNQLPARLLSREDIETIAFIKKFSLDYGAINFINLAPNNVSELAMYYMANQILRYCDHSTYFINTLTAIIAGSRRPPSVQAAAAWSAQGGAGLEAGARALMDAVDAHPGAWTSMFASCNLLRPVMAARPMVVLGLSISKYYGMAGNDRVFQAGNWASLMGGKNACPLLIFDRTRKFVLACPRAGFVCAASSLGGGAHESSLCEQLRGIISEGGAAVASSVFVATVKSLGPRTQQLQIEDWLALLEDEYLSEEMMELTARALERGNGEWSTDAALEVAHEAEALVSQLGNAGEVFNFGDFGCEDDNATPFGGPGAPGPAFAGRKRAFHGDDPFGEGPPDKKGDLTLDML
Protein: C3H1-type domain-containing protein (Q57VA5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribosomal RNA-processing protein 43
- 5'-3' exoribonuclease 2
- Pumilio/PUF RNA binding protein 5, putative
Sequence:
MARNRKHDIVKASKYKTSLCTYFMENGECQFGDRCAFAHGEDELRHEEEGPKSRDSRERGDTNVESAQGGSNAEQRSVLPCASFESGMESTANETTAGASGRVTYCSWHEAELLSPKGGSSVGSPHHLSNSEATVPFTEDTELKGVKPPPKITKGKLSRQNRANMSVFTNKARGVEAKSTIQPTSVHYPTSGNNVYLSVVNLADTSGQLVQLAPGAFLFPFPGAPPPYVGPFIPSVGIPSEAAFGDGVAWISNGHMVNSFVTTRTTEVENANCATDLAFRAFDTVGNIPVNSGSSGNRLTPQSAGEVLPSLDPSTHLGGVYETSMKTSLPHQPTTWSSASCTEGIGSSTLRKDNDASSYDVGEFGNPKVKEPPSTKSKEISDFRSLLDSRLISESLADKNAGTDPRDEKNGSIYRQCTAAGLTQLYEIRADRGSHRPVASEQSDGGVGAGGSVEEHNRNVDFTSILRGCDVNIFAHAALGGSEIQRDQAEVSSGKEWTSRAVERGEDFSAAGGSGARKVGEATSQVVCPSEQHRAIPPAQRPRPVVANYFQSSCAESDKCVPVYPL
Protein: Cytochrome c oxidase subunit V, putative (Q38FK9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRFVTPFLATVPLSRNFFGKGWDNAALDTIFSCMLRKPEVNDRIRSQYASTMDPRDADVLRRLGEVAKENKTYIRVFLPPHLGDPHRLLKCYSLTAYPILDDKGGQLTVEMDGHHLEAFADPDDDYAKVVIPHIELVDFLAKSLLETMKWEATPRGAASLLESLYRGAEIPDHVFQTPAVIERPEIFKDGNKISN
Protein: Cell surface Cu-only superoxide dismutase 5 (EC 1.15.1.1) (Predicted GPI-anchored protein 3) (Q5AD07)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. Degrades host-derived reactive oxygen species to escape innate immune surveillance. Involved in the occurrence of miconazole-tolerant persisters in biofilms. Persisters are cells that survive high doses of an antimicrobial agent. The unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:23136884}. Membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). {ECO:0000250}.
Interaction partners:
- Superoxide dismutase 1 copper chaperone
- Peroxisomal catalase
- Stress protein DDR48
- Uncharacterized protein
- Agglutinin-like protein 3
Sequence:
MKYLSIFLLATFALAGDAPISTDSKGSPSLIAKFEKTSKSNIEGTIKFTPANNGTVSVSVDLKGLPSDIGPFPYHVHEKPVPASKNCSATENHFNPYNGTVRAATPAAHEVGDLAGKHGNIMGESYKTEYDDSYISLNEKSRSYIGGLSIVIHANNGTRLNCANITLLDEGHGNANTTMSNSSSSSSQSAVNTSSSMASTAPQGNGAERAVVNGLLAAGVVGVIAALI
Protein: Protein NDR1 (Non-race specific disease resistance protein 1) (AtNDR1) (O48915)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in disease resistance. Required for resistance conferred by multiple R genes recognizing different bacterial and oomycete pathogen isolates like avirulent P.syringae or H.parasitica (downy mildew). Required for the establishment of hypersensitive response (HR) and systemic acquired resistance (SAR) after infection with the bacterial pathogen P.syringae DC3000 carrying avrRpt2. Required for resistance to the soilborne fungus V.longisporum. Interaction with RIN4 is required for the activation of the R gene RPS2 and RPS2-mediated resistance.
Subcellular location: Cell membrane {ECO:0000305|PubMed:15447649}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:15447649}.
Interaction partners:
- RPM1-interacting protein 4
- Protein EDS1
- Late embryogenesis abundant
- NDR1/HIN1-like 22
- Disease resistance protein RPS2
- Disease resistance protein RPM1
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- At5g06330
Sequence:
MNNQNEDTEGGRNCCTCCLSFIFTAGLTSLFLWLSLRADKPKCSIQNFFIPALGKDPNSRDNTTLNFMVRCDNPNKDKGIYYDDVHLNFSTINTTKINSSALVLVGNYTVPKFYQGHKKKAKKWGQVKPLNNQTVLRAVLPNGSAVFRLDLKTQVRFKIVFWKTKRYGVEVGADVEVNGDGVKAQKKGIKMKKSDSSFPLRSSFPISVLMNLLVFFAIR
Protein: RAB11A GTPase (Small GTPase Rab11) (Q9NJE8)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MEDMNLTFKVVIVGDSGVGKSNLMTRYTADEFSQDTPATIGVEFMTKSIKIEGRDAKVQIWDTAGQERFRAISRSIYHGAKGAMLVYDITNQTSFDSISTWLQELRAFVPATCSIFLIGNKCDLEHLRVIKKEVADRFARENGLSFLETSALEKTNVDKAFEWLAKSVYDHVVAPVDSAATGKRPPLNAGAAAKKPVNLSPSNSNQPAGKASGGCC
Protein: Iroquois homeobox 4 (D3ZRI4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MSYPQFGYPYSSAPQFLMTTNSLSTCCESGGRTLADSGPAASAQAPVYCPVYESRLLATARHELNSAAALGVYGSPYSSSQGYGNYVTYGSEASAFYSLNSFESKDGTGSSHAGLPPTAAAAYYPYEPTLGQYPYDRYGTVDSGTRRKNATRETTSTLKAWLQEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWPPRNKCADEKRPYGEGEEEEAGEEESREEPLKSVKSEGPAGKEDKELELSDLEDFDPLDTETSECELKTPFQPLDSVPERIPPSSDGPGTGKEAPVTLRMPLGTADGAVMDGDLERARNCLRSTVVAPDSGAEGGPQACEAKLTFAPAGAPPNLETKPRIWSLAHTATAAAATALSQTEFPSCMLKRQGSTGASAVTPASSPAVPAASGTLDRHQDSPVTSLRNWVDGVFHDPILRHSTLNQAWATAKGALLDPGPLGRNLGAGTNVLTTPLACSFRPTVPQDVSPAGASRELLATPKASGKPFCT
Protein: 3'(2'),5'-bisphosphate nucleotidase 1 (EC 3.1.3.7) (Bisphosphate 3'-nucleotidase 1) (Inositol-polyphosphate 1-phosphatase) (Q23493)
Organism: Caenorhabditis elegans
Interaction partners:
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase pps-1
- Putative inositol monophosphatase 3
- Conserved regulator of innate immunity protein 3
- Protein clpf-1
- Inositol monophosphatase ttx-7
- Transmembrane protein 208
- Inositol-3-phosphate synthase
- thiosulfate sulfurtransferase
- Partner of xrn-2 protein 1
- Probable FAD synthase
Sequence:
MFNKASFLTRLVASSVRVSEAAGGLIKNVMAGGDLKIIDKSEHGSGYDPQTEADRRAQYCIVQSLQKHFKNINIIGEEEDTTACPEIEMGFSADVLQMERLMSTELKNIQENDVVVWVDPLDGTSEVALAVKNKNMALLEQVTVLIGIAYKGRPVAGIIHQPYHEKLGRTVWAIQGCGVHGVVPATGNAQKIVVTTRSHLSESVSNALEALKTRNLADSVEKVGGAGFKVLKVLEGCAAYVFASAGCKKWDTCAVEAVLTAAGGTLTDISGRDIRYEPGVQLNNTGGVLATASWVKHKDYIDTIPQEIKNMLPEISSKK
Protein: NEDD8 ultimate buster 1 (NEDD8 ultimate buster-1, isoform CRA_d) (H3BM14)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKTNGGRCRIRALCWSRREWRGAGMAQKKYLQAKLTQFLREDRIQLWKPPYTDENKKVGLALKDLAKQYSDRLECCENEVEKVIEEIRCKAIERGTGNDNYRTTGIATIEVFLPPRLKKDRKNLLETRLHITGRELRSKIAETFGLQENYIKIVINKKQLQLGKTLEEQGVAHNVKAMVLELKQSEEDARKNFQLEEEEQNEAKLKEKQIQRTKRGLEILAKRAAETVVDPEMTPYLDIANQTGRSIRIPPSERKALMLAMGYHEKGRAFLKRKEYGIALPCLLDADKYFCECCRELLDTVDNYAVLQLDIVWCYFRLEQLECLDDAEKKLNLAQKCFKNCYGENHQRLVHIKGNCGKEKVLFLRLYLLQGIRNYHSGNDVEAYEYLNKARQLFKELYIDPSKVDNLLQLGFTAQEARLGLRACDGNVDHAATHITNRREELAQIRKEEKEKKRRRLENIRFLKGMGYSTHAAQQILLSNPQMWWLNDSNPETDNRQESPSQENIDRLVYMGFDALVAEAALRVFRGNVQLAAQTLAHNGGSLPPELPLSPEDSLSPPATSPSDSAGTSSASTDEDMETEAVNEILEDIPEHEEDYLDSTLEDEEIIIAEYLSYVENRKSATKKN
Protein: Defensin-like protein 59 (Q4VNZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MNITKSYVVIFFLVMLTNSLSNSDILVSSVIETSKYDVCFIPCTRRYEDRECNDDCLAKDFNDGGCVDGRCCCKY
Protein: Thymidine kinase 2, mitochondrial (EC 2.7.1.21) (2'-deoxyuridine kinase TK2) (EC 2.7.1.74) (Deoxycytidine kinase TK2) (EC 2.7.1.-) (Mt-TK) (Q9R088)
Organism: Mus musculus (Mouse)
Function: Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10571069, ECO:0000269|PubMed:11023833}.
Interaction partners:
- Thymidine kinase, cytosolic
- Thymidylate synthase
- Thymidine phosphorylase
- Thymidylate kinase
- Deoxycytidylate deaminase
- Deoxyuridine triphosphatase.
- 5'
- UMP-CMP kinase
- Cytidine deaminase
- Uridine phosphorylase 1
Sequence:
MLLRSLRSWAARSPRSVGPGSSGSPGSLDSGAGPLWAPRRAWPPDKDRENDKEKKAVVCIEGNIASGKTTCLEFFSNTTDVEVLMEPVLKWRNVHGHNPLSLMYHDASRWGLTLQTYVQLTMLDQHTRPQMSPVRLMERSIYSARYIFVENLYRGGKMPEVDYAILSEWFDWIVRNIDVSVDLIVYLRTTPEICYQRLKMRCREEEKVIPMEYLHAIHRLYEEWLVNGSLFPAAAPVLVIEADHNLEKMLELFEQNRARILTPENWKHGP
Protein: Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 110 kDa subunit homolog) (eIF3 p110) (Translation initiation factor eIF3, p110 subunit homolog) (P38249)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-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.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor eIF-1
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 1A
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 2 subunit gamma
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS2A
Sequence:
MAPPPFRPENAIKRADELISVGEKQAALQSLHDFITARRIRWATPSTVEPVVFKFLEIGVELKKGKLLKDGLHQYKKLIQGSTEGLVSVGAVARKFIDLVESKIASEQTRADELQKQEIDDDLEGGVTPENLLISVYESDQSVAGFNDEAITSWLRFTWESYRAVLDLLRNNALLEITYSGVVKKTMHFCLKYQRKNEFKRLAEMLRQHLDAANYQQSKSGNNLVDLSDADTLQRYLDQRFQQVDVSVKLELWHEAYRSIEDVFHLMKISKRAPKPSTLANYYENLVKVFFVSGDPLLHTTAWKKFYKLYSTNPRATEEEFKTYSSTIFLSAISTQLDEIPSIGYDPHLRMYRLLNLDAKPTRKEMLQSIIEDESIYGKVDEELKELYDIIEVNFDVDTVKQQLENLLVKLSSKTYFSQYIAPLRDVIMRRVFVAASQKFTTVSQSELYKLATLPAPLDLSAWDIEKSLLQAAVEDYVSITIDHESAKVTFAKDPFDIFASTASKEVSEEENTEPEVQEEKEETDEALGPQETEDGEEKEEESDPVIIRNSYIHNKLLELSNVLHDVDSFNNASYMEKVRIARETLIKKNKDDLEKISKIVDERVKRSQEQKQKHMEHAALHAEQDAEVRQQRILEEKAAIEAKLEEEAHRRLIEKKKREFEAIKEREITKMITEVNAKGHVYIDPNEAKSLDLDTIKQVIIAEVSKNKSELESRMEYAMKKLDHTERALRKVELPLLQKEVDKLQETDTANYEAMKKKIVDAAKAEYEARMADRKNLVMVYDDYLKFKEHVSGTKESELAAIRNQKKAELEAAKKARIEEVRKRRYEEAIARRKEEIANAERQKRAQELAEATRKQREIEEAAAKKSTPYSFRAGNREPPSTPSTLPKATVSPDKAKLDMIAQKQREMEEAIEQRLAGRTAGGSSPATPATPATPATPTPSSGPKKMTMAEKLRAKRLAKGGR
Protein: Beta-defensin 128 (Beta-defensin 28) (DEFB-28) (Defensin, beta 128) (Q7Z7B8)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Beta-defensin 125
- Beta-defensin 124
- Beta-defensin 135
- Beta-defensin 134
- Beta-defensin 129
- Beta-defensin 126
- Beta-defensin 114
- Beta-defensin 132
- Beta-defensin 116
- Beta-defensin 113
Sequence:
MKLFLVLIILLFEVLTDGARLKKCFNKVTGYCRKKCKVGERYEIGCLSGKLCCANDEEEKKHVSFKKPHQHSGEKLSVLQDYIILPTITIFTV
Protein: Zinc finger protein 470 (Chondrogenesis zinc finger protein 1) (CZF-1) (Q6ECI4)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15302581}.
Interaction partners:
- Zinc finger protein 667
Sequence:
MKSQEEVEVAGIKLCKAMSLGSVTFTDVAIDFSQDEWEWLNLAQRSLYKKVMLENYRNLVSVGLCISKPDVISLLEQEKDPWVIKGGMNRGLCPDLECVWVTKSLSLNQDIYEEKLPPAIIMERLKSYDLECSTLGKNWKCEDLFERELVNQKTHFRQETITHIDTLIEKRDHSNKSGTVFHLNTLSYIKQIFPMEERIFNFHTDKKSLKTHSVVKKHKQDRGEKKLLKCNDCEKIFSKISTLTLHQRIHTGEKPYECIECGKAFSQSAHLAQHQRIHTGEKPFECTECGKAFSQNAHLVQHQRVHTGEKPYQCKQCNKAFSQLAHLAQHQRVHTGEKPYECIECGKAFSDCSSLAHHRRIHTGKRPYECIDCGKAFRQNASLIRHRRYYHTGEKPFDCIDCGKAFTDHIGLIQHKRTHTGERPYKCNVCGKAFSHGSSLTVHQRIHTGEKPYECNICEKAFSHRGSLTLHQRVHTGEKPYECKECGKAFRQSTHLAHHQRIHTGEKPYECKECSKTFSQNAHLAQHQKIHTGEKPYECKECGKAFSQIAHLVQHQRVHTGEKPYECIECGKAFSDGSYLVQHQRLHSGKRPYECLECGKAFRQRASLICHQRCHTGEKPYECNVCGKAFSHRKSLTLHQRIHTGEKPYECKECSKAFSQVAHLTLHKRIHTGERPYECKECGKAFRQSVHLAHHQRIHTGESSVILSSALPYHQVL
Protein: Protein ROOT INITIATION DEFECTIVE 3 (Root initiation defective 3 protein) (WD-40 repeat-containing protein RID3) (Q9M3B4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in meristem development. Acts as negative regulator of the CUC-STM pathway in shoot apical meristem (SAM) neo-formation.
Interaction partners:
- Ribosome biogenesis protein WDR12 homolog
- Polynucleotide 5'-hydroxyl-kinase NOL9
- Notchless protein homolog
- Nuclear/nucleolar GTPase 2
- Ribosome biogenesis protein BOP1 homolog
- ERBB-3 BINDING PROTEIN 1
- Periodic tryptophan protein 2
- Chlorophyll synthase, chloroplastic
- ARM repeat superfamily protein
- Rix1 complex component
Sequence:
MEITVIASSSIDEGIGSWDLKTGTEQLQFKPCASPAHGLTAVGEKFLASSQLSARNTSGSIFYWSWTKPQAEVKSYPVEPIKALAANNEGTYLVGGGISGDIYLWEVATGKLLKKWHGHYRSVTCLVFSGDDSLLVSGSQDGSIRVWSLIRLFDDFQRQQGNTLYEHNFNEHTMSVTDIVIDYGGCNAVIISSSEDRTCKVWSLSRGKLLKNIIFPSVINALALDPGGCVFYAGARDSKIYIGAINATSEYGTQVLGSVSEKGKAITCLAYCADGNLLISGSEDGVVCVWDPKSLRHVRTLIHAKGSRKGPVNNIQIVRKTIVANSNKTQVSWKSRGALIPPPLEKYERPVEDTMDGIVTVDPPPFSDVPVYSSFLSADLIDEQVKELQQQGSAATEMEMERLKLEYKRSLQMNEQWQKNYENLLQVVMEEEQIGGTN
Protein: Multiple stress resistance protein BhsA (Copper-induced outer membrane component) (P0AB40)
Organism: Escherichia coli (strain K12)
Function: Reduces the permeability of the outer membrane to copper. Seems to be involved in the regulation of biofilm formation. May decrease biofilm formation by repressing cell-cell interaction and cell surface interaction.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:22089859}.
Interaction partners:
- HTH-type transcriptional repressor ComR
Sequence:
MKNVKTLIAAAILSSMSFASFAAVEVQSTPEGQQKVGTISANAGTNLGSLEEQLAQKADEMGAKSFRITSVTGPNTLHGTAVIYK
Protein: LP13067p (Omega, isoform E (EC 3.4.14.1, EC 3.4.14.2, EC 3.4.14.4, EC 3.4.14.5)) (Q29R16)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSAAGWLDMNAALQNLDSPPETVKKARTKRRSSYAGRTTATAGVHGRGSIGTISSGIIKSFRERFLSNSSGDSGKYRKLRQRDAESGRMEASGSSSSGENEDPSSSSSVEDLFANEAERRNWHRKTSEKRRRNARKKNLMHTKEKKRRVRIILTVVTTVIAVALLATALVFILRTDEKDADDSDSNSNNAIDLEDVLSGQLYAKRFNGSWSNGNSLIYKENTSIMEFDAKTGERSILLEDAQHYVLYEKSADGEFLLLAKNYKKNFRYSFLAEYDLYNLNTKEFIQLTIQNEQHYLSMVQWSPVGNALVINYDRNLYYKESALAQEIALTSDEQAGILNGIPDWVYEEEVFSSNVATWFNPSGTQLAFIKFDDSSTHLINFPYYGDAGDLRYQYPLHQVIAYPKAGSSNPRVELVMVDLKRAVAGGDFVTVMPVPSALNTETDYIVTVVSWVDDDNVLSIWMNRIQNAAYVVTFDGLNRKVIYSAESKTGWVDLYTAPFRNRNGSRLAFVLPHNNYKHVQLLSSTVASSEPQALEPLTEGKYVVDSILHWDGKNDIIFYTANTEDHPEQLHLYAIRALAKQSPKCLTCNLIKSGDVQQTYFSATFNDNNHIVITSLGPGIPTTHIYEWKYENSQVVISKVLDWETNESLRAKLKGVALPSHKILTVDIDGGFQAKVLLQLPPNLDTSGATKYPMLVDVYGGPDSYSVTNKWMVDWGTYLSSNQSVIYAKIDGRGSGLRGESLLHAIYLKLGTVEISDQINVTQKLSTLFNYIDPDHVGIWGWSYGGYAAAMALANDEAKVFKCAASIAPVTDWAYYDSIYTERYMGLPNTNELGYANSRLSTMAVKLRGKKYLLVHGTLDDNVHYQQAMILAKNLERQDILFKQISYADEDHGLSNVRPHLYHSLDRFFGECFASSRLMKSAK
Protein: Mitochondrial 2-oxodicarboxylate carrier 2 (Q99297)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transports C5-C7 oxodicarboxylates across the inner membranes of mitochondria. Can transport 2-oxoadipate, 2-oxoglutarate, adipate, glutarate, 2-oxopimelate, oxaloacetate, citrate and malate. The main physiological role is probably to supply 2-oxoadipate and 2-oxoglutarate from the mitochondrial matrix to the cytosol where they are used in the biosynthesis of lysine and glutamate, respectively, and in lysine catabolism.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Mitochondrial 2-oxodicarboxylate carrier 1
Sequence:
MSSDSNAKPLPFIYQFISGAVAGISELTVMYPLDVVKTRFQLEVTTPTAAAVGKQVERYNGVIDCLKKIVKKEGFSRLYRGISSPMLMEAPKRATKFACNDQYQKIFKNLFNTNETTQKISIAAGASAGMTEAAVIVPFELIKIRMQDVKSSYLGPMDCLKKTIKNEGIMGLYKGIESTMWRNALWNGGYFGVIYQVRNSMPVAKTKGQKTRNDLIAGAIGGTVGTMLNTPFDVVKSRIQSVDAVSSAVKKYNWCLPSLLVIYREEGFRALYKGFVPKVCRLAPGGSLMLVVFTGMMNFFRDLKYGH
Protein: DZF domain-containing protein (E9RKC7)
Organism: Caenorhabditis elegans
Interaction partners:
- DZF domain-containing protein
- DRBM domain-containing protein
Sequence:
MYGGYQGAYGAYGNQQAASQPYQQQGQQNYYPGVNPYAANYGYAAAQLPPPPPPPPVADPYAGQFQTFPSQATKIAPNPYFKKPQNQQQQGYDAAVYNYAQQNTPKNWKHGGGGRQGRQGSGDNKQYYCEVCKISCAGGITYKEHLEGQRHKKKEAMAKQGIPSTSLAKNKLSYRCDLCDVTCTGQDTYSAHVRGGKHLKTAQLHKKLGKPVPEDVPTIIAPGADGPTETKAKPKWHQQALPGGKIVIGINTVNFVGGTKLNSTGQLEEKKREVAAAVSSVGRKTGGAAATTTIEVEDEKLRAMIAAEEVQPVGEEHVTEERDATGKLVQFHCKLCDCKFSDPNAKEIHIKGRRHRVSYRQKIDPTLVVDVKPSNKRSQEKRKNQLPAVHEPPSFMKTPWFAPPAPEGREFNIVDDRTINEKYAGLNPGVEFISNVDRLISDINESLKYVSDKIERDVRKIPEDVVELPTTTTTTEQPPRTVLGCSRVGIIAKGTFIKGDRCAEVVLTCTPVPTSGLVEQIRRLFGESTTSLTIEPDPESPSSLIVTANYFPNMKCRILITSAVVRKDDDSIVTGCAADKDLCIYALASIRNTKWYDSHCQYLNSCQSVIRLLRDLRNKYPEVACLDDYKMELIVSNIIDSSPMSLGLSDAFKRIVEALASGYLYSAILSDPCETSRPNVLDALTDEQKHSLTALAQNFVRQIAFNQIHEILGIDRLQDTIDLPEDAPMLKRPLESNENAENAENLDDSPVSKKEKLDEEPADI
Protein: TATA box-binding protein-associated factor RNA polymerase I subunit B (TATA box-binding protein-associated factor 1B) (TBP-associated factor 1B) (Q9VH20)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- GEO04452p1
- LD41005p
- DNA-directed RNA polymerase I subunit RPA2
Sequence:
MEEVLETMQLENMHCDVCEGTTFQEREGFYYCVECGTQKDQIRAVDITAEDNFDDTAAGRYTARTIRQKKDTEKEDEDDITSWEFYNYVLRGFLQELLNMGAKPELKLMTLQVWAAYLDSMEVAFSKSNKTGLPKLNVRALPIDARIIYNHKTFKKGKKGKKSTLTGDPNDERAKFRLWNRTKRNLDASGYRSHGGASESEGEQSLHLQWSMRARKSLKRHMPLKHLDKHSRDSKGSMSCHSLRPRVKQLHNFDRNIYCLNIIKLYVVLGIALNMVEDDIQLSDLLRFIDEEHLTKRCMLNYLPGNVAAKGKALLKDMELSKMKDKVTNKLLRVNIACMSRFINLSEYQKPNLHSLAERYILELALPPRLLKYVNSLLDLHPPTFFNAMTVHPYPRYEARTMAYILYAMKLLFGLDDLKERNISESAAKINEKLLEVGGDEAPLLFVFTEWMEFVEMRKVIVSHYNQSFARRFGVSTRTGCQVDDILAKEWKEKEQGETFGWMQGSAAMKRQHENLTHIIETMLKDHFGESSKESMEKEHIEFQPSLTPAHSYFNRILLQVSRSDGAKMKITIPDHMKVDHSARNLDPFVLETTELSQYLSQHGLKLRVEELACQEDIQNVGIFRPLTIIRGDGREYRANTEIKTETWISELKRKEKRPDFRFTQPTGTYGARYLKRITMRDARRVQLEINNPFWDVTETPSFLLKLNDNEIPLDSLSSLQTFEEGTMDPLNIPLDLPRRNLEKILNPEGSDRASDQVASDINDEPPSPETLLLQVSNFDCWLLHGYMKRIRRHDKHELRQLFPCSFRWLLETCASTIGIVWEELYEELLIVEVMYHHSIRDWSNHRNYLCIQHNTQEKDIRTLARTYKELW
Protein: Epidermal growth factor-like protein 8 (EGF-like protein 8) (Vascular endothelial statin-2) (VE-statin-2) (Q99944)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- G-protein-signaling modulator 3
- Lysosomal thioesterase PPT2
Sequence:
MGSRAELCTLLGGFSFLLLLIPGEGAKGGSLRESQGVCSKQTLVVPLHYNESYSQPVYKPYLTLCAGRRICSTYRTMYRVMWREVRREVQQTHAVCCQGWKKRHPGALTCEAICAKPCLNGGVCVRPDQCECAPGWGGKHCHVDVDECRTSITLCSHHCFNTAGSFTCGCPHDLVLGVDGRTCMEGSPEPPTSASILSVAVREAEKDERALKQEIHELRGRLERLEQWAGQAGAWVRAVLPVPPEELQPEQVAELWGRGDRIESLSDQVLLLEERLGACSCEDNSLGLGVNHR
Protein: Uncharacterized protein (Q384T2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTQLVREVIFSSVVWTAGDFLAQFLDVHIDAARRRAAGEPKSDHPSGKQMIIMVDQQRLGFAAVFGAIVAPGMIHFRGILARVVGSAHGNTLAAFSILTAQQLFATPLMLLFYHNSATMVRGGFTDPSFLSAHETSVIARLRGRYDAMAVERRIAIDILPQTLLASWCVFLPQVLHSYMRGRSLRSRYAACLHIPWLAYVSYVQSTMLL
Protein: IP15284p (RIC3 acetylcholine receptor chaperone, isoform E) (Q058V3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGCCDVVLDREQFLNATKKDTVEPFGPHLYRKQINVYTGEISLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLGWREHQTRAATATAAAKKPAAKDTEKELYNASVSATEVASSLSASLKSHQQLKEAEQLMEIEKLRQKLESTERAMAQLVAEMNTDQYEAKKNDNEKTREQPLDKQNLSNGHASSTDQNPEQETVAKGARKRRDLSAEQELTSKLEDNLPEPQSIYLEGALAHESQILVADSQIKREEVYDSELNGSAEEPAIILSSRMTLSLINLDANQQNGNAGKSAVESPLADDIEIIGHDEQ