wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein, isoform C (M9PHU0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform C
- IP09718p
- Cysts, isoform C
- Uncharacterized protein, isoform B
Sequence:
MESLGLGSRRNNGSNSTAAPTTGQGGVVGGGGVAGKVLVHTKLKQQQQQQHSNQNYYTQQQTQLQRLKQQQQKLQQQQQQQQQQQLEAVHGGVAKQCLQFPPPPDYPPPITGGGGSPVNTTPGRRQQLPRYPDPDPDAIEICNESATLETSPYHLKQLAARHSKTLGRNLGHQPHHHHTVHLHHDYSYAYYEPGAAMRHSNVPGAVSSGGGGGGGGAGRVSSVVDTSSSSSPTAEPPPNSIRALLSKGKKNKQLVSPATLQSYQTRYHKLTTKSGMGQSENFYEEINAAALQTSSGHHLRSTVGSHSAGSLNQTLVEEELRRVQNRHHKILGELNLSVEAMLMPESPPKSIDQQPLGSGSGGSGGAEATPPQPSVSVTAASGQPPTILARLTSASADNICDSGGEAGKRTKTAPGCPGGGVEQLLTTTCGDLDSGFSGSSGASYIGSLRLSKTQHIKCARQTPTVGTQSCRSFQRAATVYDEAGMSGGGGQSGSSFLTRASCGRRILSCARIRAAEDPGPNHRIAGGNGIQTVQTTATESKARSFWSRKGWRKLPGFSTSTSSINDTGLSDEHKLNSGSWEDTLDEPHHHHAHHSHHQQHLHQHHSHLSQRHQQQQQQQQQLQQTSFIGSPPSSASITTAQLHSAFSRRIAEQRERDQRDQRDQREAVGCTAATIAGGSFSANGGQAAVGVGVGSSSSCGSSSERDTKSPCRERDRNLERDRDRERDKNDDLGEEEVLTEEEQTSSSVSSLSAGNQRNSQLRSTFNKAKQHLSFDKWRTAATGSATGSASGPGSSATDSNNAASNMIMRRASACTMPSSGGGGGAGVGSSQREEATTPGESPGGRLSRWFSIRRGSSHQYDVGGRDGRHSTASSFDTPDSGSGNSPKNGSNAVAGTGGAGSQGVALDAASPQKLANLGASKMMPGVPESEDDEATANRFDVDLMMTPGSRANGTARTAHNRLIVPMLPPAPAGLSQQQLKRRHIVAAIVHSENSYVATLQRLVNDYKKPLEECSPPVLNPVKIATLFHCLPDILHSHKLFRISLAECVRNWDRDEKIGDCFVSAFGKPQLLEIYSGFINNFSAAMELAKMEEKRKSALADFFKVKQISAHDRLSFFGLMVKPVQRFPQFILFLQDLLKYTPQGHHDRMSLQLALSQLELLAELLNESKREAEQYQAFKEMLGHISGTFNARSLSLSSVSVSDSAGGHRPRYLLREDNVTHMEFNQAGFIVKCKQRRLLLLNDKVICVSVAPKQSHDFGATEKLTFKWMFPVNDVEIVDNSTSATLSRILTAGLNRGGSLKSNGSSGANGSPYANSTLPGHGGGVSGFSGFGDPHSSPAAQLTNGADNLCSEMSTLMYDYEVISRIQDLVSSLKGSYKELNANTTRNVLNLIQGSIQRKDEEMAWVDSCCLQLIGRHKSGKEETFTFQTQTPAVKKEWITELRLAQLALDPNNSPAWERGGSHPQPAHHHPHHHPLQHPHAGAGDPRQTQEQLQLQEAVQQKQSRKMPLFVKAMPVYKSQHQTEVRCGCYYSIANDTKQSGNARRRHKQLNYLWMCSSDGTSSHITVLAQHPQQAGNLREAGAFDLFETQVSALEFVKGLDQLKSRDEPASLLGDLVWLGTDSRKILIYSARNPEQEEQLGSYSVPGAVQRILYHFDAVYVALSGATVLIFRRGNDGVWQLRDPQTIRLGDTDLVVPSLLPINMCIYASCGNRVYVMNALNGEIQRSFEVQHGATQQVNLMAHSGIGLWISLKNSTMLCLYHTETFKHLQDINIASSVLRHDGKKEQPLNNSSVYVTALMACKGLLWVGTNVGIAVTIPLPRLEGVPIISGGINMSCHAHFGPITFLLPLIPKVYPAYKPPTVGAAPLVPSMGDDLQLPAIDADPKIQELDDGAVVLRRDLAKEEMSSSNPGADSTASSPRSSKLDKQNSLDQSFTAKIRASLANSPAFHRKRFRDDPNRMSKTLPRGLGAAAAGSGAGGASAAGSGTASGNTSQHGEHGICDVYGLYGKLIFVKEDYDAEEGNQGNLMDMMYEGMRRSDPELAAIPGKVCTLDRRLRMKASRPRSLDLSNWSVDSKSSSLYTSSGSEESMGIRHFGGRSVSRNSSSASHKTSGTGSDLGNISENGLMTTADIHHHQQQQQQLNSSAKPDEMSRLGAGNSGLDKPAAAVATLKRKQKQNSKQQQQQNADGPRTVITLMGGRGYWRQMWYNGAGGSPSHKNSSSGGGGGSGSGFSGQTMQSGNPSCSPLTANSNDAHIVVWEKKL
Protein: Protein arginine N-methyltransferase 7 (TbPRMT7) (EC 2.1.1.-) (Q582G4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19254949}.
Interaction partners:
- Histone H4
- Histone H4
- Histone H3, putative
- Histone H3 variant
- Arginine N-methyltransferase, putative
- Probable eukaryotic initiation factor 4A
- Methyltransferase, putative
- Uncharacterized protein
Sequence:
MPPKQHRHQKKDKNDNALQNTIGFVPPGATLASVSGYRPPDAFVNRIDRNIPVPARLRHTPVSLIEAVNDFHYAMMNDEERNNFYYEVLKKHVTPETGVLEIGAGSGLLSLMAAKLGAKWVVAVEGSEELAKLARENIRANNMEHQVKVLHMMSTELKSKHLPEPPDVLLSEIFGTMMLGESALDYVVDVRNRLLKPTTKIIPQFGTQYAVPIECDALHRISSVSGWRDLDLKHMMTLQDTVSIVFAKHYGIRMNSVNFRRLSDPIELFRVDFSSSNRNDIPRRKHFDVVAKESGTAHAMLFYWKVTDDEFVMSTDPEDTVNNFPRDMQWGQALQLLDASNGPLPTPVVFTEGKNYNFECNFSGDRVILHMQLCPESGNGEMTECEGKTT
Protein: Expressed protein (SWIB/MDM2 domain superfamily protein) (Q93W30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Single-stranded DNA-binding protein WHY2, mitochondrial
- Uncharacterized protein At5g08430
- Heat shock 70 kDa protein 9, mitochondrial
- Chromatin structure-remodeling complex protein BSH
- Chaperone DnaJ-domain superfamily protein
- NADH-cytochrome b5 reductase-like protein
Sequence:
MSRVFGACRVLMAKAASSTGAKTGRQGTGILKVVPVSKPLANFIGENEVSRTTAVKKIWEYIKLNNLQNPVNKREILCDEQLKTIFSGKDTVGFLEISKLLSQHFPKSA
Protein: Protein flightless-1 homolog (Flii actin remodeling protein) (F8WK50)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9JJ28}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9JJ28}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9JJ28}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9JJ28}. Note=Colocalizes to actin-rich structures in blastocysts and, together with HRAS, RHOA and CDC42, in migrating fibroblasts. {ECO:0000250|UniProtKB:Q9JJ28}.
Interaction partners:
Sequence:
MAATGVLPFIRGVDLSGNDFKGGNFPEHVKSMTSLRWLKLNRTGLCYLPEELASLQKLEHLSVSHNSLTTLHGELSSLPNLRAVVARANNLKNSGVPDDIFQLDDLSVLDLSHNQLTEIPRDLENSRNMLVLNLSHNSIDNIPNQLFINLTDLLYLDLSDNNLDSLPPQMRRLVHLQTLILNNNPLMHAQLRQLPVMVSLQTLHLRNTQRTQNNMPTSLEGLSNLTDVDLSCNDLTRVPECLYSLVNLKRLNLSSNQISELSLCIDQWTKLETLNLSRNQLTSLPSAICKLSKLKKLYVNSNKIDFDGLPSGVGKLSNLVEFMAANNNLELVPEGLCRCGKLKKLVLNKNRLVTLPEAIHFLTELEVLDVRENPNLVMPPKPVDRTAEWYNIDFSLQNQLRLAGASPATVAAAGGGNSPRDHMARKMRLRRCKDSAHDDQAKQVLKGMSDVAQEKNKSIEENGDLKYSDLKTKRWDKNLEKPQLDYSEFFLEDVGQIPGVSVWQIENFIPIQVDEAFHGKFYEADCYIILKTFLDENGALNWQIFYWIGQDATLDKKAGAAIHAVNLRNYLGAECRTIREEMGDESEEFTVVFDHEISYIEGGTASGFYTVEDTQYPTRLYRVYGKKNIRLESVPLKASSLDPQFVFLLDTGLEIYVWRGGNATLGGTTKARLFAEKINKNERKSKAEITTLMQNQEPPEFWEVLGGQPEEIKKHVPDDFTPIRPKLYKVGLGLGYLELPQINYKLSVEHKDKLKLDVVPELRLVQGLLDTKGVYILDCWSDVFIWIGRKSPRLVRAAALKLGQEVCGMLHRPKHAVVIRNLEGTECQVFKSKFKNWDDVLKVDYTRNAESVKQEAGLSGKVKKDVEQKDQMKADLTALFLPRQPAMPLTEAEQMMEEWNEDLDGMEGFVLEGKKFARLPEEEFGHFHTQDCYVFLCRYWVPVEYEDDKEKGKEKGEEGDDEEKQPEEDFQCVVYFWQGREASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENLKFLSHFKRKFIIHKGKRKLKVDSVQPSLYHIRTNGSALCTRTIQIATDSSNLNSEFCFILKVPFESTDNQGIVYTWVGRAADPDEAKLAEEIMNTMFDDTYSKQVINEGEEPENFFWVGIGSQKTYDEDAEYMKYARLFRCSNEKGYFAVSEKCSDFCQDDLADDDIMLLDNGKEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKDTENPRKLRLVRKGNEPHCFTRCFHAWSAFKTAPA
Protein: Ferredoxin CarAc (Carbazole 1,9a-dioxygenase, ferredoxin component) (CARDO) (Q8GI16)
Organism: Metapseudomonas resinovorans (Pseudomonas resinovorans)
Function: Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Acts as a mediator in the electron transfer from CarAd to CarAa.
Interaction partners:
Sequence:
MNQIWLKVCAASDMQPGTIRRVNRVGAAPLAVYRVGDQFYATEDTCTHGIASLSEGTLDGDVIECPFHGGAFNVCTGMPASSPCTVPLGVFEVEVKEGEVYVAGEKK
Protein: Exocyst complex component 2 (Exocyst complex component Sec5) (Q9D4H1)
Organism: Mus musculus (Mouse)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96KP1}. Note=Recruitment to the midbody does not require RALA, nor RALB. Colocalizes with CNTRL/centriolin at the midbody ring. {ECO:0000250|UniProtKB:Q96KP1}.
Interaction partners:
- Exocyst complex component 4
- Exocyst complex component 1
- Exocyst complex component 6
- Exocyst complex component 8
- Ras-related protein Ral-A
- Ras-related protein Ral-B
- Exocyst complex component 7
- Exocyst complex component 3
- Exocyst complex component 5
- Serine/threonine-protein kinase TBK1
Sequence:
MSRSRQPPLVTGISPNEGIPWTKVTIRGENLGTGPTDLIGLTICGHNCLLTAEWMSASKIVCRVGQAKNDKGDIIVTTKSGGKGTSTVSFKLLKPEKIGILDQSAVWVDEMNYYDMRTDRNKGIPPLSLRPANPLGIEIEKCKLPQKNLEVLFHGMSADFTSENFSAAWYLIENHSTTSFEQLKMAVTNLKRQANKKSEGSLAYVKGGLSTFFEAQDALSAIHQKLEADGTEKVEGSMTQKLENVLNRASNTADTLFQEVLGRKDKADSTRNALNVLQRFKFLFNLPLNIKRNIQKGDYDVVINDYEKAKSLFGKTEVQVFKKYYAEVEAGIEDLRELLLKKLLETPSTLHDQKRYIRYLSDLHAPGDPAWQCIGAQHKWTLKLMQDCKEGHMKSLKGHPGPHSPMLDLDNDVRPSVLGHLSQTASLKRGSSFQSGRDDTWRYKTPHRVAFVEKLTKLVLSQLPNFWKLWISYVNGSLFSETAEKSGQSERSKNVRQRQNDFKKMIQEVMHSLVKLIRGALLPLSLREGDGRQYGGWEVQAELSGQWLAHVIQTIRLTYESLTALEIPNDMLQIIQDLILDLRIRCIMVTLQHTAEEIKRLAEKEDWVVDNEGLTSLPCQFEQSIVHSLQSLKGVVDCKPGEASVFQQPKTQEEVCQLCINIMQVFIYCLEQLSTKPDADIDTTHLSVDVSSPDLFGSIHEDFSLTSEQRLLIVLSNCCYLERHTFLNIAEHFEKHNFQGIEKITQVSMASLKELDQRLFENYIELKADPIVGSLEPGIYAGYFDWKDCLPPAGVRNYLKEALVNIIAVHAEVFTISKELVPRVLARVVEAVSEELSRLMQCVSSFSRNGALQARLEICALRDTVAIYLTSESRSSFKQALEALPQLASGADKKSLEELLNKFKSSMHLQLTCFQAASPAVMKT
Protein: HCLS1 associated protein X-1 isoform 3 (A0A0S2Z565)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLFDLFRGFFGFPGPRSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR
Protein: LD45439p (Q9W2F0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDRKKVLELDKICRLCISERKEMRPLFSEKVPEMLMDCTSVRVEPTEGWPDKICVQCVHAVSRNHAFKTLVERSDKELREYIRGLTVALVMEEQQQQEAANAKQQLQLERKQQRQLQKQQKILEEQLQQQIVQQQQHQPPAKPKLKPLLRKGSRQQKQRHLEAAPAPQSVPQPAPQPQMQLMQEHAPQQPTMQQQIQQIHMPTLQPAPAQLLSAAGATTTMPQQILLPNGQLITTAQIVAPQLAQIISTAPQSTTNGQATAAQSQFLPQLLQTPNGQTLQIVQQPNGTQTLQLVQLVPQRSLAPTGVTTVTTTTNATDMGQHVGASLGDADVQLLEDGCEVEDEELEDVYEQLDSKADHSFETIVLDDDQQQDFLKDHHEHHQVMINEDLTQSESQDHEYFDDLDQQQAMDEIEDEEEQMKPEEDQDTFIIEEIQLEDDEMLDDPDGEEIDQDCEYIGEEQDPHLSGDVDDDLEYSIMEPPDGETSVDIDQAFMDSEQSHHQQHQEEMQSISLENAVVEFSQATTTTEALVGPTMTVSSASPTPKRAKRSNHQIPAGVTLEPCDHQPPAAGSTTSSKLAAANSRQLVQTASVIAAAGADDNYEIDANLVTEFIRQHTSPLGSGRYICHLCSTEFRQFKGLQNHMHSHTNWIRANCKKQPQCQICLKSFKGPGMLRMHMKTHDAESSTPMCTICNRTFKSKAILYRHRQTHQQRAYCCGVANCRKNFSSAVNLKWHVERKHPEVVDPLFKCGECGSLYDNVDSLQLHVESTDHSAEVQISGQDDAFSGAVSIVSNGTTDMSNMMATGQGTTLAGGTGDTHAVVMGSSGEVYFVTQA
Protein: Glutamate-1-semialdehyde 2,1-aminomutase (Glutamate-1-semialdehyde aminotransferase) (Q9HWU0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glutamyl-tRNA reductase
- Delta-aminolevulinic acid dehydratase
- Glutamate-1-semialdehyde 2,1-aminomutase
- Probable aminotransferase
- Probable aminotransferase
- Putrescine--pyruvate aminotransferase
- Probable short-chain dehydrogenase
- Molybdenum cofactor biosynthesis protein F
- Benzoylformate decarboxylase
- Porphobilinogen deaminase
Sequence:
MDTTFGLDLARVETLFKRELRRFDELHPRSAQAYRENRRHWLYGAPLHWMQQWPGNCPLLVKEAQGARVTDIDGQQYVDFALGDSGAMFGHAQPAVADAIARQARRGSTLMLPTEDSLWVGAELARRFGLPYWQVTTSATDANRFVLRLCRMLSGRDKVVVFNCNYHGSVDESQVEFDAAGRMVPRAGVHPNGVRHATTTRLVEFNDLDALEAALAHGDVAAVLTEPFMTNVGMVPPAEGFHAGLRELTRRHDVALIIDETHTISCGPAGYSGAHGLEPDFFVLGKCIAGGIPSAVWGCSQAQAERIWAVLPHFRPGQAINHFGFGGTLAGNALQLAAMRATFAEVMTEDAYRHMFQLAAQLEAGVRATLEELRLPWHVTRIGARVEYLFMTHAPRNGGEAHHARNGLIEACLHLYLLNRGVLLTPFHNMALTCPATRAEDVELHDRLLRDCLGELLERPS
Protein: Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Glucocorticoid-attenuated response gene 16 protein) (GARG-16) (Interferon-induced 56 kDa protein) (IFI-56K) (P56) (Q64282)
Organism: Mus musculus (Mouse)
Function: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19856081}.
Interaction partners:
- Interferon-induced, double-stranded RNA-activated protein kinase
- Interferon-induced protein 44
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Ubiquitin-like protein ISG15
- Interferon-induced protein with tetratricopeptide repeats 3
- 2'-5'-oligoadenylate synthase-like protein 2
- Interferon-induced helicase C domain-containing protein 1
- Eukaryotic translation initiation factor 3 subunit E
- Ubl carboxyl-terminal hydrolase 18
- Interferon regulatory factor 7
Sequence:
MGENADGDQVMENLLQLRCHFTWKLLFENNDIPDLEVRISEQVQFLDIKNPLGMHNLLAYVRHLKGQQDEALQSLKEAEALIQSEQLSKRSLATWGNCAWLHYHRGSLAEAQIYLDKVEKVCKEFSSPFRYRLECAEMDCEEGWALLKCGGGNYKQAMACFAKALKVEPENPEYNTGYAVVAYRQDLDDNFISLEPLRKAVRLNPEDPYLKVLLALKLQDLGEHVEAEAHIEEALSSTSCQSYVIRYAAKYFRRKHRVDKALHLLNRALQASPSSGYLHYQKGLCYKQQISQLRTSRNRQPRRQDNVQELAQQAIHEFQETLKLRPTFEMAYVCMAEVQAEIHQYEEAERNFQKALNNKTLVAHIEQDIHLRYGRFLQFHKQSEDKAITLYLKGLKVEEKSFAWRKLLTALEKVAERRVCQNVHLVESTSLLGLVYKLKGQEKNALFYYEKALRLTGEMNPAF
Protein: Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial (EC 1.14.13.-) (2-methoxy-6-polyprenolphenol 4-hydroxylase) (EC 1.14.15.-) (Coenzyme Q10 monooxygenase 6) (Q8R1S0)
Organism: Mus musculus (Mouse)
Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03193}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03193}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03193}. Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000269|PubMed:21540551}. Cell projection {ECO:0000255|HAMAP-Rule:MF_03193}. Note=Localizes to cell processes and Golgi apparatus in podocytes. {ECO:0000255|HAMAP-Rule:MF_03193}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Atypical kinase COQ8B, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS2
- Atypical kinase COQ8A, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
Sequence:
MAARIGSMAGLLCVRWWSSAQLAARGGPLVASQRWAGSSADTVYDVVVSGGGLVGSAMACALGHDIHFHDKKILLLEAGPKKALEKLSETYSNRVSSISPGSTTLLSSFGAWDHICNMRCKAFRRMQVWDSCSEALIMFDRDNLDDMGYIVENDVIMYALTKQLEAVADRVKVLYESKAVGYSWPGAFSMADSSPWVHITLGDGSTLQTKLLIGADGHKSGVRQAAGIQNVSWKYDQSAVVATLHLSEATENNVAWQRFLPSGPIALLPLSDTLSSLVWSTSHEHAAELVSMDEEEFVDAINSAFWSDVHHTDFVDSASAMVRHAVALLKPTKVSARQLPPSIAKVDAKSRALFPLGLGHAAEYVRPRVALIGDAAHRIHPLAGQGVNMGFGDISSLVHHLSTAAFNGKDLGSMSHLTGYETDRQRHNTALLAATDLLKRLYSTSATPLVLLRTWGLQATNAVSPLKEQIMAFASK
Protein: Glutathione S-transferase (EC 2.5.1.18) (GST class-pi) (Q50LC6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368105}. Mitochondrion {ECO:0000256|RuleBase:RU368105}. Nucleus {ECO:0000256|RuleBase:RU368105}.
Interaction partners:
- Glutathione S-transferase omega 2.
- Glutathione S-transferase rho
- Glutathione S-transferase omega 1
- glutathione transferase
- Glutathione peroxidase
- Glutathione S-transferase theta 1b.
- Cytochrome P450 1A
- Glutathione peroxidase
- Microsomal glutathione S-transferase 1
- Glutathione S-transferase 3, mitochondrial
Sequence:
MAPYTLTYFAIKGRAGPLKILLADKEQQLKENVVTVQDWMKGDIRATCLFGQLPKFEDGDLVLYQSNAILRHLGRKHGAYGKNDCEASLIDMMNDAAQDLRQKYIKLIYQEYETGKEAFIKDLPNEFKPFENILAKSKTGFLVGDQISLADYNLFDLLLNLKVLSPSCLDSFPSLKSFVDKISARPKVKALLECENFKKLPINGNGKQ
Protein: Protocadherin beta-4 (PCDH-beta-4) (Q9Y5E5)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MKKLGRIHPNRQVLAFILMVFLSQVRLEPIRYSVLEETESGSFVAHLAKDLGLGIGELASRSARVLSDDDKQRLQLDRQTGDLLLREKLDREELCGPIEPCVLHFQVFLEMPVQFFQGELLIQDINDHSPIFPEREVLLKILENSQPGTLFPLLIAEDLDVGSNGLQKYTISPNSHFHILTRNHSEGKKYPDLVQDKPLDREEQPEFSLTLVALDGGSPPRSGTVMVRILIMDINDNAPEFVHTPYGVQVLENSPLDSPIVRVLARDIDAGNFGSVSYGLFQASDEIKQTFSINEVTGEILLKKKLDFEKIKSYHVEIEATDGGGLSGKGTVVIEVVDVNDNPPELIISSLTSSIPENAPETVVSIFRIRDRDSGENGKMICSIPDNLPFILKPTLKNFYTLVTERPLDRETSAEYNITIAVTDLGTPRLKTQQNITVQVSDVNDNAPAFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINADNGHLFALRSLDYEALQAFEFRVGASDRGSPALSSEALVRVLVLDTNDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGHLVDVSGTGTLSQSYQYEVCLTGDSGTGEFKFLKPIFPNLLVQDTGREVKENPKFRNSLVFS
Protein: Probable NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial (Q20412)
Organism: Caenorhabditis elegans
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- Ribosome biogenesis protein BRX1 homolog
- NADH dehydrogenase iron-sulfur protein 5
- RRM domain-containing protein
- Probable rRNA-processing protein EBP2 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Guanine nucleotide-binding protein-like 3 homolog
- Ribosomal RNA processing protein 1 homolog
- Ribosomal L1 domain-containing protein
- WD repeat-containing protein 74
Sequence:
MLGNKFVAQLALQHLRNRGLVNSPSRLTFVRNRFAWGSDAVGPNVPVGGKMGASENPELHTYDGDYRGTISKGDKPIPDYFYRTPTTGRTYIDRCVTYFISAVIWAWFSYHMYYHSGHLLGHWYMPYLSEFTDEELGIPKDSAEDPEYWGNHKKEYGTYR
Protein: Protein phosphatase inhibitor 2 (Q9N537)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein phosphatase 1 regulatory subunit SDS22 homolog
- Serine/threonine-protein phosphatase PP1-beta
- Serine/threonine-protein phosphatase PP1-alpha
Sequence:
MASPSASADDVKLTADGKICLDDPAEFLKRKPKKSILKMKQDSSLEGKDGRAHFDEMNILATYHPTDKDYGSMKIDEPKTPYHHSDGESECDEGVLGVPTTRPRRVSLGNAIDPEKVAEGLAHPESGKSLSSAEDSEDEADLTEEQRAHRRDFEKKRRAHYNEGAALKHHPELEDDEEEATAAAAGAGGNMEH
Protein: Target SNARE, putative (Q384F0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- Syntaxin binding protein 1, putative
- Syntaxin 5
- Paraflagellar rod component
- Soluble N-ethylmaleimide sensitive factor
- Soluble N-ethylmaleimide sensitive factor
- t-SNARE coiled-coil homology domain-containing protein
- Longin domain-containing protein
- Synaptobrevin-type vesicle transport protein, putative
- Vesicle-associated membrane protein, putative
- SNARE protein, putative
Sequence:
MDRLLQFHSQSGVGFMRGSPPPGSSGGLSRLTAVVPVAAPGSVEAETVTTLETFFEVVATVTESIDRVNVLMCEMSKKHEQAMDTVNVAKCDAIRKEVGDLDDEINNTIQKACKGVEDMENLTKKLKETPEMEGRFAGVIRLEENQRRFVLQKLSETMEGLQKRQLVAEKNYLSQTERRIKIAYSNPDGGEMDDETAHQLAMQVMEKGATTAIFQQSKEVLAQMLETRSDIYRIEMSMRSLNRVFSDLAILVEEQGDLMNVIIRNIDSTNLYMEKAHRELQQARAYQRASRSKLMCLLMIGVIIIALFVAAGLLGSLL
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q7WTU1)
Organism: Spiroplasma citri
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Enolase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Class II fructose-1,6-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Aldehyde dehydrogenase family protein
- Pyruvate kinase
- ATP-dependent 6-phosphofructokinase
Sequence:
MTNKKELKDVQVKGKKVLVRVDFNVPMKDGQVTDDNRIIAALPTIKYLIAQEAKVILFSHLGKVKTADDLEKRDMAPVAKVLEQKLGQPVKFINAFEGKQLEEAINEMHNKEVILFQNTRFADIINSNGQISVDSEGKAAAKRESKNDSALGKYWASLGDVFVNDAFGTAHRAHASNVGIAENITESCLGFLVEKEVKMLSQCVDNPVKPFVAIIGGAKVSDKIGVIEHLLTKADKILIGGGMAYTFFAAQGHKIGNSLLEVDKVEIAKTFLAKGQGKIILPIDALEAPEFADVPAKVTTGFDIDDGYMGLDIGPKTIELFKKELADAKTVTWNGPMGVFEFKNYSIGTKAVCEAIAELKGAFTLIGGGDSAAAAIQLGYKDKFTHISTGGGASLEYMEGKPLPGIEAVQSK
Protein: Sterile alpha motif domain-containing protein 11 (SAM domain-containing protein 11) (Q96NU1)
Organism: Homo sapiens (Human)
Function: May play a role in photoreceptor development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q1RNF8}.
Interaction partners:
Sequence:
MSKGILQVHPPICDCPGCRISSPVNRGRLADKRTVALPAARNLKKERTPSFSASDGDSDGSGPTCGRRPGLKQEDGPHIRIMKRRVHTHWDVNISFREASCSQDGNLPTLISSVHRSRHLVMPEHQSRCEFQRGSLEIGLRPAGDLLGKRLGRSPRISSDCFSEKRARSESPQEALLLPRELGPSMAPEDHYRRLVSALSEASTFEDPQRLYHLGLPSHGEDPPWHDPPHHLPSHDLLRVRQEVAAAALRGPSGLEAHLPSSTAGQRRKQGLAQHREGAAPAAAPSFSERELPQPPPLLSPQNAPHVALGPHLRPPFLGVPSALCQTPGYGFLPPAQAEMFAWQQELLRKQNLARLELPADLLRQKELESARPQLLAPETALRPNDGAEELQRRGALLVLNHGAAPLLALPPQGPPGSGPPTPSRDSARRAPRKGGPGPASARPSESKEMTGARLWAQDGSEDEPPKDSDGEDPETAAVGCRGPTPGQAPAGGAGAEGKGLFPGSTLPLGFPYAVSPYFHTGAVGGLSMDGEEAPAPEDVTKWTVDDVCSFVGGLSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQVARRLGRVFYVASFPVALPLQPPTLRAPERELGTGEQPLSPTTATSPYGGGHALAGQTSPKQENGTLALLPGAPDPSQPLC
Protein: Adenosylhomocysteinase (AdoHcyase) (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase) (P39954)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine beta-synthase
- Homocysteine S-methyltransferase 2
- Cystathionine beta-lyase
- Homocysteine S-methyltransferase 1
- Cystathionine gamma-synthase
- S-adenosylmethionine synthase 1
- Homocysteine/cysteine synthase
- Putative mitochondrial cysteine synthase
- Cystathionine gamma-lyase
Sequence:
MSAPAQNYKIADISLAAFGRKEIELAEHEMPGLMAIRKAYGDVQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWSSCNIYSTQDHAAAAIAASGVPVFAWKGETEEEYLWCIEQQLFAFKDNKKLNLILDDGGDLTTLVHEKHPEMLEDCFGLSEETTTGVHHLYRMVKEGKLKVPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMLAGKVAVVAGYGDVGKGCAAALRGMGARVLVTEIDPINALQAAMEGYQVVTMEDASHIGQVFVTTTGCRDIINGEHFINMPEDAIVCNIGHFDIEIDVAWLKANAKECINIKPQVDRYLLSSGRHVILLANGRLVNLGCATGHSSFVMSCSFSNQVLAQIALFKSNDKSFREKHIEFQKTGPFEVGVHVLPKILDEAVAKFHLGNLGVRLTKLSKVQSEYLGIPEEGPFKADHYRY
Protein: B-cell receptor-associated protein (BCR-associated protein) (A5X380)
Organism: Mesocricetus auratus (Golden hamster)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}.
Interaction partners:
Sequence:
MSVQWTAVATFLYAEVFAVLLLCIPFISPKRWQKIFKSRLVELVVTYGNTFFVVLIIILVLLVIDAAREIRKYDDVTEKVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKEAAEDGAKLDVGNTEVKLEENKTLKNDLKKLKDELANTKKKLEKAENEALAMQKQSEGLTKEYDRLLEEHAKLQASVHGPSAKKEE