wanglab/gogpt-training-data huggingface dataset:
Protein: E3 SUMO-protein ligase KIAA1586 (EC 2.3.2.-) (E3 SUMO-protein transferase KIAA1586) (Q9HCI6)
Organism: Homo sapiens (Human)
Function: E3 SUMO-protein ligase; facilitates UBE2I/UBC9-mediated SUMO2 modification of target proteins.
Interaction partners:
Sequence:
MGDPGSEIIESVPPAGPEASESTTDENEDDIQFVSEGPSRPVLEYIDLVCGDDENPSAYYSDILFPKMPKRQGDFLHFLNVKKVKTDTENNEVSKNHCRLSKAKEPHFEYIEQPIIEEKPSLSSKKEIDNLVLPDCWNEKQAFMFTEQYKWLEIKEGKLGCKDCSAVRHLGSKAEKHVHVSKEWIAYLVTPNGSNKTTRQASLRKKIREHDVSKAHGKIQDLLKESTNDSICNLVHKQNNKNIDATVKVFNTVYSLVKHNRPLSDIEGARELQEKNGEVNCLNTRYSATRIAEHIAKEMKMKIFKNIIEENAKICIIIDEASTVSKKTTLVIYLQCTIQSAPAPVMLFVALKELVSTIAECIVNTLLTTLNDCGFTNEYLKANLIAFCSDGANTILGRKSGVATKLLENFPEIIIWNCLNHRLQLSLDDSISEIKQINHLKIFIDKIYSIYHQPNKNQTKLLGTVAKELETEIIKIGRVMGPRWAACSLQAATAVWHAYPILYMHFSHSYSGLAKRLANINFLQDLALMIDILEEFSVLSTALQSRSTNIKKAQKLIKRTIRALENLKIGTGKYESQIEDLIKSDKFKDIPFNKNNKFNALPRSILLDNIIQHMNLRLLSDRNHEDIFNYFDLLEPSTWPYEEITSPWIAGEKTLFHLCKILKYEVDLNDFREFVNNNIKSNNVSIPTTIYKAKKIVSTIAINSAEAERGFNLMNIICTRVRNSLTIDHVSDLMTINLLGKELADWDATPFVKSWSNCNHRLATDTRVRQKSTKVFHENQLAIWNLK
Protein: Magnetosome protein MamL (Q2W8Q5)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Essential for magnetosome formation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:27481925, ECO:0000305|PubMed:20212111}; Single-pass membrane protein {ECO:0000255}. Magnetosome membrane {ECO:0000250|UniProtKB:Q6NE58}; Single-pass membrane protein {ECO:0000255}. Note=May associate transiently with magnetosomes; in about 10% of cells, GFP tagged protein is aligned in dots or very short filaments similar to magnetosome distribution. {ECO:0000269|PubMed:20212111, ECO:0000269|PubMed:27481925}.
Interaction partners:
- Magnetosome protein MamM
- Probable membrane transporter protein MamO
- Magnetosome protein MamN
- Actin-like protein MamK
- Magnetosome protein MamI
- Magnetosome formation protease MamE
- Magnetosome protein MamR
- Multi-heme protein MamP
- Magnetosome protein MamB
Sequence:
MVRLIGSLVFGGLIVLLASSNAHMVETRLGPLAMIAPHFVVLGITFFLGFAIGIVSVLANVMTRRKQKSPGKSIVIKR
Protein: Integrin alpha-10 (O75578)
Organism: Homo sapiens (Human)
Function: Integrin alpha-10/beta-1 is a receptor for collagen.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-1
- Integrin beta-5
- Integrin beta-3
- Integrin beta-8
- Integrin beta-2
- Integrin beta-7
- Integrin alpha-1
- Integrin beta-6
- Integrin alpha-11
- Integrin alpha-2
Sequence:
MELPFVTHLFLPLVFLTGLCSPFNLDEHHPRLFPGPPEAEFGYSVLQHVGGGQRWMLVGAPWDGPSGDRRGDVYRCPVGGAHNAPCAKGHLGDYQLGNSSHPAVNMHLGMSLLETDGDGGFMACAPLWSRACGSSVFSSGICARVDASFQPQGSLAPTAQRCPTYMDVVIVLDGSNSIYPWSEVQTFLRRLVGKLFIDPEQIQVGLVQYGESPVHEWSLGDFRTKEEVVRAAKNLSRREGRETKTAQAIMVACTEGFSQSHGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRQRDPSSFLREIRTIASDPDERFFFNVTDEAALTDIVDALGDRIFGLEGSHAENESSFGLEMSQIGFSTHRLKDGILFGMVGAYDWGGSVLWLEGGHRLFPPRMALEDEFPPALQNHAAYLGYSVSSMLLRGGRRLFLSGAPRFRHRGKVIAFQLKKDGAVRVAQSLQGEQIGSYFGSELCPLDTDRDGTTDVLLVAAPMFLGPQNKETGRVYVYLVGQQSLLTLQGTLQPEPPQDARFGFAMGALPDLNQDGFADVAVGAPLEDGHQGALYLYHGTQSGVRPHPAQRIAAASMPHALSYFGRSVDGRLDLDGDDLVDVAVGAQGAAILLSSRPIVHLTPSLEVTPQAISVVQRDCRRRGQEAVCLTAALCFQVTSRTPGRWDHQFYMRFTASLDEWTAGARAAFDGSGQRLSPRRLRLSVGNVTCEQLHFHVLDTSDYLRPVALTVTFALDNTTKPGPVLNEGSPTSIQKLVPFSKDCGPDNECVTDLVLQVNMDIRGSRKAPFVVRGGRRKVLVSTTLENRKENAYNTSLSLIFSRNLHLASLTPQRESPIKVECAAPSAHARLCSVGHPVFQTGAKVTFLLEFEFSCSSLLSQVFVKLTASSDSLERNGTLQDNTAQTSAYIQYEPHLLFSSESTLHRYEVHPYGTLPVGPGPEFKTTLRVQNLGCYVVSGLIISALLPAVAHGGNYFLSLSQVITNNASCIVQNLTEPPGPPVHPEELQHTNRLNGSNTQCQVVRCHLGQLAKGTEVSVGLLRLVHNEFFRRAKFKSLTVVSTFELGTEEGSVLQLTEASRWSESLLEVVQTRPILISLWILIGSVLGGLLLLALLVFCLWKLGFFAHKKIPEEEKREEKLEQ
Protein: Gonadotropin-releasing hormone receptor (Q9DDC9)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MCVPAALIEAEPPHHPTTEGDTNTSATHCLEHWVEPRFTKAAKVRVAITAVFFLLAACSNTAVLGSLLRKRRKCHVRPLILSLALADLLVTVAVMPLDAAWNVTVQWYGGDLSCKLLNFLKLFAMYAAALVLVVISLDRHAAVLQPFARARRRNGLLLRAAWLGSVLLASPQLFLFHVHTVPGGNFTQCVTHGSFRAHWEETVYNMFTFTTLYITPLSIMIVCYVRIIWEISKQLKINKSLVRSQNDHISKARMKTLKMTIVIVASFIICWTPYYLLGLWYWFHPAMIQRMPEYINHSFFLFGLLHTCTDPIIYGLYTPSFREDVQLCLRGIEAAISQHVRHKPISVSEKTTKDGDVNGQVTSGGSNGTTVNTVC
Protein: Arrestin (Or S-antigen), N-terminal domain protein (AFU_orthologue AFUA_5G12530) (Q5BHC4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
Sequence:
MPGRLLSSLVRPSLSHHSIFPHSNSSSSSSVNEVSQAASSKHSHTDRSHSPERRLSFSMDHFIHTYRDHHNKEKHRKHGRSSRSKERGSHEETAASAKLDVIVESPPLVCYGTPANSTGALFSGRLRITVPEATGMVILDKFDMRLMIRKTTKKPVSRDCPNCASKTEELTNWNFLTEPLHLRSGDHDFPFSYLFPGNLPASCNGSLGQIEYFLQAHGHNVNGEEYNFRMPLHMRRAILPGNDKSSIRIFPPTNLTGRIVLPSVVHPIGTFPVQMTLSGVLDKGEETQTRWRLRKMMWRIEEHQKIVSTACPKHAHKIGGEGKGVLHQETRIIGHNEEKDGWKTDFDTAGGEISMEFEANINPTANPVCDLEAPGGLETKHNLVIELIVAEEFCPNRNTRLITPTGAARVLRMQFNLHVTERSGLGISWDEEMPPVYEDVPASPPGYTMLDGSSIMEDYHGSPLPTPEYEELERMDSLRLDNSSTNSSCRGRSRLTTDDLTAEPAEFESRNRAPSADSHSS
Protein: Cell wall hydrolase Ply187 (O56785)
Organism: Phietavirus pv187
Interaction partners:
Sequence:
MALPKTGKPTAKQVVDWAINLIGSGVDVDGYYGRQCWDLPNYIFNRYWNFKTPGNARDMAWYRYPEGFKVFRNTSDFVPKPGDIAVWTGGNYNWNTWGHTGIVVGPSTKSYFYSVDQNWNNSNSYVGSPAAKIKHSYFGVTHFVRPAYKAEPKPTPPAQNNPAPKDPEPSKKPESNKPIYKVVTKILFTTAHIEHVKANRFVHYITKSDNHNNKPNKIVIKNTNTALSTIDVYRYRDELDKDEIPHFFVDRLNVWACRPIEDSINGYHDSVVLSITETRTALSDNFKMNEIECLSLAESILKANNKKMSASNIIVDNKAWRTFKLHTGKDSLKSSSFTSKDYQKAVNELIKLFNDKDKLLNNKPKDVVERIRIRTIVKENTKFVPSELKPRNNIRDKQDSKIDRVINNYTLKQALNIQYKLNPKPQTSNGVSWYNASVNQIKSAMDTTKIFNNNVQVYQFLKLNQYQGIPVDKLNKLLVGKGTLANQGHAFADGCKKYNINEIYLIAHRFLESANGTSFFASGKTGVYNYFGIGAFDNNPNNAMAFARSHGWTSPTKAIIGGAEFVGKGYFNVGQNTLYRMRWNPQKPGTHQYATDISWAKVQAQMISAMYKEIGLTGDYFIYDQYKK
Protein: AAA+ ATPase domain-containing protein (Q4GZ30)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA polymerase eta
- Replication factor C, subunit 5, putative
- Replication factor C, subunit 2, putative
- Replication factor C, subunit 4, putative
- Proliferating cell nuclear antigen
- Replication factor C, subunit 3, putative
- Flap endonuclease 1
- DNA polymerase epsilon catalytic subunit
- DNA polymerase alpha subunit B
- Protein artemis
Sequence:
MPSPKLLYSVGLPEFYADGFALAVPPPPPADMPSPFLARRQEGSSEEQGKEEESVGFTPRNFLVAPHVSQATPTPSTTLTSSDPCTVSAPHVHVSETLSDHLGPCTSSTQSFQTPNNATAGTSSTTPTYELAQLLCDAVMKCYRREDELRQQLRRVDEEKEDGGWRAYNSKLNSKEVAPRSGAFPRMVDSIHSLKCRRRQQVQLNENHMLNVTRVRETPQLVRDAVQYAQQLIEWRSNSDDNSNISVDPISSNTEFPNTEKRHQHGRAEPPTQPNHPCGEGRDSSHMLYAKYPPPLFHTTSFADGVTRLLRWIRTWQRSSSAAEAAERAPNGRRNLKRKRNTTTETESKKRAISSTGFPASNEVDLKGRKQGARGGVVGVGSTANASVESRSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSCSDASQEAQQQQKEQRTSLQRYYDTWLHVADTLASGCVNSTLESGLAMDHMAHPGLPPELCRKADRGLLSDQIMYDEHGNRMRSMRLARKMAKERAKQEKRRRVLERRRGYFARDEEENNMTALNVLLSDNIRVDDKGNMWKHDVEDDVTSIAMIYGPCGVGKTAIVYLAAAVLGYRVVEMNTAVRRCPKNIDRLLSELTRSHRLSGLASCKPLMSIEEELKKLKTEQANEAELRKSAAKSTPVKNKKGNAISAKAVAAFFKKNVPENVVDVHTEGIVEIAVSTENDNRAREKEKEAAASAAQPSTTTPNATLDETTRTILLIEDVDVILGDESMRTFYTAVKDLAQRSKVPIVLTASSPPSTTIGGSTGRPTKVVAAGNDPVQMIPMSAVQAEQYFGRRTPFTRIGPMSRSELFAQMVVVAAAERGLLSLREDTVPCPPKKKSRRRRRGKRKANSTEGETKPKKEKLISFTTVVVNDVAMFESLADALREEVYGNVEDIEQCHTLNDQTDVRRWLNRLQYLLLREFWPMNCSTFTDDITSLPLTIIEGPPTSKIHPDTDDTEVSRSEWDARLGRMLRESPNAVRSTIASCWEWNHFQYSEEAASVAIHSTTPAVTQFSAPGPGGTTGDVTDDGGADVPPCEARGSNIILSSQCPCGECDASFMPSVDMRDLFGFRTLLNGLPSPEHARNCITTNDRMNAFGSWWRRTKKKEAAKLFVAGCSEKSYMDVIGFSCLLQQSTVVLHID
Protein: G-protein coupled receptor 4 (E7FEL0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MASLRGSETMCNITTSCNVDSNIDQFFQPTLYIIVIVLGFPTNCMALWAAYMQVKQKNELGIYLMNLSIADLLYITTLPLWIDYFVHHDNWIHGQVSCKLFGFIFYTNIYVSIAFLCCISVDRYLAVAHPLKFAKVRRVKTALLVSAIVWLTEIVANSAPLFHDELFQDRFNHTFCFEKYPMEPWVAGMNLYRTFLGFLAPWGIMLAAYRGILRAVRGNVSTERQEKAKIKRLALSLILIVLLCFAPYHVLLLWRSVLFLINPCDCGGEENLFGAYHVTLALTSLNCVADPILYCFVNEGARHDVGRALATLLGLFQRGKSPETLMGASITVETPLAVKKPDFYSEVKTNAYKNDIEVLKDECLQMTILSVKK
Protein: Prostaglandin F2-alpha receptor (PGF receptor) (PGF2-alpha receptor) (Prostanoid FP receptor) (P43117)
Organism: Mus musculus (Mouse)
Function: Receptor for prostaglandin F2-alpha (PGF2-alpha). The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-14
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MSMNSSKQPVSPAAGLIANTTCQTENRLSVFFSIIFMTVGILSNSLAIAILMKAYQRFRQKSKASFLLLASGLVITDFFGHLINGGIAVFVYASDKDWIRFDQSNILCSIFGISMVFSGLCPLFLGSAMAIERCIGVTNPIFHSTKITSKHVKMILSGVCMFAVFVAVLPILGHRDYQIQASRTWCFYNTEHIEDWEDRFYLLFFSFLGLLALGVSFSCNAVTGVTLLRVKFRSQQHRQGRSHHLEMIIQLLAIMCVSCVCWSPFLVTMANIAINGNNSPVTCETTLFALRMATWNQILDPWVYILLRKAVLRNLYKLASRCCGVNIISLHIWELSSIKNSLKVAAISESPAAEKESQQASSEAGL
Protein: WD and tetratricopeptide repeats protein 1 (Q8N5D0)
Organism: Homo sapiens (Human)
Function: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- Cullin-4B
- DET1- and DDB1-associated protein 1
- DDB1- and CUL4-associated factor 4
- DNA damage-binding protein 2
Sequence:
MAKVNITRDLIRRQIKERGALSFERRYHVTDPFIRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMHTGHTANIFSVKFLPHAGDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPMWPNTFWSAAEDGLIRQYDLRENSKHSEVLIDLTEYCGQLVEAKCLTVNPQDNNCLAVGASGPFVRLYDIRMIHNHRKSMKQSPSAGVHTFCDRQKPLPDGAAQYYVAGHLPVKLPDYNNRLRVLVATYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTFLLPRKCHSSGEVQNGKMSTNGVSNGVSNGLHLHSNGFRLPESRGHVSPQVELPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRKWDGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFKGKFPEQAHSSACDALGRDITAALFSKNDGEEKKGPGGGAPVRLRSTSRKDSISEDEMVLRERSYDYQFRYCGHCNTTTDIKEANFFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRPESEDLTGRVVEDMEGASQANQRRMNADPLEVMLLNMGYRITGLSSGGAGASDDEDSSEGQVQCRPS
Protein: GMP reductase 2 (GMPR 2) (EC 1.7.1.7) (Guanosine 5'-monophosphate oxidoreductase 2) (Guanosine monophosphate reductase 2) (Q9P2T1)
Organism: Homo sapiens (Human)
Function: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation.
Interaction partners:
- GMP reductase 1
- Bifunctional epoxide hydrolase 2
- GMP synthase
- Bifunctional purine biosynthesis protein ATIC
Sequence:
MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC
Protein: Translation initiation factor IF-1, chloroplastic (P0C379)
Organism: Oryza sativa subsp. indica (Rice)
Function: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_00075}.
Interaction partners:
- Large ribosomal subunit protein uL2 C-terminal domain-containing protein
- 60S ribosomal protein L21
- 60S ribosomal protein L29
- 60S acidic ribosomal protein P1
- Large ribosomal subunit protein uL3m
- 60S ribosomal protein L17
- 60S ribosomal protein L17
- Large ribosomal subunit protein uL16c
- Small ribosomal subunit protein uS9
- 60S ribosomal protein L6
Sequence:
MTEKKNRREKKNPREAKITFEGLVMEALPNGMFRVRLENDTIILGYISGKIRSSSIRILMGDRVKIEVSRYDSSKGRIIYRLPHKDSKRTEDSKDTEDLKDTKDSKG
Protein: tRNA 2'-phosphotransferase 1 (EC 2.7.1.160) (Q86TN4)
Organism: Homo sapiens (Human)
Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Interaction partners:
- Uridine diphosphate glucose pyrophosphatase NUDT22
- Protein mono-ADP-ribosyltransferase PARP10
Sequence:
MNFSGGGRQEAAGSRGRRAPRPREQDRDVQLSKALSYALRHGALKLGLPMGADGFVPLGTLLQLPQFRGFSAEDVQRVVDTNRKQRFALQLGDPSTGLLIRANQGHSLQVPKLELMPLETPQALPPMLVHGTFWKHWPSILLKGLSCQGRTHIHLAPGLPGDPGIISGMRSHCEIAVFIDGPLALADGIPFFRSANGVILTPGNTDGFLLPKYFKEALQLRPTRKPLSLAGDEETECQSSPKHSSRERRRIQQ
Protein: N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) (CMP-N-acetylneuraminic acid synthase) (CMP-NeuNAc synthase) (Q8NFW8)
Organism: Homo sapiens (Human)
Function: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).
Subcellular location: Nucleus {ECO:0000269|PubMed:11602804}.
Interaction partners:
- N-acetylneuraminate-9-phosphate synthase
- N-acylneuraminate-9-phosphatase
- CMP-sialic acid transporter
Sequence:
MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSSTSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHICLLMEKVNNSCQK
Protein: Pyruvate dehydrogenase complex repressor (Q9HV39)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- L-lactate permease
Sequence:
MEFGQVRQRRLSDDIVAQLEAMILEGTLKSGERLPAERVLAEQFGVSRPSLREAIQKLVAKGLLVSRQGGGNYVTESLGATFSDPLLHLLEGNPEAQRDLLEFRHTLEGSCAYYAALRATSLDHQRLTEAFEALQACYARNDQVSAEEGAADARFHLAIAEASHNTVLLHTIKGLFDLLRRNVVTNIGGMYAQRTETRAQLMEQHQRLYDAIISGQAELAREVSNQHIHYVQEVLAEVQEEARRMKRSQRRRSVQED
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q386X5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Leucine-rich repeat protein
Sequence:
MIADKCGKQLSQNDALVGAGPVVPSEGIGIVQRVPPTGSRDAHSNMGDGPRIADGGGSNGDQASADQMPPEAGNCGTTDGEIKRSVVKRRPSWTQFSNPNPTLGGGSSCGGENDSLCAQQHKNGSCSKSGDEIVVATNPKSCDEDELVCCICLEGYNEENPILYGECKHHFHMPCLMAWKQRSNVCPMCDSETLRGVADDQEPPPRRTSPTSLDDHLSPTAHQRYSRREPRIPKNPGVRGHPGRPLQGRQPGSGARPTNHPLGGVSGDSGHRSVGSTGNGGRAATAKVNRQVSPAQNGQVASKPKRSFFSRVFCCFKR
Protein: Cytochrome bd-I ubiquinol oxidase subunit 2 (EC 7.1.1.7) (Cytochrome bd-I oxidase subunit II) (Cytochrome d ubiquinol oxidase subunit II) (P0ABK2)
Organism: Escherichia coli (strain K12)
Function: A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}. Note=The displayed topology is based on (PubMed:15013751) not the large scale studies (PubMed:15919996). {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Cytochrome bd-I ubiquinol oxidase subunit X
- Cytochrome bd-I ubiquinol oxidase subunit 1
- Cytochrome bd-II ubiquinol oxidase subunit 1
- Glutathione/L-cysteine transport system ATP-binding/permease protein CydD
- Uncharacterized protein YnhF
- Glutathione/L-cysteine transport system ATP-binding/permease protein CydC
- Uncharacterized protein YbgE
- Cytochrome bd-II ubiquinol oxidase subunit 2
- Cytochrome bo
- Cytochrome bo
Sequence:
MIDYEVLRFIWWLLVGVLLIGFAVTDGFDMGVGMLTRFLGRNDTERRIMINSIAPHWDGNQVWLITAGGALFAAWPMVYAAAFSGFYVAMILVLASLFFRPVGFDYRSKIEETRWRNMWDWGIFIGSFVPPLVIGVAFGNLLQGVPFNVDEYLRLYYTGNFFQLLNPFGLLAGVVSVGMIITQGATYLQMRTVGELHLRTRATAQVAALVTLVCFALAGVWVMYGIDGYVVKSTMDHYAASNPLNKEVVREAGAWLVNFNNTPILWAIPALGVVLPLLTILTARMDKAAWAFVFSSLTLACIILTAGIAMFPFVMPSSTMMNASLTMWDATSSQLTLNVMTWVAVVLVPIILLYTAWCYWKMFGRITKEDIERNTHSLY
Protein: L-aspartate oxidase (LASPO) (EC 1.4.3.16) (L-aspartate:fumarate oxidoreductase) (EC 1.5.99.-) (Quinolinate synthetase B) (P10902)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+). Can use either oxygen or fumarate as electron acceptors, which allows the enzyme to be functional under aerobic and anaerobic conditions. In vivo, fumarate is used under anaerobic conditions, and oxygen is the predominant electron acceptor under aerobic conditions due to the lower fumarate levels. In vitro, fumarate is a more efficient electron acceptor and is kinetically superior to oxygen.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Quinolinate synthase
- Nicotinamide riboside transporter PnuC
- Nicotinate phosphoribosyltransferase
- Aspartate ammonia-lyase
- L-asparaginase 1
- Adenylosuccinate synthetase
- Omega-amidase YafV
- Argininosuccinate synthase
- L-asparaginase 2
Sequence:
MNTLPEHSCDVLIIGSGAAGLSLALRLADQHQVIVLSKGPVTEGSTFYAQGGIAAVFDETDSIDSHVEDTLIAGAGICDRHAVEFVASNARSCVQWLIDQGVLFDTHIQPNGEESYHLTREGGHSHRRILHAADATGREVETTLVSKALNHPNIRVLERSNAVDLIVSDKIGLPGTRRVVGAWVWNRNKETVETCHAKAVVLATGGASKVYQYTTNPDISSGDGIAMAWRAGCRVANLEFNQFHPTALYHPQARNFLLTEALRGEGAYLKRPDGTRFMPDFDERGELAPRDIVARAIDHEMKRLGADCMFLDISHKPADFIRQHFPMIYEKLLGLGIDLTQEPVPIVPAAHYTCGGVMVDDHGRTDVEGLYAIGEVSYTGLHGANRMASNSLLECLVYGWSAAEDITRRMPYAHDISTLPPWDESRVENPDERVVIQHNWHELRLFMWDYVGIVRTTKRLERALRRITMLQQEIDEYYAHFRVSNNLLELRNLVQVAELIVRCAMMRKESRGLHFTLDYPELLTHSGPSILSPGNHYINR
Protein: Cyclin-C (P25008)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin-dependent kinase Cdk8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Required for leg and eye development and macrochaete specification or differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:8730095}.
Interaction partners:
- Cyclin-dependent kinase 8
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 21
Sequence:
MAGNFWQSSHSQQWILDKPDLLRERQHDLLALNEDEYQKVFIFFANVIQVLGEQLKLRQQVIATATVYFKRFYARNSLKNIDPLLLAPTCILLASKVEEFGVISNSRLISICQSAIKTKFSYAYAQEFPYRTNHILECEFYLLENLDCCLIVYQPYRPLLQLVQDMGQEDQLLTLSWRIVNDSLRTDVCLLYPPYQIAIACLQIACVILQKDATKQWFAELNVDLDKVQEIVRAIVNLYELWKDWKEKDEIQMLLSKIPKPKPPPQR
Protein: Thioredoxin-like reductase Rv2466c (O53193)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: In vitro, the reduced form of Rv2466c catalyzes the reduction and activation of TP053, which is a thienopyrimidine derivative drug that can kill both replicating and non-replicating M.tuberculosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24877756}.
Interaction partners:
- Twitching motility protein PilT
- Ribose-5-phosphate isomerase B
- Conserved protein
- Conserved ATPase
- Endonuclease 8 1 lyase Nei 1)
- Mycothiol acetyltransferase
- Mycothiol S-conjugate amidase
- 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
- Conserved protein
- NADPH-dependent FMN reductase-like domain-containing protein
Sequence:
MLEKAPQKSVADFWFDPLCPWCWITSRWILEVAKVRDIEVNFHVMSLAILNENRDDLPEQYREGMARAWGPVRVAIAAEQAHGAKVLDPLYTAMGNRIHNQGNHELDEVITQSLADAGLPAELAKAATSDAYDNALRKSHHAGMDAVGEDVGTPTIHVNGVAFFGPVLSKIPRGEEAGKLWDASVTFASYPHFFELKRTRTEPPQFD
Protein: Transporter (F1LNR9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Synaptic vesicular amine transporter
Sequence:
MVTRSRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQFNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFASFTLNLPWTNCGHAWNSPNCTDPKLLNASVLGDHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVIVVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVKIEDVATEGAGLVFVLYPEAISTLSGSTFWAVLFFLMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTCAVTLGTFLLAMFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYVYPPWANWVGWGIALSSMILVPAYVIYKFFSIRGSLWERVAYGITPENEHHLLALEIELSSLQSFVITSCPIDPLLSSFLFISCQKTLVFKKSGPAPLI
Protein: Probable geranyltranstransferase (A0A0H3LU29)
Organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Interaction partners:
Sequence:
MKQSHLACADWLRERAQHVEHVLDELLPGADIAPSRLHEAMRYAVLGGGKRVRAALVYAAGQACPVNGSTLAVGASMDRAAAAVELIHAYSLVHDDLPCMDDDTLRRGRPTVHVQFDEATAMLAGDALQPLAFELLAGMPIAPALVVQAAQVLARAAGSQGMAGGQAIDLHSVGRMLTRDELQTMHSMKTGAMLACSVTLGGIVAGASSTARQALDSYAQAIGLAFQVVDDILDVTADTASLGKTAGKDAADNKPTYVSLLGLDQARALAQELRQAAHQALAPLGESGARLGQLADFIVLRDR
Protein: SPE-12 (G5EEF3)
Organism: Caenorhabditis elegans
Interaction partners:
- Spermatocyte protein spe-27
- CX domain-containing protein
- Spermatocyte protein spe-8
- Spermiogenesis protein SPE-29
- Domain of unknown function DX domain-containing protein
- Serine/threonine-protein kinase spe-6
- Lon proteolytic domain-containing protein
- Trypsin-like protease try-5
- Transporter
- Spermatocyte protein spe-11
Sequence:
MNTSTFYIVLLCFLSRNLLNAEHSEEKNNQDLEDRRYKMFGNETDDKRCIHGDLISITSKTFYATEKYYYTECHTRAPSCGFQMMPIMINGLNTSNKVVRFGCFPTRDILGNQFFLNKRYYSNSFDGIYSMFDYFAFENTGIADYLIYYKPTAEELKAVRYVHENRWVENPQEFIVQKKNESSAEAHSDGLNAYFRHKKITPLMIIYILFICFSVIFKLIWLVHTAWKNMKQGYAPIAKMSEVKEDFERTVEDLD
Protein: Ladybird early homeodomain transcription factor (Q9VDA1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MLCPPTMRPASPAESEISVGGAPSPLPTQDHTHPHSHPHPLQDPRASTIDLLQQQQLLMQHHAAAAAAAAAAASGLTRSAVGNLAEDYFHPLKRLRMSSSSSEPREHTASPPSAVPEPQTNQTTKSAIEGVKSFSIADILGHSEKQREESVSPPPNANLLAPPASRPIAPSGGLLQPRTEPLDVHPAAAAAMLLPSGQIVRPWDHLLGPTMPVRPFIPSALLHYEQRLALDYHRQLQEHFNAQAQLLRHMGMNPAIIASEDGSSERSQRSSSSNGSTECCSPRQAEKLEKLTTQEGSEEAQKKKSEEQPTGSGKSNGDTPLDALFQMTTKDFDESQDKSHLDIFSDRPQPKKKRKSRTAFTNHQIFELEKRFLYQKYLSPADRDEIAASLGLSNAQVITWFQNRRAKQKRDIEELKKDFDSVKVFSAHKSFLENVNDLSILKKKPMHESDMVGLAAAAAAAGMVVLVPGSVPMGGAPPK