wanglab/gogpt-training-data huggingface dataset:
Protein: Fluoren-9-ol dehydrogenase (EC 1.1.1.256) (1,1a-dihydroxy-1-hydro-9-fluorenone dehydrogenase) (DHF dehydrogenase) (Q93UV4)
Organism: Terrabacter sp. (strain DBF63)
Function: Catalyzes the dehydrogenation of both 9-fluorenol and 1,1a-dihydroxy-1-hydro-9-fluorenone to produce 9-fluorenone and 2'-carboxy-2,3- dihydroxybiphenyl, respectively.
Interaction partners:
Sequence:
MSESGGGTVATARQRQLVERALGEWQGEVAGRVIVVTGGARGIGRSLCEGLLRAGAKVVAADLTWDDADDFRKQLESDGSGMAVDMDITDDDALDAARDAVIDRFGTVDVLVNNASLVSETLFPPTGHRNTLDTTDRDWEVMFGVNVFGTLKAIRRFIEPMRAQQRGSIVNVVSSGVLAVAAGGGYHGLRPWTVEMPYQATKAAVMALTFYLAEEVRGDGVAVNAIMPGHTRASWFDATARAFNEQGIAYFMRPAIPEHLLPISLFLAAQDSAGASGRLYYVPEWNYDHGYGDYAAWQDHELPPDMEEIYSRLEAATPSYERAGVAHLPFDAQGALYAAGMANLGAQNSWTSNDSAQ
Protein: Uncharacterized RNA-binding protein C902.04 (Q9USP9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Zinc finger CCCH domain-containing protein C337.12
- NURS complex subunit red1
- Polyadenylate-binding protein 2
- Uncharacterized helicase C17H9.02
- Uncharacterized protein C7D4.14c
- RNA binding exosome specificity factor Mmi1
- Poly
- NURS complex subunit pir2
- Rpb7-binding protein seb1
- Uncharacterized protein C4G9.04c
Sequence:
MPLFLEEHAEYLKRYLEQALEPISDADASVLSDYAMALLRHDSSEEEVRQLCYSQLEDFLRQETIPFVDKIFDVLREKSYLEGASNMPSTGMVTEEVSRYSPTSSMIPATNSMETNFNNSLPAVGKTNTFPSQVPNMFGPPLYHPAATAPSEFMPSIPGFGNLPNPAMPPIPFLPFNPAAQPPFPPPFKMRGKRGFGMRHEHNSELRRHSPGNRRFNPYKAYPQPHLGHRFSRNAGNDPTSTALEVRNIPEEHFNEENIRSFFSKFGVLEKVELNPTHHSCVLEFTSHEAANNAWSSPEPIFNNRFIKIFWYNPSKGFHNRPKKFASHKSPTTSDSSNVESSEDVDPASLLQNEEFHKLIEERQRQHEERLKRINANKKALEELNQKKRELAQQQLKEQELLMQKIKETDRSGNKRLMLLETQHSLLKAEADCLGLPVSNVSESPAASNGSHHPYASGLPQRGTNTFFRGRGRGRGDMFASMSIDNRPTKLRVINVSPEKNEALLQYLFTVGGYEEITEPSTTERLISFQNRNSAEKFFGGVRNVEKLQELELAWVPKTAVTTNTTSMETGESNTSDNMNIEVEEGRWR
Protein: Synaptic vesicular amine transporter (Monoamine transporter) (Solute carrier family 18 member 2) (Vesicular amine transporter 2) (VAT2) (Vesicular monoamine transporter 2) (Q01827)
Organism: Rattus norvegicus (Rat)
Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior to their release via exocytosis. Transports a variety of catecholamines such as dopamine, adrenaline and noradrenaline, histamine, and indolamines such as serotonin. Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates somatodendritic dopamine release in hippocampal neurons, likely as part of a regulated secretory pathway that integrates retrograde synaptic signals. Acts as a primary transporter for striatal dopamine loading ensuring impulse-dependent release of dopamine at the synaptic cleft (By similarity). Responsible for histamine and serotonin storage and subsequent corelease from mast cell granules (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:16301178}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:16301178}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:16301178}. Cell projection, dendrite {ECO:0000269|PubMed:16301178}. Note=Sorted to large dense core granules in neuroendocrine cells, presumably at the level of the trans-Golgi network. In neurons it is predominantly detected in somatodendritic tubulovesicular membranes, a distinct population of secretory vesicles that undergo calcium-dependent exocytosis in axons and dendrites upon depolarization. Localized at synaptic vesicles in axons. {ECO:0000269|PubMed:16301178}.
Interaction partners:
- Alpha-synuclein
- Vesicular inhibitory amino acid transporter
- Vesicular glutamate transporter 2
- Aromatic-L-amino-acid decarboxylase
- Vesicular glutamate transporter 3
- Tyrosine 3-monooxygenase
- Vesicular glutamate transporter 1
- Vesicular acetylcholine transporter
- Sodium-dependent serotonin transporter
- Sodium-dependent dopamine transporter
Sequence:
MALSDLVLLRWLRDSRHSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNSTEIQTTRPELVVSTSESIFSYYNNSTVLITGNATGTLPGGQSHKATSTQHTVANTTVPSDCPSEDRDLLNENVQVGLLFASKATVQLLTNPFIGLLTNRIGYPIPMFAGFCIMFISTVMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGKPMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMVIVGISILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDIAFAPLCFFLRSPPAKEEKMAILMDHNCPIKRKMYTQNNVQSYPIGDDEESESD
Protein: Sulfotransferase 1A2 (ST1A2) (EC 2.8.2.1) (Aryl sulfotransferase 2) (Phenol sulfotransferase 2) (Phenol-sulfating phenol sulfotransferase 2) (P-PST 2) (P50226)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Is also responsible for the sulfonation and activation of minoxidil. Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.
Subcellular location: Cytoplasm.
Interaction partners:
- Sulfotransferase 1A1
- Sulfotransferase 1A3
- Sulfotransferase 4A1
- Sulfotransferase 1C2
- Aspartate aminotransferase, cytoplasmic
Sequence:
MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAKKMAGCSLSFRSEL
Protein: Electron transfer flavoprotein subunit alpha (Alpha-ETF) (Q384Q2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|PIRNR:PIRNR000089}.
Interaction partners:
- Electron transfer flavoprotein subunit beta
- Electron transfer flavoprotein-ubiquinone oxidoreductase
- Isovaleryl-coA dehydrogenase, putative
- Acyl-CoA dehydrogenase, mitochondrial, putative
- Acyl-coa dehydrogenase, putative
- Acyl-CoA oxidase C-terminal domain-containing protein
- Cytochrome c
- 2,4-dienoyl-coa reductase-like protein
- Adrenodoxin reductase, putative
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MFRYTAAFFGKVLVLAETHQNSIFPGTLAAVTAGLQLGEVTTLIAGETPATAAAQLSKVKGVSQVFIASGIHYEHGLPEEYAPLVASLVQLGGYTHVLAATSAFGKGIIPRAAALCDVMPISEVSEVKDESTFVRYMYAGGVVSTVRSTDPVKFATIRSTSFERAPLEGGNALQQEVEVTPVVGTSKWLEDASVNNDAPDIQTAATVIAGGRGLKSGENFKLLHDLAKPLHAAVGATRAAVDAGYCSNDLQIGQTGKTVAPNLYVGCGVSGAIQHVAGLKDAKVIAVINNDAEAPFFQVADYGLVEDLFVAVPKLTELVTKSRK
Protein: Zinc finger CCCH domain-containing protein 7A (Q8IWR0)
Organism: Homo sapiens (Human)
Function: May be a specific regulator of miRNA biogenesis. Binds to microRNAs MIR7-1, MIR16-2 and MIR29A hairpins recognizing the 3'-ATA(A/T)-5' motif in the apical loop.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSNVSEERRKRQQNIKEGLQFIQSPLSYPGTQEQYAVYLRALVRNLFNEGNDVYREHDWNNSISQYTEALNIADYAKSEEILIPKEIIEKLYINRIACYSNMGFHDKVLEDCNIVLSLNASNCKALYRKSKALSDLGRYKKAYDAVAKCSLAVPQDEHVIKLTQELAQKLGFKIRKAYVRAELSLKSVPGDGATKALNHSVEDIEPDLLTPRQEAVPVVSLPAPSFSHEVGSELASVPVMPLTSILPLQVEESALPSAVLANGGKMPFTMPEAFLDDGDMVLGDELDDLLDSAPETNETVMPSALVRGPLQTASVSPSMPFSASLLGTLPIGARYAPPPSFSEFYPPLTSSLEDFCSSLNSFSMSESKRDLSTSTSREGTPLNNSNSSLLLMNGPGSLFASENFLGISSQPRNDFGNFFGSAVTKPSSSVTPRHPLEGTHELRQACQICFVKSGPKLMDFTYHANIDHKCKKDILIGRIKNVEDKSWKKIRPRPTKTNYEGPYYICKDVAAEEECRYSGHCTFAYCQEEIDVWTLERKGAFSREAFFGGNGKINLTVFKLLQEHLGEFIFLCEKCFDHKPRMISKRNKDNSTACSHPVTKHEFEDNKCLVHILRETTVKYSKIRSFHGQCQLDLCRHEVRYGCLREDECFYAHSLVELKVWIMQNETGISHDAIAQESKRYWQNLEANVPGAQVLGNQIMPGFLNMKIKFVCAQCLRNGQVIEPDKNRKYCSAKARHSWTKDRRAMRVMSIERKKWMNIRPLPTKKQMPLQFDLCNHIASGKKCQYVGNCSFAHSPEEREVWTYMKENGIQDMEQFYELWLKSQKNEKSEDIASQSNKENGKQIHMPTDYAEVTVDFHCWMCGKNCNSEKQWQGHISSEKHKEKVFHTEDDQYCWQHRFPTGYFSICDRYMNGTCPEGNSCKFAHGNAELHEWEERRDALKMKLNKARKDHLIGPNDNDFGKYSFLFKDLN
Protein: DNA-directed RNA polymerase subunit beta (RNAP subunit beta) (EC 2.7.7.6) (RNA polymerase subunit beta) (Transcriptase subunit beta) (Q727C7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL12
- Small ribosomal subunit protein uS17
- DNA-directed RNA polymerase subunit omega
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS8
Sequence:
MGQLTKKFGKIDVSLPIPHLLNLQVDSYVKFLQEGATERRHDEGLEGVFRSVFPIEDFNRTASLEFVSYEVGEPKYDQPECISKGLTYEAPIRIKVRLVVYDVDEDSGNRTIRDIKEQEIYFGTLPLMTEKGTFIINGTERVIVNQLQRSPGIIFEHDSGKTHSSRKVLYSCRIIPMRGSWLDFDFDHKDILYVRIDRRRKMPATILFKAMGMSKTDILDYFYKKEFYRLDPMGRLMWEVQKDMYRKDSAFVDIEDGKGGTIVKAGKPITKRAWRLISEAGLETIEVAPDTIEGMFLAEDIVNPATGEVLAEAADEITASLVENLREAGISRLPVLHTKGLETSSSLRDTLVLDKTPDMEAAQVEIYRRLRPSSPPTPEIAASFFDNLFRSADYYDLSPVGRYKLNQRLGIDQSVDLRTLTDDDILRAIRVLLHLKDSHGPADDIDHLGNRRVRPVGELVENQYRIGLVRMERAIKERMSLQEVSTLMPHDLINPKPVAAVLKEFFGTSQLSQFMDQTNALSEVTHKRRLSALGPGGLTRERAGFEVRDVHTSHYGRICPIETPEGPNIGLIVSLTTYAKVNDFGFIETPYRIIREGALTDEIKFLDASREQGEVVAQANAAVDADGKLADEYVTARVRGDVLMSHRDEVTLMDISPSQMVSISAALIPFLEHDDANRALMGSNMQRQAVPLLRSEKPIVGTGMEGDVARDSGACILAEGPGIVRYADATRIIVSYENGLYPDRGGVRAYDLQKYHKSNQNSCFGQRPTCHPGQIVKKGDVLADGPGIEDGELALGKNLVVAFMPWCGYNFEDSILISERVVKEDVFTSIHIEEFEVVARDTKLGPEEITRDIPNVGEDMLRNLDGSGIIRIGASVKPDDILVGKITPKGETQLTPEEKLLRAIFGDKARDVKNTSLKVPPGIEGTIIDVKVFNRRSGEKDERTRNIEDYETARIDKKEQDHVRALGDALRDRLADTLVGKQIAVTLPGKRKGEVLAEAGAPMTRELLDALPVKRLAGLFKSREVDEMVDTALEDYDRQVAFLKGIYDSKREKVTEGDDLPPGVIKMVKVHIAVKRKLNVGDKMAGRHGNKGVVSCILPEEDMPFFADGRPVDIVLNPLGVPSRMNIGQIMETHLGWGAKELGRQLAEMLDSGAAMATLRHEVKDVFRSATIAKLVDEMDDETFRKAVSKLRTGIVTKTPVFDGASEEDIWSWIERAGMDGDGKTVLYDGRTGDKFYNRVTTGVMYILKLHHLVDEKIHARSTGPYSLVTQQPLGGKAQFGGQRLGEMEVWALEAYGASYLLQEFLTVKSDDVTGRVKMYEKIVKGDNFLEAGLPESFNVLVKELMSLGLNVTLHQEEGKKRPKRVGFMSAL
Protein: Mitoguardin 1 (Protein FAM73A) (Q8NAN2)
Organism: Homo sapiens (Human)
Function: Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:26711011}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitoguardin 2
- Nexilin
Sequence:
MSDCCSAPGISWEAGVGRPAVPGLELQIRRGAMSEETVSESQFSLKTAALRVFDLPLTWYYSLSQIKFSPVAKKLFVVTAVSAISVIFLAHHFKRKRGKKKGKILPWEPEHLILEYTKRAASDKGSSCSSSRQNLTLSLSSTKDKGSQVCNYANGGLFSKYSGSAQSLASVQSVNSCHSCACGNSNSWDKADEDDIKLVNIPVTTPENLYLMGMELFEEALRRWEQALTFRNRQAEDEACGSIKLGAGDAIAEENVDDIISTEFIHKLEALLQRAYRLQEEFEATLGASDPNSLADDIDKDTDITMKGNVEDFGLRDTLSIASTDSFASAAELAEHREVRHTYSLESLCHCPFYEEAMHLVEEGKIYSRVLRTEMLECLGDSDFLAKLHCIRQAFQVILSESANRIFLAESGRKILSALIVKARKNPKKFEDVFDEMIYFLEQTDHWGSTEMELAARGVKNLNFYDVVLDFILMDSFEDLENPPTSIQNVVNNRWLNSSFKETAVASSCWSVLKQKRQQMKIPDGFFAHFYAICEHISPVLAWGFLGPRNSLYDLCCFFKNQVLLFLKDIFDFEKVRYSSTETLAEDLMQLLIRRTELLMAYLEADALRHTSSCLSSHGHVMSTGLLEAKVQ
Protein: Serine and arginine rich splicing factor 10 (A0A8I6AMK7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNSRPTGRPRRSRSHSDNDRPNCSWNTQYSSAYYTSRKI
Protein: poly(A)-specific ribonuclease (EC 3.1.13.4) (Carbon catabolite repressor protein 4) (Cytoplasmic deadenylase) (Glucose-repressible alcohol dehydrogenase transcriptional effector) (Q8IMX1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- poly
- CCR4-NOT transcription complex subunit 9
- Not1, isoform H
- Protein associated with topo II related - 1, isoform A
- CCR4-NOT transcription complex subunit 3
- Regulator of gene activity
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 4
- CCR4-NOT transcription complex subunit 10
- ATP-dependent RNA helicase me31b
Sequence:
MCIFKKRDAYHQAVIMKGNHYKMSRNKDKYDSANRRQQIFLSQEDIAAGKKTNWSGLEITGCVRNISPSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPYEIGKLFHLVILGLMGNPLQKEFMNIYNEPNGTQKLLTYMLDNLSFTVNPPPQRPWLPLAKPNKTRPACIFTVMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAKTMSELERKYVDGCAIFFRASKFTLIKESLIEFNQLAMANAEGSDNMLNRVMPKDNIGLAALLKVKENAWEPMSEVTQISQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDEASHSFRPGHKNDSNAVQLLLCGDFNSLPDSGVVEFLGKGRVSMDHLDFKDMGYKSCLQRLLSNDTNEFTHSFKLASAYNEDIMPHTNYTFDFKGIIDYIFYTKTGMVPLGLLGPVSNDWLRENKVVGCPHPHIPSDHFPLLVELELMHTASQQAPPNGLINRR
Protein: Uncharacterized WD repeat-containing protein C824.04 (Q9UT39)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase ssu72
- Cleavage and termination factor 1
- Serine/threonine-protein phosphatase PP1-1
- Cleavage factor two protein 2
- Protein cft1
- Polyadenylation factor subunit 2
- mRNA 3'-end-processing protein yth1
- Pre-mRNA polyadenylation factor fip1
- mRNA cleavage and polyadenylation specificity factor complex subunit pta1
- Endoribonuclease ysh1
Sequence:
MDIGILSSLKPAQSFRDNSLGSFINSIDYSDSGEYVATTCSADDTVQIYDALDPKQVHTITCFETGIEVARFTHHDHNLLLSTTKGNKDIQYVSIYDNKRISYFSGHTDIVSSIEVSPIEDQFVSTANDKTLKLWKMNQSSRCLGNLDLPSLGIPAYDPTGLVFAVACHSLSRIFLYDVRNYGSDPFSTFTIDDSRYLSRFSFPPMMPEWKHMEFSNDGKCILLSTRANVHYILDAFSGDVLSRLEDFQELPFSNNFHGGSTTFVPQGNFVIGSADDRTLNVWNLRHTFHHKGKTRPPEHRIVSQSIINPGLVKYNPRYDQLLTAGSQLVFWLPEKYALTS
Protein: ATP-dependent Clp protease ATP-binding subunit ClpC1 (P9WPC9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit 1
- ATP-dependent Clp protease proteolytic subunit 2
- ATP-dependent Clp protease adapter protein ClpS
- Aspartate 1-decarboxylase
- Protein GrpE
- Chaperone protein DnaK
- Small ribosomal subunit protein bS1
- Conserved hypothetical proline and threonine rich protein
- Hypothetical alanine and valine rich protein
- Conserved hypothetical proline rich protein
Sequence:
MFERFTDRARRVVVLAQEEARMLNHNYIGTEHILLGLIHEGEGVAAKSLESLGISLEGVRSQVEEIIGQGQQAPSGHIPFTPRAKKVLELSLREALQLGHNYIGTEHILLGLIREGEGVAAQVLVKLGAELTRVRQQVIQLLSGYQGKEAAEAGTGGRGGESGSPSTSLVLDQFGRNLTAAAMEGKLDPVIGREKEIERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGEVPETLKDKQLYTLDLGSLVAGSRYRGDFEERLKKVLKEINTRGDIILFIDELHTLVGAGAAEGAIDAASILKPKLARGELQTIGATTLDEYRKYIEKDAALERRFQPVQVGEPTVEHTIEILKGLRDRYEAHHRVSITDAAMVAAATLADRYINDRFLPDKAIDLIDEAGARMRIRRMTAPPDLREFDEKIAEARREKESAIDAQDFEKAASLRDREKTLVAQRAEREKQWRSGDLDVVAEVDDEQIAEVLGNWTGIPVFKLTEAETTRLLRMEEELHKRIIGQEDAVKAVSKAIRRTRAGLKDPKRPSGSFIFAGPSGVGKTELSKALANFLFGDDDALIQIDMGEFHDRFTASRLFGAPPGYVGYEEGGQLTEKVRRKPFSVVLFDEIEKAHQEIYNSLLQVLEDGRLTDGQGRTVDFKNTVLIFTSNLGTSDISKPVGLGFSKGGGENDYERMKQKVNDELKKHFRPEFLNRIDDIIVFHQLTREEIIRMVDLMISRVAGQLKSKDMALVLTDAAKALLAKRGFDPVLGARPLRRTIQREIEDQLSEKILFEEVGPGQVVTVDVDNWDGEGPGEDAVFTFTGTRKPPAEPDLAKAGAHSAGGPEPAAR
Protein: Interleukin-6 (H9A0J9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Gp130 protein
- Transcription factor p65
- Interleukin family protein
- Interleukin 6 receptor.
- Nuclear factor NF-kappa-B p105 subunit isoform X1
- Transcription factor Jun
- Lymphotoxin-alpha
- Colony-stimulating factor 3
- Signal transducer and activator of transcription
- Interleukin-1.
Sequence:
MPSAQKTVLFLSATLATLFMSLADPVPVFSSMGELSEISGDEVQDVDVKSLLGDRQKWHLMARDLYKDVKTLRDEQFERDFREMVNMTAFEGVRISTPLLKPSDRCLSKNFSTERCLTRIYSVLTWYKDNWNYIEKENLTSVLVNDIKHSTKRLLEAINSQLQVRDGEMDQTSSTSLSFKSAWTRKTTVHSILFNFSSVMIDACRAINYMSRRKRGKDPKRTGDWGSADKN
Protein: Disrupted in schizophrenia 1 (B8PWL7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MMFAGMVRVENTSKTLKTDIDSPCHRCAVRTGGVNPSGNHRRRSFRRPGYMRSEPINQLDVAETSCDSEHHRSPISKSPAVENTQKSASELLGEKWLTEGFERDNSSKSSNKHHLHDEEDNLPVQSRDVFNSSFSFIQQSLDTSDLLDVNTCYSPRTEHKQSESASGHQLKSKTSNSGFLKPPSDLMNHLSQSETSIVQMNQLETRTVPVSQSKSSFLKPLSALMNHLSQSETTSVPINQSETSSAPKSQSNSGFLKPLSDLMKHLTPPESSIVLMNQSETITIPMNQTKNSTIPVSQSNADFLNPPSALMNHLNQSETVLIPMNQSETSSIPVSQSNSGFLKPSSNLINHLSQSESVTVPMNQSETSTVSLSQSEPDFFSLRHLPCSIGQSAQQKGLLLDRELWLVDLDLQTSSSIMSKYTKENIQDSDSGSLDAEITSSHSIDSSDSTSSGYESTTPSSDQSQDGLMKKYEDFLQDCLQNNRTNTKIESIMMKLQRLQHKAILDDDYDTAERFGKKLEELRRERATLKPGLPSRHPEVTGYLERLRTAVNSAIHRTDSDCSTGDPSEDQRSCISQSRAQTRETLLEEKQRIQKEMCDVQRRLRDLQERSRALELQLELQEMQGPVLRAADSPHLHLTARALEDLLTSEHRQRISVSPPAHIRRLEEQERVLSLSIREAETKVLLNQRLCFSLRQKVSESETQLLALHEAKLTAVSGNDFSSAKELKAEIRSVYRERDRLELLHRKLQTLSTGSGLDLSRMKEKHKHIKLELQNGEAQYERSLKENTVKYIELLEDKLHSCGSAALEHVLEADLEACHLLLKGLDQRNLSLSQTEDLPSGSASASDVLQFTKDEEDCAMLTALGGRWCPEADLQHSQFTKKLEEFLFCLEDEAPENLCGETTELTERCELISYRLHYLEEQLQTAIDNNDKELTLSLEREVLELKSALQAMLSQLKEEDEDEEDEEKYCDVEEEQVEDEDLEEEHYFSDSWEI
Protein: Gcf1p (Q59QB8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Arp8p
- Non-histone chromosomal protein 6
Sequence:
MLRSFVTSISPIGYNAVSLVSMRALATKAATTTTKKSTTKASPKTKKTTKKSTKPPKVDTKAIRLQKKINEARSAKKNLQQQIKDISTQHKTLSKQRKFEEKARSKIHKLAPGNFYSMFQKKRAGDSVAEFYQFPEEEKAKWIAARDAYWEKAKSYFTPKPKLGANGFAKYVQENYIRGDSLTETMKKLADEWNALSETEKQQYQISKEDKEKYKKALEKWKELRLKEYSDYLKFKENYKVEDDF
Protein: Anti-DNA light chain (Q8VIJ0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
DIVMTQSQTFMSTSVGDRVSVTCKASQNVGTNVAWYQQKPGQSPKALIYSASYPYSGVPHRFTGSGSGTDFTLTISNVQSEDLAEYFCQQYNSYPYTFGGGTKLEIKR
Protein: Tubulin beta chain (Beta-tubulin) (P02557)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23001566}. Note=Colocalizes with kinesin KIP3 at the plus ends of growing microtubules and along the microtubule lattice. {ECO:0000269|PubMed:23001566}.
Interaction partners:
- Dynein heavy chain, cytoplasmic
- Tubulin alpha-3 chain
- Tubulin alpha-1 chain
- Protein STU2
- Tubulin-specific chaperone A
- WD repeat-containing protein PAC11
- Protein BIM1
- Calmodulin
- Kinesin-like protein CIN8
- Actin
Sequence:
MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVSEYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE
Protein: Beta-hexosaminidase 3 (EC 3.2.1.52) (Beta-GlcNAcase 3) (Beta-N-acetylhexosaminidase 3) (Beta-hexosaminidase 1) (AtHEX1) (N-acetyl-beta-glucosaminidase 3) (Q8L7S6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and leaves.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17644627, ECO:0000269|PubMed:21252225}.
Interaction partners:
- Glycoprotein 3-alpha-L-fucosyltransferase A
- Putative fucosyltransferase-like protein
- Alpha-
- Beta-hexosaminidase 2
- Alpha-galactosidase 1
- Alpha-galactosidase 3
- Beta-galactosidase 2
- Alpha-galactosidase 2
- Beta-galactosidase 17
- Beta-hexosaminidase 1
Sequence:
MRGSGAKIAGVLPLFMLFIAGTISAFEDIERLRIWPLPAQVSHGGRRMYLSGDFKLVTEGSKYGDASGILKEGFDRMLGVVRLSHVISGDRNSSGTGGSALLQGLHVIISSSTDELEYGADESYKLVVPSPEKPSYAQLEAKSVYGALHGLQTFSQLCHFNLKKKVIEILMTPWNIIDQPRFSYRGLLIDTSRHYLPLPVIKNVIDSMTYAKLNVLHWHIVDTQSFPLEIPSYPKLWNGAYSSSQRYTFEDAAEIVNYARRRGIHVLAEIDVPGHALSWGKGYPALWPSKNCQEPLDVSSDFTFKVIDGILSDFSKIFKFKFVHLGGDEVNTTCWSATPRIAQWLKKHRMSEKEAYQYFVLRAQKIALSHGYEIINWEETFINFGSKLNRKTVVHNWLNTGLVENVTASGLRCIVSNQEFWYLDHIDAPWQGFYANEPFQNITDKKQQSLVLGGEVCMWGEHIDASDIEQTIWPRAAAAAERLWTPYAKLAKNPNNVTTRLAHFRCLLNQRGVAAAPLVGGGRVVPFEPGSCLAQ
Protein: Basic salivary proline-rich protein 2 (Salivary proline-rich protein) (Con1 glycoprotein) [Cleaved into: Basic proline-rich peptide IB-1; Basic proline-rich peptide P-E (IB-9); Basic proline-rich peptide IB-7; Basic proline-rich peptide IB-8c (Basic peptide P-F); Basic proline-rich peptide IB-4] (P02812)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Basic salivary proline-rich protein 1
- Salivary acidic proline-rich phosphoprotein 1/2
- C4b-binding protein alpha chain
Sequence:
MLLILLSVALLALSSAQNLNEDVSQEESPSLIAGNPQGAPPQGGNKPQGPPSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSRSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDNKSRSSRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDNKSQSARSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGGSKSRSSRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGGSKSRSARSPPGKPQGPPQQEGNNPQGPPPPAGGNPQQPQAPPAGQPQGPPRPPQGGRPSRPPQ
Protein: Protein BNLF2a (P0C739)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Participates in viral evasion from HLA class I-restricted T-cell immunity. Associates with host TAP1 and TAP2 and prevents TAP-mediated peptide transport and subsequent loading.
Subcellular location: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVHVLERALLEQQSSACGLPGSSTETRPSHPCPEDPDVSRLRLLLVVLCVLFGLLCLLLI
Protein: Succinyl-CoA:acetate CoA-transferase (EC 2.8.3.18) (Succinyl-coenzyme A (CoA):acetate CoA-transferase) (SCACT) (B3EY95)
Organism: Acetobacter aceti
Function: Utilizes succinyl-CoA to convert toxic acetate to acetyl-CoA and succinate. Required for growth on acetic acid and for resistance to high levels of acetic acid. Has also low activity with acetoacetate as substrate.
Interaction partners:
Sequence:
MTERIRNVALRSKVCPAETASELIKHGDVVGTSGFTGAGYPKEVPKALAQRMEAAHDRGEKYQISLITGASTGPQLDGELAKANGVYFRSPFNTDATMRNRINAGETEYFDNHLGQVAGRAVQGNYGKFNIALVEATAITEDGGIVPTSSVGNSQTFLNLAEKVIIEVNEWQNPMLEGIHDIWDGNVSGVPTRDIVPIVRADQRVGGPVLRVNPDKIAAIVRTNDRDRNAPFAAPDETAKAIAGYLLDFFGHEVKQNRLPPSLLPLQSGVGNVANAVLEGLKEGPFENLVGYSEVIQDGMLAMLDSGRMRIASASSFSLSPEAAEEINNRMDFFRSKIILRQQDVSNSPGIIRRLGCIAMNGMIEADIYGNVNSTRVMGSKMMNGIGGSGDFARSSYLSIFLSPSTAKGGKISAIVPMAAHVDHIMQDAQIFVTEQGLADLRGLSPVQRAREIISKCAHPDYRPMLQDYFDRALKNSFGKHTPHLLTEALSWHQRFIDTGTMLPS