wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein eS25A (40S ribosomal protein S25-A) (RP45) (S31) (YS23) (Q3E792)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein uS11B
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein eS27A
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein eS26A
- Small ribosomal subunit protein uS3
Sequence:
MPPKQQLSKAAKAAAALAGGKKSKKKWSKKSMKDRAQHAVILDQEKYDRILKEVPTYRYVSVSVLVDRLKIGGSLARIALRHLEKEGIIKPISKHSKQAIYTRATASE
Protein: GM03621p (Q8MQK8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LLRNFNLFRLESTYEIRQDIEDAVSRMLPWKSEDGDVVFGGWARMALPIASFAVVEVAKPHLGEKKPSRVRADVGVTLSVRREIKAEWENLRKHDVCFLITVKPTQPYGTKYKHREPFVPQVGLVSVRGCEVEGMLDANGRVIEDGPEPRPQLQGENRCYRVWLDSNQYRLDMDDLQEGADDVYESFNILMRRKPKENNFKAVLETIRHLMNTECVVPPWLHDILLGYGDPGAAHYSNMPNQERSLEFNDTFMDYNHLEASFPQYNLKCEVPVENRQPPFRLIFEDVPIQKESDGEDPEEKPEEKLTKSILVQPYKYEARGPYPSDKPKQNSIRFTPTQVEAIRAGMQPGLTLVVGPPGTGKTDVAVQIISNIYHNHPNQRTLIVTHSNQALNQLFEKIMALDIDERHLLRLGHGEEALETEKDYSRYGRVNYVLAKRMDLLSQVQKLQEALGVSGDNAYTCETAGYFYLYNVMARWEKFQSQISVHKEEANAEKLRAEFEKEFPFGKFFADAPQPLFKGANYDELMDIACSNFRYISDIFNELEEFRAFELLRTGLDRSKYLLVKEAKIIAMTCTHAALKRKELVNLGFRYDNILMEESAQILEIETFIPLLLQNPLDGLNRLKRWIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRLVRLGVPTVDLDGQGRARASICSLYKWRYKKLEDLQHIFERDEYKQANPGFVHDYQLINVEDFKGVGESEPNPYFYQNLAEAEYIVAVYMYMRLLGYPAAKISILTTYNGQKHLIRDVINARCGNNPLIGWPHKITTVDKYQGQQNDYILISLVRTKAVGHLRDVRRLVVAMSRARLGLYVFGRVSLFKNCLELQQTFKLLTQRPLKLSLVPEDKFPTDRLASAAVASQDIKTVENMSEMAQFVYERYMAKMEELKGTLPSEEELEAMRNQLLQEDEESVPEASEEPPEKRAAKEEPLSKKKTTEAFKPTPILNEINVDDTEMGQREQIEEEATDQDKTQESAPAEES
Protein: Pseudouridine kinase (EC 2.7.1.83) (Q94AT3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of pseudouridine to pseudouridine 5'-phosphate (PsiMP). Catalyzes the first step in a pseudouridine degradation pathway. Acts together with the pseudouridine 5'-phosphate glycosidase PUMY in the peroxisome to prevent toxic pseudouridine monophosphate accumulation.
Subcellular location: Peroxisome {ECO:0000269|PubMed:31907295}.
Interaction partners:
- Pseudouridine-5'-phosphate glycosidase
- PfkB-like carbohydrate kinase family protein
- Fructokinase-like 1, chloroplastic
- Fructokinase-like 2, chloroplastic
- ARP protein
- Probable receptor-like protein kinase At3g17420
- Enoyl-CoA delta isomerase 1, peroxisomal
- 4-coumarate--CoA ligase-like 2
- Peroxisomal nicotinamide adenine dinucleotide carrier
- Lon protease homolog 2, peroxisomal
Sequence:
MEPVIIGALILDVHAKPSTTPISGTTVPGQVLFAPGGVARNVADCIFKLGITPFMIGTLGLDGPANVLLKEWKLSMKGILRREDISTPIVSLVYDTNGEVAAGVAGVDAVENFLTPEWIQRFEYNISSARLLMVDANLSSLALEASCKLAAESSVPVWFEPVSVTKSQRIASIAKYVTIVSPNQDELIAMANALCAKNLFHPFRSDENKLSIEDMFRALKPAILVLLKNGVKVVIVTLGSNGALLCSKGNPKKALNIDRKFLRSGEVFKRVQSVCSPNRFSELGSNRSPSLFAMHFPTIPAKVKKLTGAGDCLVGGTVASLSDGLDLIQSLAVGIASAKAAVESDDNVPPEFKLDLISGDAELVYNGAKMLMVHQSML
Protein: Radial spoke protein 3, putative (Q387D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
Sequence:
MQGQNQAAVDGTMAYTFQHPPQGFLHAQYRDPHSSVGRKQYANIMHDRRVYRGNTYAAVPMSTYARDEEERVVREANRRRKELQQRATSIKRRKELDAAQRKLATPPPVVGRQHIEVQTEEFLEELKDEVEVVQQETQTDPLLDRPATPPYVPVKSGRDAESQINEGDLFHFDDAVDPILDVMVGKTLEQAMLEVLQEEELELLRQQQLEFEQRRKEELLEAQRLEAREKRLFEEKERRKKQEIERIKREKATREKLQARQFAKMYLMNLENRVFARLQDEGWFRDRVLHEVEFDFFPWLMDQVAVELEKKQRARVLVDDLIRQVVAIQLNS
Protein: DNA mismatch repair protein MSH6 (AtMSH6) (MutS protein homolog 6) (O04716)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Forms the heterodimer MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. MutS alpha recognizes single base mismatches and trinucleotide insertion-deletion loops (IDL) in the DNA. Is involved in a UV-B-induced DNA damage response pathway.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein PMS1
- DNA mismatch repair protein MSH2
- DNA mismatch repair protein MLH3
- DNA mismatch repair protein MSH5
- Exonuclease 1
- Proliferating cell nuclear antigen 2
- Proliferating cellular nuclear antigen 1
- DNA mismatch repair protein MSH3
- Exonuclease 1
Sequence:
MAPSRRQISGRSPLVNQQRQITSFFGKSASSSSSPSPSPSPSLSNKKTPKSNNPNPKSPSPSPSPPKKTPKLNPNPSSNLPARSPSPGPDTPSPVQSKFKKPLLVIGQTPSPPQSVVITYGDEVVGKQVRVYWPLDKKWYDGSVTFYDKGEGKHVVEYEDGEEESLDLGKEKTEWVVGEKSGDRFNRLKRGASALRKVVTDSDDDVEMGNVEEDKSDGDDSSDEDWGKNVGKEVCESEEDDVELVDENEMDEEELVEEKDEETSKVNRVSKTDSRKRKTSEVTKSGGEKKSKTDTGTILKGFKASVVEPAKKIGQADRVVKGLEDNVLDGDALARFGARDSEKFRFLGVDRRDAKRRRPTDENYDPRTLYLPPDFVKKLTGGQRQWWEFKAKHMDKVVFFKMGKFYELFEMDAHVGAKELDIQYMKGEQPHCGFPEKNFSVNIEKLVRKGYRVLVVEQTETPDQLEQRRKETGSKDKVVKREVCAVVTKGTLTDGEMLLTNPDASYLMALTEGGESLTNPTAEHNFGVCLVDVATQKIILGQFKDDQDCSALSCLLSEMRPVEIIKPAKVLSYATERTIVRQTRNPLVNNLVPLSEFWDSEKTIYEVGIIYKRINCQPSSAYSSEGKILGDGSSFLPKMLSELATEDKNGSLALSALGGAIYYLRQAFLDESLLRFAKFESLPYCDFSNVNEKQHMVLDAAALENLEIFENSRNGGYSGTLYAQLNQCITASGKRLLKTWLARPLYNTELIKERQDAVAILRGENLPYSLEFRKSLSRLPDMERLIARMFSSIEASGRNGDKVVLYEDTAKKQVQEFISTLRGCETMAEACSSLRAILKHDTSRRLLHLLTPGQSLPNISSSIKYFKDAFDWVEAHNSGRVIPHEGADEEYDCACKTVEEFESSLKKHLKEQRKLLGDASINYVTVGKDEYLLEVPESLSGSVPHDYELCSSKKGVSRYWTPTIKKLLKELSQAKSEKESALKSISQRLIGRFCEHQEKWRQLVSATAELDVLISLAFASDSYEGVRCRPVISGSTSDGVPHLSATGLGHPVLRGDSLGRGSFVPNNVKIGGAEKASFILLTGPNMGGKSTLLRQVCLAVILAQIGADVPAETFEVSPVDKICVRMGAKDHIMAGQSTFLTELSETAVMLTSATRNSLVVLDELGRGTATSDGQAIAESVLEHFIEKVQCRGFFSTHYHRLSVDYQTNPKVSLCHMACQIGEGIGGVEEVTFLYRLTPGACPKSYGVNVARLAGLPDYVLQRAVIKSQEFEALYGKNHRKTDHKLAAMIKQIISSVASDSDYSASKDSLCELHSMANTFLRLTN
Protein: Actin, aortic smooth muscle (EC 3.6.4.-) (Alpha-actin-2) [Cleaved into: Actin, aortic smooth muscle, intermediate form] (P62737)
Organism: Mus musculus (Mouse)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Myosin-11
- Myosin regulatory light polypeptide 9
- Transgelin
- Actin, gamma-enteric smooth muscle
- Myosin-10
- Myosin-9
- Myosin light polypeptide 6
- Myosin light chain 6B
- Myosin-14
- CCN family member 2
Sequence:
MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: Eukaryotic translation elongation factor 1 beta 2 (A0A8I6AEG7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGCVIYQLGVCVFSFKGACTCFCVTCRYVPSQADVAVFEAISGPPPADLCHALRWYNHIKSYEKEKASLPGVKKSLGKYGPVSVADTTGSGAADAKDDDDIDLFGSDDEEESEDAKRLREERLAQYESKKAKKPAVVAKSSILLDVKPWDDETDMTKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDYVQSMDVAAFNKI
Protein: Retinoic acid early-inducible protein 1-alpha (RAE-1-alpha) (O08602)
Organism: Mus musculus (Mouse)
Function: Acts as a ligand for KLRK1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}.
Interaction partners:
Sequence:
MAKAAVTKRHHFMIQKLLILLSYGYTNGLDDAHSLRCNLTIKDPTPADPLWYEAKCLVDEILILHLSNINKTMTSGDPGETANATEVGECLTQPLKDLCQKLRNKVSNTKVDTHKTNGYPHLQVTMIYLQSQGQIPSATWEFNISDSYFFTFYTENMSWRSANDESGVIMNKWKDDGEFVKRLKFLIPECRQEVDEFLKQPKEKPRSTSRSPSITQLTSTSPLPPPSHSTSKKGFISVGLIFISLLFAFAFAM
Protein: V-type proton ATPase subunit G (V-ATPase subunit G) (V-ATPase 13 kDa subunit) (Vacuolar proton pump subunit G) (P48836)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:7775427}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit c
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit D
- V-type proton ATPase subunit E
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase subunit d
- V-type proton ATPase catalytic subunit A
Sequence:
MSQKNGIATLLQAEKEAHEIVSKARKYRQDKLKQAKTDAAKEIDSYKIQKDKELKEFEQKNAGGVGELEKKAEAGVQGELAEIKKIAEKKKDDVVKILIETVIKPSAEVHINAL
Protein: GH09802p (Misexpression suppressor of KSR) (Q9GU50)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-like protein 1
Sequence:
MPSAPTHTAEEAHLLGTMPVDPMDDIELRSVQLQFPNARGSILEACEQRRVPTDKGDVHVAIQGDTAKPAIITYHDLGLNYATSFAGFFNFPVMRGLLENFCVYHVTAPGQEEGAPTLPEDYVYPTMDDLAAQLLFVLSHFGLKSVIGFGVGAGANILARFAHAHPDKVGALCLINCVSTQSGWIEWGYQSFNARFLRTKGMTQGVIDYLMWHHFGRNPEERNHDLVQMYKQHFERGVNPTNLAMLINAYIHRNDLHLARTPPGTPGSETAATTLKMPVINITGSLSPHVDDTVTFNGRLDPTNSSWMKISDCALVLEEQPAKLAEAFRLFLQGEGYATPLSTPASSPCGTKYHTYSSIFFANFREQQQQAMEERDRERERERDRQRQLSLRVGNRLRETAINCTSSNSNTTAGQGDNNNADGRSVDGDDQDLENGNGCAGGNGTGTGNGNRAYVTTDTSGTLYYGTQSNKIRITENPLPEPVSS
Protein: Conserved protein (O53417)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable enoyl-CoA hydratase EchA8
- 3-hydroxyisobutyryl-CoA hydrolase
- Glycerol-3-phosphate dehydrogenase [NAD
- 6-phosphogluconate dehydrogenase, decarboxylating
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MTEPAAATTTNASDEPATGAEQAVDTAATPQTPEPQPIRSTWWIRHYTFTGTAMGLVFVWFSMTPSLLPRGPLFQGLVSGICGAFGYGLGVFAVWLVRYMRSHNSSPPPPRWAWPPLIAVGAVGMVGMAVQFHVWQDDVRDLMGVEHLRWYDYPLAAALSLVVLFTLVEIGQFIRWLFRFLVGQVDRIAPFRVSAAIVVVLLVVLTITLLNGVVLKFAMNSMNSTFAAVNNEMNPDSAPPKTPLRSGGPGSLVSWESLGHQGRIFVHSGPTIADLTAFNGTPAVEPIRTYAGLNSADGIMATAELAARELARTGGLRRAVVAVATSTGTGWINEAEASALEYMYNGDTAIVSMQYSFLPSWLSFLVDKENARHAGEALFEAVDKLIRQLPESQRPKLVVFGESLGSFGGEAPFMNLNNILARTDGALFSGPTFNNTVWNSLTANRDAGSPQWLPIYDDGRNVRFVARARDLQRPDAPWGRPRVVYLQHASDPIAWWTPRLLFREPDWLREQRGYDVLPQTRWIPVVTFVQVSADMAVATHVPDGHGHRYVATVADGWAAVLSPPGWTQQKTERLQPLLHANAKPFGS
Protein: Protein mlo1 (O74871)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- ATP-dependent RNA helicase uap56
- Uncharacterized protein P25A2.03
- PCI domain-containing protein C1105.07c
- mRNA export protein mlo3
Sequence:
MSDYKSLKVAELREKLAEKGLSTAGNKAELVSRLTAATESNDENTSNNNATDLGDLAPPEDDIDWGDMENDTISTDVNKPAEPESKETSAPAAAVEIEKENESIISKETSQAPETSTGAEEHQETTEESKQSVSNEVSSPDVAKEQEKLIQRAKRFGIPVDDEQIKKAARAARFGIQQPLASSNNKNHNQSKNPQNRSNSRSKQRNKNAPPKSAPSKRKSNILDDPIEAEKARKRAERFGVAAKN
Protein: Glutathione S-transferase omega (GSTO) (EC 1.20.4.2) (EC 1.8.5.1) (EC 2.5.1.18) (Glutathione-dependent dehydroascorbate reductase) (Monomethylarsonic acid reductase) (C1BHF6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MASEKCFAKGSSAPGLVAKGQIRLYSMRFCPFAHRTRLVLHAKGIKHDTVNINLKDKPEWFLKKNPLGLVPTLETSSGQVIYESPITCDYLDEVYTDKKLLPADPFQKAQQKMMLENFSRVTPYFYKIPMGKKNGEDISVLEGELKEKFVKLNEDLVNKKFFGGNAITMIDYMMWPWFERLEIFELKHCLDGTPELKKWTEHMSEDQTVKATMFPTETNKAFYKTYADGKPNYDYGL
Protein: Microspore-specific promoter 2 (Q1PDM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein P2v
- Polyadenylate-binding protein-interacting protein 8
- Polyadenylate-binding protein-interacting protein 9
- Polygalacturonase 1 beta-like protein 3
- Probable DNA helicase MCM8
- Copper transporter 3
- Origin of replication complex subunit 1B
Sequence:
METIEQQKHSLSSLPMLSRLEHLDFVIKNLERQQNLPKWKDESAPTTRGLIDRGTAIREAYFKGSLLDRIAALETRLFQICLELESSSGSSTSTGGSGETSSQRIKRDLTKTLPIFSSNINPFHVPLQHPQDLREMEEKIEEEKEEEINVEKPLLEKKNKKTKKNDANETCKPKKKKTKSPKKWSRFSLLGC
Protein: N-acetyltransferase 10 (E9PMU0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHRKKVDNRIRILIENGVAERQRSLFVVVGDRGKDQVVILHHMLSKATVKARPSVLWCYKKELGFSSHRKKRMRQLQKKIKNGTLNIKQDDPFELFIAATNIRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGLVVILLRTMNSLKQLYTVTMDVHSRYRTEAHQDVVGRFNERFILSLASCKKCLVIDDQLNILPISSHVATMEALPPQTPDESLGPSDLELRELKESLQDTQPVGVLVDCCKTLDQAKQEPKQSKKLKNRETKNKKDMKLKRKK
Protein: AT22944p (Q8IHA3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDEANKEDVKRASLSNSTVTIRPRLIYGLRSDVIGNIHFNLTKEVIYPVEGVLAFHDYVQNKQRFLRLPEDTRPEVISISSHRKLLAVVERHSKNGRYISIYELATLKKRRHLELPSNHRNAEIQQMIFTNDSRSVALITRPPEETLIMLVLDKTSTVIEGRATIPGSHGGAECIAGNPNDCNFMAVGGERTLLLMSKSERGFSISNNLKVKYRVTSMAFLSLDLLMIGTSDDQLILVENGEQKLAQKASDADTVDLMIDQEVFDRDKELQEQRFLPTQAVSLPDRRVLCMTAFPKGFAYIIFNRAFVFERVSKFKFERKTILTVPTNLYAEHMYQILNLAIDHKQETVIVTTSHCQIYVGILIVPETLKTKQLKFEPLGVLIHTGEIIAMSVCAWKPIIMTASRDQTIRIWNYETALVELVRKFQVDVNIVELSLTGQMAAIGFSDQLRITQIFMDDLNIVKTYNFPHCNAVRYSNFGHMMAAAYDNNIAITSVYKLDVLINLKGHNGIVLSVAWSRTDKFLISGGAEGAIYLWDIETGARLQEIVQKGTEYVTISCSTNDPLTIYAGTSIGTIREFQDSTLVREITIPSRTKGSVSDVCLARSDLIMFVADHEGNLFNMQLPFLEAGGGTFTNFRFFDGPVNKLRFSYDGTLLFAISNKGTLAIWAMDNIEGKVPYMDQDLMRSQEVLIPRSQLNDKIEQIANLELRLKQQAEEFQYQLSQNEIFDGQQLQEVHRSYCSALEELKELNNEIEARHTEEMNHITFQINSIREEHRIQLDTLATQYSERMLIEYQKFTNLRENMLELRESYEDKLKNSTGTLQDTVEALENNYKQQLNERKELIRDLMKEMQDKKAEFIEYCREVELENDRNMVSTQTEYENKLTTERNETQMWRGKAGVLQKKFESQSREIDNLLEEVEILKEEHHKSQRNIQKQMRNIEDLQKDIADRDYAINGKEKRIQDLLHKNQELDKYKQVLGHKIAELKAQIEPREFQINDKRKHIIEMEAELEGLNQNNVQLELQLKEMRDKYLSNVAELRTERHRAKASRECLHSICSDIYYVAGEINSAEALKKAVKELFRKHASDDELKRFVTLDAEVRDEFMRQRKQIENVLDRYKSVAEDKSVQKKYDKLFKENVILIEEIEKLNETNKMLRSKVKEDLRRSTKTIHK
Protein: Interleukin-12 subunit alpha (IL-12A) (Cytotoxic lymphocyte maturation factor 35 kDa subunit) (CLMF p35) (IL-12 subunit p35) (Q9R103)
Organism: Rattus norvegicus (Rat)
Function: Heterodimerizes with IL12B to form the IL-12 cytokine or with EBI3/IL27B to form the IL-35 cytokine. IL-12 is primarily produced by professional antigen-presenting cells (APCs) such as B-cells and dendritic cells (DCs) as well as macrophages and granulocytes and regulates T-cell and natural killer-cell responses, induces the production of interferon-gamma (IFN-gamma), favors the differentiation of T-helper 1 (Th1) cells and is an important link between innate resistance and adaptive immunity. Mechanistically, exerts its biological effects through a receptor composed of IL12R1 and IL12R2 subunits. Binding to the receptor results in the rapid tyrosine phosphorylation of a number of cellular substrates including the JAK family kinases TYK2 and JAK2. In turn, recruited STAT4 gets phosphorylated and translocates to the nucleus where it regulates cytokine/growth factor responsive genes (By similarity). As part of IL-35, plays essential roles in maintaining the immune homeostasis of the liver microenvironment and functions also as an immune-suppressive cytokine (By similarity). Mediates biological events through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers. Signaling requires the transcription factors STAT1 and STAT4, which form a unique heterodimer that binds to distinct DNA sites (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P29459}.
Interaction partners:
- Interleukin-12 subunit beta
- Interleukin-12 receptor subunit beta-2
- Interleukin-12 receptor subunit beta-1
- Interleukin-23 receptor
- Interferon gamma receptor 1
- Interleukin-23 subunit alpha
- Interferon alpha/beta receptor 1
- Ciliary neurotrophic factor receptor subunit alpha
- Leptin receptor
- Interleukin 22 receptor subunit alpha 1.
Sequence:
MCQSRYLLFLATLVLLNHLTSARVIPVSGPAKCLNQSQNLLKTTDDMVRTAREKLKHYSCTAGDIDHEDITRDKTSTLEACLPLELHKNESCLATKETSSIIRGSCLPPQKTSLMMTLCLGSIYEDLKMYQSEFQAINAALQSHNHQQITLDRNMLMAIDELMRSLNHSGETLHQKAPMGEADPYRVKMKLCILLHAFSTRVMTINRVMNYLSSS
Protein: Soluble-type polypeptide FZD4S (Q9BY80)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLAMAWRGAGPSVPGAPGGVGLSLGLLLQLLLLLGPARGFGDEEERRCDPIRISMCQNLGYNVTKMPNLVGHELQTDAELQLTTFTPLIQYGCSSQLQVGAPTPTPGGTPWGGTLQTNFAEPMPS
Protein: Vacuolar-sorting protein SNF8 (Q59N31)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- ESCRT-II subunit protein
- Vacuolar protein-sorting-associated protein 36
- ESCRT-III subunit protein
- Vacuolar-sorting protein SNF7
- Ubiquitin-binding ESCRT-I subunit protein
- Vacuolar protein sorting-associated protein 27
- Vacuolar protein sorting-associated protein 28
- ESCRT-III subunit protein
- ESCRT-III subunit protein
- Class E vacuolar protein-sorting machinery protein HSE1
Sequence:
MNHSNTTNTDRDAYLQLGKSLNEQHSNQLSTQLQVFQSALINFANDHGDEISSNLEFKNKFTQIVQSIGIDPLDLLLYTSQNDRNGGTSNSNSSSNSSSNYKRSNVVATNFGVALAVKIIEICQQTRDLNGGLISLKELISTLQNSCETEGISLVVSEKDIESSLNNLNTLGKGYEILIINGKKWLKFSSTENLSNDQLKIYELCEFMGGYVTYRLLRDNYGWDKVRCKTVIDEMIMNGFLWVDSQDNGEWQYWEPSWISN
Protein: Proline-rich protein-2 (Q94G50)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MMSTIHLLILLLGAVAFATPSFGTYENYGKPPTPVYKPPKVKPPPYEHKPPVYEPPKKEKPEPKPPVYTSPKKDKPEPKPPVYEPPKKEKPEPKSPVYTPPKKERPEPKPPVYEPPKKEKPKPKPSVYTPPKKEKPEPKPLVYEPPKKEKPEPKPPVYTPPKKEKPEPKPPMYEPPKKEKLEPKPLVYAPPKKEKPEPKPPVYEPPKKPPVYEPKPPKPPVYASPKKEKPEPKPPMYEPPNKPPMYEPKPQKSPVYVPPKKEKPEPKPPMYEPPKKPPVHKPPYGHYPRHLHWGSLNREAPSASHPHELS
Protein: ATP synthase subunit b (ATP synthase F(0) sector subunit b) (ATPase subunit I) (F-type ATPase subunit b) (F-ATPase subunit b) (P9WPV5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
Interaction partners:
- ATP synthase subunit beta
- ATP synthase subunit alpha
- ATP synthase gamma chain
- ATP synthase subunit a
- ATP synthase subunit b-delta
- ATP synthase subunit c
- ATP synthase epsilon chain
- Uncharacterized protein Rv1303
- Inorganic pyrophosphatase
- Cytochrome bc1 complex cytochrome b subunit
Sequence:
MGEVSAIVLAASQAAEEGGESSNFLIPNGTFFVVLAIFLVVLAVIGTFVVPPILKVLRERDAMVAKTLADNKKSDEQFAAAQADYDEAMTEARVQASSLRDNARADGRKVIEDARVRAEQQVASTLQTAHEQLKRERDAVELDLRAHVGTMSATLASRILGVDLTASAATR
Protein: Coiled-coil and C2 domain-containing protein 1B (Five prime repressor element under dual repression-binding protein 2) (FRE under dual repression-binding protein 2) (Freud-2) (Q5FVK6)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Charged multivesicular body protein 4c
- Charged multivesicular body protein 4B
Sequence:
MPGPRPRKGPKTSGQGAETAKQLGLFVEFNPEDMLLGMDETEDDGDLEAELLALTGETGSTSRKPAPKGRAPLPMAHIEKLAADCMRDVEEEGEEEEGLEDDADLLTELQEVLGVDEETGLVDDSEETSPDLSEEKTRDNTEQPVAPAAFQQALPAAVAQAGGPRGLQALLEERIQNYREAAASAKEAGEAAKARRCERGLKTLESQLATVRKGGKICEDEIPPPVALGKRPPAHQERPSKDSEIDSAGSCAMDPGDLSQPESSLPAVAALPDSDPDPQALLLARQREYKAAALSAKRAGDLDRARELMRIGKRFGTVLEALEKGQPVDLSGMPPAPEDLKALPQASEASAATQVLSPAVEQMQPVMSSDLPATPAAPAEPKTVLDALQQRLNRYREAGIQARASGDERKARMHDRIAKQYQDAIRAHQAGRKVDFAELPVPPGFPPIPGLEPRKDTEEDSVTATLAAAQKLASEDTALVDEDEERDTPAQAPLAKKPAQPLVPSSHLLNEPKASSSKESLSPSVREQVTLLEARKLQYQRAALQAKRRQDLEQAKSHLRVAKSLEAQIIQARAGQPIDLSKVPSPLTDEEGDFILIHHEDLRLSQKAEEVYAQLQKILLEQHEKCLLFSKQFMHQGNVAETTRFEKLAEDRKKQLEILQLAQAQGLDPPSHHFELKTLQTVRIFSELNSTEMHLIIVRGMNLPAPPGVTPDDLDAFVRFEFHYPNSDQAQKSKTAVVKNTNSPEFEQVFKLNINRNHRGFRRVIQSKGIKFEIFHKGSFFRSDKLVGTAHLKLERLEKECEIREIMEVLDGRKPTGGKLEVKVRLREPLSSQDVQMVTENWLVLEPRGL
Protein: Acetolactate synthase (EC 2.2.1.6) (A0A1D8PJF9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Acetolactate synthase regulatory subunit
- dihydroxy-acid dehydratase
- Ketol-acid reductoisomerase, mitochondrial
- Threonine dehydratase
- 3-isopropylmalate dehydrogenase
- 2-isopropylmalate synthase
- L-serine ammonia-lyase
- L-serine ammonia-lyase
- 2-isopropylmalate synthase
- malate dehydrogenase
Sequence:
MISRNLRTSSTKTFYGSILRSQIRSISKNNSQQATAQSTSRPQPSPAFNTADTSTQPIINDPTLNKHQSSAISRKKKEQLMDDSFIGLTGGEIFHEMMLRHKVDTVFGYAGGAILPVFDAIYNSDKFKFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMADALMDGVPLVVFSGQVPTTAIGTDAFQEADIVGISRSCTKWNVMVKNVAELPRRINEAFEIATTGRPGPVLVDLPKDVTASILRESIPINTTLPSNALSQITKKAVSEFTSEAIKRAANILNKAKKPIIYAGAGILNNEQGPKLLKELADKANIPVTTTLQGLGAFDQRDPKSLDMLGMHGSAAANTAIQNADCIIALGARFDDRVTGNISKFAPEAKLAASEGRGGILHFEISPKNINKVVEATEAIEGDVTANLQSFIPLVDSIENRPEWFNKINEWKKKYPYSYQLETPGSLIKPQTLIKEISDQAQTYNKEVIVTTGVGQHQMWAAQHFTWTQPRTMITSGGLGTMGYGLPAAIGAQVAKPDAIVIDIDGDASFNMTLTELSSAVQAGAPIKVCVLNNEEQGMVTQWQSLFYEHRYSHTHQSNPDFMKLAESMNVKGIRITNQQELKSGVKEFLDATEPVLLEVIVEKKVPVLPMVPAGKALDDFILWDAEVEKQQNDLRKERTGGKY
Protein: Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Cyclosome subunit 8) (Q9UJX2)
Organism: Homo sapiens (Human)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 13
- Anaphase-promoting complex subunit 11
- Cell division cycle protein 16 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Anaphase-promoting complex subunit CDC26
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 16
Sequence:
MAASTSMVPVAVTAAVAPVLSINSDFSDLREIKKQLLLIAGLTRERGLLHSSKWSAELAFSLPALPLAELQPPPPITEEDAQDMDAYTLAKAYFDVKEYDRAAHFLHGCNSKKAYFLYMYSRYLSGEKKKDDETVDSLGPLEKGQVKNEALRELRVELSKKHQARELDGFGLYLYGVVLRKLDLVKEAIDVFVEATHVLPLHWGAWLELCNLITDKEMLKFLSLPDTWMKEFFLAHIYTELQLIEEALQKYQNLIDVGFSKSSYIVSQIAVAYHNIRDIDKALSIFNELRKQDPYRIENMDTFSNLLYVRSMKSELSYLAHNLCEIDKYRVETCCVIGNYYSLRSQHEKAALYFQRALKLNPRYLGAWTLMGHEYMEMKNTSAAIQAYRHAIEVNKRDYRAWYGLGQTYEILKMPFYCLYYYRRAHQLRPNDSRMLVALGECYEKLNQLVEAKKCYWRAYAVGDVEKMALVKLAKLHEQLTESEQAAQCYIKYIQDIYSCGEIVEHLEESTAFRYLAQYYFKCKLWDEASTCAQKCCAFNDTREEGKALLRQILQLRNQGETPTTEVPAPFFLPASLSANNTPTRRVSPLNLSSVTP