wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (ALDOS) (Aldosterone-synthesizing enzyme) (CYPXIB2) (Corticosterone 18-monooxygenase, CYP11B2) (EC 1.14.15.5) (Cytochrome P-450Aldo) (Cytochrome P-450C18) (Cytochrome P450C11) (Steroid 11-beta-hydroxylase, CYP11B2) (EC 1.14.15.4) (Steroid 18-hydroxylase) (P15539)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase that catalyzes the biosynthesis of adrenal mineralocorticoid aldosterone. Catalyzes three sequential oxidative reactions of 11-deoxycorticosterone/21-hydroxyprogesterone, namely 11-beta hydroxylation followed with two successive oxidations at C18 to yield 18-hydroxy and then 18-aldehyde derivatives, resulting in the formation of aldosterone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 11-beta-hydroxysteroid dehydrogenase type 2
- Steroid 21-hydroxylase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 11-beta-hydroxysteroid dehydrogenase 1
- 17-beta-hydroxysteroid dehydrogenase type 3
- Aromatase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
Sequence:
MALRVTADVWLARPWQCLHRTRALGTTATLAPKTLQPFEAIPQYSRNKWLKMIQILREQGQENLHLEMHQVFRELGPIFRHSVGKTQIVSVMLPEDAEKLHQVESMLPRRMHLEPWVAHRELRGLRRGVFLLNGPEWRLNRLRLNRNVLSPKAVQKFVPMVDMVARDFLETLKEKVLQNARGSLTMDVQQSLFNYTIEASNFALFGERLGLLGHDLSPGSLKFIHALHSMFKSTSQLLFLPKSLTRWTSTRVWKEHFDAWDVISEYANRCIWKVHQELRLGSSQTYSGIVAELISQGSLPLDAIKANSMELTAGSVDTTAIPLVMTLFELARNPDVQKALRQESLAAEASIAANPQKAMSDLPLLRAALKETLRLYPVGGFLERILSSDLVLQNYHVPAGTLVLLYLYSMGRNPAVFPRPERYMPQRWLERKRSFQHLAFGFGVRQCLGRRLAEVEMMLLLHHILKTFQVETLRQEDVQMAYRFVLMPSSSPVLTFRPVS
Protein: Beta-adaptin-like protein C (At-bC-Ad) (At-betaC-Ad) (AP complex subunit beta-C) (Adaptor protein complex AP subunit beta-C) (Beta-adaptin C) (Clathrin assembly protein complex beta large chain C) (O81742)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of clathrin-associated adaptor protein complex that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with the trans-Golgi network. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (By similarity). {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit sigma
- AP-4 complex subunit epsilon
- AP-2 complex subunit mu
- AP-2 complex subunit alpha-1
- Clathrin heavy chain 2
- AP-1 complex subunit gamma-1
- AP-2 complex subunit alpha-2
- AP-1 complex subunit gamma-2
- AP-1 complex subunit sigma-1
- AP-1 complex subunit sigma-2
Sequence:
MSGHDSKYFSTTKKGEIPELKEELNSQYKDKRKDAVKKVIAAMTVGKDVSSLFTDVVNCMQTENLELKKLVYLYLINYAKSQPDLAILAVNTFVKDSQDPNPLIRALAVRTMGCIRVDKITEYLCDPLQKCLKDDDPYVRKTAAICVAKLFDINAELVEDRGFLEALKDLISDNNPMVVANAVAALAEIQENSTSPIFEINSTILTKLLTALNECTEWGQVFILDALSRYKASDPREAENIVERVTPRLQHANCAVVLSAVKMILQQMELITSTDVIRNLCKKMAPPLVTLLSAEPEIQYVALRNINLIVQKRPTILAHEIKVFFCKYNDPIYVKMEKLEIMIKLASDRNIDQVLLEFKEYATEVDVDFVRKAVRAIGRCAIKLERAAERCISVLLELIKIKVNYVVQEAIIVIKDIFRRYPNTYESIIATLCESLDTLDEPEAKASMIWIIGEYAERIDNADELLESFLENFPEEPAQVQLQLLTATVKLFLKKPTEGPQQMIQVVLNNATVETDNPDLRDRAYIYWRLLSTDPEAAKDVVLAEKPVITDDSNQLDPSLLDELLANISTLSSVYHKPPEAFVTRLKTTVQKTEDEDYVEGSETGYPEASGNPVDGAASPSATTGYVTKLAAAPAPVPDLLGDLMGSDNAAIVPVDEPTTPSGRPLPVVLPASKGQGLQISAQLTRQDGQVFYSMLLENNSQSLLDGFMIQFNKNSFGLAAVGSLQVPPLQPGASARTMMPMVLSQNMSTGSTSSVLQVAVKNNQQPVWYFEDKIVLNALFSEDGRMERGTFLETWKSLPDSNEVQKEFPGITITSVESTLDLLAASNMFFIAKRKNGNQDVLYLSAKVPRGIPFLIELTAIVGQPGLKCAVKTPTPEIAPLFFEAVEILFKA
Protein: Cytochrome P450 2J4 (EC 1.14.14.1) (CYPIIJ4) (Q9QXF7)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase that may play a major role in intestinal retinoid metabolism. Catalyzes the oxidative transformation of all-trans retinal and 9-cis-retinal to the corresponding active forms all-trans and 9-cis retinoic acids. Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates arachidonic acid predominantly at the omega-1 position. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9143331, ECO:0000269|PubMed:9606960}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:9143331, ECO:0000269|PubMed:9606960}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLATAGSLIATIWAALHLRTLLVAALTFLLLADYFKTRRPKNYPPGPWGLPFVGNIFQLDFGQPHLSIQPFVKKYGNIFSLNLGDITSVVITGLPLIKETFTHIEQNILNRPLSVMQERITNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKKSLEQRMQEEAHYLVEAIREEKGKPFNPHFSINNAVSNIICSVTFGERFEYHDSRFQEMLRLLDEVMYLETTMISQLYNIFPWIMKYIPGSHQTVFRNWEKLKLFVSSMIDDHRKDWNPEEPRDFIDAFLKEMSKYPEKTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEVQEKVQAEIDRVIGQKRAASLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAMDTTLNGFHLPKGTMVLTNLTALHRDPKEWATPDVFNPEHFLENGQFKKRESFLPFSMGKRACLGEQLARSELFIFFTSLMQKFTFKPPTNEKLSLKFRNGLTLSPVTHRICAVPRE
Protein: Endosome-lysosome associated apoptosis and autophagy regulator 1 (E9PB18)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MAEPGHSHHLSARVRGRTERRIPRLWRLLLWAGTAFQVTQGTGPELHACKESEYHYEYTACDSTGSRWRVAVPHTPGLCTSLPDPIKGTECSFSCNAGEFLDMKDQSCKPCAEGRYSLGTGIRFDEWDELPHGFASLSANMELDDSAAESTGNCTSSKWVPRGDYIASNTDECTATLMYAVNLKQSGTVNFEYYYPDSSIIFEFFVQNDQCQPNADDSRWMKTTEKGWEFHSVELNRGNNVLYWRTTAFSVWTKVPKPVLVRNIAITEKGSSSCNVRPACTDKDYFYTHTACDANGETQLMYKWAKPKICSEDLEGAVKLPASGVKTHCPPCNPGFFKTNNSTCQPCPYGSYSNGSDCTRCPAGTEPAVGFEYKWWNTLPTNMETTVLSGINFEYKGMTGWEVAGDHIYTAAGASDNDFMILTLVVPGFRPPQSVMADTENKEVARITFVFETLCSVNCELYFMVGVNSRTNTPVETWKGSKGKQSYTYIIEENTTTSFTWAFQRTTFHEASRKYTNDVAKIYSINVTNVMNGVASYCRPCALEASDVGSSCTSCPAGYYIDRDSGTCHSCPTNTILKAHQPYGVQACVPCGPGTKNNKIHSLCYNDCTFSRNTPTRTFNYNFSALANTVTLAGGPSFTSKGLKYFHHFTLSLCGNQGRKMSVCTDNVTDLRIPEGESGFSKSITAYVCQAVIIPPEVTGYKAGVSSQPVSLADRLIGVTTDMTLDGITSPAELFHLESLGIPDVIFFYRSNDVTQSCSSGRSTTIRVRCSPQKTVPGSLLLPGTCSDGTCDGCNFHFLWESAAACPLCSVADYHAIVSSCVAGIQKTTYVWREPKLCSGGISLPEQRVTICKTIDFWLKVGISAGTCTAILLTVLTCYFWKKNQKLEYKYSKLVMNATLK
Protein: Angiomotin-like 2b (B8A5S6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Recycling endosome {ECO:0000250|UniProtKB:A1YB07}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y2J4}. Cell projection, podosome {ECO:0000250|UniProtKB:Q8K371}. Cell junction {ECO:0000250|UniProtKB:Q8K371}.
Interaction partners:
- NF2, moesin-ezrin-radixin like
- Merlin
- PATJ crumbs cell polarity complex component.
- Rho GTPase-activating protein 17
- Rho GTPase-activating protein 17
- Si:dkey-92j12.5.
- Protein kinase C
- Protein kinase C iota type
Sequence:
MPLTESAWNESVGWFSSDHKYSTSSNKMRGEEASGTVLHRLIQEQLRYGNPTDAHTLLAIQQQALRRGGGAASSSQSSSESLSQDEPHSPQLSTRQEPQGQEHQVDYQHSENYTTYPHHQEELPTYEQAKAHSQYLASQWCLPHRVCSLQDSVAIQKPCEEQDSWDMKQGHVRSISDRLLHFSMESGKMPCSASYPQINGYHANQHLQYNQQGLEYNKLAPYTEYPFSVEYENGYKAPPPFHSQHNRLPTPEVCHRLSTSPPAGREVNACSRSQLEMLMNENKRLRQELEGQTEKALKIQKLEQEIQRISEAYDTLMKGCAKREALEQALRNKLMAEIKRLQHSSVQAAKQAEAADQNQHAIEKLHLQNEEQKLRCACLEQEVQHLRNEAEKHQRRSEALESTLRSTQTRSQQLWTELQRKRAYVEKVERLQGALTQLQATCEKREGLEMRLRTRLEQELRSLRNQQRQPQPVGGTSHVSVYTLQENLREKEERILSLEADKIRWEQKYLEEKTMREFAMDAAATAAAQRDTTIINHSPCHSFIEELPSTEYRNQEVENRIRSLYAQILEKDTVISILKQKLQHEQKGQLGALQPATADSSIISSHSTPAHTAQGKERSHFNDQAAGTLHSSHAPVEALAHTTDQTPHTEAKPKNIQKAPSAVDLFKGVDDVSAEAVEIFI
Protein: Protein GVP36 (Q59WJ7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSFKFPSFDFKSIQESLPSVDQVKESFTKTSDQLSKSIQPYTTKTTQLISEQLKHLEQLANNTTDDIDVSELPQDYLQLESNCDLLLKLYTDLIQTTNETYGKVSYDYPPGNYAINKIKDANVSGLIGQKFNQLKNVSSPQELEKVLLGQDVDAESKDESGVVSIQPTSPQLPKTLFGHLAEICAKHSDELKSSEHPLSFALLQVSSTYQEIAVARLDQDKKIMSGLNAELIRTLNESFIKVNELRKKVYATRGEFDLLRSKYEKSDPENEELIAKEDGFVSATEVAVVEMKKLLKPSKNIDLLKVLVAAQKDYFEVGAKKLKEVLDNLDKIPTTGEEEEDD
Protein: Probable ubiquitin-conjugating enzyme E2 18 (Ubiquitin conjugating enzyme) (A6MUS6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Anaphase-promoting complex subunit 11
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
Sequence:
MTSSSAHSRKALSKIACNRLQKELVEWQVNPPAGFKHKVTDNLQRWIIEVNGAPGTIYANETYQLQVDFPEHYPMEAPQVIFIPPAPLHPHIYSNGHICLDILYDSWSPAMTVSSICISILSMLSSATLKQRPTDNDRYVKNCRNGRSPKETRWWFHDDKV
Protein: Small ribosomal subunit protein uS7m (28S ribosomal protein S7, mitochondrial) (MRP-S7) (S7mt) (bMRP-27a) (bMRP27a) (Q9Y2R9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS12m
- Elongation factor Tu, mitochondrial
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS2m
Sequence:
MAAPAVKVARGWSGLALGVRRAVLQLPGLTQVRWSRYSPEFKDPLIDKEYYRKPVEELTEEEKYVRELKKTQLIKAAPAGKTSSVFEDPVISKFTNMMMIGGNKVLARSLMIQTLEAVKRKQFEKYHAASAEEQATIERNPYTIFHQALKNCEPMIGLVPILKGGRFYQVPVPLPDRRRRFLAMKWMITECRDKKHQRTLMPEKLSHKLLEAFHNQGPVIKRKHDLHKMAEANRALAHYRWW
Protein: Tyrosine-protein kinase Fer (EC 2.7.10.2) (P18106)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tyrosine-protein kinase which is required during embryogenesis for formation of the actin cable in leading edge cells of the dorsal epidermis and for the timely progression of dorsal closure. May play a role in regulation of adherens junctions and cell adhesion through phosphorylation of the beta-catenin arm.
Subcellular location: Membrane {ECO:0000269|PubMed:9038371}; Peripheral membrane protein {ECO:0000269|PubMed:9038371}. Cell junction, adherens junction {ECO:0000269|PubMed:9038371}. Note=At stages 11-12 of embryogenesis, localizes to adherens junctions in epidermal cells. At stages 13-14, is no longer detected in the epidermal cell junctions which border with the amnioserosa. {ECO:0000269|PubMed:16831834}.
Interaction partners:
Sequence:
MGFSSALQSRAAHEALIVRQDAELRLMETMKRSIQMKAKCDKEYAISLTAVAQQGLKIDRADEMQGSLISKSWRSYMDELDHQAKQFKFNAEQLEVVCDKLTHLSQDKRKARKAYQEEHAKIAARLNHLTDEVVRKKSEYQKHLEGYKALRTRFEENYIKAPSRSGRKLDDVRDKYQKACRKLHLTHNEYVLSITEAIEVEKDFRNVLLPGLLEHQQSVQESFILLWRNILQEAAQYGDLTADKYKEIQKRIDTVIGSINPTEEYGEFTEKYKTSPTTPLLFQFDETLIQDIPGKLQSSTLTVDNLTVDWLRNRLQELEGAVRDCQEKQMKMIEHVNGGSPVANGSIISNGSNTSNGIQSNKDSLCRQSKDLNALRCQEKQKQKLVDMIKCALNEVGCEELPSGCDDDLTLEQNFIENGYNNEQQRSNSTSSPGLGIMNELMRRGGVLTLLRGRGRHFKRKSTPQPATPMTRSRQGRFNKLQPRSQSLGSLSVIRDGNGPSPARYEPITNHRLRQAASVHYLGEEIATSSTNPPDLTRLRRTQCSMLCLGEDEEPVVLASPAPLTQLTAAVLTNTNNNHIYADLELDKKKDTSPSPECKGEQIQPKKEQIRIEINQTAPQNSIDAHLDRIDELNRVLDDRLKRTLQPSDDVNAIESAEENHIQTRKLAKDPDSQTKRSSSSSSECRSSKDTSHSKKRSLSFSQKSISNIFSNLKEFSKSPLVRMGKNHILNEEQDAKRTQPSQHHHSSGSDCPTNSSSSSSNNNNNNKNTSSNSNHSASQSTIITSTITTTITTTTTTTPSKENSRLKFKVPKIQKKSKAIRNTFRSKLLNFQLKRSKPCKQCTKRRRIHPSKSVFDFAKEFEVEQPAGSAADEQFCNCPPAGQKPVKPSVQISGHKDHPFESSSGELDENSDRDIDNDEEEEDSASDDVLSMKDHCYCVPSLAASISLSTNRPLYEEEWFHGVLPREEVVRLLNNDGDFLVRETIRNEESQIVLSVCWNGHKHFIVQTTGEGNFRFEGPPFASIQELIMHQYHSELPVTVKSGAILRRPVCRERWELSNDDVVLLERIGRGNFGDVYKAKLKSTKLDVAVKTCRMTLPDEQKRKFLQEGRILKQYDHPNIVKLIGICVQKQPIMIVMELVLGGSLLTYLRKNSNGLTTRQQMGMCRDAAAGMRYLESKNCIHRDLAARNCLVDLEHSVKISDFGMSREEEEYIVSDGMKQIPVKWTAPEALNFGKYTSLCDVWSYGILMWEIFSKGDTPYSGMTNSRARERIDTGYRMPTPKSTPEEMYRLMLQCWAADAESRPHFDEIYNVVDALILRLDNSH
Protein: Methanethiol oxidase (MTO) (EC 1.8.3.4) (Selenium-binding protein 1) (V9HWG1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU369071}. Cytoplasm, cytosol {ECO:0000256|RuleBase:RU369071}. Membrane {ECO:0000256|RuleBase:RU369071}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369071}. Note=May associate with Golgi membrane. May associate with the membrane of autophagosomes. {ECO:0000256|RuleBase:RU369071}.
Interaction partners:
Sequence:
MATKCGNCGPGYSTPLEAMKGPREEIVYLPCIYRNTGTEAPDYLATVDVDPKSPQYCQVIHRLPMPNLKDELHHSGWNTCSSCFGDSTKSRTKLVLPSLISSRIYVVDVGSEPRAPKLHKVIEPKDIHAKCELAFLHTSHCLASGEVMISSLGDVKGNGKGGFVLLDGETFEVKGTWERPGGAAPLGYDFWYQPRHNVMISTEWAAPNVLRDGFNPADVEAGLYGSHLYVWDWQRHEIVQTLSLKDGLIPLEIRFLHNPDAAQGFVGCALSSTIQRFYKNEGGTWSVEKVIQVPPKKVKGWLLPEMPGLITDILLSLDDRFLYFSNWLHGDLRQYDISDPQRPRLTGQLFLGGSIVKGGPVQVLEDEELKSQPEPLVVKGKRVAGGPQMIQLSLDGKRLYITTSLYSAWDKQFYPDLIREGSVMLQVDVDTVKGGLKLNPNFLVDFGKEPLGPALAHELRYPGGDCSSDIWI
Protein: GH10905p (Q7K3V3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAAQQQHNNSTVESEMERQRRDSTTSESSLEHLDLGRTPKKLGGNSGSTQTTSTPHELATVTSSRKRKIRHLQLNHHQQQQHHQQSDLLSDEDVAEAEAEEDEDEEDGDQVAALGSRNLGRHKQRRSGGATTQASIVMDYSSGDASSLRKKFRLNRSAASLSESGFVDASSTTGHSGYLGNSSSATNTTATSGIGASAVAPSPVGGAAINAASSSSGSSSGGSGGSSPQGQCLSSGESGIGAGDEHMKYLCPICEVVSATPHEFTNHIRCHNYANGDTENFTCRICSKVLSSASSLDRHVLVHTGERPFNCRYCHLTFTTNGNMHRHMRTHKQHQVAQSQSQSQQQQSLQQQQQSQQQRRQQQQHQPSQQQQNPAQQQLMGNTLSARAESYESDASCSTDVSSGHSHSRSSSSLNNNNNNSHKANNNLKDLEELEVSTEDQDTENKQRRLKTTINNNIIESEQQEDMDDEEADDADVAMLTSTPDVATLLAGASASGAASRSPTPSPSASPALLLSCPACGASDFETLPALCVHLDAMHSDIPAKCRDCEVIFATHRQLQSHCCRLPNALAGGLPPLLGASSSPLHNEEPEDEEHGDDEDLEQKERLASQSEDFFHQLYLKHKTANGCGAISHPPSPIKHEPADTKDLADIQSILNMTSSSSSFLRNFEQSVNTPNSSQYSLDGRDQEEEAQDAFTSEFRRMKLRGEFPCKLCTAVFPNLRALKGHNRVHLGAVGPAGPFRCNMCPYAVCDKAALVRHMRTHNGDRPYECAVCNYAFTTKANCERHLRNRHGKTSREEVKRAIVYHPAEDAGCEDSKSRLGEDLADTSFRSISPTPPPPPVNESKSQLKHMLLGENHLAPVNQQPPLKIQVKSLDQLVDKKPSAPAPQQQQQQQQQEKSGSALDFSMDVLDLSKKPTGGASLTPAVTRTPTPAAVAPVTPGGVGTPDLAAAIEQQQLLLAQQQLFGAGGEYMQQLFRSLMFQSQTSGFPFFPFMAPPPPQANPEKPPMVSPPNRINPMPVGVGVGVPVPPGGPVKMVIKNGVLMPKQKQRRYRTERPFACEHCSARFTLRSNMERHVKQQHPQFYAQRQRSGHHVMRGRGASNVAAAAAAAAAAAAATVMAGGPGSSGFGSNHHHGHGHGSHGSHGHAPISEQVKCAILAQQLKAHKNTDLLQQALAHGSSSVAGNPLLHFGYPLTNPSPMHNGSSQGNGQATAMDDDEPKLIIDEDENEHDHEVEAEDVDDFEEDEDEEEMDEPEDEPELILDEQPAEKEAEEEQELPKPLEQLGTKEAAQKMAETILEQAIKAGKPLSPPPTKENASPANPTVATTMQEPAITAPSTNPSSLKTMIAQAEYVGKSLKEVASSPFKDESQDLVPVAKLVDNATSQNMGFNSYFRPSDVANHMEQSDEEGLVASGSASESNNSGTEDVTSSSSSSEPKKKSAYSLAPNRVSCPYCQRMFPWSSSLRRHILTHTGQKPFKCSHCPLLFTTKSNCDRHLLRKHGNVESAMSVYVPTEDVSEPIPVPKSVEEIELEEQRRRQEAEREKELELERERELERERELERERQLEKEKERERQQLIQKLAAQMNAAATAAAVVAAASAVNGGASGGPHGPIADALAGGDLPYKCHLCEGSFAERLQCLEHIKQAHAHEYALLLAKGAIETESLEANPHQQPSQQAVHSDDEAPNGGGNRGKYPDYSNRKVICAFCLRRFWSTEDLRRHMRTHSGERPFQCDICLRKFTLKHSMLRHMKKHSGRAHNGDTPGSDCSDDEQVSSPPSTPHPTQPTSANNNNSCHNNNNNANNNNNNNNNNNNNSSSKLGLKLHDLLDKASEWRASRLGEHKENMGEATPSGATVAGSDLIGNLLGISDQGILNKLLSSADEAAKLLGVDNK
Protein: Cytochrome b6-f complex subunit 6 (Cytochrome b6-f complex subunit PetL) (Cytochrome b6-f complex subunit VI) (P12180)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00433}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00433}.
Interaction partners:
Sequence:
MLTITSYFGFLLAALTLTLALFIGLNKIRLI
Protein: Glutathione S-transferase theta-2B (EC 2.5.1.18) (Glutathione S-transferase theta-2) (GST class-theta-2) (P0CG30)
Organism: Homo sapiens (Human)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:1417752}.
Interaction partners:
- Hematopoietic prostaglandin D synthase
- Cytochrome P450 1A1
- Glutathione S-transferase P
- Epoxide hydrolase 1
- Glutathione reductase, mitochondrial
- Cytochrome P450 2E1
- Cytochrome P450 1B1
- Peroxiredoxin-6
- Cytochrome P450 1A2
- Phospholipid hydroperoxide glutathione peroxidase GPX4
Sequence:
MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSLGKLPTLKDGDFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGWHADCIRGTFGIPLWVQVLGPLIGVQVPEEKVERNRTAMDQALQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALGYELFEGRPRLAAWRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRIARIP
Protein: Fibrillarin (M0R2U2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAAS
Protein: Transcription and mRNA export factor ENY2 (Enhancer of yellow 2 transcription factor homolog) (E5RHX8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03046}.
Interaction partners:
Sequence:
MNKDAQMRAAINQKLIETGERERLKELLRAKLIECGWKDQLKAHCKEVIKEKGLEHVTVDDLVAEITPKGRETGFAMLPRLVLSSRTQAILLPQPSRLLG
Protein: Serine/threonine-protein kinase BSK (EC 2.7.11.1) (Brassinosteroid-signaling kinase) (F4JPT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU369005}; Lipid-anchor {ECO:0000256|RuleBase:RU369005}. Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- Enoyl-CoA delta isomerase 3
- AP2-like ethylene-responsive transcription factor PLT2
- Putative acyl-activating enzyme 19
Sequence:
MNYEEICVGSDLSLYSFQRRWRPSTISNRRVCSNLFPMDGNPRLSCFGLMKSSRDGKSYIALTWHLLLQRNLLTELHQRVYYVFSFGTVLLDLISGKHIPPSHPYRKYCLRMDLTAIQEILSKIGYKELPLSSRFKCGQPRCRNLSFQRSKGT
Protein: Cytosolic iron-sulfur assembly component 3 (Cytosolic Fe-S cluster assembly factor NARFL) (Iron-only hydrogenase-like protein 1) (IOP1) (Nuclear prelamin A recognition factor-like protein) (Protein related to Narf) (Q9H6Q4)
Organism: Homo sapiens (Human)
Function: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect.
Interaction partners:
- Probable cytosolic iron-sulfur protein assembly protein CIAO1
- MMS19 nucleotide excision repair protein homolog
- Cytosolic iron-sulfur assembly component 2B
- Cytosolic iron-sulfur assembly component 2A
- Cytosolic Fe-S cluster assembly factor NUBP1
- Anamorsin
- Cytosolic Fe-S cluster assembly factor NUBP2
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Cysteine desulfurase
- LYR motif-containing protein 4
Sequence:
MASPFSGALQLTDLDDFIGPSQECIKPVKVEKRAGSGVAKIRIEDDGSYFQINQDGGTRRLEKAKVSLNDCLACSGCITSAETVLITQQSHEELKKVLDANKMAAPSQQRLVVVSVSPQSRASLAARFQLNPTDTARKLTSFFKKIGVHFVFDTAFSRHFSLLESQREFVRRFRGQADCRQALPLLASACPGWICYAEKTHGSFILPHISTARSPQQVMGSLVKDFFAQQQHLTPDKIYHVTVMPCYDKKLEASRPDFFNQEHQTRDVDCVLTTGEVFRLLEEEGVSLPDLEPAPLDSLCSGASAEEPTSHRGGGSGGYLEHVFRHAARELFGIHVAEVTYKPLRNKDFQEVTLEKEGQVLLHFAMAYGFRNIQNLVQRLKRGRCPYHYVEVMACPSGCLNGGGQLQAPDRPSRELLQHVERLYGMVRAEAPEDAPGVQELYTHWLQGTDSECAGRLLHTQYHAVEKASTGLGIRW
Protein: Fimbrial protein (Pilin) (P17838)
Organism: Pseudomonas aeruginosa
Subcellular location: Fimbrium. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKAAQKGFTLIELMIVVAIIGILAAIAIPAYQDYTARAQLSERMTLASGLKTKVSDIFSQDGSCPANTAATAGIEKDTDINGKYVAKVTTGGTAAASGGCTIVATMKASDVATPLRGKTLTLTLGNADKGSYTWACTSNADNKYLPKTCQTATTTTP
Protein: Transcriptional regulator CRZ1 (J9VE33)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: DNA-binding transcriptional activator that interacts with calcineurin-dependent response element (CDRE) promoters. Activates expression of genes required to maintain cell wall integrity during stress. Activates expression of genes required for transepithelial migration through the host blood-brain barrier. Required for adaptation to host temperature during infection.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}. Nucleus {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:24520056, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}. Note=Localizes to the nucleus during calcium signaling, cell wall and heat stress (PubMed:21487010, PubMed:23251520, PubMed:24520056, PubMed:27611567, PubMed:28376087, PubMed:28898238, PubMed:31266771). Localizes to the nucleus following dephosphorylation by CNA1 (calcineurin) (PubMed:27611567). Localizes to the nucleus during growth on glucosamine carbon source (PubMed:28898238). Localizes to the cytosol during vegetative growth and osmotic stress (PubMed:23251520, PubMed:28376087, PubMed:28898238). {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:24520056, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}.
Interaction partners:
Sequence:
MADPASPPSFDAIFAQQPVRRSSSTSTSSFANYTYSALQQHQQFNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMMSGLADGYGVINGRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPFFNKPQSPPALIIPNSPVLPNIVTQSTSNNHSKGLNQPHTRHASNGAGGLFPPSNPALEHLTGMAGISPIAPNADGPMICIQPSTPISGLKEGRGLFDAALRRAGAARGAQRQGPQGQGESQEDRRQDGFNVPSPQSHPLPRTLSSDQVNQGVEMQGMDFAAQMQSYEQQGWANDTLRIAGPSRPRAKSDSIIPSPTADSFDRQAFLAFIGAGNAQPPPPNVEMQPGYVDVSEQWRNTVSAWKAGLGEGELNSQPTLDPRLLPGRESNEAVYQQLLMQQQTGQMPRLDPDQLHQLTQLEGQRARFSLNTNIAPPKYEPGEISPTSMVFYQSMGLYPHAAPELSGTVSAPWSQTAFGQVPGPGPVGHPATAGPAQQHFLTPTLSHATVRRRSFGGGEHPAMGAGTPGYGMEFSSPFAGKSVGQIRGVNMGHRRAARSEDFGRGGTGWGVGAGGSTAEFLQSITGDDGSLLPPSNRGHAMSHSRHSSTSSIRSASPALSISSQGSSFSHHSPRMDMPDSIYPGHPIIAPATPLQVSGLYEEQQTPARVAKMKVTSVATEVASTSRRTNSGIFKCPVPGCGSTFTRHFNLKGHLRSHNDERPFKCLYEGCPKAIVGFARQHDCKRHMLLHEGLRLFECEGCGKKFARLDALTRHHKSEQGQECAITHPLPTNFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSGKRRSKKSETSEED