wanglab/gogpt-training-data huggingface dataset:
Protein: S-adenosyl-L-methionine-dependent methyltransferases superfamily protein (Q9M266)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTTFSTSFLFLLLVFCLIGSLAADDLQHKSGRDVCSGGSDLRTPDIRLNRPTDSVVGNCPTEASPLVMADDEKYGNKMVISLTPRLYDYVLNNVREHEILKQLREETAISQIQVSPDQAQLLAMLVEILGAKRCIEVGVYTGYSSLAVALVLPESGRLVACDKDANALEVAKRYYELAGVSHKVTVKHGLAAESLMSMIQNGEESSYDFAFLDADKAMYQEYFESLLRLVRVGGVIVIDNVLWHGWVADSTVNDERTISLRNFNKKLMDDQRVSISMVSIGDGMTICRKR
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (F1REJ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MQKKKDPLLVECQPDSKDETMVPVLTSKKASELPVNEVACALQADLQFGLNREEVERRRTYHGWNEFDISEDEPLWKKYLSQFKDPLILLLLSSAVISVLMRQFDDAVSITVAIIIVVTVAFVQEYRSEKSLEELGKLVPPECHCIREGHLEHLLARELVPGDTVCLSVGERVPADLRLFESTDLAVDESSLTGETTPCTKTSAPQPAATNGDIASRSNIAFMGTLVRCGKAKGIVIGTGEDSEFGEVFKMMQAEEAPKTPLQKSMDLLGKQLSLYSLGIIGVIMFVGWLQGKYILDMFTIGVSLAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLSCCNVICSDKTGTLTKNEMTVTHLFTSDGQHAEVTGIGYNNSGEILMDGEVVHGISNTSISKIVEVGCVCNDAMIRHNTLMGRPTEGALIALAMKMGLEGLQHEFVRLEEIPFTSEQKWMAVRVVHRTQRDKPGLFYVKGAYEQVIRFCTSYNSKGVTMPLNNQQRDFYQQQKSYMGSGGLRVLAFASGSEMGSLTFLGLVGIIDPPRAGVKEAVATLISSGVAVKMVTGDSEETAVAIASRLGLYTKGSQCLSGDEVDQMDIQHLSQIVHRVVVFYRASPRHKLKIVKSLQNIGAVVAMTGDGVNDAVALKAADIGVAMGQTGTDVCKEAADMILVDDDFQTILSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLATLLNFPTPLNAMQILWINIIMDGPPAQSLGVEPVDWDVIRKPPRNVRDSIITRSLIVKILVSAFIIVCGTLFVFWRELRDNEITPRDTTMTFTCFVFFDMFNALSSRSQTRMVHEMGLCSNRMFCYAVLGSIMGQLLVIYFPPLQSVFQTESLSILDLLLLFGLTSSVCVVSEIIKKIERLRCGSEKMSDMDSEFHDV
Protein: Baicalin-beta-D-glucuronidase (EC 3.2.1.167) (Baicalinase) (Q9LRC8)
Organism: Scutellaria baicalensis (Baical skullcap)
Function: Beta-glucuronidase involved in the initiation of H(2)O(2) metabolism via the production of baicalein. Unable to use glycyrrhizin, gypsogenin-3-O-D-glucuronide, luteolin-7-O-D-glucoside and apigenin-7-O-D-glucoside as substrates.
Interaction partners:
Sequence:
MGFQVWQKGLCVLCFSLIFICGVIGEETTIVKIEENPVAQTDENYVCATLDLWPPTKCNYGNCPWGKSSFLNLDLNNNIIRNAVKEFAPLKLRFGGTLQDRLVYQTSRDEPCDSTFYNNTNLILDFSHACLSLDRWDEINQFILETGSEAVFGLNALRGKTVEIKGIIKDGQYLGETTTAVGEWDYSNSKFLIEYSLKKGYKHIRGWTLGNELGGHTLFIGVSPEDYANDAKKLHELVKEIYQDQGTMPLIIAPGAIFDLEWYTEFIDRTPELHVATHHMYNLGSGGDDALKDVLLTASFFDEATKSMYEGLQKIVNRPGTKAVAWIGEAGGAFNSGQDGISNTFINGFWYLNMLGYSALLDTKTFCRQTLTGGNYGLLQTGTYIPNPDYYSALLWHRLMGSKVLKTEIVGTKNVYIYAHCAKKSNGITMLVLNHDGESSVKISLDPSKYGSKREEYHLTPVNNNLQSRLVKLNGELLHLDPSGVIPALNPVEKDNSKQLEVAPYSFMFVHLPGPTMFSACEKPAGK
Protein: Zcf17p (A0A1D8PCF5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MTKTTVQRRRHTNSKLGCLNCKRKKVRCDESLPECKNCVKGKKETCSYLSLSTQEIQKIKLTHSLRNSQNKLLDQKYRLPASGAATTSSKRSSSSSSNETRIGKDADAFPSGDILDFKFELKNLPINIPSIVYPPLQFDNIFINDFNGDGVVHNDVNKTSEDDEEDQEVYEEVSGNGRNHSSLTGLNKLDNGVYAPVTFNCLDRRIFRRVLPENVKTKVAADFSFHVVLGKNNLLDHLSDMMLDTPTTAHRNVFSESFLCLGETIILKVFNKRQKILGTYSRSELNFISWLNKKCLDRHGFCQEEIKKLIASFHKNLGKITSWELEKQIHLGAYVSYLLNFVVLMLKFGAQAYFDSSKGIFQSFEAFLAYVEKYTISPSTTVDFLMNNIQYNIMSINVPSYPPQFLFEIESNLRSLEFVFIRPTVFKDESINERFQKIEYHFKSLLKFFSGYVLPIVYASRDENSVSIYPPQAIYEIFQEWHTNVPSETMSHHQSIDANNPSESEFLNDLSTTLYMYYYAVAAALDAVFPGCKYLYGVSFMLPTNKFYRNMKIMTISKDNYYLERLYPFKVDILLQRHVFYASRLFAFFRRRFCFYHNYTDWSSPFDDRLKKNRFKSRTIRNSFEVPIHSFNNTLIRPEHYPLRDEKVALESIEGYPIFTREDETVKQQIYTRNIETLDFFNLSQILQYDCESMLLLRDYRPFDDQIGLTRSTLSMDVIKDYYNDKTVILDSLFSSNR
Protein: Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) (15-hydroxyprostaglandin dehydrogenase [NADP(+)]) (EC 1.1.1.196, EC 1.1.1.197) (20-beta-hydroxysteroid dehydrogenase) (Alcohol dehydrogenase [NAD(P)+] CBR1) (EC 1.1.1.71) (NADPH-dependent carbonyl reductase 1) (Prostaglandin 9-ketoreductase) (PG-9-KR) (Prostaglandin-E(2) 9-reductase) (EC 1.1.1.189) (Q28960)
Organism: Sus scrofa (Pig)
Function: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Carbonyl reductase 2
- Aldo-keto reductase family 1 member C3
- Prostaglandin E synthase
- Prostaglandin E synthase 3
- Aldo-keto reductase family 1 member B1
- Cytochrome P450 family 1 subfamily A member 1
- Prostaglandin E synthase 2
- Cytochrome P450
- Cytochrome P450 2E1
- Dihydrofolate reductase
Sequence:
MSSNTRVALVTGANKGIGFAIVRDLCRQFAGDVVLTARDVARGQAAVKQLQAEGLSPRFHQLDIIDLQSIRALCDFLRKEYGGLDVLVNNAAIAFQLDNPTPFHIQAELTMKTNFMGTRNVCTELLPLIKPQGRVVNVSSTEGVRALNECSPELQQKFKSETITEEELVGLMNKFVEDTKNGVHRKEGWSDSTYGVTKIGVSVLSRIYARKLREQRAGDKILLNACCPGWVRTDMGGPKAPKSPEVGAETPVYLALLPSDAEGPHGQFVTDKKVVEWGVPPESYPWVNA
Protein: Microsomal triglyceride transfer protein large subunit (O08601)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B. May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:33168624}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}. Golgi apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P55157}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:17312007}. Golgi apparatus {ECO:0000269|PubMed:17635917}.
Interaction partners:
- Apolipoprotein B-100
- Protein disulfide-isomerase
- Apolipoprotein A-I
- Hepatocyte nuclear factor 4-alpha
- Apolipoprotein A-IV
- Apolipoprotein C-III
- Diacylglycerol O-acyltransferase 1
- Sterol regulatory element-binding protein 1
- Apolipoprotein A-II
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Sequence:
MILLAVLFLCFFSSYSASVKGHTTGLSLNNERLYKLTYSTEVFLDGGKGKPQDSVGYKISSDVDVVLLWRNPDGDDDQVIQVTITAVNVENAGQQRGEKSIFQGKSTPKIIGKDNLEALQRPMLLHLVRGKVKEFYSYENEPVGIENLKRGLASLFQMQLSSGTTNEVDISGDCKVTYQAQQDKVVKIKALDTCKIERSGFTTANQVLGVSSKATSVTTYKIEDSFVTAVLAEETRAFALNFQQTIAGKIVSKQKLELKTTEAGPRMIPGKQVAGVIKAVDSKYKAIPIVGQVLERVCKGCPSLAEHWKSIRKNLEPENLSKAEAVQSFLAFIQHLRTSRREEILQILKAEKKEVLPQLVDAVTSAQTPDSLEAILDFLDFKSDSSIILQERFLYACGFATHPDEELLRALLSKFKGSFASNDIRESVMIIIGALVRKLCQNEGCKLKAVVEAKKLILGGLEKPEKKEDTTMYLLALKNALLPEGIPLLLKYAEAGEGPVSHLATTVLQRYDVSFITDEVKKTLNRIYHQNRKVHEKTVRTTAAAVILKNPSYMDVKNILLSIGELPKEMNKYMLTVVQDILHFEMPASKMIRRVLKEMAVHNYDRFSKSGSSSAYTGYVERSPRAASTYSLDILYSGSGILRRSNLNIFQYIGKAELHGSQVVIEAQGLEGLIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPVSVVKGLILLIDHSQDIQLQSGLKANMEIQGGLAIDISGSMEFSLWYRESKTRVKNRVAVVITSDVTVDASFVKAGVESRAETEAGLEFISTVQFSQYPFLVCMQMDKAEAPLRQFETKYERLSTGRGYVSRRRKESLVAGCELPLHQENSEMCNVVFPPQPESDNSGGWF
Protein: Rfa2p (Q59Z33)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Replication protein A subunit
- Serine/threonine-protein kinase MEC1
- Replication factor A protein 3
- DNA primase
- DNA repair and recombination protein RAD52
- DNA primase large subunit
- DNA polymerase alpha subunit B
- DNA polymerase
- Proliferating cell nuclear antigen
- Histone H1
Sequence:
MSDFEYDNNNTGAFGNISQGGFNTEHAGSSQRQTTTQVRQSLTPVTIKQINDATQPVPDGEFKVNNVELNMISFVGVVRNVENTNASIAVTIEDGTGSIDVRKWVDETISSAEEDFEKYNEMKGKYVYVGGSLKQFNNRKTVQNASISLITDSNQIVYHHLSAIEHHLKAQGITAADAASAGAGQATNSTASAGSGLFMDNPTSLSKDTGSLTDQVIAVLKEASRTMPDGVPVDYVAEKLSITKEESQFQLLKLNDEGKAYAGYDDNSYLVI
Protein: Transcription factor PHYTOCHROME INTERACTING FACTOR-LIKE 13 (OsPIL13) (PIF-like protein 13) (Basic helix-loop-helix protein 152) (OsbHLH152) (OsPIL1) (Q10CH5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor that may act as negative regulator of phyB-dependent light signal transduction. Transcription activator that acts as positive regulator of internode elongation. May function via regulation of cell wall-related genes. May play a role in a drought-associated growth-restriction mechanism in response to drought stress.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21549224, ECO:0000269|PubMed:22984180}.
Interaction partners:
- DELLA protein SLR1
- Protein SLENDER RICE1-LIKE 1
- Phytochrome B
- Phytochrome A
- Protein SLENDER RICE1-LIKE 2
- Os04g0618600 protein.
- Two-component response regulator-like PRR1
Sequence:
MAICSTDNELVELLWHNGGVVAQPQAAQARVVSSSGRGQSASVLTGDDTETAAWFPDTLDDALEKDLYTQLWRSVTGDAFPAAAAAGPSSHHAPPPDLPPPAARPPMRSGIGSSWTGDICSAFCGSNHIPETAAQRCRDAGAALPPERPRRSSTHDGAGTSSSGGSGSNFGASGLPSESASAHKRKGREDSDSRSEDAECEATEETKSSSRRYGSKRRTRAAEVHNLSERRRRDRINEKMRALQELIPHCNKTDKASILDEAIEYLKSLQMQVQIMWMTTGMAPMMFPGAHQFMPPMAVGMNSACMPAAQGLSHMSRLPYMNHSMPNHIPLNSSPAMNPMNVANQMQNIQLREASNPFLHPDGWQTVPPQVSGPYASGPQVAQQNQIPKASASTVLPNSGAEQPPTSDGI
Protein: Methylenetetrahydrofolate reductase 2 (EC 1.5.1.53) (YmL45) (P53128)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Methylenetetrahydrofolate reductase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, cytosolic
- Methylenetetrahydrofolate dehydrogenase [NAD
- Serine hydroxymethyltransferase, mitochondrial
- Aminomethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, mitochondrial
- Thymidylate synthase
- S-adenosylmethionine synthase 2
Sequence:
MKITEKLEQHRQTSGKPTYSFEYFVPKTTQGVQNLYDRMDRMYEASLPQFIDITWNAGGGRLSHLSTDLVATAQSVLGLETCMHLTCTNMPISMIDDALENAYHSGCQNILALRGDPPRDAENWTPVEGGFQYAKDLIKYIKSKYGDHFAIGVAGYPECHPELPNKDVKLDLEYLKQKIDAGGDFIITQMFYDVDNFINWCSQVRAAGMDVPIIPGIMPITTYAAFLRRAQWGQISIPQHFSSRLDPIKDDDELVRDIGTNLIVEMCQKLLDSGYVSHLHIYTMNLEKAPLMILERLNILPTESEFNAHPLAVLPWRKSLNPKRKNEEVRPIFWKRRPYSYVARTSQWAVDEFPNGRFGDSSSPAFGDLDLCGSDLIRQSANKCLELWSTPTSINDVAFLVINYLNGNLKCLPWSDIPINDEINPIKAHLIELNQHSIITINSQPQVNGIRSNDKIHGWGPKDGYVYQKQYLEFMLPKTKLPKLIDTLKNNEFLTYFAIDSQGDLLSNHPDNSKSNAVTWGIFPGREILQPTIVEKISFLAWKEEFYHILNEWKLNMNKYDKPHSAQFIQSLIDDYCLVNIVDNDYISPDDQIHSILLSL
Protein: Isocitrate lyase (ICL) (EC 4.1.3.1) (Isocitrase) (Isocitratase) (Q9I0K4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
Interaction partners:
- Malate synthase G
- Aconitate hydratase A
- Aconitate hydratase B
- Isocitrate dehydrogenase kinase/phosphatase
- Glyoxylate carboligase
- Glycolate oxidase iron-sulfur subunit
- 2-dehydro-3-deoxy-phosphogluconate aldolase
- Probable 2-hydroxyacid dehydrogenase
- Glycerate dehydrogenase
- Glycolate oxidase subunit GlcD
Sequence:
MSAYQNEIKAVAALKEKNGSSWSAINPEYAARMRIQNRFKTGLDIAKYTAAIMRKDMAEYDADSSVYTQSLGCWHGFIGQQKLISIKKHLKTTNKRYLYLSGWMVAALRSDFGPLPDQSMHEKTAVSGLIEELYTFLRQADARELDLLFTGLDAARAAGDKAKEAELLAQIDNFETHVVPIIADIDAGFGNAEATYLLAKKMIEAGACCIQIENQVSDEKQCGHQDGKVTVPHIDFLAKINAVRYAFLELGVDDGVIVARTDSLGAGLTKQIAVTNEPGDLGDLYNSFLDCEEISESELGNGDVVIKREGKLLRPKRLASNLFQFRKGTGEDRCVLDCITSLQNGADLLWIETEKPHVGQIKAMVDRIREVIPNAKLVYNNSPSFNWTLNFRQQVFDAFVAEGKDVSAYDRNKLMSVEYDDTELAKVADEKIRTFQRDGSAHAGIFHHLITLPTYHTAALSTDNLAKGYFADEGMLAYVKGVQRQELRQGIACVKHQNMAGSDIGDNHKEYFAGEAALKASGKDNTMNQFH
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) (O55143)
Organism: Mus musculus (Mouse)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:32973183}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:22355118}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000269|PubMed:32973183}.
Interaction partners:
- Phospholamban
- Histidine rich calcium binding protein
- Calreticulin
- Calreticulin
- Protein S100-A1
- Sarcolipin
- Calnexin
- A-kinase anchor protein 7 isoform gamma
- Ryanodine receptor 2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
Sequence:
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDTCSLNEFSITGSTYAPIGEVQKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKIMSVIREWGSGSDTLRCLALATHDNPLKREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELSPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFDGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEQPGKECVQPATKSSCSLSACTDGISWPFVLLIMPLVVWVYSTDTNFSDMFWS
Protein: LD14485p (Q8T0B0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPTQEAQQTWQSLGLMPVADDTLNELLANPKVAQALASPASAHPKLLVAFSEPLCESTAQFEENGALRAQTREKLLGISKPALLSLVTHGIVYDKVLGILQEKKLNISRDPKLGPIAEFRKEYVNNPQFRAEINTICPQPPMTPIKSPPGTPFNSPLPLKNPVQIRMGAQMRQDTPMRRVKFGGVSTIVYDCGLPANTDYDRDPVFAQILQAEPLKHAFQEARAGRAPSSVVISNIPAPVASLAELRGLNPATRAQLQSVGLDKNMLQSAVSNAPYYDRLFRSLHDKGISHDQCHLLQPMKQVHDWLLDDDQLLDEIDKVFADMANGCKDISYPKPSLGELPTSQSSDSGFHSKPPTPGYGSEDLTAGQGRFASIPGIEDMNMYPSCAGMPEQFQQLRLHGDEASGKNSTRTILCADCNQPIAMGEVAVKADRAGKEIAWHPGCFKCITCRELLADLVYFFHQGQVFCGRDLAIRLKIPRCRACDELIFTKEYTAAEEATFHIKHFCCYQCDEPLAGQQYIADEKSNMPLCLLCYDRLFAVRCQRCKVAIGPADQGVAWGDVHWHASCFVCAGVQCSKPLIGGRFCVKENMPFCSPTCVRSLIN
Protein: Serine/arginine-rich splicing factor RS2Z32 (RS-containing zinc finger protein 32) (At-RS2Z32) (At-RSZ32) (AtRSZ32) (Serine/arginine-rich splicing factor RSZ34) (AtRSZ34) (Q9FYB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in intron recognition and spliceosome assembly.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Serine/arginine-rich splicing factor SC35
- Uncharacterized protein At2g39795
- RNA-binding protein Y14
- Serine/arginine-rich splicing factor SR45
- Serine/arginine-rich-splicing factor SR34
- Serine/arginine-rich SC35-like splicing factor SCL28
- Serine/arginine-rich splicing factor SR30
- Serine/arginine-rich splicing factor SR34B
- Protein mago nashi homolog
- Serine/arginine-rich SC35-like splicing factor SCL30
Sequence:
MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFSDPRDADDARYYLDGRDFDGSRITVEASRGAPRGSRDNGSRGPPPGSGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPSPKKARQGGSYSRSPVKSRSPRRRRSPSRSRSYSRGRSYSRSRSPVRREKSVEDRSRSPKAMERSVSPKGRDQSLSPDRKVIDASPKRGSDYDGSPKENGNGRNSASPIVGGGESPVGLNGQDRSPIDDEAELSRPSPKGSESP
Protein: Bystin (Q13895)
Organism: Homo sapiens (Human)
Function: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. May be required for trophinin-dependent regulation of cell adhesion during implantation of human embryos.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17381424}. Nucleus, nucleolus {ECO:0000269|PubMed:17381424, ECO:0000269|PubMed:26711351}. Note=Associated with 40S ribosomal subunits.
Interaction partners:
- U3 small nucleolar RNA-associated protein 4 homolog
- RRP12-like protein
- Dimethyladenosine transferase
- Small ribosomal subunit protein eS6
- U3 small nucleolar RNA-associated protein 15 homolog
- RNA-binding protein PNO1
- U3 small nucleolar RNA-associated protein 6 homolog
- DDB1- and CUL4-associated factor 13
- KRR1 small subunit processome component homolog
- WD repeat-containing protein 46
Sequence:
MPKFKAARGVGGQEKHAPLADQILAGNAVRAGVREKRRGRGTGEAEEEYVGPRLSRRILQQARQQQEELEAEHGTGDKPAAPRERTTRLGPRMPQDGSDDEDEEWPTLEKAATMTAAGHHAEVVVDPEDERAIEMFMNKNPPARRTLADIIMEKLTEKQTEVETVMSEVSGFPMPQLDPRVLEVYRGVREVLSKYRSGKLPKAFKIIPALSNWEQILYVTEPEAWTAAAMYQATRIFASNLKERMAQRFYNLVLLPRVRDDVAEYKRLNFHLYMALKKALFKPGAWFKGILIPLCESGTCTLREAIIVGSIITKCSIPVLHSSAAMLKIAEMEYSGANSIFLRLLLDKKYALPYRVLDALVFHFLGFRTEKRELPVLWHQCLLTLVQRYKADLATDQKEALLELLRLQPHPQLSPEIRRELQSAVPRDVEDVPITVE
Protein: Even-skipped homeobox 1 (F8W9J5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESRKDMVVFLDGGQLGTLVGKRVSNLSEAVGSPLPEPPEKMVPRGCLSPRAVPPATRERGGGGPEEEPVDGLAGSAAGPGAEPQVAGAAMLGPGPPAPSVDSLSGQGQPSSSDTESDFYEEIEGPAPRRWSAVRTEGARPPRATAAVVGAARKAPWRAAPVTRCVVTAPPSPESRLRGWRRNSTGRTTYPGRGDVSWRPP
Protein: ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit) (P9WPU9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00815}.
Interaction partners:
- ATP synthase epsilon chain
- ATP synthase subunit c
- ATP synthase subunit a
- ATP synthase subunit b-delta
- ATP synthase subunit alpha
- ATP synthase subunit beta
- ATP synthase subunit b
- Inorganic pyrophosphatase
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Small ribosomal subunit protein uS3
Sequence:
MAATLRELRGRIRSAGSIKKITKAQELIATSRIARAQARLESARPYAFEITRMLTTLAAEAALDHPLLVERPEPKRAGVLVVSSDRGLCGAYNANIFRRSEELFSLLREAGKQPVLYVVGRKAQNYYSFRNWNITESWMGFSEQPTYENAAEIASTLVDAFLLGTDNGEDQRSDSGEGVDELHIVYTEFKSMLSQSAEAHRIAPMVVEYVEEDIGPRTLYSFEPDATMLFESLLPRYLTTRVYAALLESAASELASRQRAMKSATDNADDLIKALTLMANRERQAQITQEISEIVGGANALAEAR
Protein: Cyclin J, isoform B (GH04281p) (Q95U62)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEQKVAAEQNIFVVDRKLKKTCPQADVERLAKTHWLTDYARDIFLTMREQELSRRPLFYLSPQLNERRRMLQLLKLATSAHKLSRCALHLAVYYMDRFVDYYKIRPDKLLLVAITCLHIAAQIENTDAFIPRYSEMNRLVKNAYTAFEYKAVERKILCFLNFELIRPTTASFVELFACSFLTRSDFKNYIEMLDEYERNHHTQPYQRYISFEEMLSILAQLLLRMADYTLYNLPTICHPFWLPPALLQFARSAGSGAGRST
Protein: ABC transporter family G domain-containing protein (D7SFK1)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Nuclear receptor domain-containing protein
- ADP-ribosylation factor-like protein 1
Sequence:
MSSEDVRIETPEDDESSGRDSIYFSTIRSRHAEHFFADMQNHNTQNEKKGIIRYLEYYEINSQSTRPYPNLLLNKLSFSKDLRSSSDKVLLRLPVLKQEVHNISFELSSSDVLAIMYTKESETISLLKIICGIKDVRGKLSGDILVNGHRMSRDRLEKTIGFVSLESPTSTLSVRQYLHVHGNFYPPMTERYGGVGHLINKLMTDLGLFPVSDIICSRLNRSQWQRVKVASQLVRDPTILVCSDIFKDIDVHDQCFLIDYLREWAVKTNRIVIMAISPTSLQILNMFSKAMILASGRMIYFGPPKSMQQYFETIGCPCPPYKNVCDYYVDLVTHDNLTSDASRESSVRIARLVNKWNQTAPPVRRTASGKFLLDLPTAGIFMNLLTLISLFWFNFINNRASRIFFLLFIFSLSTCLSLHLSDLSLTLPDAFLNRNSYLELLIFYVPLFIGLVNLKKCTFLSEFDKFYLFISARHHLKELLKLSPLKNMCSSLSIIIVSFVVELPFLLITSMVFAMPMSIFTDFHQKSSNHLTSLVSISSSFFINLSVTQLVVNSVSNLSSEPLSFFFFVISWFSLFFACGFPFPIHSILKYFNPLFFPTTSVFRFLYEDSPSLYPQLSVNLSTPIQLYSCGRTFLNTTQVTRGPCQKVSSFELLSYYGFNESFDKQKSIFHGILISNFIFNYLFFSILILFVSCVLFHFNRDKLIRRSST
Protein: Protocadherin gamma-A9 (PCDH-gamma-A9) (Q9Y5G4)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin gamma-A8
- Protocadherin gamma-A4
Sequence:
MAAPTKCQLRGRLVLLCSLLGMLWEARASQIRYSVPEETEKGYIVGNISKDLALEPRELAERRVRIVSRGRTQLFSLNPRSGTLVTAGRIDREELCAQSPRCLVNFKVLVEDRVKLYGIEIEVTDINDSAPKFQAESLEVKINEIAVPGARYPLPEAIDPDVGVNSLQSYQLSPNHHFSLNVQTGDNGAINPELVLERALDREEATAHHLVLTASDGGEPRRSSTVRIHVTVLDTNDNAPVFAQRIYRVKVLENVPPGTWLLTATASDLDEGINGKVAYKFWKINEKQSLLFQLNENTGEISTAKSLDYEECSFYEMEIQAEDGGGLKGWTKVLISVEDVNDNRPEVTITSLFSPVREDAPQGTVILLFNAHDRDSGKNGQVVCSIQENLSFTLENSEEDYYRLLTAQILDREKASEYNITVTATDRGTPPLSTEIHITLQVTDINDNPPAFSQASYSVYLPENNARGTSIFSVIAYDPDSNENSRVIYSLAEDTIQGSPLSTYVSINSDTGVLYALCSFDYEQFRDLQMQVTASDSGSPPLSSNVSLRLFVLDQNDNAPEILYPALPTDGSTGVELAPRSAEPGYLVTKVVAVDRDSGQNAWLSYRLFKASEPGLFSVGLHTGEVRTARALLDRDALKQSLVVAVQDHGQPPLSATVTLTVAIADSIPDILADLGSLQIPADLEASDLTLYLVVAVAVVSCVFLTFVITLLALRLRHWHSSHLLRATSDGLAGVPTSHFVGVDGVRAFLQTYSQEFSLTADSRKSHLIFPQPNYADTLISQQSCEKNEPLCVSVDSKFPIEDTPLVPQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Ras modification protein ERF4 (Hyperactive Ras suppressor protein 5) (P41912)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The ERF2-SHR5 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12379641}; Peripheral membrane protein {ECO:0000269|PubMed:12379641}.
Interaction partners:
- Palmitoyltransferase ERF2
- Ras-like protein 2
- Palmitoyltransferase AKR1
- Palmitoyltransferase SWF1
- Palmitoyltransferase PFA3
- Palmitoyltransferase PFA4
- Palmitoyltransferase PFA5
- Serine palmitoyltransferase 1
- Phosphatidylinositol-3-phosphatase SAC1
- Serine palmitoyltransferase 2
Sequence:
MCDSHQKEEDNANTSERALFFNYHEFSYSFYEDLGSEDAKPTEHDEDHKLCITHFPNVYAARGSAEFQVTRVVRVPRRFDESRSSLETPQFSTQLPGSEPAAIVGDDGTSFVRCGRYDIGDHVFGCSSVSPLSEYLSAAELAEVVHRVNGFLLREEGEVFGWRNLSGLLLDMLTGGLWSWVLGPLLSRPVFQESLALEQYVAQLNSPGGLLHERGVRLVLPRRSGCLSLDFVVPRPK
Protein: Caspase 2 (Caspase-2 isoform X1) (A0A288CG41)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLGECGMTKWERLALRRNSVKMLQDLVVDDLLIQCLQQDGILTDSMAESIMAKPTSQGRSHQLLFLLPKRGPRAFSTFCSALKETEQHHLCKLLMDFTEKDKCFSEPSLSLPTQECVTPAKRPRTHESMEMCLDADSPVTTAVLPCTPEFYQSHRPQAYPMRSCPRGLALVLSNVRFDSANTDLDIRRGGEVDEETLRRLFTELDFKVSLHRDLTAEAMRRCLEQFAQQQEHAAYDCAVVCLLSHGVEGSVYGTDGQLLELDWVFEVFDNARCPLLQNKPKMFFIQACRGEEMDNGVDQLDGQERTQSPGCEQRDAGREGERDNREKKEEKERERLRVKLPQRSDMICGFATLKGFSTAAMRNTKKGSWFIQELNTAIRQRANNTHLSDILVQVNGQIKSREGYAPGSAHHRCKEMSEFTSSLCKDLYLFPKYYPSN