wanglab/gogpt-training-data huggingface dataset:
Protein: NF-kappa-B essential modulator (IkB kinase-associated protein 1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (NF-kappa-B essential modifier) (C9J2V2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
Protein: Putative malate oxidoreductase [NAD] (EC 1.1.1.38) (Malic enzyme) (P9WK25)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Pyruvate carboxylase
- Malate dehydrogenase
- Fumarate hydratase class II
- Pyruvate kinase
- 2-oxoglutarate oxidoreductase subunit KorA
- 3-methyl-2-oxobutanoate dehydrogenase subunit beta
- Malate synthase G
- Pyruvate dehydrogenase E1 component
- 2-oxoglutarate oxidoreductase subunit KorB
- 3-methyl-2-oxobutanoate dehydrogenase subunit alpha
Sequence:
MSDARVPRIPAALSAPSLNRGVGFTHAQRRRLGLTGRLPSAVLTLDQQAERVWHQLQSLATELGRNLLLEQLHYRHEVLYFKVLADHLPELMPVVYTPTVGEAIQRFSDEYRGQRGLFLSIDEPDEIEEAFNTLGLGPEDVDLIVCTDAEAILGIGDWGVGGIQIAVGKLALYTAGGGVDPRRCLAVSLDVGTDNEQLLADPFYLGNRHARRRGREYDEFVSRYIETAQRLFPRAILHFEDFGPANARKILDTYGTDYCVFNDDMQGTGAVVLAAVYSGLKVTGIPLRDQTIVVFGAGTAGMGIADQIRDAMVADGATLEQAVSQIWPIDRPGLLFDDMDDLRDFQVPYAKNRHQLGVAVGDRVGLSDAIKIASPTILLGCSTVYGAFTKEVVEAMTASCKHPMIFPLSNPTSRMEAIPADVLAWSNGRALLATGSPVAPVEFDETTYVIGQANNVLAFPGIGLGVIVAGARLITRRMLHAAAKAIAHQANPTNPGDSLLPDVQNLRAISTTVAEAVYRAAVQDGVASRTHDDVRQAIVDTMWLPAYD
Protein: 5-aminolevulinate synthase, non-specific, mitochondrial (ALAS-H) (EC 2.3.1.37) (5-aminolevulinic acid synthase 1) (Delta-ALA synthase 1) (Delta-aminolevulinate synthase 1) (P13195)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}.
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Sarcosine dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Alanine--glyoxylate aminotransferase
- Threonine aldolase 1
- D-amino-acid oxidase
- Pipecolic acid and sarcosine oxidase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
Sequence:
METVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRTVSTSAAQCQQVKETPPANEKEKTAKAAVQQAPDESQMAQTPDGTQLPPGHPSPSTSQSSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMHAVRKEVAQSPVLPSLVNAKRDGEGPSPLLKNFQDIMRKQRPERVSHLLQDNLPKSVSTFQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSLITKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGASGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSNEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNFFLEKLLLTWKRVGLELKPHSSAECNFCRRPLHFEVMSEREKAYFSGMSKMVSAQA
Protein: Small ribosomal subunit protein mS29 (Q585C2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- Small ribosomal subunit protein uS5
- 60S ribosomal protein L17, putative
- 50S ribosomal protein L2, putative
- 40S ribosomal protein S13, putative
- Large ribosomal subunit protein uL3m
- 30S Ribosomal protein S17, putative
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
Sequence:
MRSKTLKKSLAAMYMRPPVTCYTDACEAPVAMWDGAIPLKETRKLKNGVPVRTVSRTYSHPPQLTPTQLSFNDINSMYCVGNDELIQFFPEGLGGRVFQTMPPGHPRGFLYRKETHLLNLFVDKVQHWHTKRSVLSSLTNGRTGFIVDGPTGCGKSALMCQVVHFARSRNIVTLYVPDAKAWTHGEWCWPSTILPGFFDAPDAARSFLKYFAVANRATLTSWKLRCTPKDLPTEQGERQPQNLYELCEWGHRAVAPASIDRQSVCVKFLMDELSEEKKLPVVIVVDGWNLFSHETHFRYPHPDFLRGLASFNESSTDIDLYPQELPRIPASRLSFVRGLNKMILSGDDPNKFFITCTTRDFKPFDGISGFPNVETDRFANSLDEYAPYDPEKDSHFHPIQIGNFDEYEYRSFLRFLINSGELAGLGWGPLWHASSDFERKLYKIGFLSGRNPQGVVDHYHQELVWRYDYQRTRQKQYLLKRRMEGMSRGASSGAVGVM
Protein: Muscle-specific protein 20 (P14318)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Myosin light chain alkali
- Troponin T, skeletal muscle
- Tropomyosin-2
- Myosin regulatory light chain 2
- Actin-57B
- Troponin C, isoform 2
- Muscle LIM protein Mlp84B
- GH21596p
- Troponin C, isoform 3
- Actin-87E
Sequence:
MSLERAVRAKIASKRNPEMDKEAQEWIEAIIAEKFPAGQSYEDVLKDGQVLCKLINVLSPNAVPKVNSSGGQFKFMENINNFQKALKEYGVPDIDVFQTVDLYEKKDIANVTNTIFALGRATYKHADFKGPFLGPKPADECKRDFTEEQLKAGQTIVGLQAGSNKGATQAGQNLGAGRKILLGK
Protein: Gap junction gamma-2 protein (Connexin-47) (Cx47) (Gap junction alpha-12 protein) (Q80XF7)
Organism: Rattus norvegicus (Rat)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a role in myelination in central and peripheral nervous systems (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Gap junction alpha-1 protein
- Gap junction beta-1 protein
- Gap junction protein
- Gap junction beta-2 protein
Sequence:
MTNMSWSFLTRLLEEIHNHSTFVGKVWLTVLVVFRIVLTAVGGESIYSDEQSKFTCNTRQPGCDNVCYDAFAPLSHVRFWVFQIVVISTPSVMYLGYAVHRLARASEQERRRALRRRPGPRRLPRAQLPPPPPGWPDTTDLGEAEPILALEEDEDEEPGAPEGPGEDTEEERTEDVAAKGGGGDGKTVVTPGPAGQHDGRRRIQREGLMRVYVAQLVVRAAFEVAFLVGQYLLYGFEVPPFFACSRQPCPHVVDCFVSRPTEKTVFLLVMYVVSCLCLLLNLCEMAHLGLGSAQDAVRGRRGASAAGPGPAPRPPPCAFPAAAAGLACPPDYSLVVRAAERARAHDQNLANLALQALRDGAAVAAVSADRDSPPCSGLNATSRGPPRAGGPASGTGSATSGGTVGEQGRSGAQEQLATKPRVGSEKGSTGSRDGKATVWI
Protein: Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (O13750)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Probable ATP-citrate synthase subunit 2
- Succinate dehydrogenase cytochrome B subunit
- 2-oxoglutarate dehydrogenase, mitochondrial
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
- Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Probable ATP-citrate synthase subunit 1
Sequence:
MFKTQTTLLTSLRRFSSSSQLKNSKSLYEQTIPNLMINSDTKVIFQGFTGKQGTFHAQHAMDYGTKVVGGTNPKKAGTTHLGKPVFGTIEEAMKETKADASAVFVPPPLAAGAIEEAIAAEVPLIVAITEGIPQHDMLRVSDILKTQSKSRLVGPNCPGIIRPGQCKIGIMPSHIHKPGCIGIVSRSGTLTYEAVNQTTQTDLGQSLVIGIGGDPFPGTNFIDALKLFLDDPNTQGIILIGEIGGSAEEDAAEFIRAANASRSTPKPVVSFIAGATAPKGRRMGHAGAIVAGGKGTAAAKFEALEAAGVRISRSPATLGSLIVEELNKLKH
Protein: Transcription factor CP2-like protein 1 (CP2-related transcriptional repressor 1) (CRTR-1) (Q3UNW5)
Organism: Mus musculus (Mouse)
Function: Transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells (ESCs). With Klf2, acts as the major effector of self-renewal that mediates induction of pluripotency downstream of LIF/Stat3 and Wnt/beta-catenin signaling. Required for normal duct development in the salivary gland and kidney. Coordinates the development of the kidney collecting ducts intercalated (IC) and principal (PC) cells, which regulate acid-base and salt-water homeostasis, respectively. Regulates the expression of IC genes including subunits B1 and D2 of the V-ATPase complex, Oxgr1, Ca12, Slc4a1, Aqp6 and IC-specific transcription factor Foxi1. Regulates also the expression of Jag1 and subsequent notch signaling in the collecting duct. Jag1 initiates notch signaling in PCs but inhibits notch signaling in ICs. Acts as a transcriptional suppressor that may suppress UBP1-mediated transcriptional activation. Modulates the placental expression of CYP11A1 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:28577314}.
Interaction partners:
- Steroid hormone receptor ERR2
- Nuclear receptor subfamily 0 group B member 1
- Sal-like protein 4
- POU domain, class 5, transcription factor 1
- Homeobox protein NANOG
- Developmental pluripotency-associated protein 3
- PR domain zinc finger protein 14
- Alpha-globin transcription factor CP2
- Zinc finger protein 42
- Krueppel-like factor 4
Sequence:
MLFWHTQPEHYNQHNSGSYLRDVLALPIFKQEEPQLSPENGARLPPLQYVLCAATSPAVKLHEETLTYLNQGQSYEIRLLENRKLGDFQDLNTKYVKSIIRVVFHDRRLQYTEYQQLEGWRWSRPGDRILDIDIPLSVGILDPRASPTQLNAVEFLWDPSKRASAFIQVHCISTEFTPRKHGGEKGVPFRVQIDTFKQNESGDYSEHLHSASCQIKVFKPKGADRKQKTDREKMEKRTAQEKEKYQPSYETTILTECSPWPDVPYQANNTPSPSYNGSPNSFGLREGNSSPNHPVEPLPLGSDHLLPSASIQDAQQWLHRNRFSQFCWLFASFSGADLLKMSRDDLVQVCGPADGIRLFNAIKGRNVRPKMTIYVCQELEQNQLPLPQKQDDSGDNSLCVYHAIFLEELTTLELTEKIASLYSIPPQHIHRVYRQGPAGIHVVVSNEMVQNFQDESCFILSTLKAESNDGYHIILKCGL
Protein: Cytochrome P450 2D6 (EC 1.14.14.-) (CYPIID6) (Cholesterol 25-hydroxylase) (Cytochrome P450-DB1) (Debrisoquine 4-hydroxylase) (P10635)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids, steroids and retinoids. 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 (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 20-hydroxyeicosatetraenoic acid ethanolamide (20-HETE-EA) and 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling. Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. Catalyzes the oxidative transformations of all-trans retinol to all-trans retinal, a precursor for the active form all-trans-retinoic acid. Also involved in the oxidative metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; Peripheral membrane protein.
Interaction partners:
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A4
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A7
- UDP-glucuronosyltransferase 2B7
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 1A3
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase 1A9
Sequence:
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYELCAVPR
Protein: MP18 (Q6T456)
Organism: Leishmania major
Interaction partners:
- Putative RNA-editing complex protein
- RNA uridylyltransferase
- MP81
Sequence:
MFRRLSPAAATRSMATMTHPLTSATQSQSVTSTRAAVSRVAMRGCSSSSGTSSGDVSSTKGAAFSVSRSGQRAPSINCVTLVGVVHDIQTGYVFEDAVTQFTLTTTSLDAANQAQECVVEKDHHTVRCYGDVFSREVRAKLSEGNVVCVNGRLRLNPQMEPSCNKYYYFPYIQVQPPHGQVSVVYGDRRSPPSPVNAATGELNNGNGDPTNSAAPAEDGDPSATTQKTP
Protein: Protein PLASTID MOVEMENT IMPAIRED 1 (Q9C8E6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for chloroplast and nuclear photorelocation movements via the regulation of chloroplast-actin (cp-actin) filaments in mesophyll cells, and together with PMIR1, in pavement cells. Required component for both the low- and high-light-dependent chloroplast movement responses via an abscisic acid (ABA) pathway. Involved in the ABA response pathway during seed germination. Modulates ABA accumulation during periods of water deficit at the seedling stage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26324877}.
Interaction partners:
- J domain-containing protein required for chloroplast accumulation response 1
- Protein WEAK CHLOROPLAST MOVEMENT UNDER BLUE LIGHT 1
- Uncharacterized protein At1g66480
- At1g21660
- Kinesin-like protein KIN-14A
- Protein CHUP1, chloroplastic
- UNC93-like protein 1
- Tetraspanin-19
- Defensin-like protein 199
- Putative methylesterase 14, chloroplastic
Sequence:
MAGEYSGSRSSNTQLLAELEALSENLYQKPQVSVGNRRTNSLALPRSSVPSLVTSADEVSTARAEDLTVSKPRARRLSLSPWRSRPKLEVEEEENVTQSNRIVKKPEESSSGSGVKEEKKGIWNWKPIRGLVRIGMQKLSCLLSVEVVAAQNLPASMNGLRLGVCVRKKETKDGAVQTMPCRVSQGSADFEETLFIKCHVYYSPANGKGSPAKFEARPFLFYLFAVDAKELEFGRHVVDLSELIQESVEKMNYEGARVRQWDMNWGLSGKAKGGELALKLGFQIMEKDGGAGIYSKQGEFGMKPSSKPKNFANSFGRKQSKTSFSVPSPKMTSRSEAWTPASGVESVSDFHGMEHLNLDEPEEKPEEKPVQKNDKPEQRAEDDQEEPDFEVVDKGVEFDDDLETEKSDGTIGERSVEMKEQHVNVDDPRHIMRLTELDSIAKQIKALESMMKDESDGGDGETESQRLDEEEQTVTKEFLQLLEDEETEKLKFYQHKMDISELRSGESVDDESENYLSDLGKGIGCVVQTRDGGYLVSMNPFDTVVMRKDTPKLVMQISKQIVVLPEAGPATGFELFHRMAGSGEELESKISSLMAIDELMGKTGEQVAFEGIASAIIQGRNKERANTSAARTVAAVKTMANAMSSGRRERIMTGIWNVEENPLTSAEEVLAVSLQKLEEMVVEGLKIQADMVDDEAPFEVSAAKGQKNPLESTIPLEEWQKEHRTQQKLTVLATVQLRDPTRRYEAVGGTVVVAVQAEEEEEKGLKVGSLHIGGVKKDAAEKRRLTAAQWLVEHGMGKKGKKKSNIKKKEKEEEEEEMLWSLSSRVMADMWLKSIRNPDVKLH
Protein: Regulating synaptic membrane exocytosis protein 2 (Rab-3-interacting molecule 2) (RIM 2) (Rab-3-interacting protein 2) (Q9EQZ7)
Organism: Mus musculus (Mouse)
Function: Rab effector involved in exocytosis. May act as scaffold protein. Plays a role in dendrite formation by melanocytes (By similarity).
Subcellular location: Synapse, synaptosome.
Interaction partners:
- Protein unc-13 homolog A
- ERC protein 2
- ELKS/Rab6-interacting/CAST family member 1
- RIMS-binding protein 2
- Peripheral-type benzodiazepine receptor-associated protein 1
- RIMS-binding protein 3
- Ras-related protein Rab-3A
- Protein unc-13 homolog B
- Liprin-alpha-2
- Ras-related protein Rab-3B
Sequence:
MSAPLGPRGRPAPTPAASQPPPQPEMPDLSHLTEEERKIILAVMDRQKKEEEKEQSVLKIKEEHKAQPTQWFPFSGITELVNNVLQPQQKQPNEKEPQTKLHQQFEMYKEQVKKMGEESQQQQEQKGDAPTCGICHKTKFADGCGHNCSYCQTKFCARCGGRVSLRSNKVMWVCNLCRKQQEILTKSGAWFYNSGSNTLQQPDQKVPRGLRNEEAPQEKKAKLHEQPQFQGAPGDLSVPAVEKGRAHGLTRQDTIKNGSGVKHQIASDMPSDRKRSPSVSRDQNRRYEQSEEREDYSQYVPSDGTMPRSPSDYADRRSQREPQFYEEPGHLNYRDSNRRGHRHSKEYIVDDEDVESRDEYERQRREEEYQARYRSDPNLARYPVKPQPYEEQMRIHAEVSRARHERRHSDVSLANAELEDSRISLLRMDRPSRQRSVSERRAAMENQRSYSMERTREAQGQSSYPQRTSNHSPPTPRRSPIPLDRPDMRRADSLRKQHHLDPSSAVRKTKREKMETMLRNDSLSSDQSESVRPPPPRPHKSKKGGKMRQVSLSSSEEELASTPEYTSCDDVELESESVSEKGDSQKGKRKTSEQGVLSDSNTRSERQKKRMYYGGHSLEEDLEWSEPQIKDSGVDTCSSTTLNEEHSHSDKHPVTWQPSKDGDRLIGRILLNKRLKDGSVPRDSGAMLGLKVVGGKMTESGRLCAFITKVKKGSLADTVGHLRPGDEVLEWNGRLLQGATFEEVYNIILESKPEPQVELVVSRPIGDIPRIPDSTHAQLESSSSSFESQKMDRPSISVTSPMSPGMLRDVPQFLSGQLSIKLWFDKVGHQLIVTILGAKDLPSREDGRPRNPYVKIYFLPDRSDKNKRRTKTVKKTLEPKWNQTFIYSPVHRREFRERMLEITLWDQARVREEESEFLGEILIELETALLDDEPHWYKLQTHDVSSLPLPRPSPYLPRRQLHGESPTRRLQRSKRISDSEVSDYDCEDGVGVVSDYRHNGRDLQSSTLSVPEQVMSSNHCSPSGSPHRVDVIGRTRSWSPSAPPPQRNVEQGHRGTRATGHYNTISRMDRHRVMDDHYSSDRDRSHPRTGSVQTSPSSTPGTGRRGRQLPQLPPKGTLERSAMDIEERNRQMKLNKYKQVAGSDPRLEQDYHSKYRSGWDPHRGADTVSTKSSDSDVSDVSAVSRTSSASRFSSTSYMSVQSERPRGNRKISVFTSKMQNRQMGVSGKNLTKSTSISGDMCSLEKNDGSQSDTAVGALGTSGKKRRSSIGAKMVAIVGLSRKSRSASQLSQTEGGGKKLRSTVQRSTETGLAVEMRNWMTRQASRESTDGSMNSYSSEGNLIFPGVRLASDSQFSDFLDGLGPAQLVGRQTLATPAMGDIQVGMMDKKGQLEVEIIRARGLVVKPGSKTLPAPYVKVYLLDNGVCIAKKKTKVARKTLEPLYQQLLSFEESPQGRVLQIIVWGDYGRMDHKSFMGVAQILLDELELSNMVIGWFKLFPPSSLVDPTLAPLTRRASQSSLESSTGPSYSRS
Protein: Zg1 (Q90410)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENSSEPSRWVSPGLLSPDPLVNYTTDSGLLPPVDVDEPFYSSSETDLLPSYYSTSVQSRASSSYRHSPVRQVYSSQSILGNIQWLDNSAGHSLNSPYNPTSTVWSSSPFPKTPLHSHTSTSIYQNTATPSFTSPKEGFPSPSRDGKDSPRLQEVLKAERLSPMSGSGSSFLNLSSATGGVYGPSPHMLSPYGSYMSTSQDYSSAALYSTGGPWMSPSSYSPKLRNKMRLSPPEARECVNCGATATPLWRQDGTGHYLCNACGLYHKMNGQNRPLIRPKKRLIVSKRAGTQCANCHTSTTTLWRRNASGEPVCNACGLYFKLHNVNRPLTMKKDGIQTRNRKVSNRNKKGKKNAASEVYPDMSHMAPPDEHVGAYSLNPGPLLSYSHPAHLLPTSTLHSSTTLPYTHHPNSGMMPTLV
Protein: methylcrotonoyl-CoA carboxylase (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta) (A0A140VK29)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTDFGIFRM
Protein: SPRY domain-containing protein (Q57U67)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGAAPSRETLRRGLYNVPTQMKNNVDSSRSQSKPDIVLIPLIKEYFPSADCPLFVQFHKMRCDPGVNYYFRHPLYPGDLSRIPNVHSNDARSSNRSRDALYSEFVEQTEERLFDTDNEMRQAHELSMSDRSAGGSPSFHMEGAKTANVGKKVLPIICAVAFLHDREKFEQLQQTQGTPGGSRVPHVLMGKENSDILEGKVVNIIGFFGMLPREIERKPLTSPVIFSPVSPGLSATGKGIAAPSMLKNSLSLPCTARGPSHGSSQDLQQLIAPLSSQASVASGNELRNRPSFVPTPHVPPERCPLTASAGAFSLVSSLGGTPAREPSARQRPFLQSEGLLREMDQALSYRCTALEERLSRFGLPAPAAPEPLTAVVFMTKSAGEQNLCRVTFVAAKTYHGQLVEAGVLKQRGNGPSPPLESERRYLPPLETFSFSSLMTNVPFISFVYEMRCRWGRFGFFSRRVDSPSLRMGSLNASSSFTYGFTGGAHSEAPNPEETHRGFAMWLTKNGVFHGRIERELAEHLCFCMAEQPDFMSVPAATLPIGGGYWRFRGLVDRNNPRPIQLCGDGAEAADPLDVYVMGSPAVGGFDEGDVLKYDQTSRSWVANRDIPLDAVVLAAMRPFCKAARTAPPDDIGWVTIEVEEQDEMGVEDQDHLETAGKRDMDTGAVVRQEDRDGTVVRKRVHVREGNFYIYRFELNGEVHYHGTVPDFANPNKKRASHSSSVGARSVAPMGPAVVARRFDNTNERGRQHSVGLTADRSTNEHSLSVTSTFSPPFVESFMGSERTSATFLASPLQPVREAISRSVGTVSYSNRGYESTGSQSSFPVVPVTPDTMFPPSRGLTTPVARRRSTFVPVGSEVEVDESQRDTNESDGGPTAFVRRFIDSTVYIWDWRYCADR
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (C9JIR6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
Sequence:
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLEDWSFFAVYDGHAGSRVANYCSTHLLEHITTNEDFRAAGKSGSALELSVENVKNGIRTGFLKIDEYMRNFSDLRNGMDRSGSTAVGVMISPKHIYFINCGDSRAVLYRNGQVCFSTQDHKPCNPREKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEILRAEEDEFIILACDGIWDVMSNEELCEYVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSIVLVCFSNAPKVSDEAVKKDSELDKHLESRVEEIMEKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRNVIEAVYSRLNPHRESDG
Protein: protein acetyllysine N-acetyltransferase (EC 2.3.1.286) (M0QZ09)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
DKGKCGLPEIFDPPEELERKVWELARLVWQSSSVVFHTGAGISTASGIPDFRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGPKQEPCAQHNGSEPASPKRERPTSPAPHRPPKRVK
Protein: Cytochrome b559 subunit alpha (PSII reaction center subunit V) (P09190)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:34937700}.
Interaction partners:
- Photosystem II extrinsic protein U
- Photosystem II extrinsic protein O
- Photosystem II D2 protein
- Cytochrome b559 subunit beta
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein J
- Photosystem II protein D1 2
- Photosystem II reaction center protein Y
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein K
Sequence:
MSGTTGERPFSDIVTSIRYWVIHSITIPMLFIAGWLFVSTGLAYDAFGTPRPDEYFTQTRQELPILQERYDINQEIQEFNQ
Protein: Rifin (Q8I2D4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYSKILLFLIPLNTLVTSSSYVHNKNKPYITPRHTPICTSRVLSECDKQSSIYDNDADMKSVKENFERQTTQRLREYDERMKDKRKKRKEERNKNIQKIIDKDKMEKSLAEKVEIGCLRCGCGLGGVAASVGLFGGLGTYGWKSAAIATATNAAMAEATAKGAEAGVKTLIDKLKEAFPIPNLFDPSFEKAITTETYCNEALISGAVKQKYELLCAKGSSCENYSLFSHYRSGGEAEGARALVEGVKKIVGEAMGKASEETLKATESQMASLKSGKLAEISETSYSSYRAIGYSVLAILIIVLVMIIIYLVLRYRRKKKK
Protein: Protein phosphatase EYA2 (EC 3.1.3.48) (Eyes absent homolog 2) (O08575)
Organism: Mus musculus (Mouse)
Function: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis (By similarity). Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10490620}. Nucleus {ECO:0000269|PubMed:10490620}. Note=Retained in the cytoplasm via interaction with GNAZ and GNAI2 (By similarity). Interaction with SIX1, SIX2, SIX4 or SIX5 is required for translocation to the nucleus. {ECO:0000250|UniProtKB:O00167}.
Interaction partners:
- Homeobox protein SIX1
- Homeobox protein SIX4
- Dachshund homolog 2
- Homeobox protein SIX2
- Homeobox protein SIX5
- Paired box protein Pax-3
- Dachshund homolog 1
Sequence:
MLEVVTSPSLATSSDWSEHGAAVGTLSDREGIAKSAALSVPQLFVKSHPRVPPGQSSTAMAAYGQTQYSTGIQQAPPYTAYPTPAQAYGIPPYSIKTEDSLNHSPSQSGFLSYGPSFSTAPAGQSPYTYPVHSTAGLYQGANGLTNTAGFGSVHQDYPSYPSFSQNQYPQYFSPSYNPPYVPASSLCSSPLSTSTYVLQEAPHNVPSQSSESLAGDYNTHNGPSTPAKEGDTERPHRASDGKLRGRSKRNSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSTDGFHSTAPGASLCLGTGVHGGVDWMRKLAFRYRRVKEMYNTYRNNVGGLIGAPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYIVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL