wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0B4KF57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|ARBA:ARBA00004132}.
Interaction partners:
Sequence:
MGEFFKSLNLNYFSSSEVNGAAGNGAPEALGGRLDNDFVGQVVEVAGHRLRIKCVIAEAQDVQTGTEYALKRLIGADMQASTAIINEINIHKQLSGHENIVAFVGSSYTAPSTQLGAQYLLLTELCKGGSLVDCFRTNNAPFNPTCVLRIFYQMARAVASLHSQSPPIAHRDIKIENFLIGNDKQIKLCDFGSASTEVLSPTFEWSANQRSMLEDQLNTVTTPMYRSPEMLDTWSNNPIGPKVDIWALGCILYFLCYRKHPYEDGGKLRIINANYMLPPDPQYQCFSDIIRGCLKVNPFERLDITMVLEGLAALAETHNWSLKGPLDLHIMPIESLPAESPLKSSAYSEVYTEPLSAAIPSSYNGHGSLLSSLRGGAGTLLKNIKDTSTKVMQTMQQSLARNDLDISHITSRILVMPCPSDGFESTYKTNNIEDVRLSLESRFVPQKLSIYNFGQRTEPRLPPPVRTVEAGSVYGCPQAHAPNLQGLFTVSADMYNFLNADPKSVVIVQTGDSGGCTAATVICALLMYADLLREPEDAVQVFAVKRHTINLRPSEFRYLYYFGDILRPTPLLPHYKNTTLVSLSCQPVPRMTKARDGCRIYMEVYCNGNLLLSTLQDYEKMRLYQAGPGKIVLPINLTACGDVTVVLFHARKGMVRPQGLKICQFQFNTGFIPEPETLITFTNQDLDDLPDPEQVTPRFCVSLSLAVTDSESPPSHKPPWMPAKPKRSPAALFSSDLEYAEMLDNFVTKPSTRSSPPPGARKSDRVSSPLVLPDVTETAHELPSPMPEPSPPIDLLNLNQQPSDVPAADPLTSAKPSTDASFDLLGAFGDDDSTGIGSAPIPDILPPPPLQQPQPKINNDPFDIFGSVDQGGVPSMKPSGFPPFVGSLPTFVAQPAATTNPSPTHPARASADPFANIADLATGLNLNFNRSTLSGKSPVNTSPQPTQFSSPTHKPSPSSQPQATFMHTPPTPQTLPSTSSIRTPTQPQAVPAQSRPDYSRLHFDSQKAAQQPGTGGSKNSDIFADILGQQGYSFGSKMNQCPRSINEMRKEDLFKDMDPKKVRIMEWTDGKKNNIRALLCSMHTVLWDNAKWQRCEMSTMVTPTEVKKAYRRACLAVHPDKHNGTENEEIAKLIFMELNNAWTDFENDATQQNMFNA
Protein: Monocarboxylate transporter 2 (MCT 2) (Solute carrier family 16 member 7) (P53988)
Organism: Mesocricetus auratus (Golden hamster)
Function: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:7829520}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Basolateral cell membrane {ECO:0000269|PubMed:7829520}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Cytoplasm {ECO:0000250|UniProtKB:O70451}. Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By similarity). {ECO:0000250|UniProtKB:O70451, ECO:0000250|UniProtKB:Q63344}.
Interaction partners:
- Embigin
- Basigin
Sequence:
MPSETAVPPPHPIPPDGGWGWVVVGAAFISIGFSYAFPKAVTVFFKDIQQIFQASYSEIAWISSIMLAVMYAGGPISSVLVNNYGSRPVVIIGGLLCCTGMILASFSNSVLELYLTIGFIGGLGLAFNLQPALTIIGKYFYRRRPMANGLAMAGSPVFLSSLAPFNQYLFNSYGWKGSFLILGGIFLHSCVAGCLMRPVQTSPRKSKSKSKVGSRQDGSMKKASKVSTAEKINRFLDFSLFKHRGFLIYLSGNVIMFLGFFAPIIFLAPYAKDKGVDEYNAALLLSVMAFVDMFARPTGGLIANSKLIRPRIQYFFSFAIVFTGICHLLCPLADTYPALVVYSIFFGYGFGSVSSVLFETLMDLVGPARFSSAVGLATIVECCPVLLGPPLAGKLVDKTKDYKYMYIASGTIVVISGIYLFIGNAINYRLLAKERKREKARKKKSATHPSRESEALSRSKQDDVSVKVSNPHNSPSDRERESNI
Protein: Tumor necrosis factor receptor type 1-associated DEATH domain protein (TNFR1-associated DEATH domain protein) (TNFRSF1A-associated via death domain) (Q3U0V2)
Organism: Mus musculus (Mouse)
Function: Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD (By similarity). Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B (By similarity). The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A.
Subcellular location: Nucleus {ECO:0000269|PubMed:22561347}. Cytoplasm {ECO:0000269|PubMed:22561347}. Cytoplasm, cytoskeleton. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000269|PubMed:22561347}.
Interaction partners:
- Baculoviral IAP repeat-containing protein 3
- Tumor necrosis factor
- TNF receptor-associated factor 3
- Caspase-8
- TNF receptor-associated factor 1
- Receptor-interacting serine/threonine-protein kinase 1
- Receptor-interacting serine/threonine-protein kinase 3
- Tumor necrosis factor receptor superfamily member 1A
- Baculoviral IAP repeat-containing protein 2
- TNF receptor-associated factor 2
Sequence:
MAAGQNGHEEWVGSAYLFLESAVDKVILSEAYTDPKKKVAIYKALQTALSESGDSSDVLQILKIHCSDPQLIVQLRFCGRVLCGRFLQAYREGALRTALQRCMAPALAQEALRLQLELRAGAEQLDSWLTDEERCLNYILAQKPDRLRDEELAELEDELCKLTCDCTGQGGAIQVASAGSKFPVSSPTEEKPLPAACQTFLFHGQLVVNRPLTLQDQQTFARSVGLKWRRVGRSLQRNCRALRDPALDSLAYEYERDGLYEQAFQLLRRFMQAEGRRATLQRLVEALEENELTSLAEDLLGQAEPDGGLA
Protein: Cytochrome P450 monooxygenase stcS (EC 1.14.-.-) (Cytochrome P450 59) (Sterigmatocystin biosynthesis cluster protein S) (Q00714)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
- Glutathione S-transferase stcT
Sequence:
MPSFSLLTGHFGALKQTIDGMPPNATLHSIMLKLSQKFRSGMFYINMWPFSGTWLVVATPSGAAQIQSLNLSKPNILRRPLETITGGPSLMSMHGETWKRWRALFNPGFNPNYLIGLAPLIADEVVVFCEQLRQKARTGTVFQLEPLTLRLTVDTICSVTLDSQLHHQTQDHPLASALQRQIEWASFGTTFNPFKRYLTVRPLVMWYNNRLMNRFIDQEVDRAYREQSGRQSKSVISLALRDYMKEKDGSLEDFKRRVAPQLRVFLFAGRDTTSSTLLYAFYLLSRHPEALAKVRLEHDQVFGPYHQQVHEKIHQDAKLLNQLPYTTAVLKETLRLFPPSASMREGRPGVEITDDNGQVYPTAGCNVWTLTVALHHNSAHWAEAESFIPERWLVGSDHPLYPAKGAWRAFEFGPRSCIGQTLAMLELRVALAMTLREFDIAPAYDKWDHIYPNDAVKEFNGHRAYQAEKGGGGAHPADGMPCLVTFRV
Protein: Large ribosomal subunit protein uL5m (Probable 54S ribosomal protein L7, mitochondrial) (O14337)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS11m
- Large ribosomal subunit protein uL6m
- Small ribosomal subunit protein uS14m
- Elongation factor 3
- mRNA export factor elf1
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL3m
Sequence:
MLGIRKNIRISVNFLQRRTITVKQKLGKNRPLPGWDPNSEYFRPGPTMLNRLQEHLHDTILPDVLAASYRHDIDTALSTDEHTQKDRLPRWIGDNPYYKNRPPQKMRGNKPLLPVKESVNPKNLPSISKVVVSTMHKEALVDKTQLLSTMMAFRSITGLQPEIVYARKDVSPWKLRSGVPVGVKVTLTGESMYTFLSILSELVLPQLHDFKGLSPTSGDQTGNISFGLPSEVMPLFPQIEAVYEMYPHSLPGFNVNITTNSKDTRLARFFVSSLIPFTDGNKEGYVG
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q49IJ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EHEAKLQRLREELSRPVIEAHHRQSHHQKQAQHRQHHQSHHRKKQHRQQQHHRRRGQSTTQYVNHSPPGFNQSQQAQQQSVPEMDLLKAETSKDEEPLRHRVARAVTAKKERIWDYGVIPYEIDGNFSGIHKALFKLAMRHWENSTCIKFVERDPEIHPNYIVFTVRSCGCCSFVGKRGNGPQAISIGRNCDKFGIVVHELGHVVGFWHEHTRPDREKHVVIEHNNIMKGQDYNFNMLSPDEVDSLGMAYDYDSIMHYARNTFSKGTYLDTILPIEMKGRKRPEIGQRLRLSQGDIAQANLLYKCPKCGRTFQESSGIFASPSHYTAGALSNETEHCEWRITATYGERVELKLENMNIFKSNNCETDYLEIRDGYFEKSPLIGRFCGKVDKEVIRTESSRMLLTYVNTHRIEGFRGFKAEFD
Protein: Probable inorganic phosphate transporter 1-5 (AtPht1;5) (H(+)/Pi cotransporter) (Q8GYF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity transporter for external inorganic phosphate.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Inorganic phosphate transporter 2-1, chloroplastic
- Phosphate transporter PHO1
- Probable anion transporter 5
- SPX domain-containing protein 1
- SPX domain-containing membrane protein At1g63010
- SEC12-like protein 1
- Probable ubiquitin-conjugating enzyme E2 24
- Protein PHOSPHATE STARVATION RESPONSE 1
- Probable anion transporter 3, chloroplastic
- Phosphate transporter PHO1 homolog 1
Sequence:
MAKKGKEVLNALDAAKTQMYHFTAIVIAGMGFFTDAYDLFSISLVTKLLGRIYYHVDSSKKPGTLPPNVAAAVNGVAFCGTLAGQLFFGWLGDKLGRKKVYGITLMLMVLCSLGSGLSFGHSANGVMATLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFIAAVFAMQGFGILAGGIVSLIVSSTFDHAFKAPTYEVDPVGSTVPQADYVWRIVLMFGAIPALLTYYWRMKMPETARYTALVARNTKQAASDMSKVLQVDLIAEEEAQSNSNSSNPNFTFGLFTREFARRHGLHLLGTTTTWFLLDIAYYSSNLFQKDIYTAIGWIPAAETMNAIHEVFTVSKAQTLIALCGTVPGYWFTVAFIDILGRFFIQLMGFIFMTIFMFALAIPYDHWRHRENRIGFLIMYSLTMFFANFGPNATTFVVPAEIFPARLRSTCHGISAASGKAGAIVGAFGFLYAAQSSDSEKTDAGYPPGIGVRNSLLMLACVNFLGIVFTLLVPESKGKSLEEISREDEEQSGGDTVVEMTVANSGRKVPV
Protein: Anther-specific protein RTS (Protein RICE TAPETUM-SPECIFIC) (Q40629)
Organism: Oryza sativa subsp. indica (Rice)
Function: Required for tapetum and pollen development.
Interaction partners:
Sequence:
MVRVAAAAAVLVLAAAAAAAAAMAAEPPTDDGAVRVAAGLTKCVSGCGSKVTSCLLGCYGGGGGAAAAATAMPFCVIGCTSDVLSCATGCSTSL
Protein: Transposon Ty2-F Gag-Pol polyprotein (TY2A-TY2B) (Transposon Ty2 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA); Ty2 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)] (P0CX63)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty2 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLHQNPHSLHGSAYASVTSKEVPSNQDPLAVSASNLPEFDRDSTKVNSQQETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDSQNQHSEVPQAETKVRNNVLPPHTLTSEENFSTWVKFYIRFLKNSNLGDIIPNDQGEIKSQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYADILTVLCKSVSKMQTNNQELKDWIALANLEYDGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYLRNQYRTKTNMKLSQLFAEIQLIYDENKIMNLNKPSQYKQHSEYKNVSRTSPNTTNTKVTTRNYHRTNSSKPRAAKAHNIATSSKFSRVNNDHINESTVSSQYLSDDNELSLGQQQKESKPTHTIDSNDELPDHLLIDSGASQTLVRSAHYLHHATPNSEINIVDAQKQDIPINAIGNLHFNFQNGTKTSIKALHTPNIAYDLLSLSELANQNITACFTRNTLERSDGTVLAPIVKHGDFYWLSKKYLIPSHISKLTINNVNKSKSVNKYPYPLIHRMLGHANFRSIQKSLKKNAVTYLKESDIEWSNASTYQCPDCLIGKSTKHRHVKGSRLKYQESYEPFQYLHTDIFGPVHHLPKSAPSYFISFTDEKTRFQWVYPLHDRREESILNVFTSILAFIKNQFNARVLVIQMDRGSEYTNKTLHKFFTNRGITACYTTTADSRAHGVAERLNRTLLNDCRTLLHCSGLPNHLWFSAVEFSTIIRNSLVSPKNDKSARQHAGLAGLDITTILPFGQPVIVNNHNPDSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQDKQSKLDQFNYDTLTFDDDLNRLTAHNQSFIEQNETEQSYDQNTESDHDYQSEIEINSDPLVNDFSSQSINPLQLDKEPVQKVRAPKEVDADISEYNILPSTIRSRTPHIINKESTEMGGTVESDTTSPRHSSTFTARNQNRPGSTNEMIDLTSQDRVNYGLENIKTTRLGGTEEPYIQRNSDTNIKYRTTNSTPSIDDRSSNSESTTPIISIETKAVCDNTPSIDTDPPEYRSSDHATPNIMPDKSSKNVTADSILDDLPLPDLTHKSPTDTSDVSKDIPHIHSRQTNSSLGGMDDSNVLTTTKSKKRSLEDNETEIEVSRDTWNNKNMRSLEPPRSKKRINLIAAIKGVKSIKPVRTTLRYDEAITYNKDNKEKDRYVEAYHKEISQLLKMNTWDTNKYYDRNDIDPKKVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSDMQSNTVHHYALMTSLSIALDNDYYITQLDISSAYLYADIKEELYIRPPPHLGLNDKLLRLRKSLYGLKQSGANWYETIKSYLINCCDMQEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRSKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGHYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Glutamate receptor ionotropic, kainate 1 (GluK1) (Glutamate receptor 5) (GluR-5) (GluR5) (P22756)
Organism: Rattus norvegicus (Rat)
Function: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus.
Subcellular location: Cell membrane {ECO:0000305|PubMed:10023812}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000305|PubMed:10023812}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor ionotropic, kainate 2
- Keratin, type I cytoskeletal 12
- Glutamate receptor ionotropic, kainate 3
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 3A
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor 2
Sequence:
MERSTVLIQPGLWTRDTSWTLLYFLCYILPQTSPQVLRIGGIFETVENEPVNVEELAFKFAVTSINRNRTLMPNTTLTYDIQRINLFDSFEASRRACDQLALGVAALFGPSHSSSVSAVQSICNALEVPHIQTRWKHPSVDSRDLFYINLYPDYAAISRAVLDLVLYYNWKTVTVVYEDSTGLIRLQELIKAPSRYNIKIKIRQLPPANKDAKPLLKEMKKSKEFYVIFDCSHETAAEILKQILFMGMMTEYYHYFFTTLDLFALDLELYRYSGVNMTGFRKLNIDNPHVSSIIEKWSMERLQAPPRPETGLLDGMMTTEAALMYDAVYMVAIASHRASQLTVSSLQCHRHKPCALGPRFMNLIKEARWDGLTGRITFNKTDGLRKDFDLDIISLKEEGTEKASGEVSKHLYKVWKKIGIWNSNSGLNMTDGNRDRSNNITDSLANRTLIVTTILEEPYVMYRKSDKPLYGNDRFEAYCLDLLKELSNILGFLYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQSALVKNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEDSKEASALGVENIGGIFIVLAAGLVLSVFVAIGEFLYKSRKNNDVEQKGKSSRLRFYFRNKVRFHGSKKESLGVEKCLSFNAIMEELGISLKNQKKLKKKSRTKGKSSFTSILTCHQRRTQRKETVA
Protein: Alpha-benincasin (P83960)
Organism: Benincasa hispida (Wax gourd) (Cucurbita hispida)
Function: Has weak antifungal activity toward C.comatus and P.piricola but not toward M.arachidicola. Inhibits cell-free translation in rabbit reticulocyte lysate system.
Interaction partners:
Sequence:
RDWERREFERRQNELRREQEQRREELL
Protein: Galactose-1-phosphate uridylyltransferase (Gal-1-P uridylyltransferase) (EC 2.7.7.12) (UDP-glucose--hexose-1-phosphate uridylyltransferase) (E8MF11)
Organism: Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
Function: Transfers the UMP unit from UDP-glucose (UDP-Glc) to Gal1P. Can also transfer the UMP unit to GlcNAc1P and GalNAc1P. Involved in the general galactose metabolism, and also involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00571}.
Interaction partners:
Sequence:
MNDQLTEVYASIDALIDYALAHLDLDPRNADWTRNQIFALFRLDSYPGPKTTTSAASVSDVVQDIVGSRSQAPYGEKTPDPLLAAFRAAATTAGLFKPEEGPAYADTIMGILSANPADLDDRFLLVEHRDGGMAAMQWFYDYCVANNYVKRAQLDRNPRFDSHGLTVTINLAKPEFKNMKKAAAGNAVAGGYPKCTICHENEGFAGRDKRTLRTLPVTLGGESWFWQFSPYGYFDQHGICVNTDHTPMHVDRDTFGHLLDFVDRFPGYFLGCNAALPRIGGSVLAHDHYQGGGELLPMHKAATWAAFTLADYPDAVVEILDWPGTAVRVVSKSRQSIIDVSDIIREAWVGYDDAANGIASHDADGNRQSALSPSAIITERGYEMSLIFRNNAISDEYPEGIFHAHPEYWPVKQEPIGLIEAQGLFILPGRLVDQLGIVEEALAEGRDLPDEVSEFSLEWGELAETLAGNHDREAIRQAVHDELGSVCYRILGNTAVFKQKATTQTFLESLGFAAR
Protein: Uncharacterized protein (Q4GYP2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MEEVLDNKETNFEAANNTGSECDVSSCGSNNGVDEHRNRVVALRPADALDAPLHLTEIPKQFLLEPGAAGVGVGIGTRQLVLKDKTEAAQRSWPRFRVPVDRPLPRAVWSPSCRRRRPSQVESYLAPLFTASGNEEEKATLSFLHPPEGNPRQVVEERKRQEMSQRWVDAEGNPRLSVAEVPIRVPNLKKKVPKDFVPQCALVFTQSRMAEVEETRKRQAEIAELSSKRLSRQMRDDRFSEERHEEENTPMA
Protein: TBC1 domain family member 30 (Q9Y2I9)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein (GAP) with broad specificity. Acts as a GAP for RAB3A. Also exhibits significant GAP activity toward RAB22A, RAB27A, and RAB35 in vitro.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19077034}; Peripheral membrane protein {ECO:0000269|PubMed:19077034}.
Interaction partners:
Sequence:
MDVLPTGGGRPGLRTELEFRGGGGEARLESQEEETIPAAPPAPRLRGAAERPRRSRDTWDGDEDTEPGEACGGRTSRTASLVSGLLNELYSCTEEEEAAGGGRGAEGRRRRRDSLDSSTEASGSDVVLGGRSGAGDSRVLQELQERPSQRHQMLYLRQKDANELKTILRELKYRIGIQSAKLLRHLKQKDRLLHKVQRNCDIVTACLQAVSQKRRVDTKLKFTLEPSLGQNGFQQWYDALKAVARLSTGIPKEWRRKVWLTLADHYLHSIAIDWDKTMRFTFNERSNPDDDSMGIQIVKDLHRTGCSSYCGQEAEQDRVVLKRVLLAYARWNKTVGYCQGFNILAALILEVMEGNEGDALKIMIYLIDKVLPESYFVNNLRALSVDMAVFRDLLRMKLPELSQHLDTLQRTANKESGGGYEPPLTNVFTMQWFLTLFATCLPNQTVLKIWDSVFFEGSEIILRVSLAIWAKLGEQIECCETADEFYSTMGRLTQEMLENDLLQSHELMQTVYSMAPFPFPQLAELREKYTYNITPFPATVKPTSVSGRHSKARDSDEENDPDDEDAVVNAVGCLGPFSGFLAPELQKYQKQIKEPNEEQSLRSNNIAELSPGAINSCRSEYHAAFNSMMMERMTTDINALKRQYSRIKKKQQQQVHQVYIRADKGPVTSILPSQVNSSPVINHLLLGKKMKMTNRAAKNAVIHIPGHTGGKISPVPYEDLKTKLNSPWRTHIRVHKKNMPRTKSHPGCGDTVGLIDEQNEASKTNGLGAAEAFPSGCTATAGREGSSPEGSTRRTIEGQSPEPVFGDADVDVSAVQAKLGALELNQRDAAAETELRVHPPCQRHCPEPPSAPEENKATSKAPQGSNSKTPIFSPFPSVKPLRKSATARNLGLYGPTERTPTVHFPQMSRSFSKPGGGNSGTKKR
Protein: Protein CREG1 (Cellular repressor of E1A-stimulated genes 1) (O88668)
Organism: Mus musculus (Mouse)
Function: May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MAARAPELARSLLAALLAPALVALLVSPASGRGGRDHGDWDVDRRLPPLPPREDGPRVARFVTHVSDWGSLATISTIKEVRGWPFADIISISDGPPGEGTGEPYMYLSPLQQAVSDLQENPEATLTMSLAQTVYCRNHGFDPQSPLCVHIMMSGTVTKVNKTEEDYARDSLFVRHPEMKHWPSSHNWFFAKLKISRIWVLDYFGGPKVVTPEEYFNVTLQ
Protein: Histidine kinase/HSP90-like ATPase domain-containing protein (A0A0G2JH20)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Melanosome {ECO:0000256|ARBA:ARBA00004223}.
Interaction partners:
Sequence:
MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDAGEPMGRGTKVVLHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEDKQPDDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEVNPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTAAAVTEEMPPLEGDDDTSRMEEVD
Protein: Alpha-mannosidase 2 (EC 3.2.1.114) (Golgi alpha-mannosidase II) (AMan II) (Man II) (Mannosidase alpha class 2A member 1) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) (Q16706)
Organism: Homo sapiens (Human)
Function: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:P28494}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P28494}.
Interaction partners:
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- ER degradation-enhancing alpha-mannosidase-like protein 3
- Alpha-mannosidase 2x
- Coatomer subunit beta'
- Beta-1,4-galactosyltransferase 1
Sequence:
MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLERLLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFASQSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRDKGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIGNSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDRISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKILESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMTKEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTCFFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQIQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQDDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPMANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFSSKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFRIQLR
Protein: Probable M18 family aminopeptidase 1 (EC 3.4.11.-) (P0C925)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- Putative phosphotransferase enzyme IIB component BB_0367
- Outer surface 22 kDa lipoprotein
Sequence:
MKKQNPWIYLNEEEKNQILNFSESYKKFISKFKTEREVTAYALDKAKKLGFINAEEKKNLMPGDKIFYTCREKSVAFAIIGKNPIEDGMNFIVSHTDSPRLDAKPSPISEENELTFIKTNYYGGIKKYQWLSTPLSIRGVVFLKNGEKVEINIGDNENDPVFVIPDILPHLDRKIQRNKKSDEIVEGENLKILIGSLPIETKEKNKVKLATLQLIKEKYKIEEEDFVSSEIEIVPAGTAKDVGFDKALIGAYGQDDKICVFTSLESIFDLEETPNKTAICFLVDKEEIGSTGSTGLDSRYLEYFVSDMIFKIKKSEYNNLHVQKALWNSKSISADVCAAINPLFSSVHDEQNAPQLGYGIPIMKYTGHGGKSMASDADAELVSYIRQLLNKNNIAWQVATLGKVEEGGGGTVAKFLAGYGIRTIDMGPAVISMHSPMEITSKFDLYNAYLAYKAFYRE