wanglab/gogpt-training-data huggingface dataset:
Protein: Polyketide synthase module (Q2UA48)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Multicopper oxidase-domain-containing protein
- Uncharacterized protein
- Alpha/Beta hydrolase protein
Sequence:
MEGPRGVYLFGDQTSDFDAGLRRLLQVKNNTIVASFFQRCFHALRQEIARLSPSERKIFPRFTSIVDLLARHRESDPNPALESALTCIYQLGCFINYYGDLGNVYPSASDCHIVGLCAGLLSSAAVSCSNNVGELLPAAVEAVVVALRLGLCVLKVRELVSSDQASSTSWSVLISGISEKDASQLIGEFTAERAIPPSSKPYISAVGYNSITISAPPKVLDDLIDSRLSKSHKPVRAQIHGPYHAAHLYYGRDVDRIIESCHNEVVSNYTPRIPVLSSTTGQPIEAKHMKDLLKAALEEILLRQLCWEKVTDACYSILKTARHQPCKLFPISSTATQSLFTALTKAGITDIEVENGLGDVPTNPKDNLNISGRADCSKIAIIGMSGRFPEADGTESFWDLLYNGLDVHRKVPAERWDVDAHVDPTGTKRNTSKVPYGCWINEPGLFDPRFFNMSPREALQADPAQRLALLTAYEALEMAGFIPDSTPSTQRDRVGLFYGMTSDDYREINSGQDIDTYFIPGGNRAFTPGRINYYFKFSGPSVSVDTACSSSLAAIHMACNSIWRNDCDAAIAGGVNILTNPDNHAGLDRGHFLSRTGNCNTFDDGADGYCRADGVGTIILKRLEDAQADNDPILGVINGAYTNHSAEAVSITRPHVGAQAFIFNKLLNDANIDPKDVSYVEMHGTGTQAGDAVEMQSVLDTFAPDYRRGPGQSLHLGSAKANVGHGESASGVTALVKVLLMMKKNTIPPHCGIKTKINHNFPTDLAQRNVHIAFQPTPWNRPASGKRQCFINNFSAAGGNTALLMEDAPIAEVKGQDTRPVHVVSVSARSQSALKNNINSLVKYIDEQGRSFNVNEADFIPSLAYTTTARRIHHPFRVTAIGSSLQELRDSLNNSSRLESFTPVPATAPGVGFVFAGQGAQHTGMGRQLYEKCSQFRATMQHFDCISQNQGFPSILPLVDGSVPVEELGPIVTQLGTTCLQMALVNYWGSLGIKPAFVLGHSLGEFAALNTAGVLSTSDTIYLCGRRATLLTEYCQVGTHAMLAVKASYPQVKQLLKEGVDEVACVNSPSETVVSGLTADIDDLAQRCSTEGWKSTKLRVPFAFHSAQVTPILERFQEEAQGVTFRKPSLPFVSSLLGEVITESNYDVLGAQYMVKQCRKSVNFLGALEATRYAKLMTDKTVWLEVGAHTICSGMIKATFGPQVTTVASLRREENAWKVLSNSLSALHLAGIDINWKEYHQDFSSSHQVLPLPSYKWDLKNYWIPYTNNFCLTKGAPQTAIQAAPQTTFLTTAAQKVVESRDDGTTATVVVQNDIADPELNRVIQGHKVNGAALCPSSLYADIAQTLGEYLIEKYKPEFKDLGLDVCDMVVPKPLIAKGGEQLFRVSAIANWAEKKASVQVYAVNADGKKTVDHAYCTVKFFDTNASELEWKRISYLVKRSIDSLHQNAETGEAHRIQRGMVYKLFSALVDYDENFKSIREVILDSDNNEATARVKFQAPPGNFHRNPFWIDSFGHLSGFIMNASDATDSKNQVFVNHGWDSMRCLKKFSPDVTYRTYVRMQPWQNNIWAGDVYIFEGDDIIAVFGGVKFQALARKILDTVLPPVGGSKAPITAKSPPPARTQKANTGAKTRPKAPVPSKSFTKSSGPSVVVRALSILASEVGLAESEISDDMVFADYGVDSLLSLTVTGRYREELNLDLDSSVFTDHPTVNDFKRLIAQVSPSESHDGSSSEQESNFSFNGGESSSASTPDITSPPNEKVAQVEQNGTMKEIRNIMAEEIGVPAEEIDPDENLGEMGMDSLLSLTVLGRIRETLDMDLPGEFFIENQTLNDIEVALDLKPKTTSAPIPMPEPVKFPEAIHDLQPKLAQHPKATSILLQGNPRTATKTLFLFPDGSGSATSYATIPGLSPDVCVYGLNCPYMKTPEKLKCSLDELTAPYVAEIRRRQPKGPYSFGGWSAGGICAYDAARHLMFEEGEQVDRLLLLDTPFPIGLEKLPQRLYGFFNSIGLFGEGKTAPPSWLLPHFLAFIDALDAYKAAPLPFKDEKWAKKLPKTYIIWAKDGVCGKPGDPRPDPPTDGSKDPKEMVWLLNDRTDLGPNKWDTLVGPENIGGITVMEDANHFTMTKGEKAKELSTFMANAMA
Protein: Uncharacterized protein (Q38CE6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTLGPTTRVTVNVTGTVTVPLHLNALESLDDAPLQEEIMREAVRLSLAEQLGGFDNFTVTSARKGGNHVCEARLDVGDLCSIIADVKNAYEHGERRLRELQQLITAIREQLKESGREGGSEDEDITVPGIVKVVSDMVEDALRGPGESSLSAAIREVSNDKSWLEEVPVGDRSGGAASKSDEDSPSGVGYTRLPDSGEDSNGSERQLE
Protein: E3 ubiquitin-protein ligase RNF135 (EC 2.3.2.27) (RIG-I E3 ubiquitin ligase) (REUL) (RING finger protein 135) (RING finger protein leading to RIG-I activation) (Riplet) (RING-type E3 ubiquitin transferase RNF135) (Q8IUD6)
Organism: Homo sapiens (Human)
Function: E2-dependent E3 ubiquitin-protein ligase that functions as a RIGI coreceptor in the sensing of viral RNAs in cell cytoplasm and the activation of the antiviral innate immune response. Together with the UBE2D3, UBE2N and UB2V1 E2 ligases, catalyzes the 'Lys-63'-linked polyubiquitination of RIGI oligomerized on viral RNAs, an essential step in the activation of the RIG-I signaling pathway. Through a ubiquitin-independent parallel mechanism, which consists in bridging RIGI filaments forming on longer viral RNAs, further activates the RIG-I signaling pathway. This second mechanism that synergizes with the ubiquitin-dependent one would thereby allow an RNA length-dependent regulation of the RIG-I signaling pathway (Probable). Associated with the E2 ligase UBE2N, also constitutively synthesizes unanchored 'Lys-63'-linked polyubiquitin chains that may also activate the RIG-I signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19484123, ECO:0000269|PubMed:23950712}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23950712}.
Interaction partners:
- Antiviral innate immune response receptor RIG-I
- Interferon-induced helicase C domain-containing protein 1
- Mitochondrial antiviral-signaling protein
- ATP-dependent RNA helicase DHX58
- Arf-GAP with dual PH domain-containing protein 2
- Protein EVI2A
- Protein EVI2B
- Interferon regulatory factor 3
- Ubiquitin-conjugating enzyme E2 N
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MAGLGLGSAVPVWLAEDDLGCIICQGLLDWPATLPCGHSFCRHCLEALWGARDARRWACPTCRQGAAQQPHLRKNTLLQDLADKYRRAAREIQAGSDPAHCPCPGSSSLSSAAARPRRRPELQRVAVEKSITEVAQELTELVEHLVDIVRSLQNQRPLSESGPDNELSILGKAFSSGVDLSMASPKLVTSDTAAGKIRDILHDLEEIQEKLQESVTWKEAPEAQMQGELLEAPSSSSCPLPDQSHPALRRASRFAQWAIHPTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRTMDSCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLYGLHPGNYLIIKQVKV
Protein: Histone deacetylase 7 (EC 3.5.1.98) (Q9FH09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. May be involved in flowering induction. Histone deacetylases act via the formation of large multiprotein complexes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- WD40 repeat-containing protein HOS15
- High mobility group B protein 9
- NAD-dependent protein deacylase SRT2
- Putative high mobility group B protein 11
- High mobility group B protein 15
- High mobility group B protein 10
- Histone deacetylase-related / HD-like protein
- NAD-dependent protein deacetylase SRT1
- Paired amphipathic helix protein Sin3-like 3
- Retinoblastoma-related protein 1
Sequence:
MASLADGGKRRVSYFYEPMIGDYYYGVNQPTKPQRIRVTHNLILSYNLHRHMEINHPDLADASDFEKFHSLEYINFLKSVTPETVTDPHPSVSENLKRFNVDVDWDGPVFHNLFDYCRAYAGGSISAAAKLNRQEADIAINWAGGMHHVKKDKASGFGYVNDVVLAILELLKSFKRVLYIEIGFPHGDEVEEAFKDTDRVMTVSFHKVGDTGDISDYGEGKGQYYSLNAPLKDGLDDFSLRGLFIPVIHRAMEIYEPEVIVLQCGADSLAGDPFGTFNLSIKGHGDCLQYVRSFNVPLMILGGGGYTLPNVARCWCYETAIAVGEQLDNDLPGNDYMKYFRPDYKLHILPTNRQNLNTRLDIITMRETLLAQLSLVMHAPSVPFQDTPSSSQATEAAEVDMEKRNDPRI
Protein: Pentraxin family member (Q7SZ53)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362112}.
Interaction partners:
Sequence:
MLLFFCLLSVTLAAAEVGLSGKTLLFPTATDTSYVKLSPRKPLSLSAFTLCMRVATELPAKREIILFAYRTPDDDELNVWREKDGRFSVYIQSSKDAAFFRLHPLSTFQTHLCVTWESATGLTAFWVDGQRSLHQVYRKGYSIRPGGTVLLGQDPDSYVGSFNAAQSFVGEITDLQMWDYVLSGTQIKAVYYNQDNRVKGNVFDWNTIKYDVTGNVLVVPDN
Protein: Ethylmalonyl-CoA decarboxylase (EC 4.1.1.94) (Enoyl-CoA hydratase domain-containing protein 1) (Methylmalonyl-CoA decarboxylase) (MMCD) (Q9NTX5)
Organism: Homo sapiens (Human)
Function: Decarboxylates ethylmalonyl-CoA, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:22016388}.
Interaction partners:
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 3
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Acyl-CoA synthetase short-chain family member 3, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
Sequence:
MALKQEMAKSLLKTASLSGRTKLLHQTGLSLYSTSHGFYEEEVKKTLQQFPGGSIDLQKEDNGIGILTLNNPSRMNAFSGVMMLQLLEKVIELENWTEGKGLIVRGAKNTFSSGSDLNAVKSLGTPEDGMAVCMFMQNTLTRFMRLPLISVALVQGWALGGGAEFTTACDFRLMTPESKIRFVHKEMGIIPSWGGTTRLVEIIGSRQALKVLSGALKLDSKNALNIGMVEEVLQSSDETKSLEEAQEWLKQFIQGPPEVIRALKKSVCSGRELYLEEALQNERDLLGTVWGGPANLEAIAKKGKFNK
Protein: Zinc finger protein ZIPIC (Zinc-finger protein interacting with CP190) (Q9VAB8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:25342723}. Chromosome {ECO:0000269|PubMed:25342723}. Note=On polytene chromosomes of third-instar larvae colocalizes with Cp190. {ECO:0000269|PubMed:25342723}.
Interaction partners:
- Insulator binding factor 2
- Insulator binding factor 1, isoform A
- Centrosome-associated zinc finger protein Cp190
- Boundary element associated factor
- Modifier of mdg4
- Early boundary activity protein 2
Sequence:
MNCCICQFSVRVPKDIHTDTVGHPPVLISELVLQCTRGTNYVLTEESSTICKKCCEKLARYHKSIQIARKLRGEILELIHSPYMSKDHKQTSYKEDDLDRETTISKFDGNIEEAQQQDEEEQELESVGTTVTLVGPAGIVEEVAEEEHTFIIKQSEEEDEFHSVDLELDIDNEIIINEEEAHEVEEVAHEIEEVAHEIEEEDLLPHDKQEAQEEDFFKEDTMSDFDEHLDGAIEYIISDGEDQEQDNESSGEYTVNIQCPSCPEKFSSRRAYNVHTKREHFPGYVCDQCGKTLQSYSGFIGHLQNHEPVKQFACPVCPERFSRKFRLKHHMAWHSGETPYQCDVCSKRFVHKVALYKHKMIHDSETKRLECQVCGFKTRTKAHLERHMRSHTGDKPFACPVCNKRFSQMYNMKAHLREHESPGTNRHRRFHCSKCTHTFINEQNYDAHVQRDDCTPV
Protein: Expressed protein (WRC protein) (P93743)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- E3 ubiquitin-protein ligase RMA
- Chaperone DnaJ-domain superfamily protein
- Nudix hydrolase 23, chloroplastic
- At2g42060
- Chaperone DnaJ-domain superfamily protein
- Tetratricopeptide repeat
- Shaggy-related protein kinase iota
- Protein ABIL2
- Chaperone DnaJ-domain superfamily protein
Sequence:
MRIRKRQVPLPLSSLLPVPLSDLYFNRSPTATARYFRGGYKDGGDDFGSLQLSLPPPSQISDRLIQRDLIKKKEEVKALDDDNGDVDVKSRTDASGSKNVNPRGESVSSIQVVEKNEKVVSLRKRRGFINFEDYEDEEDEEASGGGGRINKGKKKAKKSGGGLEEGSRCSRVNGRGWRCCQQTLVGYSLCEHHLGKGRVRSMNKSGGGRGGEKKAVVVEVKKKRVKLGMVKARSISSLLGQTSTSGGTSGDVDQGEISAPADQFAACDK
Protein: Uncharacterized protein C29A3.21 (Q9C0X0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MLRYNFRYLHNVLSHTVVFCFTEVSLHIVKQLGVESYACTVHASRFQKSYSASIDYCQRFLFSSNLKHNYVNLNIIFTSCIFRSLREFLRFYIAAIMCFL
Protein: 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) (CNPase) (EC 3.1.4.37) (P16330)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (By similarity). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.
Subcellular location: Membrane {ECO:0000269|PubMed:18076147}; Lipid-anchor {ECO:0000269|PubMed:18076147}. Melanosome {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane structures of brain white matter.
Interaction partners:
- Myelin basic protein
- Myelin-associated glycoprotein
- Myelin proteolipid protein
- Myelin-oligodendrocyte glycoprotein
- Oligodendrocyte transcription factor 2
- Glial fibrillary acidic protein
- Platelet-derived growth factor receptor alpha
- Galactocerebrosidase
- Myelin-associated oligodendrocyte basic protein
- Outer dynein arm-docking complex subunit 4
Sequence:
MNTSFTRKSHTFLPKLFFRKMSSSGAKEKPELQFPFLQDEDTVATLHECKTLFILRGLPGSGKSTLARLILEKYHDGTKMVSADAYKIIPGSRADFSEAYKRLDEDLAGYCRRDIRVLVLDDTNHERERLDQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRHFISGDEPKEKLELVSYFGKRPPGVLHCTTKFCDYGKAAGAEEYAQQEVVKRSYGKAFKLSISALFVTPKTAGAQVVLTDQELQLWPSDLDKPSASEGLPPGSRAHVTLGCAADVQPVQTGLDLLDILQQVKGGSQGEAVGELPRGKLYSLGKGRWMLSLTKKMEVKAIFTGYYGKGKPVPIHGSRKGGAMQICTII
Protein: Xyloglucan endotransglucosylase protein 34 (XET protein 34) (EC 2.4.1.207) (PttXET16-34) (PttXET16A) (Xyloglucan endotransglucosylase protein 16A) (XET protein 16A) (Xyloglucan endotransglucosylase/hydrolase protein 34) (XTH protein 34) (Q8GZD5)
Organism: Populus tremula x Populus tremuloides (Hybrid aspen)
Function: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Involved in early phases of secondary (S) cell wall formation in fibers of the xylem and phloem vascular tissues of wood stems. May play a role in restructuring primary cell walls, possibly creating and reinforcing the connections between the primary and S cell wall layers. Functions in the gelatinous (G) layers of the tension wood fibers that are involved in bending of the wood stems. May play a role in G fiber shrinking by repairing broken xyloglucan cross-links between G and S2 cell wall layers via its XET activity to maintain connections between the layers.
Subcellular location: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:12468728, ECO:0000269|PubMed:17504814}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. Cytoplasm {ECO:0000269|PubMed:12468728}. Note=Localizes to the cytoplasm of cambial cells. Localizes to the cytoplasm of xylem fibers in the early stages of secondary cell wall formation. {ECO:0000269|PubMed:12468728}.
Interaction partners:
Sequence:
MAAAYPWTLFLGMLVMVSGTMGAALRKPVDVAFGRNYVPTWAFDHIKYFNGGNEIQLHLDKYTGTGFQSKGSYLFGHFSMQMKLVPGDSAGTVTAFYLSSQNSEHDEIDFEFLGNRTGQPYILQTNVFTGGKGDREQRIYLWFDPTKEFHYYSVLWNMYMIVFLVDDVPIRVFKNCKDLGVKFPFNQPMKIYSSLWNADDWATRGGLEKTDWSKAPFIASYRSFHIDGCEASVEAKFCATQGARWWDQKEFQDLDAFQYRRLSWVRQKYTIYNYCTDRSRYPSMPPECKRDRDI
Protein: Dissimilatory sulfite reductase SirA (EC 1.8.99.-) (Q8EJI6)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Function: Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process. Required for sulfite respiration under anaerobic growth conditions. Does not contribute to nitrite reduction.
Subcellular location: Periplasm {ECO:0000250|UniProtKB:Q7MSJ8}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
- Menaquinol oxidase SirD
- Sulfurtransferase SirB
Sequence:
MKRWKTKTALGVLFCLGSAVSATTIASDAKSDGKVVPGVGNKQQTHYTQDILANPKVSENLMEKSRGVKTLQDYIVQEQELFDFLFENHPVFKYDAEGRLKGTYKVSDRGEEYLHGGDSVAYSKHSKEVNSTDGTAVRYSAYEDGQRPKALQYRLGAKSILDFPNKFVGPEKCGECHGPQYEKWRRSRHSKTIRFPGEHPEVDNDLKKPMYTTKDTSILPSGITPDAIYATVGTPRTKYGFIDAYLVRGTYHVKDGLLKDGTGTMVAGGNQFSRGWAEWLTPEMAAKINKAIPSFPLKMEDFGTSGSHQWGMSSYGAKYEKEFLFQPASSYCEMCHSFKFDFQTKEEFFAALGNPKELQKHTISKGITCEECHGAGGHLDGGIGGGMPSNCERCHQRFNFVEELAETPQGQEKLEYAFNVKMKSSCPSCGTEGSQMFASAHYDKGMRCSTCHDPHEVTDGDWKSGITKPKIIKECTDCHTAQAEIAKNTNTHSNQTCQSCHMPNMGSCENFTAIQFPDMAGFDNVRKSHMWKIDVDPLRKTLNPPEGKSRDATTKGWTVAKDENGYNYLDLMWTCARTSASDHDVTENKGCHSQFQSELEVGLHFEDQMEIYGEVQKWQKPVKDLFGQVLQGLQRIDKLLEVTQLPVDKKTEVLMLTDKAQDVIKLVEADGSWGAHGPRYTQKRLDAALTYVQQAQAIIDGNGYNAKM
Protein: 3-oxo-5-alpha-steroid 4-dehydrogenase 1 (EC 1.3.1.22) (SR type 1) (Steroid 5-alpha-reductase 1) (S5AR 1) (P18405)
Organism: Homo sapiens (Human)
Function: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Subcellular location: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Polyprenal reductase
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Aldo-keto reductase family 1 member D1
- Aldo-keto reductase family 1 member C3
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 17-beta-hydroxysteroid dehydrogenase type 3
- Aldo-keto reductase family 1 member C2
- 17-beta-hydroxysteroid dehydrogenase type 2
- 17-beta-hydroxysteroid dehydrogenase type 6
- Aldo-keto reductase family 1 member C1
Sequence:
MATATGVAEERLLAALAYLQCAVGCAVFARNRQTNSVYGRHALPSHRLRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTCNGYLQSRYLSHCAVYADDWVTDPRFLIGFGLWLTGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHEWYLRKFEEYPKFRKIIIPFLF
Protein: Centrocortin, isoform A (Centrocortin, isoform B) (LD41224p) (Q9VIK6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Centromeric protein-C, isoform A
- CENP-meta, isoform C
- Kinetochore protein NDC80
- Histone H3.3A
- Histone H3
- CENP-ana, isoform A
- Aurora kinase B
- Chromosome alignment defect 1
Sequence:
MEESNHGSAGCENVSQFMLDDLQLAAELGKTLLERNKELETFIKEYKIKGDEQELEILHLRKHINAMTEVNDSRLKVYEQLEVGIQDLERANQRLNLEKNRDKKQIKTLTTNTEVLEARCEELSQLLSDARQSLSTERRKVDQYQQERYRMQHSTEGSVSSHSIQSLCKEQSVEFSKLDVMAIANSTGLEDISFSNATMCERTAVKGEDNEELVKLLSEMEVLKRDFLAEQQRCTELEEQLVTIIQDNQGLQTRLLENSANEGTMSMHEEFSLLDDVRQGQMCSRCLRDINESNTNMDDQSSIAPTEEIYEDDDRSILSESTSKCDNSGADYKERFRIPEDLNPNSSDKPNPYRDLVEKYEALVEVKRTSNAVKSNFTSNPDGKTMTESSQGKKSETIVNSSKESDLMLDSTRKRTPTEFSESETTSSGFSDETSNKSTQTDERPSYFLCSISNGNDCKFSIYDDVSPIESHFRNRPEYRELFKEIFGVLKKAADNNEEDKLPSLHDDAQITEKLPLVAAKVPPVTPEREESPDDFIDDTQSVVSSVISNQSIAMSECVTKLERKTAKKHIFDVRNQQNQSSLTQSTLLNSSSKETTVGEPNYKPIRENGQILTPLKREPLEYLTVGVGIKKKNRRKHRNQSSSGDRIELFNSREFTPRNSPLAMNNRGGGQGSSKMCTDTLNAEFGRSNRRRTTPSSSNWNGSPMVIYNKNMNTPQTSRGRVIELNGVEFYHNTVSQDLHKLKKLDLSYAEVLRRADAGEHGPTRSHSQRQQHNGANIRKSHHHQFRQK
Protein: Countin-2 (Q8WSR7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Cell-counting factor that limits the minimum size of the multicellular structure. May up-regulate the expression of both gp24 and gp80, which mediate cell adhesion.
Subcellular location: Secreted {ECO:0000269|PubMed:11737154}.
Interaction partners:
Sequence:
MMIKYITIAILFIASLVKADLQFSLCPTCVDFINNDMGDLEKIISGGIATSCGAVCSLLPNNIEQGACNLLCDIVGIDEFLKVFNNIGEDADPVWICEELTVCPKNQNSNATVLTSDVSPASGPHGTTFTIGVAYKVESTLGTGEVAVMVTDPTGSNGFGDAQLIVNTQPGQYSTSFSFAATPSEDEQFPAGVYQVQLMICEGSCGAKHSVTFNSVYANFTVTSGPSVTGQMTGTGSGSGSGSGSSSGAAYLRY
Protein: Heterogeneous nuclear ribonucleoprotein K, isoform D (A1ZBW4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNFDRVYADEYGGYGTGSGSTRPSQRGNNRNGGGAGGVAGGAAGGNGGGFNAGGARGNAGGRGGADRFGGAAGGAVAGAGMGQRDNPFINPWANGGGGDVDGFGNNAGGAGGFAGNSFGGGAGGPFGGGSFGNNGFGGGPSDFGGNSGNFGQAQGTNSLPSLGSFSQNQGGTSSLPSLGSFGQNPGGPGGLGNGLSGGANGGVGTLGGANGAGGFNAVGGANGGPNGSPNAATNVPQGHDPNNSTQVTIPKELAGAIIGKGGGRIRRIRNESSAYITIDEPLPNSNDRIITISGTPKQIQMAQYLLQQRLVSQSE
Protein: Uncharacterized protein (Q57Z15)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVTLRYLRSKEEAEARRARLEEARRIANQIGVQRARTYAAQKREQARCIMKDLRTQWLLERQRESDLIDRMLYEAHARQGEGMKGAANLEAHQHEQAINELSAWGAEYALERERHKLALEKASVTRALQQEPQRRIIERKKAVRAAEEARAKVIVSKREKRSVPGFTGDDVARPSPLAGAYPQTMPTRLRKGKTRMEQPTNTVEWPAREDIVEDAAAAAAHYLEERQRAIESNHESVERKRREAAERAASLKRKQEEESKHAEEEMRRREKNLLALKQHATEGPRTEEVCTRMQDTRRSVALKSKGEAEFEAIFLRDTLGTEAKPRQLEDSVSFNTFERLLQLSTISSLLPTDADIVAQLPTTSLCVFADEDPEQSGELSSGFHATKRDSGDHVLRAAAATDDVEVESHAVTPTSGGEPPLLHPLKASEEVPPHPTSICDHSACDDDNSSTHTGSTDSTNKIEERSERREQFLTNLKLLQARLERAMGEVPPSNNPQGPPSQTNVTVSSMSSISTPPRREGGGGDFPSEDYKNMSSEGTSDVSFKSRDAGFSSASSAYTRTHPTMTAEQLKAALLRMKLRLHSEL
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJF0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Calcineurin subunit B
- Calmodulin
- Candida glabrata strain CBS138 chromosome G complete sequence
- Serine/threonine-protein phosphatase
- Calcium-channel protein CCH1
- Candida glabrata strain CBS138 chromosome E complete sequence
Sequence:
MGDNEEDRRKKFLNGLQLQPDQDNMFLDQYLDQAAELQRHLQGNNSMNGDVYEQDNNNHNFSTGQNILSESTFSPSSDMSNPVSNLFNSKSINFSDMPYEMGVGEETPNDDRDRQDSNQNNNNNLMNTPTLKIECFDEDGVFLPGDTTNDPFTQDSGPKYDSSQNINAGIVSDMNNFENMDSNFLDFGGDNQVSKEDGTYLDLYDNNLKNASTEKIASSNNLSVSRNSEDNLSRVSSTLNSPFMQPTDRSVSPILSPPVMYLGDHSHTDDNDDVVSILSNNSNILLPVNSHGYKYVTDFNQLGQLIGGDPFELDFNGDNDIINSNDLKVDAETLLNSENVHLQAPQPNNNSSNNNNVSSPSGSNKMPTTPIISIEEYDDNNKNSNDDEYAIDMDSSNALQENRGFLGISLLPAEDSDATHDEILQGRKQKLKNRRVSQSSSRRSSRSSMRSLTPEEKARSLSSNRNKLLEMADLLPKSPSSNNGSNNNSRRSSFYEESEDISMDTNISENNNTNNNTGTDYVCEVCGKVFSRPYNLKSHLRTHTDEKPYQCSICGKAFARQHDKKRHEDLHTGKKRYVCGGKLKDGTFWGCGKKFARSDALGRHFKTSSGRKCITPLYEETARERNLPSIDDTNIQATEMGVTLE
Protein: Peroxisome proliferator-activated receptor gamma coactivator 1-beta (PGC-1-beta) (PPAR-gamma coactivator 1-beta) (PPARGC-1-beta) (PGC-1-related estrogen receptor alpha coactivator) (Q86YN6)
Organism: Homo sapiens (Human)
Function: Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcriptional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energy expenditure. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:11854298}.
Interaction partners:
- Steroid hormone receptor ERR1
- Nuclear respiratory factor 1
- Sterol regulatory element-binding protein 1
- Estrogen-related receptor gamma
- Carbohydrate-responsive element-binding protein
- Peroxisome proliferator-activated receptor gamma
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 1
- MLX-interacting protein
- Mediator of RNA polymerase II transcription subunit 4
Sequence:
MAGNDCGALLDEELSSFFLNYLADTQGGGSGEEQLYADFPELDLSQLDASDFDSATCFGELQWCPENSETEPNQYSPDDSELFQIDSENEALLAELTKTLDDIPEDDVGLAAFPALDGGDALSCTSASPAPSSAPPSPAPEKPSAPAPEVDELSLLQKLLLATSYPTSSSDTQKEGTAWRQAGLRSKSQRPCVKADSTQDKKAPMMQSQSRSCTELHKHLTSAQCCLQDRGLQPPCLQSPRLPAKEDKEPGEDCPSPQPAPASPRDSLALGRADPGAPVSQEDMQAMVQLIRYMHTYCLPQRKLPPQTPEPLPKACSNPSQQVRSRPWSRHHSKASWAEFSILRELLAQDVLCDVSKPYRLATPVYASLTPRSRPRPPKDSQASPGRPSSVEEVRIAASPKSTGPRPSLRPLRLEVKREVRRPARLQQQEEEDEEEEEEEEEEEKEEEEEWGRKRPGRGLPWTKLGRKLESSVCPVRRSRRLNPELGPWLTFADEPLVPSEPQGALPSLCLAPKAYDVERELGSPTDEDSGQDQQLLRGPQIPALESPCESGCGDMDEDPSCPQLPPRDSPRCLMLALSQSDPTFGKKSFEQTLTVELCGTAGLTPPTTPPYKPTEEDPFKPDIKHSLGKEIALSLPSPEGLSLKATPGAAHKLPKKHPERSELLSHLRHATAQPASQAGQKRPFSCSFGDHDYCQVLRPEGVLQRKVLRSWEPSGVHLEDWPQQGAPWAEAQAPGREEDRSCDAGAPPKDSTLLRDHEIRASLTKHFGLLETALEEEDLASCKSPEYDTVFEDSSSSSGESSFLPEEEEEEGEEEEEDDEEEDSGVSPTCSDHCPYQSPPSKANRQLCSRSRSSSGSSPCHSWSPATRRNFRCESRGPCSDRTPSIRHARKRREKAIGEGRVVYIQNLSSDMSSRELKRRFEVFGEIEECEVLTRNRRGEKYGFITYRCSEHAALSLTKGAALRKRNEPSFQLSYGGLRHFCWPRYTDYDSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH
Protein: EBNA1 binding protein 2 (EBNA1 binding protein 2, isoform CRA_a) (EBNA1BP2 protein) (Q6IB29)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MDTPPLSDSESESDESLVTDRELQDAFSRGLLKPGLNVVLEGPKKAVNDVNGLKQCLAEFKRDLEWVERLDVTLGPVPEIGGSEAPAPQNKDQKAVDPEDDFQREMSFYRQAQAAVLAVLPRLHQLKVPTKRPTDYFAEMAKSDLQMQKIRQKLQTKQAAMERSEKAKQLRALRKYGKKVQTEVLQKRQQEKAHMMNAIKKYQKGFSDKLDFLEGDQKPLAQRKKAGAKGQQMRKGPSAKRRYKNQKFGFGGKKKGSKWNTRESYDDVSSFRAKTAHGRGLKRPGKKGSNKRPGKRTREKMKNRTH
Protein: Rhomboid-type serine protease (EC 3.4.21.105) (A0A1D8PFE0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362115}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362115}.
Interaction partners:
- Band 7 domain-containing protein
Sequence:
MPLNTPYPVEKNTFNISDEDDDFPTRNLNESSPLTQSTKRYMKQDFANSVTSLPSLPPKPSHLQPQNRPQHQQQQQQQQYPYGNLSAKQSNKHKQMFENSVPETNKKDYLGNTTTVRELPPIPDNEKLHSKNPFSDSRYASRDYDDVDLPPSPPHSDPFRNDEISDDDSHSDLKHKMKRNEKNRIRSLRRKPRFHYTKLPYFTMVISLIQIIVFIVELAKMAHLTGSAFQTKPYFNPMLGPSTFLLINMGARYVPCMHQIKDITDDTSILFPCANSTSVDTYVCSLSELCGLTKLKLSSDGSAYLPDQWYRIFIPIFLHAGFLHIIFNLLLQVTMGSSIERNIGIIKYAIIYISSGIGGFLLGANFTPQGIASTGASGALFGIVATNIILFIYTGKKNTNMYGTKHYALFICIMIGEIVISLVLGLLPGLDNFSHIGGFAMGILSSIVVLKDPFWVFIDGIITYPKNPSTWQQFLNNWNPMYSIEDKIRSRFFIWCGVRIIALILMIIYLVLLCKNFFNNDINRGNNCKWCKYFNCIPVKGWCDIGQVSVTSTTTTSDSNSNSNSNSNPTTTASSSSSSVPTTRYSTMTYTTSMPSSVENPKSNTNSEGTNGGLRKRFASSFTGGNSGGTANIAARAGGDIQQQYGIGSGLYVIVIFFTISFLKKKKII