wanglab/gogpt-training-data huggingface dataset:
Protein: Histone H2A type 1-D (Histone H2A.3) (Histone H2A/g) (P20671)
Organism: Homo sapiens (Human)
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 H2B type 1-O
- Histone H2B type 1-H
- Histone H2B type 1-C/E/F/G/I
- Histone H2B type 1-B
- Histone H2B type 2-E
- Histone H4
- Histone H2B type 1-D
- Histone H3.1
- Histone H2B type 1-M
- Histone H2B type 1-N
Sequence:
MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
Protein: Proteasome regulatory non-ATP-ase subunit 3 (Q8WRU6)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MQTTGELTLKQQLQQSGSKGNDELLGRLMSLYRALCVRHDEVGQEMLLNDILALLTLNHQHDLAERVIATCEISLPHRSNNQAARYFYYVGLTHALRLGYVEADQFLQYALRKAPERASGFRVAATKLSLVVQLLLGEIPPRSDFLQKDMRECLSPYLQLTSCVRFGQLGRFMSILQQHKAIFEHDRTYSLILRVRQHVIRTGLRRICQAYSRISIPDVCAKLSMENPDDAEYIIAKAIRSGVIDAVIDHEQRHLISSETVDVYSTSEPLLALQRRIQFLNATHNEVKRSMRYSAADPDLEEERRKVDREEMDSLLRAIEDEELGGADFEDGLP
Protein: DNA damage-inducible protein DIN7 (EC 3.1.-.-) (Q12086)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 5'->3' double-stranded DNA exonuclease.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA mismatch repair protein MSH2
- DNA repair protein RAD51
- Proliferating cell nuclear antigen
- ATP-dependent helicase SGS1
- Large ribosomal subunit protein mL67
- DNA damage response protein kinase DUN1
- DNA mismatch repair protein MLH1
- Ribonucleoside-diphosphate reductase small chain 1
- Cell division control protein 6
- Cell division control protein 45
Sequence:
MGIPGLLPQLKRIQKQVSLKKYMYQTLAIDGYAWLHRASCACAFELVMNKPTNKYLQFFIKRLQLLKRLKIKPYIVFDGDSLFVKNHTETRRRKKRLENEMIAKKLWSAGNRYNAMEYFQKSVDITPEMAKCIIDYCKLHSIPYIVAPFEADPQMVYLEKMGLIQGIISEDSDLLVFGCKTLITKLNDQGKALEISKDDFSALPENFPLGELSEQQFRNLVCLAGCDYTSGIWKVGVVTAMKIVKRYSEMKDILIQIERTEKLCFSKAFKQQVEFANYAFQYQRVFCPLSNQITTLNNIPKAVTNSHAEIIKIMKCIGSVVERGSGVRKDVINTKNIDHKVHEMIAKGELHPVDMASKLINRERKLKARKLFKVGLLGGESNSFNKKVEQPLVDTQDVLSERENSLDNKNASSIYMTSPAAISGTVPSIF
Protein: Zinc finger protein 778 (Q96MU6)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAAPDLAHGGHVSRDSVCLHEEQTQAAGMVAGWLINCYQDAVTFDDVAVDFTQEEWTLLDPSQRDLYRDVMLENYENLASVEWRLKTKGPALRQDRSWFRASNETQTARSHNGGQLCDRTQCGEAFSEHSGLSTHVRTQNTGDSCVSNHYERDFFIPCQKTLFKIGEQFSVLGQCGKAFSSTPNVVSQQACTRDRSLDYSSCGEVFLNQSYLQARAGSHNGEETWKWKPCGKALTHSMGCATPVEMHAVRNPHVCRECGKAFRYTAYLTGRVQVHPGEKPCELEECGKASPVSSSLTQHVRIHAAEKPCECKECGKAFTGLSGLSKHVQTDPGQKPYECKDCGKACGGFYLLNEHGKTHTREKPFACVVCGKYFRNSSCLNNHVRIHTGIKPYTCSYCGKAFTVRCGLTRHVRTHTGEKPYTCKDCGKAFCTSSGLTEHVRTHTGEKPYECKDCGKSFTVSSSLTEHARIHTGEKPYECKQCGKAFTGRSGLTKHMRTHTGEKPYECKDCGKAYNRVYLLNEHVKTHTEEKPFICTVCRKSFRNSSCLNKHIQIHTGIKPYECKDCGKTFTVSSSLTEHIRTHTGEKPYECKVCGKAFTTSSHLIVHIRTHTGEKPYICKECGKAFASSSHLIEHRRTHTGEKPYICNECGKAFRASSHLHKHGRIHTGQKPYKCKECGKAYNRFYLLKEHLKTYTEEQVFVCKDCGKSFKNSSCLNHHTQIHTDEKPF
Protein: Keratin, type I cytoskeletal 25 (Cytokeratin-25) (CK-25) (Keratin-25) (K25) (Keratin-25A) (K25A) (Type I inner root sheath-specific keratin-K25irs1) (Q7Z3Z0)
Organism: Homo sapiens (Human)
Function: Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs) (By similarity). Plays a role in the cytoskeleton organization.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8VCW2}.
Interaction partners:
- Keratin, type I cytoskeletal 27
- Keratin, type II cytoskeletal 71
- Keratin, type I cuticular Ha5
- Keratin, type II cytoskeletal 74
Sequence:
MSLRLSSASRRSCPRPTTGSLRLYGGGTSFGTGNSCGISGIGSGFSSAFGGSSSGGNTGGGNPCAGFTVNERGLLSGNEKVTMQNLNDRLASYLDSVHALEEANADLEQKIKGWYEKFGPGSCRGLDHDYSRYFPIIDDLKNQIIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIETYCLLIGGDDGACKSGGYKSKDYGSGNVGSQVKDPAKAIVVKKVLEEVDQRSKILTTRLHSLEEKSQSN
Protein: Cytochrome c oxidase assembly protein COX14 (P39103)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the synthesis of yeast cytochrome oxidase.
Subcellular location: Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- Protein MSS51, mitochondrial
- Cytochrome c oxidase assembly factor 3, mitochondrial
- Uncharacterized protein YPR153W
- Cytochrome c oxidase assembly factor 1
- Cytochrome oxidase assembly protein SHY1
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 4, mitochondrial
Sequence:
MSKYAWYTRVTDTLHRLTVLTLVGGTLYMSGGLAYTLYMNGKKYEQQVTQQKALEEDNQQLQSPTAPPTE
Protein: Nuclear transcription factor Y subunit B-9 (AtNF-YB-9) (Protein LEAFY COTYLEDON 1) (Q9SFD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters. Acts as a central regulator of the embryogenesis. Required for the speciation of cotyledon identity and the completion of embryo maturation. Controls seed storage protein genes through the regulation of FUS3 and ABI3. Involved in the blue light (BL) and abscisic acid (ABA) signaling pathways.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- B3 domain-containing transcription factor LEC2
- Nuclear transcription factor Y subunit C-2
- B3 domain-containing transcription factor FUS3
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit A-1
- Nuclear transcription factor Y subunit A-5
- Nuclear transcription factor Y subunit C-4
- B3 domain-containing transcription factor ABI3
Sequence:
MERGAPFSHYQLPKSISELNLDQHSNNPTPMTSSVVVAGAGDKNNGIVVQQQPPCVAREQDQYMPIANVIRIMRKTLPSHAKISDDAKETIQECVSEYISFVTGEANERCQREQRKTITAEDILWAMSKLGFDNYVDPLTVFINRYREIETDRGSALRGEPPSLRQTYGGNGIGFHGPSHGLPPPGPYGYGMLDQSMVMGGGRYYQNGSSGQDESSVGGGSSSSINGMPAFDHYGQYK
Protein: Flagellar Member 7 (Q380Z7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSIAASSARKDGPHHPSSGLTGKETLQDARKMEYRASTLEAGGNDMECLQLMETALQIRCKEYGTGSSSPELLKEACDAAERVVMKCNVLGVKLFKEGKYDVATPLFGYAMEMTGEGSFPLRKDDERRRLLRGVTLNNHGCMERHRGHFTTALDYMQQSMQCTGQQSPVAFLNISAVQVQLRLCEEAAHSAVCAIQSLGPNPEDPSLLAVAHHNLAMALELIDPPRAHEEYRLALGLAQNTISRRSEVTRTIESNMQRFVMVLHECRPGNSALTGTNSPRSSCGHTLFVSPRSCSRERSPSGRDAASRTHRVDIFPHPFAVSAKETVAKRSISRPARADAGHPPSAAAAAATAPGVNSKTSLSRPAAWQSQTNGGSASHGSGLKGGNSTKSGGASPNASRLPPISQGSRATLRESGGPSEHHRGANVGEQSKSLTKNNERVSNKGGVALSVATRSPVAATRMPYKREATARPGDVGSQGKGAGFADNESVHTKSNAKSGASRSECRPPMKGSMRSNISLSQPNAQSSPVSVGATGSNQRTPGQRNSPKGRTQSAAVEPSAPSRPTQQAVGGRSAVGRKLSPNAERTRPVAQSPAARDSSGRKMQSVAADPDAPFLYNQQAGGTGNKTGRRVSSSARESSPSSRPTHQAVGGRSAVGRKLSPNAERTRPVAQSPAARDSSGRKMQSVAADPDAPFLHNQQAGGTGNKTGRRVSSSARESSPSSRPTHQAAATHDATKKKLHTVTMEVEGAARRGQHAADAHSAVGRLSPNAPSNDTGSPVRKFPQPKASPFSAAKDKQGRSPISKSSVMGPGVPPLSVDAPSRRIQGLPPGANLVTYVVDRLDMLLFDEEDLWRKSGCAVTIQRAYRAFKARQLFEAVKSKSARDRVLDGVRRSIAARKIQRTFRRHLSIRSGSTARYKNRDVLANEINRAAVRIQCCARQWRARRRLARRQFLKNNASSAAFRLQTWWRKVMATRRVEKLREMHQLVKNEVALRERQEVAATVIQSQWRRRRAEQQTREARLRAARLRRRHLEARYLSAARKIQKAWRLYISRKELNKMRELRAAREERLREHQRRCDAAKKLQAFGRRIIVARNAGPLLDVARENAARRIRGHCLQSRAASKIQRAYRLYRSKSLLKRMKKERRRQLLDSRLSAFAFTMQRIGRAYFVRLSLGRSLYQMAVEVQEFVRRERDLEEANRSSTVVSGHHRVHEPSSVRGGLEGVPFMRRSLPDGCTNDRHHSALSPTPLDVMPKVKGSLTSHRSVCQLLPSPAEDSRLPKPLANGAGRLLPLAGDEQIERLPGVGGLGSASGAVQEEPAISCQQVPEKPTPRAEGVKLELTMPCSPGDVGVVPELQHLATPIIPEERVGLSLIKEHAMYSEPGERPALYLEGVEPSATELNLDINEPVGEFARPDNGGHSAEEIVKPLGHEGIDRSFDVVGECEVVGHQEKSALGAALAEEREKWRQVRKDEIKFYNDCCNSRLEANEYRLRKIAEAETAEEVLTLLPRPPLMRQRPVAPRRTYSKSAESSSNLQSQHRSQDEEANNLRDQAALAITRLARGYLARLHYRVLRELFADYVNCRIGVDRSESPDLEYKELQKCSRLVMDGTDQFRRLRRVNVVLSFLRAKVSMMHVSCRMPPRTPRQFAERPQPECVSNVGDALEVLKGFMRIIQSKKEVASRRAAATINRRNEEPLEALEVLNGLALIFRAKQERRARKDAIEARMAQQEGMCSVLEKPSSTIESFLLCAVARRELQRRRSLVEERRRLSAACEKILPFMQMHLARREVERRKALVEERRRHSAACEKILPLMQMHLARCEVERRRSLVEERRRHSAACEKILPSMQMHLARCEVERRRSLVEERRRHSAACEKILPFMRMYLARREVERRKALVEERRRLSAACEKILPFMRMYLARREVERRKALVEEKRVTDSDAECLLDEAAMKVQRAFRSYKARRSVKERLVAKERYWGSIQAHDEEIAAAVAAIVSDSPEGADLWASLGHYYYQVTTQKVGSVGDSASIADQYVVVMQQHMRGLASWKLVQALRSEQRPPRGAL
Protein: Beta-2-microglobulin (Q91966)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKSILSIVVLGLIYSAVEAKESPPKVQVYSRNPGNFGDKNTLICHVSGFHPPDISIQLLKNGVEIPDAKQTDLAFEQGWQFHLTKSVGFTPASGEEYTCRVRHLKNLKTYTWEADM
Protein: Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) (Q23651)
Organism: Caenorhabditis elegans
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Interaction partners:
- Elongator complex protein 2
- Elongator complex protein 1
- Elongator complex protein 4
- Elongator complex protein 5
- Cytoplasmic tRNA 2-thiolation protein 1
- Tetraspanin-17
- Protein KTI12 homolog
- Diphthamide biosynthesis protein 3
- DNA replication licensing factor mcm-5
- Cytoplasmic tRNA 2-thiolation protein 2
Sequence:
MDQKGSQRALLAQTINEIVKLLIEAHNQKKDVNLNRLKCIVAQKNGLSFQPKLVDIIAGVPSDYKDSLLPKLKAKPVRTASGIAVVAVMSKPHRCPHINFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPYLQTRGRLNQLMQLGHSVDKVEFIVMGGTFMSLPEDYRDFFIRNLHDALSGHTSASVEEAVAYSERSKMKCIGITIETRPDYCLPRHLNDMLLYGCTRLEIGVQSTYEDVARDTNRGHTVKSVCETFHMAKDTGYKVVIHMMPDLPNVGLERDKEQFLELFESPAFRPDGLKLYPTLVIRGTGLYELWKTGRYQSYPPSVLVDLIATILSLVPPWTRVYRVQRDIPMPLVSSGVEHGNLREHAMAKMKELGLKCRDVRTREVGIQEIHNKVRPEDVELIRRDYTANGGWETFISYEDPKQDILIGLLRLRKISDKAHRPELKGNVSVVRELHVYGSVVSVADRDPKKFQHQGYGSLLMEEAERIAREEHGSDKIAVISGVGTREYYRKLGYELDGPYMSKMLDSAAA
Protein: Helix-turn-helix domain-containing protein (O53221)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTADWVVTFTFDADPSMETMDAWETQLEGFDALVSRVPGHGIDVTVYAPGDWSVFDALAKMAGEVMPVVQAKSPIAVQIISEPEHRLRAEAFTTPELMSAAEIADELGVSRQRVHQLRSTAGFPAPLADLRGGAVWDAAAVRRFAETWERKPGRPHTGTAKFAYSWAVGPAVGRSGKAPNVRWRVENPDKIRFVLRNIGDDIAEDVEIDLSRIDAITRNVPKKTVIRPGEGLNMVLIAAWGHPLPNQLYVRWAGQDEWAAVPLHPAH
Protein: Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1) (O54834)
Organism: Mus musculus (Mouse)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Holocytochrome c-type synthase
Sequence:
MSAQSLLHSVFSCSSPASGGTASAKGFSKRKLRQTRSLDPALIGGCGSEMGAEGGLRGSTVSRLHSPQLLAEGLGSRLASSPRSQHLRATRFQTPRPLCSSFSTPSTPQEKSPSGSFHFDYEVPLSRSGLKKSMAWDLPSVLAGSGSASSRSPASILSSSGGGPNGIFSSPRRWLQQRKFQPPPNSRSHPYVVWRSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLGCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQREEQKDASSDFVSSLLPFGNKKQNKELSSSNSSLSSTSETPNESTSPNTPEPAPRARRRGAMSVDSITDLDDNQSRLLEALQLSLPAEAQSKKEKARDKKLSLNPIYRQVPRLVDSCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGVDVCLEEEHSVHDVAALLKEFLRDMPDPLLTRELYTAFINTLLLEPEEQLGTLQLLIYLLPPCNCDTLHRLLQFLSIVARHADDNVSKDGQEVTGNKMTSLNLATIFGPNLLHKQKSSDKEYSVQSSARAEESTAIIAVVQKMIENYEALFMVPPDLQNEVLISLLETDPDVVDYLLRRKASQSSSPDILQTEVSFSMGGRHSSTDSNKASSGDISPYDNNSPVLSERSLLAMQEDRARGGSEKLYKVPEQYTLVGHLSSPKSKSRESSPGPRLGKEMSEEPFNIWGTWHSTLKSGSKDPGMTGSYGDIFESSSLRPRPCSLSQGNLSLNWPRCQGSPTGLDSGTQVIRRTQTAATVEQCSVHLPVSRVCSTPHIQDGSRGTRRPAASSDPFLSLNSTEDLAEGKEDVAWLQSQARPVYQRPQESGKDDRRPPPPYPGSGKPATTSAQLPLEPPLWRLQRHEEGSETAVEGGQQASGEHQTRPKKLSSAYSLSASEQDKQNLGEASWLDWQRERWQIWELLSTDNPDALPETLV
Protein: Septin homolog spn5 (Mei4-dependent protein 9) (Meiotic expression up-regulated protein 28) (P48010)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Septin-like protein involved in the correct orientation of forespore membrane extension during sporulation.
Subcellular location: Nucleus. Forespore membrane; Peripheral membrane protein. Note=The sporulation-specific septin complex associates to the forespore membrane and forms partial or complete ring-like structures that curl around each haploid nucleus.
Interaction partners:
- Septin homolog spn2
- Septin homolog spn6
- Septin homolog spn7
- Septin homolog spn4
- Septin homolog spn3
- Septin homolog spn1
- Sporulation protein kinase mde3
- Meiotically up-regulated gene 126 protein
- Meiotic expression up-regulated protein 23
- Sporulation protein kinase pit1
Sequence:
MDSSNLSSSMPQEGQLKLTEEAIITIKQVDESSAKRSVSNESRKSKDVTRKEQIASDQQGDDQCPQSDTAKDKKTEFKQDEVPNSNGKSIPTFHPCNNIGINDFNHQHYSRVCRNGIDINLIVVGESSLGKTTFVNSFLQSNDTNFRPKKTMDFVEHKATLSDGDQKFNLTIVDTPGFGDKSDNSNCWRPIATNLLHRLNAYFQNEVKMDRETSEIDSRIHGCLFFINPNGHRLQPLEIYIMKKIDQFVNIIPVIGKADTMTSDELNHFKKRVIADMVREKIRYFREPHNEKKAKIPIPFAIVGAGAPIEHDGKCIRGRAYPWGLVDIDDPKQSDFCQLRNFLLYTHIEGLKHKTHKLIYDTFRTEKLVALNATPGSQFISAEEMNQKYISEQTQLVEEALTKVMKEKYREKENNLELLETNLKTHHKDYKHALKKRITALEEEKNRLIKEIGPEKVKKAGILA
Protein: 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) (P14773)
Organism: Drosophila melanogaster (Fruit fly)
Function: Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation. Provides spatial information during embryogenesis to guide migrating primordial germ cells (the pole cells) from the ectoderm to the mesoderm. Also required for association of the pole cells with the gonadal mesoderm.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- Mevalonate kinase
- Farnesyl pyrophosphate synthase
- isopentenyl-diphosphate Delta-isomerase
- UbiA prenyltransferase domain-containing protein 1 homolog
- LP12374p
- E3 ubiquitin-protein ligase HRD1
- Diphosphomevalonate decarboxylase
- Protein TRC8 homolog
- Quemao, isoform A
Sequence:
MIGRLFRAHGEFCASHPWEVIVALLTITACMLTVDKNNTLDASSGLGTATASAAAAGGSGSGAGSGASGTIPPSSMGGSATSSRHRPCHGWSQSCDGLEAEYNAADVILMTIVRCTAVLYCYYQFCSLHRLGSKYVLGIAGLFTVFSSFIFTTAIIKFLGSDISELKDALFFLLLVIDLSNSGRLAQLALSGSNQAEVTQNIARGLELLGPAISLDTIVEVLLVGVGTLSGVQRLEVLCMFAVLSVLVNYVVFMTFYPACLSLIFDLSRSGVDMSVVREKAKGSLLLKSLTEEEQKANPVLQRVKLIMTTGLMAVHIYSRVAFSGSDYDAVDKTLTPTLSLNVSNNRTESGEIADIIIKWLTMSADHIVISIVLIALVVKFICFDNRDPLPDQLRQSGPVAIAAKASQTTPIDEEHVEQEKDTENSAAVRTLLFTIEDQSSANASTQTDLLPLRHRLVGPIKPPRPVQECLDILNSTEEGSGPAALSDEEIVSIVHAGGTHCPLHKIESVLDDPERGVRIRRQIIGSRAKMPVGRLDVLPYEHFDYRKVLNACCENVLGYVPIPVGYAGPLLLDGETYYVPMATTEGALVASTNRGCKALSVRGVRSVVEDVGMTRAPCVRFPSVARAAEAKSWIENDENYRVVKTEFDSTSRFGRLKDCHIAMDGPQLYIRFVAITGDAMGMNMVSKGAEMALRRIQLQFPDMQIISLSGNFCCDKKPAAINWIKGRGKRVVTECTISAATLRSVLKTDAKTLVECNKLKNMGGSAMAGSIGGNNAHAANMVTAVFLATGQDPAQNVTSSNCSTAMECWAENSEDLYMTCTMPSLEVGTVGGGTGLPGQSACLEMLGVRGAHATRPGDNAKKLAQIVCATVMAGELSLMAALVNSDLVKSHMRHNRSSIAVNSANNPLNVTVSSCSTIS
Protein: NDT80 domain-containing protein (Q5A6P1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Transcription factor NDT80
- Protein kinase
- Rep1p
- Ngs1p
Sequence:
MTNLSFHRKQKSKNKACNLDFKSDSVLELLNSKSKVAPRSGLQFKVGPPFQDTIQVSQLFIKESHQKIVPVLNARIDRGFDLTNNEWVGYKRNYFSVVASFSFEEYEINKSILPKNGFFIVSGEKEYQVKQFAIRLVSKSVQDNTEISLIQHTAKRDRGPISEPPIVPVITGSIPSHIVVKEGSNIRKISKIRQFDSLFFQDYKTLPILQSGSILNNYDKNKDYVKVVKYERIQFSSAINCKKQSITEKKRFILQIQLLAALSGENTYAIIAISNTPSLIIRGRSPSSYNSRGEGIEQSQNTECEEDVQSFLTTTANDKYTVYPESRDLGELSIMDNLYKNKENFEILKSYDSMDSYTINTIMSSEATASNWLDCSKLDFEEHSKLELQGGFPDVNIYSSPGPTPGLLEQESDPESLEPSYFLMKARTKYLQNPDNMIVGCQKTFSNEFFNHRKQAANLAYKIFEDGVEDDESDLDIVSKYVTPSDVMTA
Protein: Large ribosomal subunit protein eL43B (60S ribosomal protein L43-B) (L37B) (O94686)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL22
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS3
Sequence:
MTKRTKKVGVTGKYGVRYGASLRRDVRKIEVQQHSRYQCPFCGRLTVKRTAAGIWKCSGKGCSKTLAGGAWTVTTAAATSARSTIRRLREMVEV
Protein: tRNA-dihydrouridine(47) synthase [NAD(P)(+)] (EC 1.3.1.89) (mRNA-dihydrouridine synthase dus3) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 3) (Q9UTH9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the synthesis of dihydrouridine, a modified base, in various RNAs, such as tRNAs and mRNAs. Modifies the uridine in position 47 (U47) in the D-loop of tRNAs. Also able to mediate formation of dihydrouridine outside of the D-loop of tRNAs. Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation. Dus3-mediated dihydrouridylation of the mRNA encoding alpha-tubulin nda2 is required for meiotic chromosome segregation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06053}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- Ribosome biogenesis protein erb1
- Pseudouridine-metabolizing bifunctional protein C1861.05
- tRNA
- tRNA
Sequence:
MAELETGAVPIREEFLVKQDGNKKRKRKERGQNKRREKIHVKENNALCPAISIGNECPYKENCKFPHDVEAYLATKAPDIGDKCPIFERYGVCPAGFKCRWLAGHVVINADGKYELIKKPDGQFTLFTVNTVGKEVQRKLRTKQLDLSKAESIISAVLGEEKPDPSSKVSNIPEENRDATSAISEGKETESVSLEETGVLKNQTVSVNVDLKEISSQARSNIALPTLRPQEKNLIDWRDRKILAPLTTVGNPPFRRLCGSLGADTFYSEMAMCYPLMQGHQPEWALVRGLNYEREMMRGGRRGILGVQLATGKLWQATKTAQVIAEQCDGVDFLDLNCGCPIDLVFRQGAGSSLLENPGRLLRNLQGMDAVSGQIPVTVKLRMGNKDDHPVVKNLIGRIFNETNTSAATLHGRSRQQRYSKNANWDYIGEIASKVKSMNERIDELPEDSLRTQPLSLIGNGDCYSWQDWYDGVNKGVDTVMIARGALVKPWIFEEIEARQFIDKSSTQRLEMLEQYCNNGLEYWGSDSQGVNTTRRFFLEFMSFFHRYTPIALYEVQRPRLNDRPPLYTARDEMETLLASNKVTDWVKLSEFFLGPTPERFTFTPKHKSNSVEEAEG
Protein: Ubiquitin-like protein ATG12 (Autophagy-related protein 12) (APG12-like) (Q9CQY1)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes.
Subcellular location: Cytoplasm {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:O94817}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94817}. Note=TECPR1 recruits the ATG12-ATG5 conjugate to the autolysosomal membrane. {ECO:0000250|UniProtKB:O94817}.
Interaction partners:
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy-related protein 16-1
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagy protein 5
- Mitochondrial antiviral-signaling protein
- WD repeat domain phosphoinositide-interacting protein 2
- Antiviral innate immune response receptor RIG-I
- Microtubule-associated protein 1 light chain 3 beta
- Protein Atg16l2
Sequence:
MSEDSEVVLQLPSAPVGAGGESLPELSPETATPEPPSSAAVSPGTEEPPGDTKKKIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHYCKSQAWG
Protein: Sentrin-specific protease 3 (EC 3.4.22.-) (SUMO-1-specific protease 3) (Sentrin/SUMO-specific protease SENP3) (Q9H4L4)
Organism: Homo sapiens (Human)
Function: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Deconjugates SUMO2 from KAT5.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:19680224}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224}. Cytoplasm {ECO:0000250|UniProtKB:Q9EP97}. Note=Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress (PubMed:19680224). Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). {ECO:0000250|UniProtKB:Q9EP97, ECO:0000269|PubMed:19680224}.
Interaction partners:
- Testis-expressed protein 10
- Proline-, glutamic acid- and leucine-rich protein 1
- Ribosomal biogenesis protein LAS1L
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- WD repeat-containing protein 18
- Histone-lysine N-methyltransferase 2A
- WD repeat-containing protein 5
- Retinoblastoma-binding protein 5
- Polynucleotide 5'-hydroxyl-kinase NOL9
Sequence:
MKETIQGTGSWGPEPPGPGIPPAYSSPRRERLRWPPPPKPRLKSGGGFGPDPGSGTTVPARRLPVPRPSFDASASEEEEEEEEEEDEDEEEEVAAWRLPPRWSQLGTSQRPRPSRPTHRKTCSQRRRRAMRAFRMLLYSKSTSLTFHWKLWGRHRGRRRGLAHPKNHLSPQQGGATPQVPSPCCRFDSPRGPPPPRLGLLGALMAEDGVRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGQSGPEGERSLAPPDASILISNVCSIGDHVAQELFQGSDLGMAEEAERPGEKAGQHSPLREEHVTCVQSILDEFLQTYGSLIPLSTDEVVEKLEDIFQQEFSTPSRKGLVLQLIQSYQRMPGNAMVRGFRVAYKRHVLTMDDLGTLYGQNWLNDQVMNMYGDLVMDTVPEKVHFFNSFFYDKLRTKGYDGVKRWTKNVDIFNKELLLIPIHLEVHWSLISVDVRRRTITYFDSQRTLNRRCPKHIAKYLQAEAVKKDRLDFHQGWKGYFKMNVARQNNDSDCGAFVLQYCKHLALSQPFSFTQQDMPKLRRQIYKELCHCKLTV
Protein: Guanine nucleotide-binding protein G(T) subunit gamma-T1 (Transducin gamma chain) (P02698)
Organism: Bos taurus (Bovine)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Rhodopsin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
- GNB4 protein
- Regulator of G-protein signaling 9
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Sequence:
MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPLVKGIPEDKNPFKELKGGCVIS