wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized helicase-like protein YBL111C (Q3E7Y5)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative uncharacterized helicase-like protein YBL112C
- Uncharacterized protein YBL113C
- Putative UPF0479 protein YBL113W-A
- Putative uncharacterized protein YBL109W
Sequence:
MKVSDRRKFEKANFDEFESALNNKNDLVHCPSITLFESIPTEVRSFYEDEKSGLIKVVKFRTGAMDRKRSFEKIVVSVMVGKNVQKFLTFVEDEPDFQGGPIPSKYLIPKKINLMVYTLFQVHTLKFNRKDYDTLSLFYLNRGYYNELSFRVLERCYEIASARPNDSSTMRTFTDFVSGTPIVRSLQKSTIRKYGYNLAPYMFLLLHVDELSIFSAYQASLPGEKKVDTERLKRDLCPRKPTEIKYFSQICNDMMNKKDRLGDVLATAQRIRRRYNKNGSSEPRLKTLDGLTSERWIQWLGLESDYHCSFSSTRNAEDVVAGEAASSDHDQKISRVTRKRPREPKSTNDILVAGRKLFGSSFEFRDLHQLRLCHEIYMADTPSVAVQAPPGYGKTELFHLPLIALASKGDVKYVSFLFVPYTVLLANCMIRLGRRGCLNVAPVRNFIEEGCDGVTDLYVGIYDDLASTNFTDRIAAWENIVECTFRTNNVKLGYLIVDEFHNFETEVYRQSQFGGITNLDFDAFEKAIFLSGTAPEAVADAALQRIGLTGLAKKSMDINELKRSEDLSRGLSSYPTRMFNLIKEKSEVPLGHVHKIWKKVESQPEEALKLLLALFEIEPESKAIVVASTTNEVEELACSWRKYFRVVWIHGKLGCCRKGVSHKGVCH
Protein: Protein Dicer (Cell cycle control protein dcr1) (RNA interference pathway protein dcr1) [Includes: Endoribonuclease dcr1 (EC 3.1.26.-); ATP-dependent helicase dcr1 (EC 3.6.4.-)] (Q09884)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for G1 arrest and mating in response to nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints occurs downstream of dcr1. Required, indirectly, for regulated hyperphosphorylation of cdc2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21847092}.
Interaction partners:
- Protein argonaute
- RNA-dependent RNA polymerase 1
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Chromatin-associated protein swi6
- RNA-induced transcriptional silencing complex protein tas3
- Chromo domain-containing protein 1
- 3'-5' exonuclease eri1
- Uncharacterized protein C328.01c
- Histone H3.1/H3.2
- Histone deacetylase clr3
Sequence:
MDISSFLLPQLLRKYQQDVYNIASKQNTLLVMRTGAGKTLLAVKLIKQKLEEQILIQESNLEHKKISVFLVNKVPLVFQQAEYIRSQLPAKVGMFYGELSIEMSEQLLTNIILKYNVIVITADLFYLFLARGFLSINDLNLIIFDECHHAIGNDAYARIMNDFYHRAKAVLSKKHFTLPRIFGMTASPFTGKKGNLYHRLYQWEQLFDSKAHVVSENELADYFCLPEESYVMYSNKLVVPPSDSIIKKCEETLQGCKLISRAVKTALAETIDMGLWFGEQVWLYLVDFVETKRLKKKALGKQLSDDEELAIDRLKIFVEDWKNNKYSDNGPRIPVFDSTDVTDKVFKLLELLKATYRKSDSVRTVIFVERKATAFTLSLFMKTLNLPNIRAHSFIGHGPSDQGEFSMTFRRQKDTLHKFKTGKYNVLIATAVAEEGIDVPSCNLVIRFNICRTVTQYVQSRGRARAMASKFLIFLNTEELLIHERILHEEKNLKFALSELSNSNIFDSLVCEERERVTDDIVYEVGETGALLTGLYAVSLLYNFCNTLSRDVYTRYYPTFTAQPCLSGWYCFEVELPKACKVPAAQGSPAKSIRKAKQNAAFIMCLDLIRMGLIDKHLKPLDFRRKIADLETLEEDELKDEGYIETYERYVPKSWMKVPEDITRCFVSLLYTDANEGDNHIFHPLVFVQAHSFPKIDSFILNSTVGPRVKIVLETIEDSFKIDSHLLELLKKSTRYLLQFGLSTSLEQQIPTPYWLAPLNLSCTDYRFLENLIDVDTIQNFFKLPEPVQNVTDLQSDTVLLVNPQSIYEQYAFEGFVNSEFMIPAKKKDKAPSALCKKLPLRLNYSLWGNRAKSIPKSQQVRSFYINDLYILPVSRHLKNSALLIPSILYHIENLLVASSFIEHFRLDCKIDTACQALTSAESQLNFDYDRLEFYGDCFLKLGASITVFLKFPDTQEYQLHFNRKKIISNCNLYKVAIDCELPKYALSTPLEIRHWCPYGFQKSTSDKCRYAVLQKLSVKRIADMVEASIGACLLDSGLDSALKICKSLSVGLLDISNWDEWNNYFDLNTYADSLRNVQFPYSSYIEETIGYSFKNKKLLHLAFIHPSMMSQQGIYENYQQLEFLGDAVLDYIIVQYLYKKYPNATSGELTDYKSFYVCNKSLSYIGFVLNLHKYIQHESAAMCDAIFEYQELIEAFRETASENPWFWFEIDSPKFISDTLEAMICAIFLDSGFSLQSLQFVLPLFLNSLGDATHTKAKGDIEHKVYQLLKDQGCEDFGTKCVIEEVKSSHKTLLNTELHLTKYYGFSFFRHGNIVAYGKSRKVANAKYIMKQRLLKLLEDKSNLLLYSCNCKFSKKKPSDEQIKGDGKVKSLT
Protein: Histone H3.1 (Q6LED0)
Organism: Rattus norvegicus (Rat)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H4
- Histone-arginine methyltransferase CARM1
- Histone H2B
- Histone acetyltransferase type B catalytic subunit
- Histone deacetylase 1
- WD repeat-containing protein 5
- Lysine-specific demethylase 6B demethylase 6B)
- DNA
- DNA
- Histone H2B type 1-A
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Cell death protein 4 (P30429)
Organism: Caenorhabditis elegans
Function: Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development. During oogenesis, required for germline apoptosis downstream of ced-9 and upstream of ced-3 but independently of egl-1. May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway. Regulates CEP neuron apoptosis in response to high Al(3+) levels. During male tail morphogenesis, promotes apoptosis of the tail-spike cell upstream of ced-3 but independently of egl-1 and ced-9. May play a role in sex-specific cell apoptosis, probably by promoting ced-3-mediated cleavage of sex-determining protein fem-1. During larval development, required for the elimination of transient presynaptic components downstream of egl-1 and ced-9 and upstream of ced-3 apoptotic pathway. Downstream of calreticulin crt-1 and upstream of ced-3 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy. Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), and probably upstream of ced-3, regulates temporal cell fate patterning during larval development. May play a role in resistance to S.typhimurium-mediated infection.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}. Note=In non cell death induced cells, ced-9 is required for mitochondrial localization. Perinuclear in cell death induced cells. {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}.
Interaction partners:
- Cell death protein 3
- Apoptosis regulator ced-9
- Baculoviral IAP repeat-containing protein bir-2
- Chromosomal passenger complex protein bir-1
- Programmed cell death activator egl-1
- Putative inactive caspase B
- Ran GTPase-activating protein 2
- Non-catalytic caspase homolog csp-3
- Cell death abnormality protein 1
- Calreticulin
Sequence:
MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQSHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGRAGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLKSEDDLLNFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDECYDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMALQRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDHIIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQKFYDSLKNFACC
Protein: Transmembrane protein (Q9C8L8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5
- Vacuolar protein sorting-associated protein 32 homolog 2
- Vacuolar protein sorting-associated protein 20 homolog 1
- Vacuolar protein sorting-associated protein 32 homolog 1
- Vacuolar protein sorting-associated protein 20 homolog 2
- ESCRT-related protein CHMP1B
- ESCRT-related protein CHMP1A
- Putative vacuolar protein sorting-associated protein 24 homolog 2
- Vacuolar protein sorting-associated protein 24 homolog 1
- Protein LSD1
Sequence:
MEPVVNVIIILGACVIFVLTVICCISHRKKEPLFQPRDLENGLAGIKDGGLVVLTGTAVVAAGVTTERSGGCGGGGDGGGCDGDAGGGDGGGCGGCGGCGG
Protein: Uncharacterized protein YMR315W (Q04869)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Large ribosomal subunit protein eL32
- Uncharacterized protein YBR053C
Sequence:
MSPLNVGIVGTGIFARDRHLPSYQEFPDKFKVIAAFNRHKAKALDFAKVADIPENKVYDNLDEILNDPHVDYIDALLPAQFNADIVEKAVKAGKPVILEKPIAANLDQAKEIVKIAESTPLPVGVAENWLYLPCIKIAKEQIEKIGPVVAFTHNSTGPFVTQNKYLTTTWRQKPEHIGGFLSDGGVHQLALVISLLGEFGSVSALTRQVRERSGADDIVFATVQLKNKEVIGSFTYGSAFGATEKSVFLKVYGKNGTVTVDLSDKKDPVVKVKLGGSAEDNGDEQIFKVDNDESFGVNAEFLNFHEAVSKKDKSLYLGTPRTAFHHLACVDAFLKSSAKNGDYVKIEQP
Protein: Alpha-galactosidase Mel36A (LaMel36A) (EC 3.2.1.22) (G1UB44)
Organism: Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Function: Hydrolyzes the short-chain alpha-galactosaccharide raffinose.
Interaction partners:
- Beta-galactosidase large subunit
- beta-fructofuranosidase
- Sucrose-6-phosphate hydrolase
- Sucrose phosphorylase
- Beta-galactosidase small subunit
- ABC transporter sugar binding protein
- Beta-galactosidase
- Beta-galactosidase LacZ
- Oligo-1,6-glucosidase
- Galactose-1-epimerase
Sequence:
MTSNLIKFDDQNKVFHLHNKQISYLLSIEDGGTLSHLYFGGAVKNYNNQLKYPRLDRGFSGNLPESLDRTFSRDSLPKEYSSAGEMDFHTPATIVRNPDGSNALFLAYKSYKIEDGKPDLKGLPHSWTKEDDEAQTLIVTLEDKVSKLEYDLLYTIYRDRPVIVRSVQVHNHGEEAVYLEKVASMQMDYVDKDFEVITLPGAHANERRVQRENIGQGIKVFSSYRGTSSHQMNPFMALVDHDTNEFMGEAYGFALAYSGNHKFEVERDQFGQIHVNTGINDYNFKWKLNPNEEFQTPEVLMVYSDQGLNKMSQAFHSLIHERIMRSKFKDQIRPVLVNNWEATYFDFNEDKLKTIVDKAKKLGLEMFVLDDGWFGHRDDDNSSLGDWKVYKKKFPNGLGHFADYVHEQGLKFGLWFEPEMISYESNLYKEHPDYLMHVPGRKPCPSRNQYVLELGRKEVRDNIFEQMVKILDSKKIDYIKWDMNRSLSDIYESDLPADQQGEAYHRYVLGYYDLLNKLVTRYPDILFEGCSGGGGRFDVGQAYYTPQIWASDNTDAIERLKIQYGTSLVYPQSMMTSHVSVSPNEQNGRITPFNTRGAVAMWGDLGYELDLTKMSDEESDQVVKQVTEYKKIREVTQFGTLYRLKASASNQCAWMMVDSNKNEAVVTVVNVMAHAQPYCTKTKLAGLDPDKRYKNLETDEVFGGDELMHLGFYDPIERGDFKAKMYHFKAIN
Protein: Transmembrane inner ear expressed protein isoform b (Transmembrane inner ear isoform a) (D2ITC5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MRRGRRRGKMAMEGPGNQPPSLVPLLMSVTAVLISHHFFNAAAQIPDPELLPTDPPKKPDPVTSETVVFWGLRLWQVVGIFSMFILAIIITLCCIFKCRIPRTKKEIEARHAQRLAAKKYANTLETVPPLNELTEVPGAAKVEVKEEVPTVAGKVDGEKEKKKKEKESKKEGKGAKEGKEEEKEEPAKKKGEKGEKGEKGAPKKEASDGGKGKKGGEKAEEKGGAKKPAKK
Protein: Large ribosomal subunit protein uL22A (60S ribosomal protein L17-A) (O14339)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL18A
- Elongation factor 3
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL29
Sequence:
MVRYSASPALETKCAKARGAYLRTHFKNSREVAFTINGMSLKKAFIFLDNVKEHKQAVPFRRFNGGVGRTAQGKEFGVTQARWPVKSVKFFYDLLKNAEANAEAKGLDMDKLIIKHVQVNAAPKQRRRTYRAHGRVTAYLSSPSHIEIIVAEEEEAVPKANDTVSRVSLKQGAKARNLAARKAITAA
Protein: Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CDw127) (CD antigen CD127) (P16871)
Organism: Homo sapiens (Human)
Function: Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP).
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:31748347}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted.
Interaction partners:
- Thymic stromal lymphopoietin
- Interleukin-7
- Cytokine receptor common subunit gamma
- Cytokine receptor-like factor 2
- Tyrosine-protein kinase JAK1
- Tyrosine-protein kinase JAK3
- Interleukin-15
- Interleukin-2
- T-cell surface glycoprotein CD4
- Interleukin-4
Sequence:
MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ
Protein: DNA repair protein complementing XP-A cells homolog (Xeroderma pigmentosum group A-complementing protein homolog) (P28518)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- DNA excision repair protein ERCC-1
- General transcription and DNA repair factor IIH helicase subunit XPD
- DNA repair endonuclease XPF
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 1
- Replication protein A 70 kDa DNA-binding subunit
- CG9273 protein
- Probable DNA mismatch repair protein Msh6
- Crossover junction endonuclease MUS81
- ATP-dependent DNA helicase Q4
Sequence:
MSAEVSTNESAPPAEKKSKLTNAQKARIERNQAKAQKLREAKLVSHPFKELASNKEGGTHPEAALSQGSSVIKVQGTKYIDSGGGFLLEQPVMPTGVGPAGLNKSGEEAPPILDDAIAIPVQYEECLECGDMFADSYLFNNFGHSVCDKCRDKDERYALITRTEAKAEYLLKDCDFDKREPKLRYISRKNPHNVRWGEMKLYLHLQIHQRALEVWGSEEELVRQHEAREDKREEGKARKYNKKMKQLRMEVRSSIYTKKTHEVHEHEFGPDTYDEEEDTYTHTCITCPYSETYEKM
Protein: Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR) (zfpsr) (Q6PFM0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as u2af2/u2af65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of u2af2/u2af65, affecting the pre-mRNA splicing activity of u2af2/u2af65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation. Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. In collaboration with brd4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. Demethylates other arginine methylated-proteins such as esr1. Has no histone lysine demethylase activity (By similarity). Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6NYC1}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6NYC1}. Cytoplasm {ECO:0000250|UniProtKB:Q6NYC1}.
Interaction partners:
- Histone H3.2
- Histone H3
- Bromodomain-containing protein 4
- Lysine-specific demethylase 8
- Bifunctional lysine-specific demethylase and histidyl-hydroxylase
- tRNA wybutosine-synthesizing protein 5
Sequence:
MNHKSKKRIKEAKRSARPELKDSSDWTKHEYCKSFDLSHRSVKDNVERADVQRLSPEEFIQRFEKPYKPVVLLNVEDSWPAREKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYVEYLESTHDDSPLYIFDSSFGEHAKRRKLLEDYQVPLFFRDDLFQFAGEKRRPPYRWFVMGPARSGTGIHIDPLGTSAWNALVQGHKRWCLFPTHTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQQSTWPDEFRPLEILQRPGETVFVPGGWWHVVLNLDTTIAVTQNFASTTNFPIVWHKTVRGRPKLSRKWYRILKQERPDIAAIADKVDLQESTGIASDSSSDSSSSSSSSSSDSDSEADSGSEGDAMTHRRKKRRTGGMMGNGDITSQDDCASKERSSSR
Protein: thioredoxin-disulfide reductase (EC 1.8.1.9) (A0A182DWF2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEDQAGQRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCCG
Protein: 2-oxoglutarate dehydrogenase subunit, putative (Q387A7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoyl dehydrogenase
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MMRRAFTRGACAAQSFSMVRFYTDAKTVRQPHRYDQAITAENEVYIEQLLKQYEQNPCEVDGSWIPILEKLRSGSPDAPLVQDFTRPVKDAPKSDSERRQSMGITWMVTAYERYGHHYAKVNPLRSEQDVESDRRDLLNLHYSNFGFTDQDLTKVFPVDIGGGLKEAFGENVKEATLQQIVEKLQMMYCGSIGFEFLLTEGDDVRHWFHKEILKTFEPLSKEERIHILDDVVKSCGFETFIQLKYGTQLRFGLDGAEALVPAVIALMQEASDLGVTSFVQGMPHRGRLNLLANVKVKPLTDILAEFEGKTHRNAIARLGDNKYHLGADRQIELRNGKVINFDLLCNPSHLEAMNPLVLGKARARMVVEKDSECVRTLPIIAHGDAAISGLGMGHETMGLWDLDNYRVGGTVHIITNNQVGFTTDSVDARRAKYCSDISKIHATPVLHVNSNDVEACVRAARIAARFRQTFHRDIIIDLIGYRRNGHNEADFPDFTQPQMYQIVRSLRPLVDLYSDTLVEEGVLTKEDVKAKKKEYESRLREAYETAQSCPEYTKVIPNLREDAGNASEGYDLAAEKEANLPKAVETGVDIEVLRRVGLHVTTIPSEVKKVHPVVERTYAARKKAIESGEGAEWCLAEMLAFGATALEGTHVRLAGEDVERGTFTQRHAAVTDLETNKKYIPLCSLSEDQALVTICNSSLSEFGVSGFELGYNAVNPHTLGMWEAQFGDFANGAQVIFDQFLCCGEEKWNAKYSLVLSLPHGYSGAGPEHSSARIERYLQLCSDTDVVPHNFRRGCPLQLLEVRIQRFNWQVCYPSTPANYFHVLRRQVRRGDPKPLVVFFSKARLRAPNVSSLSEMSTGTSFKPVIDTAVNDEVIARKVLFCTGQIESIVDDRRKKLQAEKPGVHDDVVLVKLEQLSPFPWEQVADVLEKYHSRNPNVQFAWLQEEPKNMGSWAYVRPRLQRLLRHLGMAGSSDFLPYVGRVTAASPSTGYATVHAEEEAEIIRQALA
Protein: Anti-Muellerian hormone type-2 receptor (EC 2.7.11.30) (Anti-Muellerian hormone type II receptor) (AMH type II receptor) (MIS type II receptor) (MISRII) (MRII) (Q8K592)
Organism: Mus musculus (Mouse)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Muellerian-inhibiting factor
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein receptor type-1A
- Activin receptor type-1
- Growth/differentiation factor 6
- Bone morphogenetic protein 6
- Bone morphogenetic protein 4
- Bone morphogenetic protein 7
- Growth/differentiation factor 5
- Growth/differentiation factor 7
Sequence:
MLGTLGLWTLLPAAAQVSPNRRTCVFFEAPGVRGSTKTLGEMVDAGPGPPKGIRCLYSHCCFGIWNLTHGRAQVEMQGCRDSDEPGCESLHCDPVPRAHPNPSSTLFTCSCGTDFCNANYSHLPPSGNQGAPGPQEPQATPGGPVWMALLLLGMFLVLLLSSIILALLQRKACRVQGGSDPEPGSGGDCSEELPELAELRFSQVIQEGGHAVVWAGRLQGEMVAIKAFPPRAVAQFRAERAVYQLLGLQHDHIVRFITAGQGGPGPLPSGPLLVLELYPKGSLCHYLTQYTSDWGSSLRMALSLAEGLAFLHEERWQDGQYKPGIAHRDLSSQNVLIREDRSCAIGDLGLALVLPGLAQPPALAPTQPRGPAAILEAGTQRYMAPELLDKTLDLQDWGTALQRADVYSLALLLWEILSRCSDLRPDHRPPPFQLAYEAELGSNPSACELWALAVEERKRPNIPSTWSCSATDPRGLRELLEDCWDADPEARLTAECVQQRLAALAYPHGASSFPESPQGCPENCLSAPASAVFPCRPQQSSCLLSVQQGPGSRSPDPVGDTVQVYVNE
Protein: Izumo sperm-egg fusion protein 3 (A6PWV3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:34114279}.
Interaction partners:
- Izumo sperm-egg fusion protein 2
- Izumo sperm-egg fusion protein 4
- Izumo sperm-egg fusion protein 1
- CD9 antigen
Sequence:
MGDLWVLLFSSLSLAAFHGVRGCLECDPKFTEDVRTLLGNLVPLEVPDRNQLLDRQHKEITHISSKVSHKDKMLRLLAVRNVIKLREWLKDEFYRLGNETWKGVFIIQGNLLEIRQNLEKKLTQIIKNFSEVACSEDCIVIEGPVLDCWNCLRMTTRCFKGDYCQDEDPKTAENREISLYLIFIAEAVILASAVLLFHVCISHRRKMKAIRRTLKTYLEKKLEELVEMIYKDDGEKNLEFGRSNSNSLTGEPTCAESEMQTGT
Protein: ABC transporter G family member 19 (ABC transporter ABCG.19) (Q8T675)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ABC transporter C family member 13
Sequence:
MKEFELNEYSFQEVENLNINTPNNNNNFGVVGDDFQLNSPDIQNSENQFKYIANELETDSKQYLSNLDAENNHNENDEDFKLRKYFENSQRVALGNGQKPKKMGVSVRNLTVVGVGADQSVISDLSTPIFKILNLFKPSTWKEKGSTFDILHDITLFNRDGGMLLVLGRPGSGCSTLLRLISNQRGSYVEVKGDITYGGIPAKEWKRYQGESIYTPEEDTHHPTLTVRQTLDFALKCKTIHNRLPDEKKRTYRKRIFDLLLGMFGIVHQADTIVGNEFIRGLSGGERKRLTITEAMVSSASITCYDCSTRGLDAASALDYAKSIRIMSDTLDKTTIASFYQASDSIYNLFDNVAVIEKGRLIYFGPGNKAKQYFIDLGFDCEPRKSTPDFLTGVTNPQERIIRQGFEGRVPETFADFEAAWRNSSMYRDMLEEQKEYERKIEIEQPAVDFIQEVKAEKSKTTSKRSIYTTSFLTQVKALIVRNFQIIWGDKLSLGSRYLSVFTQSFVYGSIFYNLETNINGLFTRGGTLFSVILFNALLCECEMPLTFGQRGILQKQHSYAMYRPSALHIAQIVTDIPLTIIQVFLFSIVVYFMFGLQYDAGKFFIFCFTLVGATLATTNLFRMFGNFSPSLYISQNVMNIFIISMITYTGYTIPKPKMHPWFSWFYWCNPFSYAFKALMANEFGDLSFDCQDTAIPSDPNKIIVYDNSYRICASPGASMGNLTVSGSKYIEESFHFRSDDLTQNVFILYLWWILYIVLNMFAMEYFDWTGGGYSHKVYKKGKAPKMNDVEEEKKQNQIVANATSKMKDTLKMRGGIFTWQNINYTVPVKGGKRLLLDNVEGWIKPGQMTALMGSSGAGKTTLLDVLAKRKTMGEVQGKCFLNGKPLEIDFERITGYVEQMDVHNPGLTVREALRFSAKLRQEPSVLLEEKFDYVEHVLEMMEMKHLGDALIGTLETGVGISVEERKRLTIGVELVAKPHILFLDEPTSGLDAQSSYNIVKFIRKLADAGMPLVCTIHQPSSVLFEHFDRILLLAKGGKTVYFGDIGEGSKTLTSYFERYGVRPCTESENPAEYILEATGAGVHGKSDVNWSETWKQSPELQEIERELAALEAQGPSSTEDHGKPREFATPIWYQTIEVYKRLNIIWWRDPFYTYGSFIQASMAGLIMGFTFWSLKGSSSDMSQRVFFIFETLILGILLIFVVLPQFIMQQEYFKRDFASKFYSWFPFAISIVAVEIPIVIISGTFFFFCSFWTAGLYTKFNEINFYFWFILILYLLFCVSFGQAVSAISFNLFLAHTLIPLLIVFLFLFCGVMVIPSSIPTFWRGWVYHLNPCRYFMEGIVTNVLKHTDVKCTSEDFTHFTNPEAVNGVTCKQYFPISEPLTGYVEAINEGDESKCGYCLYNNGEEYYNTLGWSFDNRWRNLAILICFWIFNILMVITFVYITRKPRR
Protein: Transmembrane protein 135 N-terminal domain-containing protein (Q388J7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAEADCSPYGAKRDDRALVVSGLKRTVSTASRNALYAAAGRLAFGVVTGLLKSGLRTGVHKVFLREVLSADPLKWAFLSAGLSCFRLLKHIASKLCSHLSIPEKFSYVVAGFISVLPVMVMERGTRVELCLHVLVRALQVVGTSCVLPLFPKVFRDFEHYDIVVMCLSASQILYGFVFAPYTMPPSYLSFLSKTSMLDERVVRSYAGLTRHQISPELVELCVERGRRLPHDPSEHLSVCCSYAHEGLTCNQFCFMLFCKNMVQVGLPLYLPLKVATIVVQYKKLIRKPLQSLCRAARSVFFSTLFLALYSVCSTRYACLAAQRNIRGGLLFAIASSLAGISTLIEPKGRRADLAFYCLIYAIRSFVLTQCQFGRLPYPRQSSIFMLYLFSVVLLIFQYDYDPDKLDHRSRYVISRIAGGEILTPTEQYE