wanglab/gogpt-training-data huggingface dataset:
Protein: Proteasomal ubiquitin receptor ADRM1 homolog rpn1302 (Regulatory particle non-ATPase 13ba protein) (Q9USM1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 26S proteasome regulatory subunit rpn12
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn11
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit rpn1
- Probable 26S proteasome regulatory subunit rpn9
- Probable 26S proteasome regulatory subunit rpn3
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 7 homolog
Sequence:
MESVFGRVRNETSERGKYGLVSVKAGKLQRKPGTNILQADHRKGVIYMQMASDELLHFYWKERARVSREVEDDYIIFPEEAEFIKIDECTTGRVYALKFKSSSQIHFYWMQEYSDEKDKETASLINQLIADPVNTTRTINSHNNSSSRGTDDSSTSQLLQLFGAASQDALQDFNWEVLSPTAEAPAILPRFPNVNESANMYRASSESNLNGPHATAGENGEDHEEATASPLDENIDYTHSRTLELLEQLQPLILNETTFVEPFSIDRESHRVITHPRVYPKIFPHSPSDLLRISGRAELSENRDFFKHLSSLMEAVAKPESESLREICNLSLEQVQSASGAELFLHALYDRLVNEGVIVISHITQEGSDGEVEEEGDVEMRESNEKDE
Protein: Stevor (O96118)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKMYYLKMLLFTFLINTLVLPHYENHKNNHYNVSLIQNNTQRTTINSRLLAQTQNKNPHYHNDPELKEIIDKLNEEAIKKYQQTHDPYEQLKDVVEKNGTKHVGGHVSEPMSTIEKELLETYEDVFGDKNHVMLKSGRYPNDDDKSDDSSSCECTDVNNTKLEKTKGKDKYLKHLKHRCIGGICSCSVGSAFLTILGCAFAKSAALTAFASSESTKTCISSVAIYNLFQNSTMLSALKTVGGTCANGAPDIAGTVSTLASAAFPPYGIAALVLLILAVALIILYIWLYRRRKNSWKHECKKHLCR
Protein: Zinc finger CCHC-type and RNA-binding motif-containing protein 1 (U11/U12 small nuclear ribonucleoprotein 31 kDa protein) (U11/U12 snRNP 31 kDa protein) (U11/U12-31K) (Q8TBF4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:16959469}.
Interaction partners:
- RNA-binding region-containing protein 3
- U11/U12 small nuclear ribonucleoprotein 48 kDa protein
- Zinc finger matrin-type protein 5
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- Splicing factor 3B subunit 2
- Splicing factor 3B subunit 1
- Programmed cell death protein 7
- U11/U12 small nuclear ribonucleoprotein 25 kDa protein
- Y-box-binding protein 1
- Splicing factor 3B subunit 6
Sequence:
MSGGLAPSKSTVYVSNLPFSLTNNDLYRIFSKYGKVVKVTIMKDKDTRKSKGVAFILFLDKDSAQNCTRAINNKQLFGRVIKASIAIDNGRAAEFIRRRNYFDKSKCYECGESGHLSYACPKNMLGEREPPKKKEKKKKKKAPEPEEEIEEVEESEDEGEDPALDSLSQAIAFQQAKIEEEQKKWKPSSGVPSTSDDSRRPRIKKSTYFSDEEELSD
Protein: ADP-ribosylation factor-like protein 6-interacting protein 1 (Q9VES1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Ribosomal protein
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS17
- 40S ribosomal protein S15
- Eukaryotic translation initiation factor 4C
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS3
Sequence:
MAASQVDQKRALNKLKHDLEPFRTAIVGAYGVLTWEKQYYAGVVFGVISCLYLVLWYLDLSLITLLSLLGVISILLNYAFPMVSRLIFGGVNWDGDQEAKFEDVCGQVCAVKGSLVVWYEYLFNERKSTVFVIVMSLGLLAMAWIGAIINNLLLMYLATLLILMWPGLQNKDIFKAITQRASKIINEKIQCGKRKLQ
Protein: Ribosomal protein L36a (H0Y5B4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVNVPKTRRTFCKKCGKHQPHKVTQYKKGKDSLYAQGKRRYDRKQSGYGGQTKPIFRKKAKTTKKIVLRLECVEPNCRSKRMLAIKRCKHFELGGDKKRKVYNYGWKVQSFS
Protein: Sodium-dependent nutrient amino acid transporter 1 (B3NV41)
Organism: Drosophila erecta (Fruit fly)
Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELKGVQPSNGSANGNGTTNAASTEKTDAEKHTPERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSRPQEYVDNLLSGVSLANESARNFSAIGSVANEETEKLQSSSELYFLNVVIKEKLDISDGVGDPDWKLTLALLAAWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGILFFLEPQWGELLNPTVWKEAVVQCFFSLAVGSGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLQIENIRDVVRSGTGLAFISYPDAISKFKAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKGLKYWKVALITSACGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWVYGLQNFCDDIEFMCNRRVSLYWRMCWSFFTPVMMIIIFIYSMVTIEPIKYSELYFPEAANIAGWLLFAIGAAQFPLWGLWYVSRHPQGTYWKSLKASMKPSERWGPANPETRREWVIFKNHKAAQRATQKDVSKLGFFWRKLTNFCGSNK
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (DNA 3'-5' helicase BLM) (A0A3B3IT82)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAVPQNNLQEQLERHSARTLNNKLSLSKPKFSGFTFKKKTSSDNNVSVTNVSVAKTPVLRNKDVNVTEDFSFSEPLPNTTNQQRVKDFFKNAPAGQETQRGGSKSLLPDFLQTPKEVVCTTQNTPTVKKSRDTALKKLEFSSSPDSLSTINDWDDMDDFDTSETSKSFVTPPQSHFVRVSTAQKSKKGKRNFFKAQLYTTNTVKTDLPPPSSESEQIDLTEEQKDDSEWLSSDVICIDDGPIAEVHINEDAQESDSLKTHLEDERDNSEKKKNLEEAELHSTEKVPCIEFDDDDYDTDFVPPSPEEIISASSSSSKCLSTLKDLDTSDRKEDVLSTSKDLLSKPEKMSMQELNPETSTDCDARQISLQQQLIHVMEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLTEVDFNKSDASLLGSLWRYRPDSLDGPMEGDSCPTGNSMKELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSFVSSNWAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPSYDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAYQPIKEGRPIKSVSERLSSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSLSFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLYSMVHYCENITECRRIQLLAYFGENGFNPDFCKKHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNIKHVGPSGRFTMNMLVDIFLGSKSAKIQSGIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGNKAQTVLNGNLKVDFMETENSSSVKKQKALVAKVSQREEMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPAEDSSPGISLSSSRGPGRSAAEELDEEIPVSSHYFASKTRNERKRKKMPASQRSKRRKTASSGSKAKGTKSDSVAQARVQWHNLGSLQPLPPVLK
Protein: HCG1778014 (PXN protein) (Q7Z7K5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPDTFNSRSPSVEGSLWAVGTESQGRDWRHLPTITSELSGAPRCHTVPCAGSTALQEPGEPQGPPASPSCPEEALAATWEQPWASEVFGPERMPPSGAARSFQEVTEPAVVAVDRQAIFPDTWTLTEEHGLQQERPRPEPGRLGSSSPASVTTEQLGAKMTERGSVARPTQGPETPRSPEGTTEAATQDGKEQPELPCAMAMGTPSTTERISTSGQAGTSSHGCWAWPLAGLSVGRSSLTACSLPLCACLLGQKMLRHCGRT
Protein: Diamine acetyltransferase (EC 2.3.1.57) (Spermidine/spermine N(1)-acetyltransferase) (CpSSAT) (Q5CPU3)
Organism: Cryptosporidium parvum (strain Iowa II)
Function: Enzyme which catalyzes the acetylation of polyamines. Displays higher substrate specificity for spermine than for spermidine. May function to acetylate host-derived polyamines, thus alleviating the necessity for de novo synthesis of these molecules.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17289169}.
Interaction partners:
Sequence:
MISSFEVRKATIDDYFELRNLICDVTRCTETLSREQAEERFRYNTYHPYCLVDTENGRIVGYAGFYIIPHLGRKNDSRIEHVIISKEYRNRGLGRLLCKQIIEDAKNKFNCGRIDLTVESHIAKKLYSSLEFEKVNTEVMRNSFLDLTPKSD
Protein: Ecdysone-induced protein 63E, isoform A (EC 2.7.11.22) (Ecdysone-induced protein 63E, isoform B) (Ecdysone-induced protein 63E, isoform C) (Ecdysone-induced protein 63E, isoform J) (IP09007p) (LD15250p) (Serine/threonine protein kinase variant L63B2) (Q7KM05)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAELISQPTKINNNNFGAGVTMREKKGGALQKLKKRLSHSFGRLTISREDGDESTHHHHHHHHHRGGHGGHHNHGNKVPYNGYNSEEYLDRLEPNGNIPADKTNCRYGDWRSTDSTDHHDRVQRQLSVSSDSKLLDEDIREEMKYHSHVVMRPKKPPRPKSEVFLNKQETHPRRKRFSAFGGDSPFGKQEAYVKLEPLGEGSYATVYKGFSKLTYQRVALKEIRLQEEEGAPFTAIREASLLKELKHSNIVTLHDIVHTRETLTFVFEYVNTDLSQYMEKHPGGLDHRNVRLFLFQLLRGLSYCHKRRVLHRDVKPQNLLISDCGELKLADFGLARAKSVPSHTYSHEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFVEMVTGMPTFPGIRDTYDQLDKIFKLLGTPTEDTWPGVTHFPGYKPHKLGFYRPRKLGHNFPRLYDIIEGETIANGFLQLNPEQRLGADDALQHPYFAQLPKKLYELPDETSIFTVEGVQLYTEPNRQNK
Protein: F-box and leucine-rich repeat protein 13 (Dynein regulatory complex subunit 6) (F-box/LRR-repeat protein 13) (Q8CDU4)
Organism: Mus musculus (Mouse)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8JHD7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8NEE6}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- Dynein regulatory complex subunit 3
Sequence:
MASLRSATPRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAIIKRGLENLLWDTCIHPSLKSRVRRLSETYLDELFGLDDQLVTPELMIKACTFYTGHLVKTHFSGWKKVAIPRANQEEIMAEKMDKAIAHDNFRCQKYIFNRWFAYTVMSRERLITTLLRLRHLFYMQRQRIILAKWKERARHKSKTREDDLISKHELQLKKWKFKLGKPISLEGSLSDIAVENRRIAFDISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSIDFSTVKNIADKCVVTTLQKWRLNVLRLNFRGCDFRTKTLKAVSHCKNLQELNVSDCQSFTDESMRHISEGCPGVLYLNLSNTTITNRTMRLLPRYFHNLQNLSLAYCRKFTDKGLQYLNLGNGCHKLIYLDLSGCTQVLVEKCPRISSVVLIGSPHISDSAFKALSSCDLKKIRFEGNKRISDACFKSIDRNYPGINHIYMVDCKGLTDSSLKSLSLLKQLTVLNLTNCIRIGDIGLKHFFDGPASIRLRELNLTNCSLLGDSSVIRLSERCPNLHYLNLRNCEHLTDLAIEYIASMLSLISVDLSGTLISNEGMTILSRHRKLREVSVSDCVNITDFGIRAYCKTSLLLEHLDVSYCSQLTDDIIKTIAIFCTRITSLNIAGCPKITDAGMEILSARCHYLHILDISGCIQLTDQIIQDLQIGCKQLRILKMQFCKSISPAAAQKMSSVVQHQEYNSDNPPHWFGYDSEGNPLDKIHSRVQLRTYSKLIVKEPFSIDEEDPDSKHQ
Protein: Site-specific recombinase Flp (FLP) (Protein Able) (P03870)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the plasmid amplification system, which corrects any decrease in copy number caused by a rare missegregation event. Catalyzes the recombination between the large inverted repetitions of the 2-micron plasmid during plasmid replication. This recombination event changes the direction of one of the two replication forks in the bidirectionally replicating molecule, effectively resulting in multiple rounds of replication from a single initiation event. Binds specifically to the FLP recognition target (FRT) site where it induces DNA to bend. Three types of bend exist. Type I is approximately 60 degrees and results from 1 FLP molecule binding to 1 symmetry element. Type II is >144 degrees and results from FLP molecules binding to symmetry elements a and b. Type III is approximately 65 degrees and results from FLP molecules binding to symmetry elements b and c.
Interaction partners:
Sequence:
MPQFGILCKTPPKVLVRQFVERFERPSGEKIALCAAELTYLCWMITHNGTAIKRATFMSYNTIISNSLSFDIVNKSLQFKYKTQKATILEASLKKLIPAWEFTIIPYYGQKHQSDITDIVSSLQLQFESSEEADKGNSHSKKMLKALLSEGESIWEITEKILNSFEYTSRFTKTKTLYQFLFLATFINCGRFSDIKNVDPKSFKLVQNKYLGVIIQCLVTETKTSVSRHIYFFSARGRIDPLVYLDEFLRNSEPVLKRVNRTGNSSSNKQEYQLLKDNLVRSYNKALKKNAPYSIFAIKNGPKSHIGRHLMTSFLSMKGLTELTNVVGNWSDKRASAVARTTYTHQITAIPDHYFALVSRYYAYDPISKEMIALKDETNPIEEWQHIEQLKGSAEGSIRYPAWNGIISQEVLDYLSSYINRRI
Protein: Superoxide dismutase [Mn] 3.2, mitochondrial (EC 1.15.1.1) (P41978)
Organism: Zea mays (Maize)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Superoxide dismutase 4A
- Large ribosomal subunit protein uL23m
- Ribosomal protein S5 family protein
- Ribosomal protein S24/S35 mitochondrial
- Large ribosomal subunit protein mL46
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein bL27c
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS14c
- Large ribosomal subunit protein uL5c
Sequence:
MALRTLASKNALSFALGGAARPSAASARGVTTVALPDLSYDFGALEPVISGEIMRLHHQKHHATYVVNYNKALEQLDAVVVKGDASAVVQLQGAIKFNGGGHFNHSIFWENLKPISEGGEPPHGKLGWAIDEDFGSFEALVKRMNAEGAALQGSGWVWLALDKEPKKLSVETTANQDPLVTKGASLVPLLGIDVWEHAYYLQYKNVRPDYLNNIWKVMNWKYAGEVYENVLA
Protein: Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit) (P08067)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b (COB) to cytochrome c1 (CYT1) (Probable).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome c isoform 1
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Intron-encoded RNA maturase bI4
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG
Protein: BARP protein (Q38CV9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFHNLWLLLTVLCTAGIRAHGDWRDCYAGRKPPPAGHVRVVCSLAEQLRGLPDTISSALVTAAAASSKAFEAKVQAEEAVELAESRGLNVTKAKEAAVRATLAAEAAATAASNVEIDAANVTSSRLARRNPNTGFEKVAMCENLDKDLREAAAKCTKKAENVTTQSLSETLHRLENLYTNMSALESLRVEHVEIERFFEMLEEHVEEAVRAQRQAEEAAAEAIKIVAADEEVRGYKKEEINQVAGTKKGHEANQTTGTNTGPVVNSVASPEGSVLLLMAGLFLGSVL
Protein: Uncharacterized protein (Q586V4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSTPNNDVEQMYQELTQAFSPFIAWKAAVPPHQGKETTTQGFISENSFDGVSSIMQQPVGTPLRHLLPRSGSPRTITCTHGTSKRNVVISDKSDHVGRCDEASAYGGNSFSGKGDRHNGSSAIEERLTHILRSHRTMAESIELDNASASIDGLNEEIKHLTTMEWSPHAGNGGDEVNGSFPTNISSSSSSSYSCWLCGAPCSNALGWLNAPNIFRRPIVARARPHLLQANDRSTTHSTTISLLTLCRRCGDVCDSLLNAPYEEVLRIANEGNRMAAARTPLFICFLRSYKSLIHFLASEAKLDNEGAETFAECPLETRVSILQRMIGMVESYVRVEGHASCDGNVRGSIKTPSDLEERHLYERELEWLRKQLHMLGYTGLSHKNAVEGPPPNGGNGVDDHEHSTYGHAVISEHQWTIPELGAVTSRSTSLHPNERLSPLLDSRQCRKDTLIVATPQDGQLVQEHEKRRQELVAEARERGSRALDKMIERAVTYRLKRIHNHDVLVSASSATADGTRCHSDGDSGEGKAVTAATATNVYPKNMENKEGVQPSVFLCGGKDADNILMQYFEGKLDKVPRLTIYPHEVSGTFRERAVTATSPSVLRDSGDGQLQMAQTRKEQESILTMSNDLPFCLHTVDNGMIEFAALSREELMKRLRKEIQRRGEAERALRESNAQIAVLEKATDHMSEVILSHRMNSILANHLSSMHQLHRSMVQNCVEITVQKSLFFADEMVILMRQAQNWFYSRPIECQLGQSARSSDTITSEEERDGREGDEEETEKVRRMNYGDSARTSDGGKKEGIQGRTSVVRDVPITQFPVSLHLKPLHTRTSPSAS
Protein: Large ribosomal subunit protein bL32m (39S ribosomal protein L32, mitochondrial) (L32mt) (MRP-L32) (Q9V9Z1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BYC8}.
Interaction partners:
- Large ribosomal subunit protein bL9m
- Ribosomal protein
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS13
- FI01658p
Sequence:
MSRNLFLSITNFIRNLESLFLPHGGHPPALALAGFQHDHSPKSSQEFSLKQLIGDGLLWAVPKHRRSVEKRLKRKFGYPEYNWKPLREKRNLRSCLQCGHDHEMGVLCPFCYQKVLKETELMQSKIQETLGLDPVDKEVIVLYEGEKAEQSTDDLKNKRIVEMKKPRPMWFTKNLLQKSTQQLSETKEVKPSDLA
Protein: Protein ROG3 (Revertant of glycogen synthase kinase mutation protein 3) (P43602)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in resistance to GST substrate o-dinitrobenzene (o-DNB).
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- Protein LDB19
- Transcription factor CSR2
- pH-response regulator protein palF/RIM8
- Protein ECM21
- Arrestin-related trafficking adapter 10
- Pheromone alpha factor receptor
- Ubiquitin ligase-binding protein BUL1
- Ras-like protein 2
Sequence:
MGFSSGKSTKKKPLLFDIRLKNVDNDVILLKGPPNEAPSVLLSGCIVLSINEPMQIKSISLRLYGKIQIDVPLERPQDASSSSLSSSPPKIRKYNKVFYNYAWDNVNLKEYLSGLRGQSGLAGSSSSSNILGTRQRAQSTSSLKSLKGSSSPSSCTLDKGNYDFPFSAILPGSLPESVESLPNCFVTYSMESVIERSKNYSDLICRKNIRVLRTISPAAVELSETVCVDNSWPDKVDYSISVPNKAVAIGSATPINISIVPLSKGLKLGSIKVVLFENYQYCDPFPPVISENRQVTELNLEDPLNESSGEFNGNGCFVNNPFFQPDHSFQDKWEIDTILQIPNSLSNCVQDCDVRSNIKVRHKLKFFIILINPDGHKSELRASLPIQLFISPFVALSIKPLSSSNLYSLFSTTNQKDENSSQEEEEEYLFSRSASVTGLELLADMRSGGSVPTISDLMTPPNYEMHVYDRLYSGSFTRTAVETSGTCTPLGSECSTVEDQQQDLEDLRIRLTKIRNQRDNLGLPPSASSAAASRSLSPLLNVPAPEDGTERILPQSALGPNSGSVPGVHSNVSPVLLSRSPAPSVSAHEVLPVPSGLNYPETQNLNKVPSYGKAMKYDIIGEDLPPSYPCAIQNVQPRKPSRVHSRNSSTTLSSSIPTSFHSSSFMSSTASPISIINGSRSSSSGVSLNTLNELTSKTSNNPSSNSMKRSPTRRRATSLAGFMGGFLSKGNKR
Protein: Transcription factor APG (Basic helix-loop-helix protein 106) (OsbHLH106) (Protein ANTAGONIST OF PGL1) (bHLH transcription factor bHLH106) (Q6AT90)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Atypical bHLH transcription factor that acts as negative regulator of grain size. Binds the transcription factor ILI6 and forms a heterodimer of antagonistic bHLH transcription factors that regulates grain length and weight by controlling cell elongation in lemma and palea. May be involved in the control of lamina inclination through brassinosteroid signaling pathway.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:22363621}.
Interaction partners:
- DELLA protein SLR1
- Phytochrome B
- Phytochrome A
- Protein SLENDER RICE1-LIKE 1
- Transcription factor PHYTOCHROME INTERACTING FACTOR-LIKE 15
- Protein SLENDER RICE1-LIKE 2
- Helix-loop-helix DNA-binding domain containing protein, expressed
Sequence:
MLRGNDTGSDLAELLWDNGAPAPLRPPPPPPFQPFTCSAAATTSPPAHDYLFIKNLMRGGGAANHHHHDDDDDDDDDVPWLHYHPVVDDDDDADADTAPLPPDYCAALLSGLSDHLPPPAAAASRVDPDPCSSSHGAVVPSTSAAAAKQARTSGGGGGGVMNFTFFSRPLQQRPSGGETASASASAAATSTVPVESTVVQAATNRLRSTPLFSDQRMAWLHPPKPSPRAAAPPPPPPLAPTTRHRLDTAAATATVAQRLPPSEARAPDAPPPAATATATTSSVCSGNGDRRQLNWRDSHNNQSAEWSASQDELDLDDELAGVHRRSAARSSKRSRTAEVHNLSERRRRDRINEKMRALQELIPNCNKIDKASMLEEAIEYLKTLQLQVQMMSMGTGMFVPPMMLPAAAAAMQHHHMQMQQMAGPMAAAAHFPHLGAAAAMGLAGFGMPAAAQFPCPMFPAAPPMSMFAPPPPPPPFPHAAATAVEQTPSPPGAADAGNAPAVKQA
Protein: Transcription factor p65 (V-rel avian reticuloendotheliosis viral oncogene homolog A) (V-rel reticuloendotheliosis viral oncogene homolog A) (B3DHW2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- V-rel avian reticuloendotheliosis viral oncogene homolog B.
- Nuclear factor NF-kappa-B p105 subunit isoform X1
- Proto-oncogene c-Rel
- NF-kappa-B inhibitor alpha
- NF-kappa-B inhibitor alpha
- Interleukin-6
- Interleukin-1.
- Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, epsilon.
- Serine/threonine-protein kinase TBK1
- Interferon
Sequence:
MDGMFHQWGTSQVPQGPPHVEIIEQPKSRGMRFRYKCEGRSAGSIPGEKSNDTTKTHPAIRVHNYSGPVRVRISLVTKNQPYKPHPHELVGKDCKHGYYEADLQERRIHSFQNLGIQCVKKKDVGEAVSCRLQTQNNPFKIPDAKIWEEEFDLNAVRLCFQVSITLSSGDLFPLEPVVSQPIYDNRAPNTAELKICRVNRNSGSCRGGDEIFLLCDKVQKEDIEVRFFLDSWESKGSFSQADVHRQVAIVFRTPPYCDTNLTEPLRVKMQLRRPSDREVSEPMDFQYLPSDPDEHRLMEKRKRTEGMLHNLKLSSIITGSSMSAERRPFPTAKRTLPVSKQPVAASAPASVPAVSAAPPLKPPPTSFFSPPPGQLFTQQKMEPSPLPASSSDIWKYLQAMSVDSQPKAVPVLPFPSGTVSTGRDARLITAARGENTVLHPYTLHYTHLTHVLLLV
Protein: Amastin (Q57TV6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSFVVRKCRLLALIFSIFSLALTGLTFLTPIFEAQGERPGIITLWKYDMEDISESADGGEEKNINISNSINKNGTSRATKADDSVGKRKKDQPHENEAGDTDDIILYEDYFTCNYGRFHIQVVEGLSIVAASLNFMNFFMCIFFFGTHSFLRVPLVTYFLLAACCSGVVFGLLLDWYKNEWCDSQPCLSCLEEDGWQLGYGWMFLVASSSFSFVGAITAIISS
Protein: Oxysterol-binding protein-related protein 10 (ORP-10) (OSBP-related protein 10) (Q9BXB5)
Organism: Homo sapiens (Human)
Function: Probable lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane. Its ability to bind phosphatidylserine, suggests that it specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P (Probable). Plays a role in negative regulation of lipid biosynthesis. Negatively regulates APOB secretion from hepatocytes. Binds cholesterol and acidic phospholipids. Also binds 25-hydroxycholesterol. Binds phosphatidylserine.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19554302, ECO:0000269|PubMed:22906437}. Note=Associates with microtubules. {ECO:0000269|PubMed:19554302, ECO:0000269|PubMed:22906437}.
Interaction partners:
- Oxysterol-binding protein-related protein 11
- Vesicle-associated membrane protein-associated protein B/C
- Vesicle-associated membrane protein-associated protein A
Sequence:
MERAVQGTDGGGGSNSSSRSSSRATSAGSSPSCSLAGRGVSSRSAAAGLGGGGSRSSPGSVAASPSGGGGRRREPALEGVLSKYTNLLQGWQNRYFVLDFEAGILQYFVNEQSKHQKPRGVLSLSGAIVSLSDEAPHMLVVYSANGEMFKLRAADAKEKQFWVTQLRACAKYHMEMNSKSAPSSRSRSLTLLPHGTPNSASPCSQRHLSVGAPGVVTITHHKSPAAARRAKSQYSGQLHEVREMMNQVEGQQKNLVHAIESLPGSGPLTALDQDLLLLKATSAATLSCLGECLNLLQQSVHQAGQPSQKPGASENILGWHGSKSHSTEQLKNGTLGSLPSASANITWAILPNSAEDEQTSQPEPEPNSGSELVLSEDEKSDNEDKEETELGVMEDQRSIILHLISQLKLGMDLTKVVLPTFILEKRSLLEMYADFMAHPDLLLAITAGATPEERVICFVEYYLTAFHEGRKGALAKKPYNPIIGETFHCSWEVPKDRVKPKRTASRSPASCHEHPMADDPSKSYKLRFVAEQVSHHPPISCFYCECEEKRLCVNTHVWTKSKFMGMSVGVSMIGEGVLRLLEHGEEYVFTLPSAYARSILTIPWVELGGKVSINCAKTGYSATVIFHTKPFYGGKVHRVTAEVKHNPTNTIVCKAHGEWNGTLEFTYNNGETKVIDTTTLPVYPKKIRPLEKQGPMESRNLWREVTRYLRLGDIDAATEQKRHLEEKQRVEERKRENLRTPWKPKYFIQEGDGWVYFNPLWKAH