wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor Sox-19a (P47792)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional activator.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor Sox-3
- Hairy-related 3.
- POU domain, class 5, transcription factor 1
Sequence:
MYSMLEHDMKSAVPPTHQSAQGMTQLNGGVTHGSAKPAVNSQQQQSSDPMDKVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLTDAEKRPFIDEAKRLRALHMKEYPDYKYKPRRKTKPVLKKDNPAAKYPLSAGNLLAAAAAQGSGGSPRMDSYGWGHTGGYPGMQTDALGYSQQLHRYDLSALQYPSAMATAQTYMNGANSYNPMSYSSTPQQPSPVMSMVKPEQVSHSPTGAHSHQRGPLQGDLRDMISMYIPGGDTTDSGAQRGYSNIQQHYLTGTAPLTHI
Protein: Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC 2.4.1.265) (Asparagine-linked glycosylation protein 8 homolog) (Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase) (Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase) (Q6P8H8)
Organism: Mus musculus (Mouse)
Function: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol before it is transferred to the nascent peptide (By similarity). Required for PKD1/Polycystin-1 maturation and localization to the plasma membrane of the primary cilia.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVK2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Glc:Glc
- Dol-P-Man:Man
- GDP-Man:Man
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Neutral alpha-glucosidase AB
- Dol-P-Man:Man
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- UDP-N-acetylglucosamine transferase subunit ALG13
Sequence:
MAASGSATAGGHWFSALALGVTLLKCLLIPTYHSTDFEVHRNWLAITHSLPISQWYYEATSEWTLDYPPFFAWFEYALSHIAKYFDQEMLNIHNLNYYSSRTLLFQRFSVILTDALFVYAVHECCKCIDGKRTGKDLTEKPKFILSVLLLWNFGLLIVDHIHFQYNGFLSGLLLLSIARLFQKRHIEGALLFAVLLHLKHIYLYVAPAYGVYLLRSYCFTASKPDGSVRWSSFSVVRVTSLGLIVFLVSALSLGPFLALNQLPQVFSRLFPFKRGLCHAYWAPNFWALYNALDKVLSVIGLKLKLLDPSQIPRASMTSGLVQQFQHTVLPSVSPLATLICTLIAILPSVFCLWFKPQGPRGFLRCLVLCALSSFMFGWHVHEKAILLAILPMSLLSVEKAGDATVFLILATTGHYSLFPLLFTAPELPIKILLMLLFTVYSISSLKTLFRKEKPLFNWMETVYLLGLGPLEVCCEFLLPFTSWKLKYPFIPLLLTSVYCAVGITYAWTRLYASVLTGSLVSKTKKH
Protein: TNF receptor superfamily member 10b (A0A1W2Q6I0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
VWQSFFVPVTAKLAQDRPADLQRLKQSPLECPAGQYLSKEDGSCKACIDGENYTSGPNVLPSCLSCRVCKEDKVIKSRCVKARNTECECKPGSFEDKDSTEICQTCSNCTDGEDEVIPCTPKANRKCVPKNTQIPQHNLGLIIGLLASVISVVLFVAVIWKTKAWESVCLFMTRVYPGCEQDHENTVGLSLLDAQTSRKTNGSHHNTEPDRTQSSPLGRKLLVLANGNNPADALKLIFERCSTEVPFNSWDRLMRHMGLTDNQIQMVRAETQVPCEVLYQMLLKWLYQTGLGASINHLLGALEAVGERCALEEIEDYAVKSGKFVYQNTTA
Protein: UBA domain-containing protein 7 (O13773)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable clathrin heavy chain
- ADP-ribosylation factor 1
- Oxysterol-binding protein homolog C2F12.05c
- Clathrin light chain
- Heat shock protein homolog pss1
- Endoplasmic reticulum chaperone BiP
- Uncharacterized Rab geranylgeranyltransferase C15C4.03
- Probable heat shock protein ssa2
- Probable heat shock protein ssa1
- Ribosome-associated molecular chaperone sks2
Sequence:
MDDLLDFNFYDKSTPSNQNNYSNNNSRTPSYSLPAPVAQKKNAQIPLKASKPEDPFANLFQKKTDNKISLKELERQKVGTPDSNSTPKSSNYDPFENLEILHQLSNTPRDKDAVIHDKIEENKRPISQPQVSASEKVTLKDLSLEPHQPVSLPAFENIGSETSIPFENHNEITNMNTAKDKLSSNEMYEKLRDLGFSDDQSRLALENSGSLEDAIEYILEKDNAKGQYREGEAYEAFSDSSAKTQFSDFQALSNQLKSQLFEKANDLWNIGRKKLRDAVEERRAVKDPSKPRWMDASHDFGREATPEILPKTPIPKRKPHKVPMNEKVSEDRITTNQSRSGNDESSLVDFLTSKSDNSSFNFPSDTYEGTENILETAYESTTARQVNNNKPGKSTVKKREEETLNNMVSALVEEQQSTGNELFRKGDFSQAIEEFTNSLSQLPAKHTKRVPLLSNRSLCYQKVGDLKTCLQDVDELVDIIGEEKGHGESIRDKSMNDYYVKNMVRKAQVLEQLEKYQESLNIWKDLIADGQISKLYIDGKHRCEAAISSHSSESHSKRTTQQPKSTPNHTNIKVKSERLQHVRMAQQKAEQLDEERSRLREPVQQIVNKWKEGKESNLRALLASLDTILWPECRWQKVSLSELVLPKKVKIAYMKAVSRVHPDKLPQQTSVEHQLIAESAFSILNHAWELFKQQNDL
Protein: Growth hormone (Q0QBH3)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFTLLCLLWTQVVGAFPAMSLSCLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTSKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDVTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: Vang-like protein 2-B (Protein strabismus-B) (Van Gogh-like protein 2-B) (Xstrabismus-B) (Xstbm-B) (Q90Z05)
Organism: Xenopus laevis (African clawed frog)
Function: Has a role in non-canonical Wnt/planar cell polarity (PCP) signaling; can recruit dvl/dsh and prickle from the cytoplasm to the plasma membrane. Acts in a PCP complex to regulate the polarized assembly of fibronectrin on the surface of the mesoderm during gastrulation. Regulates convergent extension in both dorsal mesoderm and neural tissue without affecting cell fate. Regulates neural fold closure during neurulation. May be required for cell surface localization of fzd3 and fzd6 in the inner ear (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q90X64}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q90X64}. Note=Cell membrane localization is regulated by prickle. {ECO:0000250|UniProtKB:Q90X64}.
Interaction partners:
Sequence:
MDNDSQYSGYSYKSGQSRSSRKHRDRRERHRSKSREGSRGDKSVTIQAPGEPLLDNESTRGEDRDDNWGETTTVVTGTSEHSISHDDITRITKDMEDSAKLDCSRHLGVVIAGALALLSFLTPIAFMLLPQILWREDLEQCGTACEGLFISVAFKLLILLLGSWALFFRRPKAFFPRVFVFRALLMVLVFLLVVSYWLFYGVRILESRDKNYQGIVQYAVSLVDALLFVHYLAVVLLELRQLQPQFTIKVVRSTDGASRFYNIGHLSIQRVAVWILENYYHDFPVYNPALLNLPKSILSKKMSGFKVYSLGEENNTNNSTGQSRAVIAAAARRRDNSHNEYYYEEAEHERRVRKRKARLVVAVEEAFTHIKRLQDEDPKNPREIMDPREAAQAIFASMARAMQKYLRTTKQQPYHTMESILQHLEFCITHDMTPKAFLERYLGPGPTIQYHKDRWLAKQWTLVSEEPVTNGLKDGVVFELKRQDFSLVVSTKKIPFFKLSEEFVDPKSHKFVMRLQSETSV
Protein: Serine/threonine-protein kinase PAK 3 (EC 2.7.11.1) (p21-activated kinase 3) (PAK-3) (Q8AXB4)
Organism: Xenopus laevis (African clawed frog)
Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways. Involved in early neuronal development; required for cell cycle exit and differentiation of primary neurons. May be required for the formation of dendritic spines and excitatory synapses (By similarity). Cooperates synergistically with mturn to promote primary neural differentiation within the neural plate. Involved in the cement gland formation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSDSVDIEEKPPAPPLRMNSNNRDSSALNHCSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLCGSQMGTGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHSLNAKTASEPPLAPPVSEEEDEEEEEEEDDNEPPPVIAPRPEHTKSIYTRSVIEPVALTAPAKEASTSPVTPQPENSNSSTSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAIFRDFLNRCLEMDVDRRGSAKELLQHPFLKIAKPLSSLTPLIIAAKEAIKNSSR
Protein: Transmembrane protein 231 (Q22804)
Organism: Caenorhabditis elegans
Subcellular location: Cell projection, cilium membrane {ECO:0000256|ARBA:ARBA00004272}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004272}.
Interaction partners:
- Transmembrane protein 237 homolog
- Nephrocystin-1-like protein
- TMEM
- B9 domain-containing protein 1
- NePHronoPhthisis
- MecKel-Gruber Syndrome
- B9 domain-containing protein 2
- Protein fantom
- Tectonic domain-containing protein
- Transmembrane protein 138
Sequence:
MPHVDIFTEPVYRTYRSSECSWSAFYIKLVNVFRYFLPILIIFITDGLWKKTNTFREVPNISVTGDFIAYAYGHDRSIISSSYSVLNSAASSEQLSTSQLLHHFSDVSEENKQNFNNQNSLQTLNIEFQMSTQNLSINTLIYAFSLRMRLDYHSIVDTELFLTDTIQLTSPIAQIQTIARLSMDQSNPFFTKEHIRIIDRRRQDVEHYQIHSVLKRITGAPIALKMERKSTLLLSAPSSPQSLSISLSLAVPEMEFIYKTGFWELLKWFWIQYLASFTIVDYVFTSCTSYMFRNRVFYVNDVVR
Protein: Bitesize isoform 1 (Bitesize, isoform B) (Q6XK20)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNTMPGMGVGVGVTVGDCENYVQQQQPQQQQPQLEVTPTHHRLQVRRQSTLPAQPTPAIYMSTSPNRLYSRSPERSPGEQQRYPPFMRQTSFPEPPSTYHRTKLLPSTGAPPPTVAPPPLNYESQTSSLASDEQDVGPMPKPRMTRQATLPNPEQHVKLLPTSPPKRQTSPQFRRSPEFMRQQTLPNPEAFSSGNTLTVHSTPPAKFMPISPRAKQNFLFPSVPNPRQFLSQPHVPAVGGTELGSGGSVASTGVVGGGEQYSSSQSVNIHHSRDPHSKMIKVRSHSNEEYSNTKGHPENRRLLPEIPTAVQRPGGRSPSRLVRQDCLKEERTFGEAKQQFHQFPDVTEELDNRPEYVDYFGDSATSFLESDEVQYERNYNAGFSSEPRIIYNNGSDDGSYQNSSQRPIYSAENVLADSGYGGGAGVGLGASGGSGGVPGYYPDMGTPQGFYGGAALPRTPLMHNRIRRRQSRELQMQQEELAQLSQVSDANGKGSGNEGAASGSATDSHAAERRKPEQMRSVSEDSGAKTTPKPVTRRSFSHPEKDTQPTKKTEISKIPSPRPLADILDKTRGNSKIPQARRRNSRTGIGEAEEASTGQEEEKPHGESGQGSGAEQPVNGKSLESSANKEGGDPNSSAEATHTSTLGEQELQNAVEAAAVVFKKVVLQRRKEKEKAAEEEEAKVAAEELSRSPVIGQRQADGSGSPIQSRASSETWPTQSDEDIDRLVAMHQNRSSLSSLGVRSESMASVYSGAGEGRYGTVVVKGQVEFAMQYNYKLSALEVHVVRCKDLAAVDAKRNRSDPYVKVYLLPDKSKAGKRKTKVKKHTLNPIFDETMRFHTPISSLESRTLWLTVWHSDMFGRNDFLGEVSVNLQGRLFDNPQSQWYLLQERSEPFDEVATYRGDIVVGLKYIPPENIKSSFFSRGSSITGSSSNLRKFGGSIKSVASKSERTSKGGQLHVLVKEAKHLSPIKANGTCDAFCKSYLLPDRTRSSKQKTPVVKRTLHPSWNYTFVYEDVSLEELSERALELTVWDHDRLASNEFVGGIRFSLGTGRSYGRQVEWMDATGKELSLWQNMLDRPNFWVEGSLVLRSSLDGIRANLP
Protein: V-type proton ATPase subunit c2 (V-ATPase subunit c2) (V-type proton ATPase 16 kDa proteolipid subunit c2) (V-ATPase 16 kDa proteolipid subunit c2) (Vacuolar H(+)-ATPase subunit c isoform 2) (Vacuolar proton pump 16 kDa proteolipid subunit c2) (Vacuolar proton pump subunit c2) (P59228)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane; Multi-pass membrane protein. Note=Tonoplast.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit F
- V-type proton ATPase subunit a3
- ATP synthase subunit b, chloroplastic
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit d1
Sequence:
MASTFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE
Protein: Phospholipase A2 (EC 3.1.1.4) (Q9BS22)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361236}.
Interaction partners:
Sequence:
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPVDELDKQKQRV
Protein: Signal peptidase complex subunit 3 (Microsomal signal peptidase 22/23 kDa subunit) (SPC22/23) (SPase 22/23 kDa subunit) (P61009)
Organism: Homo sapiens (Human)
Function: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center of the complex close to the lumenal surface (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P61008}.
Interaction partners:
- Signal peptidase complex subunit 2
- Signal peptidase complex catalytic subunit SEC11C
- Signal peptidase complex subunit 1
- Signal peptidase complex catalytic subunit SEC11
- Translocon-associated protein subunit alpha
- Protein transport protein Sec61 subunit beta
- Translocon-associated protein subunit gamma
Sequence:
MNTVLSRANSLFAFSLSVMAALTFGCFITTAFKDRSVPVRLHVSRIMLKNVEDFTGPRERSDLGFITFDITADLENIFDWNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKGNRNVTLTLSWNVVPNAGILPLVTGSGHVSVPFPDTYEITKSY
Protein: Defective proboscis extension response 12, isoform D (A0A0B4KED6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPMVPPRLLLRLRRPLHLMELRILLLCLPTLLLATTLEPDQKSILTDNDWKKLWMRGGINGDSKLDNNLDSSDSPMFEDSELMAHNTTVQLGGTAFLVCKVSGVDRNQISWIRRRDWHILSSGAQLYTNDERFAILHTPGSNMWTLQIKFVQRRDHGMYECQVSTPTGIISHFVNLQVVVPEAFILGSGELHVDMGSTINLVCIIEKSPTPPQYVYWQKNDRLINYVDSRRDITIETTPGPRTQSRLIIREPQVTDSGNYTCSASNTEPASIYVFVSKGDNMAAISRRKTSSADRLTHIFRSMLAPCLLLNTVVVRHIFLT
Protein: Pseudouridylate synthase PUS7L (EC 5.4.99.-) (Pseudouridylate synthase 7 homolog-like protein) (Q9H0K6)
Organism: Homo sapiens (Human)
Function: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs.
Interaction partners:
- RNA pseudouridylate synthase domain-containing protein 1
- Pseudouridylate synthase RPUSD2
- Mitochondrial mRNA pseudouridine synthase RPUSD3
- Pseudouridylate synthase RPUSD4, mitochondrial
- tRNA pseudouridine
- Pseudouridylate synthase TRUB2, mitochondrial
- Pseudouridylate synthase TRUB1
- tRNA pseudouridine synthase Pus10
- Pseudouridylate synthase 1 homolog
- Large ribosomal subunit protein uL13m
Sequence:
MEEDTDYRIRFSSLCFFNDHVGFHGTIKSSPSDFIVIEIDEQGQLVNKTIDEPIFKISEIQLEPNNFPKKPKLDLQNLSLEDGRNQEVHTLIKYTDGDQNHQSGSEKEDTIVDGTSKCEEKADVLSSFLDEKTHELLNNFACDVREKWLSKTELIGLPPEFSIGRILDKNQRASLHSAIRQKFPFLVTVGKNSEIVVKPNLEYKELCHLVSEEEAFDFFKYLDAKKENSKFTFKPDTNKDHRKAVHHFVNKKFGNLVETKSFSKMNCSAGNPNVVVTVRFREKAHKRGKRPLSECQEGKVIYTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIEKEIEKKRMNVFNIRSVDDSLRLGQLKGNHFDIVIRNLKKQINDSANLRERIMEAIENVKKKGFVNYYGPQRFGKGRKVHTDQIGLALLKNEMMKAIKLFLTPEDLDDPVNRAKKYFLQTEDAKGTLSLMPEFKVRERALLEALHRFGMTEEGCIQAWFSLPHSMRIFYVHAYTSKIWNEAVSYRLETYGARVVQGDLVCLDEDIDDENFPNSKIHLVTEEEGSANMYAIHQVVLPVLGYNIQYPKNKVGQWYHDILSRDGLQTCRFKVPTLKLNIPGCYRQILKHPCNLSYQLMEDHDIDVKTKGSHIDETALSLLISFDLDASCYATVCLKEIMKHDV
Protein: Iodotyrosine deiodinase 1 (IYD-1) (EC 1.21.1.1) (Iodotyrosine dehalogenase 1) (Q9DCX8)
Organism: Mus musculus (Mouse)
Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (By similarity). During thyroid hormone biosynthesis, facilitates iodide salvage by catalysing the oxidative NADPH-dependent deiodination of the halogenated by-products of thyroid hormone production, monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT). The scavanged iodide can then reenter the hormone-producing pathways (By similarity). Acts more efficiently on 3-iodo-L-tyrosine than 3,5-diiodo-L-tyrosine (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6PHW0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6PHW0}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q6PHW0}.
Interaction partners:
- Dual oxidase maturation factor 2
- Pendrin
- NAD
- Sodium/iodide cotransporter
Sequence:
MFLLTPVLVAVVCILVVWVFKNADRNLEKKKEEAQVQPWVDEDLKDSTEDLQVEEDAEEWQEAEESVEHIPFSHTRYPEQEMRMRSQEFYELLNKRRSVRFISSEHVPMEVIENVIKAAGTAPSGAHTEPWTFVVVKDPDMKHKIREIIEEEEEINYMKRMGKRWVTDLKKLRTNWIKEYLDTAPVLILIFKQVHGFAANGKKKVHYYNEISVSIACGLLLAALQNAGLVTVTTTPLNCGPRLRVLLGRPSHEKLLVLLPVGYPSRDATVPDLKRKALDQIMVTV
Protein: Class II MHC mutant RJ2.2.5 (Class II major histocompatibility complex transactivator) (Q29704)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRCLAPRPAGSYLSEPQGSSQCATMELGPLEGGYLELLNSDADPLCLYHFYDQMDLAGEEEIELYSEPDTDTINCDQFSRLLCDMEGDEETREAYANIAELDQYVFQDSQLEGLSKDIFKHIGPDEVIGESMEMPAEVGQKSQKRPFPEELPADLKHWKPAEPPTVVTGSLLVGPVSDCSTLPCLPLPALFNQEPASGQMRLEKTDQIPMPFSSSSLSCLNLPEGPIQFVPTISTLPHGLWQISEAGTGVSSIFIYHGEVPQASQVPPPSGFTVHGLPTSPDRPGSTSPFAPSATDLPSMPEPALTSRANMTEHKTSPTQCPAAGEVSNKLPKWPGREVPRKTQLGSSLLFGT
Protein: Acyltransferase-like protein (At5g39080) (HXXXD-type acyl-transferase family protein) (Q9FID2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Emb|CAB68146.1
- RING-H2 finger protein ATL16
- 1-AMINOCYCLOPROPANE-1-CARBOXYLATE OXIDASE-like protein
- ATPase E1
- Short-chain dehydrogenase reductase 5
- Protease inhibitor/seed storage/lipid transfer protein
- Cleavage and polyadenylation specificity factor
- Lecithin-cholesterol acyltransferase-like 1
- AP-1 complex subunit mu-1
- Late embryogenesis abundant protein M10
Sequence:
MVSSLNIIEVARVTPSNSDSAESLSLPLTYFDLIYYKLRAVERVIFYRITNVTRPFFDSVIVPNLKTSLSSCLSHYLPLAGKLIWEPLDHKPTIVYSQNDDVSFSVAETNADFSSLSGNEPFPSTELYPLVPALQSSDDSASIVSFQVTLFPNQGFCIGVSAHHAVLDGKTTTMFLKSWAHICKHQDFSLPQDLIPTYDRTVIKSPTDSENKVLNEWRSFTKILAGGKEPANPKSLKLNPSFEIGPDVVRYTLQLTREDIQTLRERLKREVSSSSSSTSSSKELRLSTFVIVYSYVLVCIIRARGGEPHRPVGYAFSVDCRSLMNPPTPNYFGNCIAGCSRMMLTAKMFMGEEGLLAAATMVSDSIEEWDESFAWKIPDFVAYATLPPETQLILVSGSNRFGVYELDFGWGRPDKVMVVSISPGNGISMAESRDQNGSVEIGFSLKKHEMDTLIDLLHCELTI
Protein: Transient receptor potential cation channel subfamily V member 4 (Transient receptor potential cation channel, subfamily V, member 4) (A0A6I8RQZ3)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MADPSHLLKHNASVDIDDSQGDDGSNHNDSFPLSSLANLFENEESSAPNEGVRSPQVPGDNKQNLRIRFQGPFRKGISNPMDLLESTIYESSAPKKAPMDSLFGYETYHHHPTENRRKRKKILLEKENLNSQAPSPDPPPVIKMFNRHMLFDIVSRGSTAELEGFLPFLLAQKKRLTDEEFREASTGKTCLTKALMNLNGGKNDTIPMLIDIAEKTGNLREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPDIVHYLTENAHKKADIRRQDSRGNTVLHALVAIADNTRENTKFVTKVYDLLVIKCVKLYPDSSLEAIFNNDSMSPLMMAAKLGKIGIFQHIIRLEIKDEEARHLSRKFRDWAYGPVYSSLYDLSMLDTCGEEVSVLEILVYNSKVENRHEMLAVEPINELLRDKWQKFGAVSFYISVVSYLIAMIIFTLIAYYRPMDGTPPYPYRTTMDYMRLAGEIVTLLTGVVFFITNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIITAVLYLVGIESYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMLQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCTSQESCIETSSNCTVPEYPSCRDSSTFSKFLLDLFKLTIGMGDLEMINSAKYPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTILDIERSFPVCMRKAFRSGEMVTVGKNLDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGRNDGYQYYGFSQTVGRLRRDRWSVVVPRVVELNKAPQHSDDVVVPLGNIPQVQTYSQRQENAQNWKKDETHI
Protein: FI23714p1 (Nardilysin (EC 3.4.24.-)) (Q9VYT3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heat shock protein 83
- Cyclophilin 40, isoform A
- Uncharacterized protein, isoform C
- 2-oxoglutarate dehydrogenase, mitochondrial
- GH21273p
- T-complex protein 1 subunit gamma
- BLOC-1-related complex subunit 5
Sequence:
MLWQRYSAHLFRRFEFHVRTKRRSPITQLAGVRAITYSSLCKMTDQVKYLDIPDKSETDKKLYKTLLLGNGLHALIVSDPSPMPHDGFTTSESSSSKSTVSTSSSIISRSESTSSTSTDSESSEESSSEEGDEKLAACALLIDYGSFAEPTKYQGLAHFLEHMIFMGSEKYPKENIFDAHIKKCGGFANANTDCEDTLFYFEVAEKHLDSSLDYFTALMKAPLMKQEAMQRERSAVDSEFQQILQDDETRRDQLLASLATKGFPHGTFAWGNMKSLKENVDDAELHKILHEIRKEHYGANRMYVCLQARLPIDELESLVVRHFSGIPHNEVKAPDLSSFNYKDAFKAEFHEQVFFVKPVENETKLELTWVLPNVRQYYRSKPDQFLSYLLGYEGRGSLCAYLRRRLWALQLIAGIDENGFDMNSMYSLFNICIYLTDEGFKNLDEVLAATFAYVKLFANCGSMKDVYEEQQRNEETGFRFHAQRPAFDNVQELVLNLKYFPPKDILTGKELYYEYNEEHLKELISHLNEMKFNLMVTSRRKYDDISAYDKTEEWFGTEYATIPMPEKWRKLWEDSVPLPELFLPESNKYVTDDFTLHWHSMGRPEVPDSPKLLIKTDTCELWFRQDDKFDLPEAHMAFYFISPMQRQNAKNDAMCSLYEEMVRFHVCEELYPAISAGLSYSLSTIEKGLLLKVCGYNEKLHLIVEAIAEGMLNVAETLDENMLSAFVKNQRKAFFNALIKPKALNRDIRLCVLERIRWLMINKYKCLSSVILEDMREFAHQFPKELYIQSLIQGNYTEESAHNVMNSLLSRLNCKQIRERGRFLEDITVKLPVGTSIIRCHALNVQDTNTVITNFYQIGPNTVRVESILDLLMMFVDEPLFDQLRTKEQLGYHVGATVRLNYGIAGYSIMVNSQETKTTADYVEGRIEVFRAKMLQILRHLPQDEYEHTRDSLIKLKLVADLALSTEMSRNWDEIINESYLFDRRRRQIEVLRTLQKDEIINFVISIDGDNMRKLSVQVIGHRPAGMPEPLCGEDTAKCASKSDDESESENDDDDDEDEEEEESSEEEEEEEKEKEGLKGEDEDDLFYSLENKLNIVFLPAKFNNAFIITDIEKFKDDQYVYPQQKTQPKEEDELISAHIADAIRQV
Protein: transketolase (EC 2.2.1.1) (Q9VHN7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable transaldolase
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate isomerase
- Enolase
- Fructose-1,6-bisphosphatase isozyme 2
- Phosphoglucomutase 1
- deoxyribose-phosphate aldolase
- ATP-dependent 6-phosphofructokinase
- Triosephosphate isomerase
- ribose-5-phosphate isomerase
Sequence:
MSYHKPEAKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNNLRKIDSDLEGHPTPRLNFIDVGTGSLGQGVAVGAGMAYVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGDKAAEVVKHLEGLIVNKNVKLTPKPVPKTGAAPDVDINNIKLSSPPAYKLGDSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPNTCVIYDNEEPFTIGRGKVVRQKSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCGGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVPTVPRSGPPSVLIDMFGISARHVVNAVNEILKD
Protein: Iron-sulfur clusters transporter ATM1, mitochondrial (EC 7.-.-.-) (P40416)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins. Hydrolyzes ATP. Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:24604199, ECO:0000269|PubMed:7828591}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:24604199, ECO:0000269|PubMed:25006243, ECO:0000269|PubMed:7828591}.
Interaction partners:
- Cytosolic Fe-S cluster assembly factor NBP35
- Frataxin homolog, mitochondrial
- 3-isopropylmalate dehydratase
- Fe-S cluster assembly protein DRE2
- NADPH-dependent diflavin oxidoreductase 1
- Cysteine desulfurase, mitochondrial
- Adrenodoxin homolog, mitochondrial
- Cytosolic Fe-S cluster assembly factor CFD1
- Cytosolic Fe-S cluster assembly factor NAR1
- Protein ISD11
Sequence:
MLLLPRCPVIGRIVRSKFRSGLIRNHSPVIFTVSKLSTQRPLLFNSAVNLWNQAQKDITHKKSVEQFSSAPKVKTQVKKTSKAPTLSELKILKDLFRYIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLFGELRNAVFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILTYQFGASFAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDSQIKVSQSLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFKLRKNEVKIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESGRILINGRDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGLMISGGEKQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVREEGKHLELLAMPGSLYRELWTIQEDLDHLENELKDQQEL
Protein: DNA binding protein with PIN domain (Q72P16)
Organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Interaction partners:
Sequence:
MYLLDTNICIFLIKKKNATLLENLKKKLNKDLFVSSLTVAELEFGIQKSEFKEKNKVALIEFLTIFNILSFSDKDAESYGIIRADLERKGNVIGSIDMLLAAQAIANNYIFVTNNTKEFKRIKALKIENWTQ
Protein: Uncharacterized protein (Q386L4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- uracil phosphoribosyltransferase
Sequence:
MRPRPVGRRADGGKPVCTLTRPPAPPPLEGSDPEIAVVGSRVVRLLRDARAVIREQRPPNTPPRTQPKFAPKRVTRLTALNPTSGNDPPKLTTNQQRMDPIAFVTSLDSAKDAPPQQLEQLNQLKRWLCEPQHVLWDTLTGRLVDIVLSPKTDAQVSVCAASILLRYCDVNRFPSLPVVTRRLHELCEVGLEGQSLEEVVVRESLLQPLVQLLKNDELLLCQPCVLWDALEALRSCSSSEAMLSQMVTLGTIPSTNSLVERIIQLFQNSSSPPQPEVSPANKNLIRSLLSSTCLLFRDFSAGYSHHLRKLGSLDRVIDTLDHFRDDMDVVQAAARTMSKTVFNDTCLEHYRENIRTCRVVVAALESSMEVGGIIVTRLCSVLARLVECSKEMRDWFMENHHQILLRLVQTHIAQLKVDGKEDEPVAQNFEDPEQEDLLQSVTWLVGVALMSPGCSTAFVRKITPLLVGFLKDFDVAKWHLTFIYTLMCLSNLSFFFTSLEKSEGGPAELQQLYETLGPMLAGVLFDGDTEATVEATRVLGNICLTNAGRDWMESNRCDEVCVVFLGHEDPRVVYNCFGVLLNLTAADSCQVAADPELTKMLLQHTARYTRAETIALEKERELRHFQASANSQSPEGTNYTDQIADVVEKLLLNLSGLL
Protein: Cyclin-dependent protein kinase inhibitor EL2 (Q10SY2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle. May coordinate biotic and abiotic stress perception and cell cycle progression. Inhibits CDKs activity in vitro.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSASPEFYRPSPPAFSPSCAAGTSTTEVDEYSCCRTPTPGIREPATCPPAPRKPRPVACRKLLFDPAQQQGKGKAISLRLDELERLFRPITNNANLHLQTNKPTHT