wanglab/gogpt-training-data huggingface dataset:
Protein: 2,4-dienoyl-CoA reductase 2 (A0A8I6GLH8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004654}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004654}.
Interaction partners:
Sequence:
MELSQPTSLSDHDEPASGPQRGVKGLVGPDAPRGWSDEPEEHAQLQRWPEGPNAPICWPEEVEEPHAPRRWAEEPSASRCLSQEPYESCHLAKELEEPDAPRCSSQEPDAPCHLAKDLEETDSPRCWPLEPDAPCHLAKEWEEPDVPRCWPQEPDAPCHLAKYLEEPDAPLCWPQEPDAFCYLLKEVEEPDVPRCRPQEPDAPCHLAEELEDLDAPRCWTQEPNESCNLAKELDEPDTPRCLSQEPDAPCLLAKEWEESDAPSCWPQEPDVGPQEPDVGCHLAKEREESDAPCLLTEELKEPDALQCWPQESDAPCLLAEELEEPDAPHCCSQEVDTECLSAKESEEPDASHLWPGEPDAPCLLVKEPEEADAPHCWPEEPEEPDALNAPCFWANEPDEPDAPRCWSEEPQVLCLWPEEQNTTQCWQEEPDASCFWSEDREEPKVSCLQFKEPEKPKVACSWPEELEDCCPTRGLPLEPLLAEGELLQACPGPPPDPGLALSLPSEPGTAQEEGARLRTVFDALDRDGDGFVRIEDFIQFATVYGAEQVKDLTQYLDPSGLGVISFEDFYQGIVAIRNGDPDGQLYSVEPVQDEEPPACADEFDDFVTYEANEVTDSAYMGSESTYSECETFTDEDTSTLVHPELQPEGDVDSAGGSGVPSECLDTMEEPDHGALLLLPGRSRPHSQAVVMVIGSEEHFEDYGEGSEAELSPETLCNGELDCEDPAFLTPSSNPLASKLCTVLTDEAFEFYCSQCHKQINRLEDLSARLTDLEMNSPAKRLSSRKVARYLHQSGTLTMEALEDPPPEPVECPEEDIADKVIFLERRVSELEKDSAAAGEQHGRLRQENLQLVHRANALEEQLKEQEFRAQEKVLEETRKQKELLCKMEREKSIEIENLQARLQQLDEENSELRSCTPCLKANIERLEEEKQKMLDEIEELTQRLSEEQENKRKMGDKLSHERHQFQRDKEATQELIEDLRKQLEHLQLLRLEMEQRRGRSSSLGLQEYNSRARESELEQEVRRLKQDNRNLKEQNDELNGQIITLSIQGAKSLFSTSFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAILETNPSILEVK
Protein: L-Lys-D/L-Arg epimerase (EC 5.1.1.-) (Cationic dipeptide epimerase) (Q607C7)
Organism: Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Function: Catalyzes the epimerization of L-Lys-L-Arg to L-Lys-D-Arg. Can also catalyze the epimerization of other cationic dipeptides, such as L-Arg-L-Arg, L-Lys-L-Lys and L-Lys-L-His, but with lower efficiency (in vitro).
Interaction partners:
- DUF1611 domain-containing protein
- DUF2721 domain-containing protein
Sequence:
MKIADIQVRTEHFPLTRPYRIAFRSIEEIDNLIVEIRTADGLLGLGAASPERHVTGETLEACHAALDHDRLGWLMGRDIRTLPRLCRELAERLPAAPAARAALDMALHDLVAQCLGLPLVEILGRAHDSLPTSVTIGIKPVEETLAEAREHLALGFRVLKVKLCGDEEQDFERLRRLHETLAGRAVVRVDPNQSYDRDGLLRLDRLVQELGIEFIEQPFPAGRTDWLRALPKAIRRRIAADESLLGPADAFALAAPPAACGIFNIKLMKCGGLAPARRIATIAETAGIDLMWGCMDESRISIAAALHAALACPATRYLDLDGSFDLARDVAEGGFILEDGRLRVTERPGLGLVYPD
Protein: Peptidase A1 domain-containing protein (O01531)
Organism: Caenorhabditis elegans
Interaction partners:
- Nicastrin
- Gamma-secretase subunit pen-2
Sequence:
MKTTLLAFVAILGMCSATVVQHKLIYRESPKMQMMRRGEWGAYVQHKAALRDANPAVFASAPQNVNDFGDVEYLGNITIGTPPQQFIVVLDTGSANLWVPGSNCDGTCKGKSEFDSSKSTTFKKNGQSWQIQYESGSAKGIMGVDTVAFGGASEQQLLVPSTTFGIASHISSNFKNDAAEGILGLAFTSLAVDGVTPPLINAINKKILDQPLFTVFLEHKGTAKNVGGGVFTYGAVDTTNCGPVIAYQPLSSATYYQFVADGFKLGSYSNNKKSQVISDTGSSLIGGPSAVINGFAQALGAKYHSDDDAYYLPCSTSKGTLDITIGGNVYSIEPVNYILDVGMGDTCVFAAFSFDFGGFGPSWIFGDPFIRQYCNIYDIGQQRIGFAKSLQPSSK
Protein: Triphosphate tunnel metalloenzyme 3 (Adenosinetriphosphatase) (ATPase) (EC 3.6.1.-) (Triphosphatase) (PPPase) (EC 3.6.1.25) (Q9SIY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), however it does not display significant activity towards long-chain polyphosphates. The existence of PPPi in living cells is still unclear, and PPPase activity might be the ancestral function of CYTH domain. It also has gamma-phosphatase activity on NTP substrates, but no adenylate cyclase or RNA triphosphatase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:24004165}.
Interaction partners:
- Protein MICRORCHIDIA 6
- mRNA guanylyltransferase
- Anaphase-promoting complex subunit 13
- ALC-interacting protein 1
- Inorganic pyrophosphatase TTM1
- SNF1-related protein kinase catalytic subunit alpha KIN10
- Putative E3 ubiquitin-protein ligase RING1b
- Cell division cycle protein 27 homolog B
- GRR1-like protein 1
- Cell division cycle protein 27 homolog A
Sequence:
MEVEVKLRLLTAAAHLRLTTLLTPYHLKTLHQRNTFFDTPKNDLSLRRAVLRLRFLQNAAVSAASPSPPRCIVSLKAKPTLANGISRVEEDEEEIEYWIGKECVESPAKLSDIGSRVLKRVKEEYGFNDFLGFVCLGGFENVRNVYEWRGVKLEVDETKYDFGNCYEIECETEEPERVKTMIEEFLTEEKIEFSNSDMTKFAVFRSGKLP
Protein: Neurotransmitter-gated ion-channel ligand-binding domain-containing protein (O17274)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Neurotransmitter-gated ion-channel ligand-binding domain-containing protein
- Neurotransmitter-gated ion-channel ligand-binding domain-containing protein
- Neurotransmitter-gated ion-channel ligand-binding domain-containing protein
- Costars domain-containing protein
- Ligand-Gated ion Channel
- Amino acid transporter transmembrane domain-containing protein
Sequence:
MRNIFLFLVLLSIGVCSAQKAFHSRRLGTEGQIVGRILSEYDSSSRPPVRDHADNSAILVITNIFINRLIWHNNYAEVDLYLRQQWQDSRLKYDVDTREGIDEIRLPGNRKIWEPDTYFTSGKELSRNEKNSKHIVVEPSGYIRSSERVLLELPYAYGTMFPFTNSRQFTIKLGSYNYDIDDIVYLWANSPPLVNPIEVSQDLLKGDLTFEEASAGDCVGNYTVGVYSCIDAHVYFSASTISGLMSWFLPSLFLLIGSWLHFWIHGSWSVPRTISAAVPFFILAAYYIFMREDSYTQAQGAWLAFCLVLTFFSFVEYFLVICCGGRRSIRYKTLGPQEDHPMGAAKETVEVAYNEGCASFRDNNGIDVISRVAFPIVTIVFLIIYFIFIV
Protein: Polyribonucleotide 5'-hydroxyl-kinase Clp1 (EC 2.7.1.78) (Polyadenylation factor Clp1) (Polynucleotide kinase Clp1) (Pre-mRNA cleavage complex II protein Clp1) (E9PL17)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|HAMAP-Rule:MF_03035}.
Interaction partners:
Sequence:
MTDLHSSYTEEMGEEANDDKKPTTKFELERETELRFEVEASQSVQLELLTGMAEIFGTELTRNKKFTFDAGAKVAVFTWHGCSVQLSGRTEVAYVSKDTPMLLYLNTHTALEQMRRQAEKEEERGPRVMVVGPTDVGKSTVCRLLLNYAVRLGRRPTYVELDVGQGSVSIPGTMGALYIERPADVEEGFSIQAPLVYHFGSTTPGTNIKLYNKITSRLADVFNQRCEVNRRASVSGCVINTCGWVKGSGYQALVHAASAFEVDVVVVLDQERLYNELKRDLPHFVRTVLLPKSGGVVERSKDFRRECRDERIREYFYGFRGCFYPHAFNVKFSDVKIYKVGAPTIPDSCLPLGMSQEDNQLKLVPVTPGRDMVHHLLSVSTAEGTEENLSETSVAGFIVVTSVDLEHQVFTVLSPAPRPLPKNFLLIMDIRFMDLK
Protein: Ventral anterior homeobox 1 (Q801E0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that is required for closure of the choroid fissure and together with Vax2 is required for optic nerve differentiation and to limit retinal development to the optic cup.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Paired box protein Pax-2a
Sequence:
MEVRYSQDSESGMLLKNGLKEGKEGKDSQGSISKTFLKDQQESFSPSGAVENCEKSRASSGDPDYCRRILVRDAKGSIREIILPKGLDLDRPKRTRTSFTAEQLYRLEMEFQRCQYVVGRERTELARQLNLSETQVKVWFQNRRTKQKKDQGKDSELRSVVSETAATCSVLRLLEQGRLLTPPGLPGLLPHCGSSSLGSALRGPSLGITANGGSSSSSRSSAGSSGTAGGSPPLPTVTSSGTVTGLQGSPPAHGLFSFPMPSLLGSVASRISSTPLGMAGSLAGNLQELSARYLCSSAFEPYSRTNGKEALDKKVLE
Protein: Cyclin-dependent kinase 19 (EC 2.7.11.22) (CDC2-related protein kinase 6) (Cell division cycle 2-like protein kinase 6) (Cell division protein kinase 19) (Cyclin-dependent kinase 11) (Death-preventing kinase) (Q9BWU1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32330417}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32330417}. Nucleus {ECO:0000269|PubMed:32330417}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 12
- Cyclin-C
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 13-like
- Mediator of RNA polymerase II transcription subunit 12-like protein
- Cyclin-dependent kinase 8
- Zinc finger CCCH domain-containing protein 13
- Mediator of RNA polymerase II transcription subunit 14
Sequence:
MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDDPEEKGDKNQQQQQNQHQQPTAPPQQAAAPPQAPPPQQNSTQTNGTAGGAGAGVGGTGAGLQHSQDSSLNQVPPNKKPRLGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQSTLGYSSSSQQSSQYHPSHQAHRY
Protein: Penicillin-binding protein 1A/1B (PBP1) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (P39793)
Organism: Bacillus subtilis (strain 168)
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (Probable). Required for vegetative growth (Probable). Has a partially redundant function with PBP-2A (pbpA) during spore outgrowth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10322023}; Single-pass type II membrane protein {ECO:0000269|PubMed:10322023}. Forespore inner membrane {ECO:0000269|PubMed:3080407}; Single-pass type II membrane protein {ECO:0000255}. Note=Probably found all over the whole cell at low concentrations. Also localizes to the division site in vegetative cells.
Interaction partners:
- Cell cycle protein GpsB
- D-alanyl-D-alanine carboxypeptidase DacA
- Septation ring formation regulator EzrA
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein FtsZ
- Peptidoglycan glycosyltransferase RodA
- Cell shape-determining protein MreB
- Cell division protein FtsA
- Penicillin-binding protein 1F
- Holliday junction resolvase RecU
Sequence:
MSDQFNSREARRKANSKSSPSPKKGKKRKKGGLFKKTLFTLLILFVLGVVGGAVTFAVMVSDAPSLDESKLKTPYSSTIYDKNGKEIAEVGAEKRTYVSIDEIPDVVKEAFIATEDARFYEHHGIDPVRIGGALVANFKDGFGAEGGSTITQQVVKNSLLSHQKTLKRKVQEVWLSIQLERNYSKDEILEMYLNRIYFSPRAYGIGKAAEEFFGVTDLSKLTVEQAATLAGMPQSPTAYNPVKNPDKAEKRRNIVLSLMKKQGFISDSQYNKAKKVAVKDEGVVSQKEYEKASTNKYSAFVEEVMKEIDEKSDVDPSADGLKIYTTLDTKAQDKLDELMDGDTVGFTEGMQGGVTLLDTKNGEVRAIGAGRNQPVGGFNYATQTKAQPGSTIKPILDYGPVIENKKWSTYEQIDDSAYTYSNGKPIRDWDRKYLGPISMRYALAQSRNIPALKAFQAVGKDTAVDFANGLGLGLTKDNVTEAYSIGGFGGNDGVSPLTMAGAYSAFGNNGTYNEPHFVKSIEFNDGTKLDLTPKSKSAMSDYTAFMITDMLKTAVKTGTGQLAQVPGVEVAGKTGTTNFDDNEVKRYNIASGGARDSWFVGYTPQYTAAVWTGMGENEAGKKSLSAEEQKVAKRIFAQLIADVDDGSGSFEKPDSVVEATVEKGSNPAKLAGPNTPSDKKLTEYFVKGTAPSTVSKTYEKEEKEETAKLSGLNVKYDKDNQSLTLSWNYDGDATFAVKQSVDGGSYSEIQNSSAKEAVISGVQPGSVYKFEVTAVSDDGKSTASTSYEVPKAEDDEDKKDQQQTDDEKQDDEKTQDDTQTDDSQKDDGQTDQDQTDDSTNDQDKKQDNTNTNPSDNNNQDQSNDNDNDNSNNQDTSDGDSNSGKNDSTGSDTNKNKTDTSNKTQTNSSSIEKTN
Protein: Transcription factor ILI6 (OsILI6) (Protein INCREASED LEAF INCLINATION 6) (Protein POSITIVE REGULATOR OF GRAIN LENGTH 1) (Q0DUR2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Atypical and probable non DNA-binding bHLH transcription factor that acts as a positive regulator of grain size. Binds the transcription repressor APG and forms a heterodimer of antagonistic bHLH transcription factors that regulates grain length and weight by controlling cell elongation in lemma and palea. May be involved in the control of lamina inclination through brassinosteroid signaling pathway.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:22363621}.
Interaction partners:
Sequence:
MSSRRSRSRQSGSSRITDEQISDLVSKLQDLLPEARLRSNDRVPSSRVLQETCNYIRSLHQEVDDLSERLSELLATSDMSSAQAAIIRSLLM
Protein: Transmembrane protein 127 (Q8BGP5)
Organism: Mus musculus (Mouse)
Function: Controls cell proliferation acting as a negative regulator of TOR signaling pathway mediated by mTORC1. May act as a tumor suppressor.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Association of TMEM127 with the cell membrane is enhanced by inhibition of endocytosis. In the cytoplasm, it colocalizes with markers of early endosomal structures, Golgi apparatus and lysosomes. {ECO:0000250}.
Interaction partners:
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Kinesin-like protein KIF1B
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Neurofibromin
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Protein max
Sequence:
MYAPGGAGLPGGRRRRSPGSSALPKQPERSLASALPGALSITALCTALAEPAWLHIHGGTCSRQELGVSDVLGYVNPDLLKDFCMNPQTVLLLRVIAAFCFLGILCSLSAFLLDVFGPKHPALKITRRYAFAHILTVLQCATVIGFSYWASELILAQQQQHKKYHGSQVYVTFAVSFYLVAGAGGASILATAANLLRHYPTEEEEQALELLSEMEENDPYPAEYEVINQFQPPPAYTP
Protein: Syntaxin 16 (B7ZBM5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MALVSGISLDPEAAIGVTKRPPPKWVDGVDEIQYDVGRIKQKMKELASLHDKHLNRPTLDDSSEEEHAIEITTQEITQLFHRCQRAVQALPSRARACSEQEGRLLGNVVASLAQALQELSTS
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (F4JD48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MLVLLQNLDLAMLLLLLVSMKILVLSLKSRHTFAFGSPDIIPIFCSALPHSTWNSYPHEYEDFATDASFLDEWSFDQFEGLLNRSHADPKLKELLHQDKLVVFLHLLGCDSNGHAHRPYSSIYLNNVKVVDKIAERVYHLLEDYYRDNRTSYIFTADHGMSDKGSHGDGHPTNTDTPLVAWGAGIQYPKPASGNSHSDSVTTFVDKHAHDMPTPYDWGLRRVERVDVNQADIAPLMSTLLGLPCPVNSVGNLPLGYMKLNEAEEVEAVVANTKQILNQLLRKSYIKSSNSLFFKPFKPLVHHSFSLSQIDELISAKSYEAAMKLAVDLRNLSLEGLHYFQTYDWLMLMTVITLGYTGWMIVLALHVLQCYSSLSGDLSKKEHLSVQKKDSGKVYISGCLLMAILSVLNLVEHSPPLYHAYIGMTVFLWTQIFSEYRLIRGLWKYLRERRADYFIKLLFAAAVAVVIVELLVHSFTERKLYTWFFLIAGVVASILLHFSIPWRSGIPVFVCISCWFLSVFTLMPAEIPDNNNLVVTSGAIIIVISLAAKWLDTHAEGNKFWQSITFHESRTQMCSMLYCIQIFLVGVSSVMVFLSTKHRTQNQELHSSHQFINWLVAGSSMVLPLFSANGILSRLSSIFLGFAPPFLLLSIGYEAVFYSALAVVLMAWILFENASHHSSKVKESSLSENNTEEHITIGSDERYLQLSDVRIPLVFMVLFNVAFFGTGNFASIASFEISSVYRFITIFSPFLMAALLIFKLFIPFMLVICAFSAITKLVRVPRLGCYFLVILFSDIMTIHFFFLVKNTGSWMEIGNSISHFGIVSAQVVFVLLLFALTNLYTRSIRIKPLSTSPSLKTL
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (H0VCR8)
Organism: Cavia porcellus (Guinea pig)
Interaction partners:
Sequence:
LCDGKPLGQHYNFNLEKTTHTLTSSGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSEQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEASEGGEGPEPWETISEEVNMAGDSLGLALPPPPSSPVSRTSPQELSEELSRRLQITPDSSGEQFTSLIQREPSRLRSCSVTDTVAEQAHLPPPSTPTRRARSSTVTGGEEPTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKASLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGEQHASDSASPVAQECCAGWEAPAGHFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD
Protein: Glutathione S-transferase A1 (EC 2.5.1.18) (13-hydroperoxyoctadecadienoate peroxidase) (EC 1.11.1.-) (Androst-5-ene-3,17-dione isomerase) (EC 5.3.3.-) (GST class-alpha member 1) (Glutathione S-transferase Ya) (Glutathione S-transferase Ya1) [Cleaved into: Glutathione S-transferase A1, N-terminally processed] (P13745)
Organism: Mus musculus (Mouse)
Function: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid (By similarity).
Interaction partners:
- Glutathione S-transferase theta-1
- Epoxide hydrolase 1
- Cytochrome P450 1A1
- Glutathione S-transferase theta-2
- Cytochrome P450 1A2
- Glutathione S-transferase omega-1
- Cytochrome P450 1B1
- Hematopoietic prostaglandin D synthase
- Glutathione peroxidase 1
- Cytochrome P450 2B10
Sequence:
MAGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYSEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLEVLLYVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLQPGSQRKPPMDAKQIQEARKAFKIQ
Protein: Nucleoside diphosphate kinase (EC 2.7.4.6) (Q8ID43)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Guanylate kinase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- CTP synthase
- Thymidylate kinase
- Inosine triphosphate pyrophosphatase
- Ribonucleoside-diphosphate reductase
- UMP-CMP kinase, putative
- Ribonucleoside-diphosphate reductase small chain, putative
- Ribonucleoside-diphosphate reductase small chain, putative
- Adenylate kinase 1
Sequence:
MEKSFIMIKPDGVQRGLVGTIIKRFEKKGYKLIAIKMLNPTEEILKEHYKELSDQPFFKNLVAYISKGPVVAMVWEGVDMVKQGRKLIGETNPLTSNTGTIRGDFCLEVSKNVIHGSDSVASANKEINIWFKAEELTQWKHHMKEWICS
Protein: Urotensin-2B (Urotensin II-related peptide) (Urotensin IIB) (U-IIB) (UIIB) (Urotensin-2 domain-containing protein) (Q765I2)
Organism: Rattus norvegicus (Rat)
Function: Potent vasoconstrictor.
Subcellular location: Secreted.
Interaction partners:
- Urotensin-2 receptor
- Urotensin-2
Sequence:
MKFFSTSLCFGLLALLSVTTLLHSVRGRPHLSSGHELFPAEEHTTQEKLPLGLLIRNPGFQRPAHAGVDLPSKVEELRQLKKLREWFMEAKSAEPSNALDKLSSSHPIKRACFWKYCV
Protein: StAR related lipid transfer domain containing 10 (H0YFF3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
CRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKPWLHPEQSPLPSLALSELSVQHADSLEN
Protein: Abnormal spindle-like microcephaly-associated protein ASH domain-containing protein (Q388P3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDFIAFKDGGLRDDRYRIIDEVEERLPDRPKVNHRQRSVKDYGLTCAQQQDRSQAEGLFTVTPRTVDFRDIVVGQTYTKKVTLTNCTNKLYAFRILPVSPKYKEVLQYEYRLPPKLPSGLSWSVNIRFTPSKEDDLETTIVFRTEQGVFVVPVRAFRRKSVVSASPDKLDYGCVIFGEKLSKRVTLRNDGALAATVSVGGSVRDWTDVLHKNPINGKEESVVVFNPAGYTLTIEPYSASYFDVIFSPHEDVVIDGDIEIRYDVDGSAAVKKIQVRGTGGSLPVHVSSAAEIDFEWCFFETTYCEKITIQNTTNVLTTVIPEVPPTLSSSLSFSPKSVCVQAKSTSEICVFFTPQRGLGHTVQSVILMSVRDQKTPLSVKLNARLTERGFGVSTNELHFGSRSVCEEIVQPLRVENLSDLPQTLGFLTLPDNVKVAPYPIVTLLPKEVMEFKVGVRPPTLGQFTHVVNITNEYDVSRAIQLTGCGCEYPVRFSKSCIDLPACPLGGEINYSVTLQNNGNAQQSFFISSPLEYLRASPSFGTLQGGEHCPIVVFFAPLAQPSTPPLEETMPRPSTKRISRRGREREHTPPLEKVTDSEEACLNELYKAWECNSSGEGWSRHSSFFLKCVVGEAASEQVVMLQINCVVVKPTLSVSLVSRVHQKAVLRKASKRGAKKNERRGVEQSLTLEISPSAVKQSVDFGKVPLNSRVERVFLLRYTGEGSMYLQMRPVAAYSPFFVSKPPQFILSHDEECAVTVCFTPAECGYYREEVVFSSACSNDVTLSLQGSCEPADLLVTGDRELGEQTKSIEVIVLEPAQVGQESRQQLFFHNMSNLPLEVNVAFITGEGKTPAWPEGCSFTFECDQFVIPGRTKVPKTIVFTPQVVGMVSLHLRVSDGSSVQTILVEGRGCDLPVFLTFPSCKELAAGESAPYTGFRKNPFPETGASAIDPVRLYFAAEQTRSISVGSLKAGSSFECIVGGWSETFTENGWKLEPLKITGPAGSHGTFTVSYNPRRDHTDVSFCTFSLAIKCALVPEERVYHVQCTGTA
Protein: RE50346p (Q8IGP8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNFDRVYADEYGGYGTGSGSTRPSQRGNNRNGGGAGGVAGGAAGGNGGGFNAGGARGNAGGRGGADRFGGAAGGAVAGAGMGQRDNPFINPWANGGGGDVDGFGNNAGGAGGFAGNSFGGGAGGPFGGGSFGNNGFGGGPSGFGGNSGNFGQAQGTNSLPSLGSFSQNQGGTSSLPSLGSFGQNPGGPGGLGNGLSGGANGGVGTLGGANGAGGFNAVGGANGGPNGSPNAATNVPQGHDPNNSTQVTIPKELAGAIIGKGGGRIRRIRNESSAYITIDEPLPNSNDRIITISGTPKQIQMAQYLLQQRLVSQSE
Protein: phosphatidylinositol 3-kinase (EC 2.7.1.137) (Q57YM2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein kinase, putative
- Atg6 BARA domain-containing protein
- Protein kinase, putative
- non-specific serine/threonine protein kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol-3-phosphate 5-kinase
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- non-specific serine/threonine protein kinase
- Phosphoinositide phospholipase C
Sequence:
MATNEDTVAYTLKEENCGTLRGAPPSNEFLLANDMEEPFMVHLCAVDGYARWCRRRNEETRRRCNGNGGEGEGRNNSSFNSAFTPYGQLVGSMSSLPLRGEAHYPSYSEDDTLCVTLQMFHMGMPITPILQSSHTYGCHQRLEEWIIFPIAIQDIPLDALVHCHVYAPHGLVGRTSFHPFTACGELKTGRRRYELQAGTAAGTERADHDDSDSVNGNKRAPSRMGMNPQELMLRDLRRGLVPQIPWMDKMIKRQVGELQTKNDETTGSQSIALSVLFPSTNGDQRVFLLSAPRDKLPASIVSLIPPPDRVVTSRTSPFAALAATPKQPYVDLCVDDENLCEAKVAALSNPRLFLSSANTQPGPVERAQLKEIAQKPLIHLEELKLGERTLLCRFRHFLTRDPAYFVPFMRSVNWDDKIEKREALKVMQQWKPIGFTQALICLSFYFRKVVDVRIYAINVLDKSSDDRLFRFLIQLVQGVRYDVNGELETFLLRRAANCWEICSNLFWYVLTEASLGSGNSQGDGQRYGDGQEERYTTFLQNIKATLQRTKPCFLQRIHQQVKLMGTLRTLNKSLLKASDRVKRMELATSLIDSKECGIRELFFPSPISSLSEDPRETAAVQGRIVTLPTHPSAVVEDIISEGFYMFKSAMMPIKVPFVLHPEPLGSNTCHRSPVVEDGTNTGPSTVPVTVSRPEGGLLFKVGDDVRQDQLVVQLVQLIDMILRQDGLDLCLCPYRVIATGPTEGLVELIPNVVTLQSVQRDITGFIRSRNQSQEGYTAAMSRFTKSCAGYCVLTFILGIGDRHLENILLTHDGRLLHIDFGYILGNDPKPFPPPMKINKEMVEALGGPQSTGYMEFKSYCCSSYNIIREHAQVILSMLLLMVDASIPHISGDGKVDPRVNLLKVQEKLRLDLSNAEASQYIQNVIADSVGSIFTNLWDVLHAAAQARRA
Protein: Putative uncharacterized protein MGC163334 (Q5W150)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDCKSPKRANICPHLPGGGLFSTPPSQAAWRTLLTALCFPGPTCTGPMREGPRAVYNPPRAHRNSSDNCVMKHLLCAGDKNGTRRHALPSPLEGSFQPGRQIPPPQTPSTDPQTLPLSFRSLLRCHQLCAASLPPSLKLP
Protein: Uncharacterized protein, isoform B (Uncharacterized protein, isoform C) (Uncharacterized protein, isoform D) (Uncharacterized protein, isoform E) (A1Z9K0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- LD36772p
- GH05812p
- EG:BACR42I17.11 protein
Sequence:
MTKNKKNIINNNNGNATPPDFPTPPPTPPINAGIKPPGTYANGMPRKPTVPWERELMGSFLLEMARLQVISAQTEWYVDKAKMRKLFEVHLNALPNSSEIRQKLSSQGATNIGSLLHRTNFLINTPRGNPNYRIKNFSLMDFRKEKFNLLDEQHRLRGIASTTDVPGGAPAEGNKPIIEEYKLDTDVKPTLLKFQKRLLLQSDKDFELQSLGCYICQENFEKIEKYEEHVEYHGDESDFQSLKKMKKYPTPIVSLSYQTCVDSHYFGFTLKTFRKDLVVDKFIIVQLRQFYYVYGAQMPLPVNGSGELVFFVDSHVFMILREQPIVIGFTIQGEKYVEQHHFMRTEALPKASFNINPYRLSSKETFKSKGLPPANPPIQVLSALKHEDAQMCLASFDNQYQNYCERGREITQENLTGTLRTLLQVEDIERLQHYLSLKQSEMELHQFGRELSVKMQMGTTSMSVEDILSPGDDVLIINEKGNPKSAVRKMLENNNNVLELALKDFDSILRWARNVDGMVGSLDKQPRVYFARILGVSTQRVNITCERQLPDNTTYTLIFRPLRAVMRYQYRALQQLSFTRHSDVQRILFPGEIPNTPLASGVLQLNNKLISTNPEQMQAVRQIALSPRLKAPYIVFGPPGTGKTSTIVEAIYQLYINRPETHILVLAGSNTACDEVALRLLRAIAKAPQSQPRPLTRIFSANCDRRIDNIDDLLLEYSNMYTVHFYPAVQAVHQYRIVICTLSLAGKLSTGGFAANNVYTHVFVDEAAASTEAEVLMGITCTLSPTLNLILSGDHKQLGPVLQSQRANEWGLGLTLFERLLQRKCYQVEEDGSYNASVQTRLIRNFRSHPEIVSLYNNMYYEGHLRTEAPMEIVCRFHNWFYLPNATFPIMFHSVFGTTMNTKSSVSLCNNKEIDVVMDYVKDLMYFGLNGEKLLQTDIGIISPYKNQYQRIQEQLNMRNWSQIDCGSVELFQGKEKHVIIVSFVRSFTPKLGFLNNERRLNVLLSRPISLLILIGNPRTLSQNSDFQHIIEMCRNRKTLVGEQYLNEDFITNKKTGANNVNKGGAAGDQPASGLRQPLKRKNHAKNPVQDAKIFYSKNELLNLGNECQRKKSELETIFDELPKVPRSVDHDLDEVRSIEAQLKDFQLETKQDAAGTSILVTNAPVTNAAAPSVIPRAGLMKQETPALHSSSVSRPAIRKPTVSAATPVAKSRSPMPEIPSSSKHPISMSSNPLSTNTERCVNGVLCGIEAVPPSENKTTRSSAYNHIPSGNFRFENVRPTPEEVRRFNGANDQRRARPFREPHGNWSNFGWSPPPRDPTPPRRNKKFNCIIS