wanglab/gogpt-training-data huggingface dataset:
Protein: Lysosome membrane protein 2-A (Lysosome membrane protein II-1) (LIMP II-1) (Q9XYS8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act as a lysosomal receptor (By similarity). May be involved in macropinocytosis and fluid phase exocytosis. Binds to the anionic phospholipid phosphoinositol 4,5-bisphosphate, but not to phosphatidylcholine and only weakly to phosphatidylserine.
Subcellular location: Lysosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to membranes of endolysosomal vesicles and macropinosomes. {ECO:0000269|PubMed:10189376, ECO:0000269|PubMed:11489884}.
Interaction partners:
Sequence:
MVKRGCCHRKMVNHKGCLVSGIFLAVIGAVLFILAFALLPHLINQTTQNAVIQAVIVDSTSSQRYNDWAGQQSIENYYQQYFYAWNLTNPNEFLNGSIPIFETVGPFNYKYEFNFSNVTFQDGGNLATYTQSKSFIYQSDMSPNDPNEIMITNINPAYLGLMFQLAPNAELLDNMPAENLLIALSGCGQMRLFLEYLSSDNFTNIVYFTQNPKLYQEQYLNILKSLNGDEQYFYQQWANATSIPQKGNGWYGMLVSSVNNNNESSNISILSAKLLFNSSNENSILNQEIGSTLWINALLGDKTSITVLTSELQLTVDQIDMILNWWLNDFSKVYTESYVNEICDIPDISMLGVCQFVTGNALNGRSISNYTFLTQPFDQGPIEIPLLYQSIGIDVKLSVSVQQAYKSLFNESDSNSILNLNGLVNFLTASKSFDTFKQYNVTLFDAIKIIGYATAELYEQYNKPTILGLYEKYGGLIVTRSMDDWLWNCQDGILDYLGVDQPCALQQNNTVNKPSTIFTGQQDLSMTNQIFEFQEQTFLTCWNGSVQVEGFTESGQFPPLQSDPPQTMTLFEENVIRPVQLELSGDSQVQGIDTKRYYLVNNSFPISTTFKTTIPGFANLTDIQNLPIYVSLWDMYEVPPQYSSNNLQGLNQTYQSAQVPLDLEPITGNALYYNLKLQINLAIPEFSNWFSSNSTFKNMKSNVFYPILKIGQTATPSQSNIDLLNSQFKLIKILGFVPVIVVSIIGGIILIAGISMFAFGFKKLRQQKQQGYQAIINNE
Protein: Nodulin-like domain-containing protein (Q385B2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSVTEGDERATEVGPEPKLVISEPKRFAILVVGVFGCVCVSLTFGFNIFSGDLQERYHFTQAEMTTISTVGLVLSYFGLPYAFVYDYFGVFPVLVMGFVMMATGLLFMALTFGGTITASVVLLCVFNGIFNFASGLYDLACVVTTLTQFPTAKGWIVAVMKTFIGLGSALLGAIQLAFFEDDPTNYFYFLLAFGAVVGIVVMLVMRSAPYIITDYMLKHLTEEEITRREATKAVYLRQEPPTLRFAIGLLIITVLIIVLPLQSALIAYTDVSPFNRKASTIVFVVIWLLYPIVCLPAKCLDKSWRFWRKESQVSAGSIEDQRRDDGSSEGEIDELDYIPPQYQTRFIDSVKTLRLWALFWSLFCTLGAEFVVLINTRFLFAALAGKEIDDSLNTLLTVLNGTGSAAGRLIMSYLEIWSQKRKAEDRIPITVTLFIPTAAITIMLVLFLTVSNEYVLPFAFVVGAIGNGIIASVTILVVNTIYAKDLGLHYNYCFVATACSTILYNRLLYGEWYTYEANKLGVEVCLERVCVQMPLLVMLGLNLTAFGTNTYVHCEYLKLVRSALEGRRVAAESLPKKPEGANDINSIRLELPAETSAAPYGSRDRRGTE
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.-) (B7USF9)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Interaction partners:
Sequence:
MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHISK
Protein: Alpha-ketoglutarate dehydrogenase component 4 (Alpha-ketoglutarate dehydrogenase subunit 4) (P82909)
Organism: Homo sapiens (Human)
Function: May be necessary to recruit DLD/E3 to the mitochondrial 2-oxoglutarate dehydrogenase complex (OGDC) core composed of OGDH/E1-DLST/E2, hence stabilizes the complex.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82908}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein bS21m
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS37
Sequence:
MMGSKMASASRVVQVVKPHTPLIRFPDRRDNPKPNVSEALRSAGLPSHSSVISQHSKGSKSPDLLMYQGPPDTAEIIKTLPQKYRRKLVSQEEMEFIQRGGPE
Protein: Putative uncharacterized protein encoded by LINC00518 (Q8N0U6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSSDETGSSFMSFWPHLQSDDLARNGITGFPYFSFIILNESDQILELDGTLVKIWLLVPSHQPATHFKFEETKTHGPYVITGDYPRSLWQKSASSLPASPPCLWYFLPTLGCFCDHT
Protein: Otoraplin (Melanoma inhibitory activity-like protein) (Q9JIE3)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MARILILLLGGLVVLCAGHGVFMDKLSSKKLCADEECVYTISLARAQEDYNAPDCRFIDVKKGQQIYVYSKLVTENGAGEFWAGSVYGDHQDEMGIVGYFPSNLVKEQRVYQEATKEIPTTDIDFFCE
Protein: Chitinase 1 (EC 3.2.1.14) (Class I chitinase a) (OsChia1a) (Pathogenesis related (PR)-3 chitinase 1) (Q42993)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydrolyzes chitin and may play a role in defense against fungal pathogens containing chitin.
Interaction partners:
Sequence:
MRALAVVVVATAFAVVAVRGEQCGSQAGGALCPNCLCCSQYGWCGSTSAYCGSGCQSQCSGSCGGGGPTPPSGGGGSGVASIVSRSLFDQMLLHRNDAACPAKNFYTYDAFVAAANAFPSFATTGDAATRKREVAAFLAQTSHETTGGWATAPDGPYSWGYCFKEENNGNVGSDYCVQSSQWPCAAGKKYYGRGPIQISYNYNYGPAGQAIGSNLLSNPDLVASDATVSFKTAFWFWMTPQSPKPSCHAVMTGQWTPNGNDQAAGRVPGYGVVTNIINGGVECGHGADSRVADRIGFYKRYCDMLGVSYGANLDCYNQRPFNS
Protein: Vesicular acetylcholine transporter (VAChT) (O17444)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in acetylcholine transport into synaptic vesicles.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Choline O-acetyltransferase
- Vesicular inhibitory amino acid transporter
- Synaptotagmin 1
- Ras-related protein Rab-3
- Glutamate decarboxylase
- Vesicular glutamate transporter, isoform A
- Unc-13, isoform E
- Synaptobrevin
- Choline/carnitine acyltransferase domain-containing protein
- Acetylcholinesterase
Sequence:
MASFQIPVINLEVREVKDIVWEKIQEPVNQRRLILVIVSIALLLDNMLYMVIVPIIPDYLREIGSFDDGPTPPPLRDNITGKIIPVHHDHHGQDSATGILFASKAIVQLMVNPFSGGLIDKIGYDLPMMIGLTIMFFSTAVFACGSSYSVLFFARSLQGAGSAFADTAGLAMIADRFTEENERSQALGIALAFISFGCLVAPPFGGALYQFAGKEVPFLILALVCLLDGLMLLLVMKPVKEAMKQSKDVQDQVIPIWRLLMDPYIAVCAGALTMSNVALAFLEPTISLWMEDNMTTDNWKIGMVWLPAFFPHVLGVVITVKMARKYPQHQWLMAAGGLALEGFSCFIIPFCSGYKMLMLPICVICFGIALIDTALLPTLGYLVDVRYVSVYGSIYAIADISYSIAYAVGPIIAGGVVEAIGFTALNFLIAFSNLAYVPVLRKLRNIYDFKPFENEANILMQDPPNKEYQTYVMHDQKPVEGGVKNHLEYGQQYQQEQETNLDDQQYEYQQQQQGYQQGYQQDQGYQPGYQEQGGSYAPQGQPRVANPFQQQQQQQQQQQQQVQSRGPAAPANPFRQGF
Protein: 40S ribosomal protein S4 (Q3V1Z5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MARGPKKHLKRVAAPRHWMLDKLTGVFAPRPSAGPHRLRECLPLAIFLRNRLKYALTGDEVKKICMQRLIKVDGKVRTDVAYPAGFMDVISIDKSGENFRLVYDTKGRFAVHRITPEEAKYKLCKVRKVFVGTKGIPHLVTHDARTIRYPDPLIKVNDTVQISLDSGKITDAIKFDTGNLCMVTGGANLGRIGVITNRERHPGSFDVVHVKDANGNGFATRLSNIFVIGKGNKPWISLPRGKGIRLTIAEERDKRLAAKQSG
Protein: Polyphosphate kinase (EC 2.7.4.1) (ATP-polyphosphate phosphotransferase) (Polyphosphoric acid kinase) (P9WHV9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
Interaction partners:
- GDP-polyphosphate phosphotransferase
- Exopolyphosphatase 1
- Exopolyphosphatase 2
- Inorganic pyrophosphatase
- 8-oxo-
- Mycothiol acetyltransferase
- Phosphoenolpyruvate guanylyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MMSNDRKVTEIENSPVTEVRPEEHAWYPDDSALAAPPAATPAAISDQLPSDRYLNRELSWLDFNARVLALAADKSMPLLERAKFLAIFASNLDEFYMVRVAGLKRRDEMGLSVRSADGLTPREQLGRIGEQTQQLASRHARVFLDSVLPALGEEGIYIVTWADLDQAERDRLSTYFNEQVFPVLTPLAVDPAHPFPFVSGLSLNLAVTVRQPEDGTQHFARVKVPDNVDRFVELAAREASEEAAGTEGRTALRFLPMEELIAAFLPVLFPGMEIVEHHAFRITRNADFEVEEDRDEDLLQALERELARRRFGSPVRLEIADDMTESMLELLLRELDVHPGDVIEVPGLLDLSSLWQIYAVDRPTLKDRTFVPATHPAFAERETPKSIFATLREGDVLVHHPYDSFSTSVQRFIEQAAADPNVLAIKQTLYRTSGDSPIVRALIDAAEAGKQVVALVEIKARFDEQANIAWARALEQAGVHVAYGLVGLKTHCKTALVVRREGPTIRRYCHVGTGNYNSKTARLYEDVGLLTAAPDIGADLTDLFNSLTGYSRKLSYRNLLVAPHGIRAGIIDRVEREVAAHRAEGAHNGKGRIRLKMNALVDEQVIDALYRASRAGVRIEVVVRGICALRPGAQGISENIIVRSILGRFLEHSRILHFRAIDEFWIGSADMMHRNLDRRVEVMAQVKNPRLTAQLDELFESALDPCTRCWELGPDGQWTASPQEGHSVRDHQESLMERHRSP
Protein: Uncharacterized protein, isoform C (M9PGT2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLIEIYDYAAKLLNNMTARGVRNSVGKSAESRTKESTGKLGSLLGRTLAKVAKVARSNPAQHVTNLPVSALLLQALDVADVARGQGIDYPITSTTGTTFNIITTTTTTTTTTTGSDPTDVLGSQPPAFSFPANVTGAPGSAGNANAYLPAGNLSGFIESSTTAVMSTLPIPTSTMATLQAQTVATFIAATGSKNRPTTIVVYPTVSPESIVIPIVSCIFGFPILALLVICCLRRRAKLARERDRRRNYDMQDHAVSLVRFSPIHRLNYRSSRAISLRPERSLSQGFTSLELDTVLEERCSDVEQTQTEMFNAESPMDTTSYKMSFSSSXQLAKQQQLEQASPQVEIRDGQADGQEPGMKIPPARSPSQLAPPAQLRKTASVRDDPAGLAKRRSRLQEIRAASSSAGGGGGGGEAAAAFTKRESKRDRRRGGGGGAGAAAAAAAGSGSSGSGSQSPTMRKSHSLDAAESYTLASIQAPLWVTLTNARTIDELAQQKM
Protein: Dimethylsulfoniopropionate lyase DddP (DMSP lyase) (EC 4.4.1.3) (A3SK19)
Organism: Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM)
Function: Able to cleave dimethylsulfonioproprionate (DMSP), releasing dimethyl sulfide (DMS). DMS is the principal form by which sulfur is transported from oceans to the atmosphere. The real activity of the protein is however subject to debate and it is unclear whether it constitutes a real dimethylsulfonioproprionate lyase in vivo: the low activity with DMSP as substrate suggests that DMSP is not its native substrate.
Interaction partners:
- Sel1 repeat family protein
Sequence:
MNQHYSETRKIDPSRGATLGDNTPNDNNRIEIGPTQLAFGEWATAGLALPDLQRMREFRWNRLTQAVVDRDYGGVLMFDPLNIRYATDSTNMQLWNAHNPFRALLVCADGYMVIWDYKNSPFLSTFNPLVREQRFGADLFYFDRGDKVDVAADAFSNEVRTLIAEHGGGNMRLAVDKIMLHGLRALEAQGFEIMEGEELTEKTRAIKGPDEILAMRCAVHACETSVAAMEHFAREAVPQGNTSEDDVWAVLHAENIKRGGEWIETRLLASGPRTNPWFQECGPRIIQNNEIISFDTDLIGSYGICVDISRSWWVGDAAPPADMVYAMQHAHEHIMTNMEMLKPGVTIPELSERSHRLDEQFQAQKYGCLMHGVGLCDEWPLVAYPDQAVPGSYDYPLEPGMVLCVEAAVGAVGGNFTIKLEDQVLITETGYENLTSYPFDPALMGR
Protein: ATP synthase F(1) complex subunit delta, mitochondrial (ATP synthase F1 subunit delta) (F-ATPase delta subunit) (Q9D3D9)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
Sequence:
MLPASLLRHPGLRRLMLQARTYAEAAAAPAPAAGPGQMSFTFASPTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE
Protein: Conserved oligomeric Golgi complex subunit 8 (COG complex subunit 8) (Component of oligomeric Golgi complex 8) (Q96WW5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for normal Golgi function.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 5
- t-SNARE affecting a late Golgi compartment protein 2
- Vacuolar protein sorting-associated protein 53
- Vacuolar protein sorting-associated protein 52
- Vacuolar protein sorting-associated protein 54
Sequence:
MDSIGDNVTEMDAFVRDLTMKPYAELEKRKAELHAQKLKLVQKRQQLLRDNYNVLVDYARNQDAFYQLLENSRHDFKELVLHTNQLYEPVKRSQNFLTSISEHYRDAKLMHQVQPQLSSILELPELMNACIERNYFSETLEFQALAYRLKDRFGTNSIIQELITQVETLVVKLTEKLILQLQKPLKLYSLIKVVTYLRVTAKLSEAQLKYVFLYFSWKQLQTSLRNLVPLLDYNNPELYLRRYIQVIRDRAFSLLFQYQSVFGESSNDRLNAAGTVDIPNSTSTSASPFEMDPEGFNNFGQNILSSFVRKLQLEICYVLQKFMPNVKDSTSKFSLLLQLYYCNQSLTKVGTDISIPLSKILGSEWLEMIHSQSSEKQA
Protein: Thyroid hormone-inducible hepatic protein (Spot 14 protein) (S14) (SPOT14) (Q92748)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of lipogenesis, especially in lactating mammary gland. Important for the biosynthesis of triglycerides with medium-length fatty acid chains. May modulate lipogenesis by interacting with MID1IP1 and preventing its interaction with ACACA (By similarity). May function as transcriptional coactivator. May modulate the transcription factor activity of THRB.
Subcellular location: Nucleus {ECO:0000269|PubMed:18299245}. Cytoplasm {ECO:0000269|PubMed:18299245}.
Interaction partners:
- Mid1-interacting protein 1
- Fatty acid synthase
- Acetyl-CoA carboxylase 1
- Very long chain fatty acid elongase 6
- Perilipin-1
- ATP-citrate synthase
Sequence:
MQVLTKRYPKNCLLTVMDRYAAEVHNMEQVVMIPSLLRDVQLSGPGGQAQAEAPDLYTYFTMLKAICVDVDHGLLPREEWQAKVAGSEENGTAETEEVEDESASGELDLEAQFHLHFSSLHHILMHLTEKAQEVTRKYQEMTGQVW
Protein: Sodium channel and clathrin linker 1 (Clathrin-associated protein 1A) (CAP-1A) (Sodium channel Nav1.8-binding protein) (Sodium channel-associated protein 1) (Q8CJ99)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein that links SCN10A to clathrin. Regulates SCN10A channel activity, possibly by promoting channel internalization.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Localizes to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. {ECO:0000250}.
Interaction partners:
- Centrosomal protein of 83 kDa
- Fas binding factor 1
- Centrosomal protein 89
- Centrosomal protein of 164 kDa
- Sodium channel protein type 10 subunit alpha
- Clathrin heavy chain 1
- Synergin gamma
- Leucine-rich repeat neuronal protein 3
- Clathrin light chain B
- Clathrin light chain A
Sequence:
MATEIDLLRDQNVKLNDILRQHQIEHIFRDPAMQNSMSKGGRGDTLTNSVNDQSALPPLIAEYEKHLEELNRQLTYYQKHMGEMKLQLETVITENERLHSKLKDAVEKQLEALPFGTGIGNDICADDETVRNLQEQLQIANQEKNWAVQLWQTASQELESVQKLYQEHMTEAQIHVFENRKQKDQLNNFQQLTKKLHVANENIEMTNHHFLKTVTEQNMEIEKLRKQLRQAKLDLRVAVTKVEELTKVTEGLQEQMLKKEEDIMSAQGKEEASDRRVQQLQSSIKQLESRLCIAIQEANVLKTGKTQLEKQIKELQAKCSESENEKYEAISRARDSMQLLEEANIKQNQILLEEKQKEVEREKMKKTISHLIQDAAIKARKEVESTKKQYEVLILQLKEELSALQMDCDEKQGQIDRAIRGKRAVEEELEKIYREGKQDEGDYRKLEEMHQRCLAAERSKDDLQLRLKTAENRIKQLEINSSEEISRSHEMIQKLQTVLESERENCGFVSEQRLKLQQENEQLQKETEDLRKVALEAQKKAKLKVSTMEHQFSIKEHGFEVQLREMEDSNRNSIVELRHLLAAQQKTANRWKEETKKLTESAEMRISSLKSELSRQKLHTQELLSQLEMANEKVAENEKLILEHQEKANRLQRRLSQAEERAASASQQLSVITVQRRKAASMMNLENI
Protein: ATP-dependent 6-phosphofructokinase 5, chloroplastic (ATP-PFK 5) (Phosphofructokinase 5) (EC 2.7.1.11) (Phosphohexokinase 5) (Q8VYN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17485088}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Aldolase-type TIM barrel family protein
- transaldolase
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- Hexokinase-like 1 protein
- Hexokinase-3
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
- Mannose-6-phosphate isomerase 1
Sequence:
MDALSQAISSGISVPYKNNSSSLVPSHGLTSLILRKSRSPVNPSSRSRVSVRASEIQHSKTSASSIDLSDPDWKLKYEKDFEQRFSIPHITDVLPDAEAIRSTFCLKMRSPTEDFVGGYPSDEEWHGYINNNDRVLLKVISYSSPTSAGAECLDHDCSWVEQWIHRAGPREKIYFRPEEVKAAIITCGGLCPGLNDVIRHIVITLEIYGVKNIVGIPFGYRGFSDKDLTEMPLSRKVVQNIHLSGGSLLGVSRGGPSVSEIVDSMEERGINMLFVLGGNGTHAGANAIHNECRKRKIKVAVVGVPKTIDNDILHMDKTFGFDTAVEEAQRAINSAYIEAHSAYHGIGVVKLMGRNSGFIAMQASLASGQVDICLIPEVPFNLHGPNGVLKHLKYLIETKGSAVICVAEGAGQNFLEKTNAKDASGNAVLGDFGVYIQQETKKYFKEISTPIDVKYIDPTYMIRAVRANASDGILCTVLGQNAVHGAFAGYSGITVGIINTHYAYLPITEVIAYPKSVDPNSRMWHRCLTSTGQPDFI
Protein: Zinc finger PHD-type domain-containing protein (A0A178VXH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAKTLDLFWHEHPLYEKYRMFTCQECHRSAIPFFEVFYGCFRCNIKWHPYCVPRSTKNINHPCHPNHPLEVLLQGPPSYSDEKCSLCQRKLSNFVYHCKLCNFSIDMECGNRPPPHKVDHPKCHEHALTLMGREVSFTCNACGTHGERNPYVCLPCSVMFHYDCIDLPHVININRHDHRISHSYPLKRGNWVCEICRQDINTTYGGYSCNKCPDFFVHSKCATRKDVWDGTELEGIPEEVVDVAPFEVIEEGVIYHFSHEKHNLFLIEDVFIDGAEDMHCEACARPVSSEKHYKCVECKFILHEECANLPLTKRHGLSTGIFYLRFGKDFSEQNFSCDACNRDGRGFSYKDEEGVVLDVLCASLSFFKHPKLHPHTLFLTTIDRGTCLACGENKLNVLRCVDCDYSLDYKCATLPLVIKHRCDTHYLVLRSGEEAPEGKYWCEICEAETNPERWFYTCDDCGVVCHIECVTGDFLNIKPGIIMKNRENKFEVGFNDHDSRPKCTDCGSRCRFPRFFKVTRKNIEYYYCSKACFQNAKF
Protein: Purine nucleoside phosphorylase DeoD-type (PNP) (EC 2.4.2.1) (P0ABP8)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Acts on 6-amino and 6-oxopurines including deoxyinosine, deoxyguanosine, deoxyadenosine, adenosine, guanosine, and inosine. Does not act on xanthosine (Probable). May also catalyze a phosphate-dependent transfer of the pentose moiety from one purine base to another.
Interaction partners:
- Phosphopentomutase
- Thymidine phosphorylase
- Purine nucleoside phosphorylase 2
- Adenine phosphoribosyltransferase
- Adenosine deaminase
- Deoxyribose-phosphate aldolase
- Thymidine kinase
- Xanthine-guanine phosphoribosyltransferase
- Uridine phosphorylase
- Cytidine deaminase
Sequence:
MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE
Protein: Transmembrane protein 237B (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog B) (Q66IE4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250}. Note=Localizes to the transition zone. {ECO:0000250}.
Interaction partners:
Sequence:
MDPEAKVSSSRRRDLPPIPQGQRRTPRALPSMPSQDTAEEMPAPKSRKKKAKRDAESVDEPDDGGMEMGGLASRRQSECPEPLTPEPLDNPPQRRKKKKKAQAIDAEGDQTDLVSNGDTLDQNTDEEVTRKPKKRKVKPKVTETQSNNELDVEDDDVITDPQSPIPQHSLFSAPQGPSQPVGKVFVEKSRRFQAADRVEQWKPSGPIEQSIMDIRSMWTTRDVSMRVHSGFRVIGLFSHGFLAGYAVWNIIVVYVLAGDQMSSLSNLLQQFHTLAYPAQSLLYLLLALSTVSAFDRVNLAKAPAAMRSLLRLSPVALASVFYFSALVLSLSQQMTSDRINLYKYSSYNTTLWPPGSESSILYPWITVNLVVSLLVGLAWILMSTSPDIDNTEAFLMSMEMEYPNSEEKGNVTA
Protein: GDP-mannose transporter 1 (GMT 1) (Low dye-binding protein 3) (Morphogenesis checkpoint-dependent protein 3) (Vanadate resistance glycosylation protein 4) (P40107)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. Defective copy causes severe glycosylation defect and abnormal retention of soluble endoplasmic reticulum proteins. Involved in vanadate sensitivity.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Recycles between the Golgi apparatus and the endoplasmic reticulum.
Interaction partners:
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
- Mannan polymerase I complex VAN1 subunit
- GDP-Man:Man
- Mannan polymerase complexes subunit MNN9
- UDP-N-acetylglucosamine transporter YEA4
Sequence:
MSELKTGHAGHNPWASVANSGPISILSYCGSSILMTVTNKFVVNLKDFNMNFVMLFVQSLVCTITLIILRILGYAKFRSLNKTDAKNWFPISFLLVLMIYTSSKALQYLAVPIYTIFKNLTIILIAYGEVLFFGGSVTSMELSSFLLMVLSSVVATWGDQQAVAAKAASLAEGAAGAVASFNPGYFWMFTNCITSALFVLIMRKRIKLTNFKDFDTMFYNNVLALPILLLFSFCVEDWSSVNLTNNFSNDSLTAMIISGVASVGISYCSGWCVRVTSSTTYSMVGALNKLPIALSGLIFFDAPRNFLSILSIFIGFLSGIIYAVAKQKKQQAQPLRK
Protein: Amino acid transporter AVT1A (AtAvt1A) (O80668)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Endochitinase EP3
- Transcription initiation factor IIB-1
Sequence:
MEDKNNDKEKKTDVTFEDDEDNEDLEDNSSKYENDSETDQSDLGDLPGDAVDRDDDIDEPFISQVQWPQSFRETTDSYTIAASPIFGSLRSNPPSFYRASRSNLDVESKAPLLPERHDDSDKASATQSAWSHKGSFAEELPIGGYGCSVIQTIFNAINVMAGVGLLSTPYTVKEAGWASMVILLLFAVICCYTATLMKDCFENKTGIITYPDIGEAAFGKYGRILICMLLYTELYSYCVEFIILEGDNLTGLFPGTSLDLLGFRLDSKHLFGILTALIVLPTVWLKDLRIISYLSAGGVIATALIAVSVFFLGTTGGIGFHHTGQAVKWNGIPFAIGIYGFCYSGHSVFPNIYQSMADKTKFNKAVITCFIICVLLYGGVAIMGYLMFGEATLSQITLNMPQDQFFSKVAQWTTVVSPFTKYALLMNPLARSIEELLPERMSENIWCFLLLRTALVASSVCSAFLIPFFGLMMALIGSLLSILVAIIMPALCFIKIMGNKATRTQMILSSIIVAIGVVSGTLGTYSSVAKIIRNYQ
Protein: LIM domain protein (G5EDJ5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRAMVRGMVGRGKKKEKNGGVPPSVPSSASQPPPSTTKHAKILPSFSCSPPMERKDSRPTLITANTADHSVGSPPARRQPPKRVGSGKSASNGPSGVVRTDLAVKVCVHCKSDRSDHELPPNQALNVYNRLGIQPPAGMPQSGVAEPEVPGSVGHGYAWVPPGLSRKKVEEYMSQLPNNVVPRTNSNGEKLREKQLLLQLPRQDLSVAYCRHLTSQTERKVYEEFVNARNEIALDIGYVSSNINKAMECHKCSGILETNEMAVIAPKLGDSTGWHPACFTCQACEQLLVDLTYCVKDNQIYCERHYAELHKPRCSACDELIFAGEYTKAMNKDWHSDHFCCWQCDQTLTGQRYIMRDEQPYCIKCYEDVFANQCDECAKPIGIDSKDLSYKDKHWHEHCFLCSMCKISLVDMPFGSKNDRIFCSNCYDQAFATRCDGCNEIFRAGMKKMEYKGKQWHDKCFCCAHCKLAIGTKSFIPKNDDVFCGPCYEEKFATRCSKCKKVITAGGVTYKNEPWHRECFCCTNCNSSLAGQRFTSKDEKPYCANCYGDLFAKRCNACTKPITGIGGAKFISFEDRHWHNDCFICAQCTTSLVGKGFITDGHEILCPECAKARLMAANS
Protein: Putative ADP ribosylation factor 3 (E9ADU4)
Organism: Leishmania major
Interaction partners:
- C2 domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Integral membrane protein
- PB1 domain-containing protein
- Proteophosphoglycan ppg4
- GMP phosphodiesterase delta subunit domain-containing protein
- C-CAP/cofactor C-like domain-containing protein
- Uncharacterized protein
- Uncharacterized protein L8530.02
Sequence:
MGLLTLLRKLKKSETEPRMLILGLDNAGKTSILRKLSDEDPTTTQATQGFNIKSINCEGFKLNMWDIGGQKAIRTYWPNYYDEVDCLIYVVDAADRRRLEETATELDTLLQEEKLREAPVLIFSNKCDLATALSPESVSTALNLHSLRDRTWSIQKCSAKTGEGLHEGLEWAVKSLKPK
Protein: Opt4p (Q59LT5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNYDQMWDACTSFWRVIKDFRKSTYDGFDDPHSTMMRAYPEVPEWAYLIIVVISLVLAILCVKLYPAQTPVWGIFFALGINFVFLIPLTTIYARTGFAFGLNVLVELIVGYAIPGNGLALAFIKALGYNIDAQAQNFVNDLKQGHYAKLPPRAVYRVQLLSIFVSSFIQLGILNFQINGIKDYCKPGNTQKFTCPGGRTFFSASVLWGVIGPKKVFNGLYPVLAWCFLIGFLLAFPCIAIKKYAPRKYVKYFEPSIVIGGFLKYAPYNLSYYIPGVYVSYAFMSYIKRKYEAWWQKYTYVLSTGLNAGIAFSSIIIFFAVMYHEKDINWWGNTVMYSGVDYAMTGWLNATVDAPDGYFGPRRGNFP