wanglab/gogpt-training-data huggingface dataset:
Protein: Sorbitol dehydrogenase (SDH) (EC 1.1.1.-) ((R,R)-butanediol dehydrogenase) (EC 1.1.1.4) (L-iditol 2-dehydrogenase) (EC 1.1.1.14) (Polyol dehydrogenase) (Ribitol dehydrogenase) (RDH) (EC 1.1.1.56) (Xylitol dehydrogenase) (XDH) (EC 1.1.1.9) (Q00796)
Organism: Homo sapiens (Human)
Function: Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with D-sorbitol (D-glucitol), L-threitol, xylitol and ribitol as substrates, leading to the C2-oxidized products D-fructose, L-erythrulose, D-xylulose, and D-ribulose, respectively. Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism. The polyol pathway is believed to be involved in the etiology of diabetic complications, such as diabetic neuropathy and retinopathy, induced by hyperglycemia. May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility. May have a more general function in the metabolism of secondary alcohols since it also catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol. To a lesser extent, can also oxidize L-arabinitol, galactitol and D-mannitol and glycerol in vitro. Oxidizes neither ethanol nor other primary alcohols. Cannot use NADP(+) as the electron acceptor.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:Q64442}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64442}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q64442}. Note=Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface. {ECO:0000250|UniProtKB:Q64442}.
Interaction partners:
- Aldo-keto reductase family 1 member B1
- Xylulose kinase
- Ketohexokinase
- Aldo-keto reductase family 1 member B10
- L-xylulose reductase
- Hexokinase-1
- Hexokinase-2
- Hexokinase HKDC1
- Hexokinase-3
- Triokinase/FMN cyclase)
Sequence:
MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNFIVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFCATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCGAGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGQLGCKPEVTIECTGAEASIQAGIYATRSGGNLVLVGLGSEMTTVPLLHAAIREVDIKGVFRYCNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP
Protein: S-adenosylmethionine synthase 4 (AdoMet synthase 4) (EC 2.5.1.6) (Methionine adenosyltransferase 4) (MAT 4) (Q9LUT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14505352}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- Homocysteine S-methyltransferase 3
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- S-adenosylmethionine decarboxylase proenzyme 1
- At1g77670
- S-adenosylmethionine decarboxylase proenzyme 2
- S-adenosylmethionine decarboxylase proenzyme 3
Sequence:
MESFLFTSESVNEGHPDKLCDQISDAILDACLEQDPESKVACETCTKTNMVMVFGEITTKANVDYEQIVRKTCREIGFVSADVGLDADNCKVLVNIEQQSPDIAQGVHGHLTKKPEEVGAGDQGHMFGYATDETPELMPLTHVLATKLGAKLTEVRKNGTCPWLRPDGKTQVTIEYINESGAMVPVRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVASGLARRVIVQVSYAIGVPEPLSVFVDSYGTGKIPDKEILEIVKESFDFRPGMISINLDLKRGGNGRFLKTAAYGHFGRDDADFTWEVVKPLKSNKVQA
Protein: Calcineurin B homologous protein 2 (Chp-2) (Q810D1)
Organism: Rattus norvegicus (Rat)
Function: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Binds to and activates SLC9A1/NHE1 in a serum-independent manner, thus increasing pH and protecting cells from serum deprivation-induced death. Also plays a role in the regulation of cell proliferation and tumor growth by increasing the phosphatase activity of PPP3CA in a calcium-dependent manner. Activator of the calcineurin/NFAT signaling pathway. Involved in the cytoplasmic translocation of the transcription factor NFATC3 to the nucleus (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12576672}. Nucleus {ECO:0000269|PubMed:12576672}. Cell membrane {ECO:0000269|PubMed:12576672}. Note=Exported from the nucleus to the cytoplasm through a nuclear export signal (NES) pathway. May shuttle between nucleus and cytoplasm (By similarity). Predominantly localized in a juxtanuclear region. Colocalizes with SLC9A3 in the juxtanuclear region and at the plasma membrane. {ECO:0000250}.
Interaction partners:
- Sodium/hydrogen exchanger 1
Sequence:
MGSRSSHVALIPDVDQIRRETGFSQASLLRLYHRFQALDREEKGFLSRLDLQQIGALAVNPLGDRIIDSFFPNGSQRVYFAGFARVLAYFRPIDEDDATLRDPKQPEPLNSRMNKLRFAFQLYDLDRDGKISRNEMLQVLRLMVGVQVTDEQLESITDRTVQEADEDGDGAVSFLEFAKSLEKMNIEQKMSIRILK
Protein: V-type proton ATPase subunit E 1 (V-ATPase subunit E 1) (V-ATPase 31 kDa subunit) (p31) (Vacuolar proton pump subunit E 1) (P36543)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:29993276}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit d 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit G 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase subunit F
- V-type proton ATPase 116 kDa subunit a 1
Sequence:
MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMNQARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCRKQDFPLVKAAVQKAIPMYKIATKNDVDVQIDQESYLPEDIAGGVEIYNGDRKIKVSNTLESRLDLIAQQMMPEVRGALFGANANRKFLD
Protein: Uncharacterized transporter C1002.16c (Q9US44)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Barrier septum. Cell tip. {ECO:0000255, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative glutamine-dependent NAD
Sequence:
MKSLSHTSSNKSNGSIFTKADESEKVISRSNTASPISIENTHLTKSERDSLLFRLDLVLAPTIMILYLVAFLDRSNIGNAKVAGLPEDLKLKGDQFNIIASVFYVTFILFEMPTTLLMKKVQPKRMLAFIVISYSLTTIFTGFCHNFGGLLAARLVLGFCEAGLFPCLALYLTMIYSRVELAPRIAYLFASSALSGAFGGLFAYAVLHMDGVGGFAGWRWLFIIEGLIGFVCGVAVYFIIPNDITKAWFLSKTHQEMMRKRQLERAADLEAAHFDWKGVKSAFTDFKVYLYALSEFGQDTCLYGFSTFLPAIISGMGYTSLSVQYMTIPVYILGAATYIAASFLSDRFHHRGIILIIGNIFPIVGYILLLACQNNKSVLYFACYLCSVGVYTGAGLNVTWLSANIAPHYKRATAISLQLAIANSSGILAGQIYRYPPKYIAGHLTSLIAIFISTVLHVVNIFFLKHQNSKKQKSLASSSTIDLSEQPKDDKDARFHYIL
Protein: Zyxin (H0Y2Y8)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
AAPRPSPAISVSVSAPAFYAPQKKFGPVVAPKPKVNPFRPGDSEPPPAPGAQRAQMGRVGEIPPPPPEDFPLPPPPLAGDGDDAEGALGGAFPPPPPPIEESFPPAPLEEEIFPSPPPPPEEEGGPEAPIPPPPQVSSGYVPPPVATPFSSKSSTKPAAGGTAPLPPWKSPSSSQPLPQVPAPAQSQTQFHVQPQPQPKPQVQLHVQSQTQPVSLANTQPRGPPASSPAPAPKFSPVTPKFTPVASKFSPGAPGGSGSQPNQKLGHPEALSAGTGSPQPPSFTYAQQREKPRVQEKQHPVPPPAQNQNQVRSPGAPGPLTLKEVEELEQLTQQLMQDMEHPQRQNVAVNELCGRCHQPLARAQPAVRALGQLFHIACFTCHQCAQQLQGQQFYSLEGAPYCEGCYTDTLEKCNTCGEPITDRMLRATGKAYHPHCFTCVVCARPLEGTSFIVDQANRPHCVPDYHKQYAPRCSVCSEPIMPEPGRDETVRVVALDKNFHMKCYKCEDCGKPLSIEADDNGCFPLDGHVLCRKCHTARAQT
Protein: DNA-binding response regulator (Response regulator homolog TrcR) (Transcriptional regulatory protein TcrX) (Two component transcriptional regulator TrcR) (Q50806)
Organism: Mycobacterium tuberculosis
Interaction partners:
- Sensor-type histidine kinase PrrB
- Sensor-type histidine kinase PrrB
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MTTMSGYTRSQRPRQAILGQLPRIHRADGSPIRVLLVDDEPALTNLVKMALHYEGWDVEVAHDGQEAIAKFDKVGPDVLVLDIMLPDVDGLEILRRVRESDVYTPTLFLTARDSVMDRVTGLTSGADDYMTKPFSLEELVARLRGLLRRSSHLERPADEALRVGDLTLDGASREVTRDGTPISLSSTEFELLRFLMRNPRRALSRTEILDRVWNYDFAGRTSIVDLYISYLRKKIDSDREPMIHTVRGIGYMLRPPE
Protein: C-reactive protein (Dare-CRP) (Short-chain pentraxin) (Dare-PTX) (Q0IIP8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis, and complement fixation through its calcium-dependent binding to phosphorylcholine.
Subcellular location: Secreted {ECO:0000255|RuleBase:RU362112}.
Interaction partners:
Sequence:
MLVVFLCLLSVTLEATEGFKNLSGKVLQFKTATDNSYVKLYPEKPLSLSAFTLCMRVATELPLDREVILFAYYTPDVDELNVWRERDGRVSLYIQSSKDAAFFRLPPLSTLQTHLCVAWESATGLTAFWMDGRRSLHQVYRKGYSIRSGGTVVLGQDPDSYVGSFDVDQSFVGEIANLQMWDYVLSSAQIKAVYYNQDNRVKGNVFDWDTIEYDVTGNVLVATDN
Protein: NADH-cytochrome b5 reductase 1 (b5R.1) (EC 1.6.2.2) (Humb5R2) (NAD(P)H:quinone oxidoreductase type 3 polypeptide A2) (Q9UHQ9)
Organism: Homo sapiens (Human)
Function: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome b5 type B
- Cytochrome b5
- Sulfite oxidase, mitochondrial
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Uridine 5'-monophosphate synthase
- Stearoyl-CoA desaturase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- NADPH--cytochrome P450 reductase
Sequence:
MGIQTSPVLLASLGVGLVTLLGLAVGSYLVRRSRRPQVTLLDPNEKYLLRLLDKTTVSHNTKRFRFALPTAHHTLGLPVGKHIYLSTRIDGSLVIRPYTPVTSDEDQGYVDLVIKVYLKGVHPKFPEGGKMSQYLDSLKVGDVVEFRGPSGLLTYTGKGHFNIQPNKKSPPEPRVAKKLGMIAGGTGITPMLQLIRAILKVPEDPTQCFLLFANQTEKDIILREDLEELQARYPNRFKLWFTLDHPPKDWAYSKGFVTADMIREHLPAPGDDVLVLLCGPPPMVQLACHPNLDKLGYSQKMRFTY
Protein: Glutamate receptor IIC (Q9VPV3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}.
Interaction partners:
- FI04462p
- FI23915p1
- Glutamate receptor IIB
- Bruchpilot, isoform J
- Neuropilin and tolloid-like, isoform B
- Vesicular glutamate transporter, isoform A
- Microtubule-associated protein futsch
- Glutamate receptor IIA
- Glutamate receptor 1
- Glutamate receptor IB, isoform B
Sequence:
MWQRILLLGCMWSAFFMCRSRGQQINIGAFFYDDELELEKEFMTVVNAINGPESEQTMRFYPLIKRLKPEDGSVTMQEHACDLIDNGVAAIFGPSSKAASDIVALVCNSTGIPHIEFDISDEGIQAEKPNHQMTLNLYPAQAILSKAYADIVQNFGWRKFTIVYDADDARAAARLQDLLQLREVHNDVVRVRKFHKDDDFRVMWKSIRGERRVVLDCEPNMLVELLNSSTEFGLTGQYNHIFLTNLETYTDHLEELAADNETFAVNITAARLLVNPDPPPYSLPYGYVTQRDNIVYESSDPPRTLIHDLIHDALQLFAQSWRNASFFYPDRMVVPRITCDFAASGGRTWAMGRYLARLMKGTSGVNNTNFRTSILQFDEDGQRITFNIEVYDPLDGIGIAIWDPRGQITQLNVDVKAQKKMIYRVATRIGPPYFSYNETARELNLTGNALYQGYAVDLIDAIARHVGFEYVFVPVADQQYGKLDKETKQWNGIIGEIINNDAHMGICDLTITQARKTAVDFTVPFMQLGVSILAYKSPHVEKTLDAYLAPFGGEVWIWILISVFVMTFLKTIVARISKMDWENPHPCNRDPEVLENQWRIHNTGWLTVASIMTAGCDILPRSPQVRMFEATWWIFAIIIANSYTANLAAFLTSSKMEGSIANLKDLSAQKKVKFGTIYGGSTYNLLADSNETVYRLAFNLMNNDDPSAYTKDNLEGVDRVRKNRGDYMFLMETTTLEYHREQNCDLRSVGEKFGEKHYAIAVPFGAEYRSNLSVAILKLSERGELYDLKQKWWKNPNASCFEEPDPDATPDMTFEELRGIFYTLYAGILIAFLIGITEFLVYVQQVALEERLTFKDAFKKEIRFVLCVWNNRKPIVAGTPISSVRTTPRRSLDKSLDRTPKSSRRVVIGRSSEEMREMAQGSGSSSGSNNAGRGEKEARV
Protein: C2H2-like zinc finger protein (T1K7.2 protein) (Q9FZE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- B3 domain-containing protein REM17
- Putative F-box/kelch-repeat protein At1g20940
- Homeobox-leucine zipper protein-like protein
- Zinc finger protein ZAT3
- At1g80245 component)
- 2-oxoglutarate
- Pentatricopeptide repeat-containing protein At1g71060
- Pentatricopeptide repeat-containing protein At1g33350
- Transcription factor TCP23
- 2-oxoglutarate
Sequence:
MEQFKERKFVCKFCSKRFPCGKSLGGHIRTHMNENSADSDEDEADKLKMIDENGGQSSYGLRENPKKNKRFVDHRQIMALKQQQQQQQLQELRRCRECGKGFVSSKALCGHMACHSEREKIVMDSQSDTEASSSPIRRRSKRVVVKPHHKAAFVVGGNGIMNQSISASSDASEIEPEQEEMARSLMMLSRDSSFKKGHNSLAESSDNNSVILETKSSSGEQVKMFNVKNVEELCKKNKLVVDNQMRSGEENGDVHYDSDNSDSGYFRNGPKKLDSDVSVDGFFRNKTIMGSGSGFNSSPTKQDRDMNRFRKEWYKEGGSGSGSGSGRSSTKYDLRKSKRGFPSHGRKKIKYEFTESVYDSGEHSLETDSCADTNRTIKIHSKSPMVKKANGAKKKSKGHECPICFRVFKSGQALGGHKRSHFIGNQEHRTLVIQHQVAHEMHTLIDLNLPAPIDE
Protein: C-C motif chemokine (G3V896)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU361150}.
Interaction partners:
- C-C chemokine receptor type 10
- C-C motif chemokine ligand 26
- C-X-C motif chemokine ligand 17
- C-X-C motif chemokine 14
- C-C motif chemokine 5
- C-X-C motif chemokine 10
- Stromal cell-derived factor 1
- C-C motif chemokine
- C-X-C motif chemokine ligand 13
- C-X-C motif chemokine
Sequence:
CPAVGDVSVPFLVAILPIASSCCTEVSHHIPRRLLERVNSCSIQRADGDCDLAAVILHVKRRRICVSPHNPTLKRWMSASEMKNGKENLCPRKKQDSGKDRKGHTPRKHGKHGTRRIHGTHGHEAPR
Protein: DNA topoisomerase I (EC 5.6.2.1) (DNA topoisomerase 1) (F4K3F4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGTETVSKPVMDNGSGDSDDDKPLAFKRNNTVASNSNQSKSNSQRSKAVPTTKVSPMRSPVTSPNGTTPSNKTSIVKSSMPSSSSKASPAKSPLRNDMPSTVKDRSQLQKDQSECKIEHEDSEDDRPLSSILSGNKGPTSSRQVSSPQPEKKNNGDRPLDRASRIIKDESDDETPISSMFRKKIDSGMSGGNQLSNDEKKPLVQKLHQNGSTVKNEVPNGKVLGKRPLEKNSSADQSSLKKAKISASPTSVKMKQDSVKKEIDDKGRVLVSPKMKAKQLSTREDGTDDDDDDDVPISKRFKSDSSNSNTSSAKPKAVKLNSTSSAAKPKARNVVSPRSRAMTKNTKKVTKDSKYSTSSKSSPSSGDGQKKWTTLVHNGVIFPPPYKPHGIKILYKGKPVDLTIEQEEVATMFAVMRETDYYTKPQFRENFWNDWRRLLGKKHVIQKLDDCDFTPIYEWHLEEKEKKKQMSTEEKKALKEEKMKQEEKYMWAVVDGVKEKIGNFRVEPPGLFRGRGEHPKMGKLKKRIHPCEITLNIGKGAPIPECPIAGERWKEVKHDNTVTWLAFWADPINPKEFKYVFLGAGSSLKGLSDKEKYEKARNLTDHIDNIRTTYTKNFTAKDVKMRQIAVATYLIDKLALRAGNEKDDDEADTVGCCTLKVGNVECIPPNKIKFDFLGKDSIQYVNTVEVEPLVYKAIGQFQAGKSKTDDLFDELDTSKLNAHLKELVPGLTAKVFRTYNASITLDEMLSQETKDGDVTQKIVVYQKANKEVAIICNHQRTVSKTHGAQIEKLTARIEELKEVLKELKTNLDRAKKGKPPLEGSDGKKIRSLEPNAWEKKIAQQSAKIEKMERDMHTKEDLKTVALGTSKINYLDPRITVAWCKRHEVPIEKIFTKSLLEKFAWAMDVEPEAKRKPAFLLFIFLPCLEFYYLSE
Protein: Alkylglycerone-phosphate synthase (Alkyl-DHAP synthase) (EC 2.5.1.26) (Q7YWB6)
Organism: Leishmania major
Subcellular location: Peroxisome {ECO:0000256|RuleBase:RU363113}.
Interaction partners:
- Dihydroxyacetonephosphate acyltransferase
- Peroxin-7
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate acyl transferase
- Putative peroxisome targeting signal 1 receptor
- RING-type E3 ubiquitin transferase
- Peroxin-12
- Peroxin-13
- Peroxisomal membrane protein PEX14
- Putative sterol carrier protein
Sequence:
MPADEAQAPTQTEVYDRLKWNGWGVEDVQMQIDDENPLWVRHVDGKPIKNLLEFLYQEISGGVGPKEIPPLSPSIPLEKALAKLNKANINEAFMKDISAVLEKSQIRPDGKSRLCHIAGKNYRDLWRVRKGMVEHAPDCILLPNSHKDCVEIMRLAHKHNVVVIPFGGGTNVTGGVEADPFERARMIISVDMRRMNRMISIDRESRLATFETGVLGPDLDAQLFRHGFMLGHDPDSYIYSTLGGWIGARGSGAMSNQYGDIEDMVVAVKVATPTGIIETPTTSRTCGVDLNGLFIGSEGSFGIITEATIKLETIPETKLYEGYLFPTFEAGFSAFYTCTAKGIHPCTMRLYDEDDFRMSMAMSTTKHSFFQRLVSMGVKSFLERYRGWNLRRISLVIVGFEGTPDRVKFQRSETAAVFKQYGGVGVGRSAGATWQDKKYDLPYIRDFALSLSHWADVFETSVLYSQAIPCWRAVKAAVRQVWKEHGHRGWIGCHTAHQYKYGCCLYFTFASAQKDDMDMKIFLAIKKRATEAMLAHTGNLTHHHGIGYEHVPWMSRYMGPDALDLLFAVKQKVDPKNICNPGKLLPSPPRENESAAALKARQQRELMFDKMGVPGAVASHI
Protein: Iron-sulfur cluster assembly protein, putative (Q38DM2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ferroxidase
- cysteine desulfurase
- cysteine desulfurase
- Aminotransferase class V domain-containing protein
- Cytochrome oxidase assembly protein, putative
- Iron-sulfur assembly protein 2
- Uncharacterized protein
- Adrenodoxin, putative
- Electron transfer protein, putative
- Heat shock 70 kDa protein, mitochondrial, putative
Sequence:
MRRLISSHIVLPTLAASLRSLYSPLVEEHYNNPRNVGKLDKSDPNVGTGLRGAPECGDMTQMQVKVNPETMVIEDVKFKAFGCGSAIAASSYASQAIRGKTLAEALQLTNKRIARELSLPPVKLHCSMLAEETIQAAVENYLSKNPSLKSKVHKKKTETPSISQTSQVASKSEAVGEVSS
Protein: Nuclear pore complex-interacting protein family member B3 (Nuclear pore complex-interacting protein-like 3) (Protein pps22-1) (Q92617)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVKLSIVLTPQFLSHDQGQLTKELQQHVKSVTCPCEYLRKVINTLADHHHRGTDFGGSPWLHVIIAFPTSYKVVITLWIVYLWVSLLKTIFWSRNGHDGSTDVQQRAWRSNRRRQEGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINHHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKALCNWVRMAAAEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSADDNLKTPPECVLTPLPPSADDNLKTPPECVLTPLPPSADDNLKTPPECLLTPLPPSADDNLKTPPECLLTPLPPSALPSAPPSADDNLKTRAECLLHPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTALPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQQMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQQMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPPLATQEAEAEKPRKPKRQRAAEMEPPPEPKRRRVGDVEPSRKPKRRRAADVEPSSPEPKRRRVGDVEPSRKPKRRRAADVEPSSPEPKRRRVGDVEPSRKPKRRRAADVEPSLPEPKRRRLS
Protein: Checkpoint protein hus1 (P78955)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential in controlling the S-M checkpoint that couples mitosis to the completion of DNA replication. It is also required for the response to DNA damage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Checkpoint protein rad17
- DNA repair protein rad9
- DNA damage checkpoint control protein rad1
- Replication factor C subunit 2
- Protein kinase rad3
- Replication factor C subunit 4
- S-M checkpoint control protein rad4
- Replication factor C subunit 5
- Replication factor C subunit 3
- DNA repair protein crb2
Sequence:
MRFKTRISNLYTLTRLVQALDKIGRFCWLRLMPETVNFVIVPDFRMTQVWSVLEVETIFEDYVVQSNADNVINLEVPIDNFYKALRSAANASDSTVRLSKKNNQPLLSLSTTWSGRAFGSNIVTHNIPVRVLSQSYVSVIKEPTAPEPDCHIFLPQLNFLRHVVDKYKSLSDRIIMSANMSGELQLSVNIPSARVSTKWKGLENPELDPSQVEDISRHPSQTRAPEEFVHMRLDSKDLVNMLKISSVAKRVIACFCEGHALVLYVYITDPEDEHTAVLTYYISTYVD
Protein: Uncharacterized protein YqcG (C1P612)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YnbG
- Uncharacterized protein YobI
- UPF0603 protein YgcG
- Protein YobF
Sequence:
MSEENKENGFNHVKTFTKIIFIFSVLVFNDNEYKITDAAVNLFIQI
Protein: UPF0193 protein EVG1 (Q9BZE7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASQKQMEVVTKGTGFRRRPKTITYTPGTCELLRVMMKESKLTNIQQRHIMDIMKRGDALPLQCSPTSSQRVLPSKQIASPIYLPPILAARPHLRPANMCQANGAYSREQFKPQATRDLEKEKQRLQNIFATGKDMEERKRKAPPARQKAPAPELDRFEELVKEIQERKEFLADMEALGQGKQYRGIILAEISQKLREMEDIDHRRSEELRKGLATT
Protein: Small ribosomal subunit protein uS13 (40S ribosomal protein S18) (Ke-3) (Ke3) (P62270)
Organism: Mus musculus (Mouse)
Function: Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS8
Sequence:
MSLVIPEKFQHILRVLNTNIDGRRKIAFAITAIKGVGRRYAHVVLRKADIDLTKRAGELTEDEVERVITIMQNPRQYKIPDWFLNRQKDVKDGKYSQVLANGLDNKLREDLERLKKIRAHRGLRHFWGLRVRGQHTKTTGRRGRTVGVSKKK
Protein: Putative fatty-acid--CoA ligase fadD11 (EC 6.2.1.-) (Acyl-CoA synthetase) (P9WQ53)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv1549
- Putative acyltransferase plsB1
- Probable fatty acid synthase Fas
- Probable fatty-acid-CoA ligase FadD4
- Long-chain-fatty-acid--CoA ligase FadD15
- Galactose-1-phosphate uridylyltransferase
- Triacylglycerol lipase
- Esterase LipQ
- Probable aldehyde dehydrogenase
Sequence:
MARLRGAGAAGRCRPGRFGSSARRHGLADDGEPDRVLPARRRCSARRRHLVFGVQHPARRAADLRVRQRGDQGGHLRATVRRSRSRQRCAHRTHRLRRWRAPGTLSLTDLYAAASGDFFDFESTWRAVQPEDIVTLIYTSGTTGNPKGVEMTHANLLFEGYAIDEVLGIRFGDRVTSFLPSAHIADRMTGLYLQEMFGTQVTAVADARTIAAALPDVRPTVWGAVPRVWEKLKAGIEFTVARETDEMKRQALAWAMSVAGKRANALLAGESMSDQLVAEWAKADELVLSKLRERLGFGELRWALSGAAPIPKETLAFFAGIGIPIAEIWGMSELSCVATASHPRDGRLGTVGKLLPGLQGKIAEDGEYLVRGPLVMKGYRKEPAKTAEAIDSDGWLHTGDVFDIDSDGYLRVVDRKKELIINAAGKNMSPANIENTILAACPMVGVMMAIGDGRTYNTALLVFDADSLGPYAAQRGLDASPAALAADPEVIARIAAGVAEGNAKLSRVEQIKRFRILPTLWEPGGDEITLTMKLKRRRIAAKYSAEIEELYASELRPQVYEPAAVPSTQPA
Protein: Zinc finger protein 679 (Q8IYX0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAKRPGSPGSREMGLLTFRDVVIEFSLEEWQCLDHAQQNLYRDVMLENYRNLVSLGIAVSKPDLITCLEQNKEPWNIKRNEMVTKHPVMCSHFTQDLPPELGIKDSLQKVIPRRYGKSGHDNLQVKTCKSMGECEVQKGGCNEVNQCLSTTQNKIFQTHKCVKVFGKFSNSNRHKTRHTGKKHFKCKKYGKSFCMVSQLHQHQIIHTRENSYQCEECGKPFNCSSTLSKHKRIHTGEKPYRCEECGKAFTWSSTLTKHRRIHTGEKPYTCEECGQAFSRSSTLANHKRIHTGEKPYTCEECGKAFSLSSSLTYHKRIHTGEKPYTCEECGKAFNCSSTLKKHKIIHTGEKPYKCKECGKAFAFSSTLNTHKRIHTGEEPYKCEECDKAFKWSSSLANHKSMHTGEKPYKCE
Protein: RNA helicase (EC 3.6.4.13) (A0A0D9SF53)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGSSRSQEEMKGTISSPVQKDHAPLWSKCLHEMPYFVKKVHAGIFRSPACSHGSLRYLRPTNPPDEDNHNSCRHESNLERDAQKCVNWSVTTKMRTAC