wanglab/gogpt-training-data huggingface dataset:
Protein: Excitatory amino acid transporter 2 (Glutamate/aspartate transporter II) (Sodium-dependent glutamate/aspartate transporter 2) (Solute carrier family 1 member 2) (P43004)
Organism: Homo sapiens (Human)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Essential for the rapid removal of released glutamate from the synaptic cleft, and for terminating the postsynaptic action of glutamate (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14506254, ECO:0000269|PubMed:15265858, ECO:0000269|PubMed:26690923, ECO:0000269|PubMed:7521911}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Excitatory amino acid transporter 1
- Glial fibrillary acidic protein
- Vesicular glutamate transporter 1
- Glutamine synthetase
- Alpha-synuclein
- Vesicular glutamate transporter 2
- Glutamate receptor ionotropic, NMDA 2A
- ATP-sensitive inward rectifier potassium channel 10
- Vesicular inhibitory amino acid transporter
- Cytosolic 10-formyltetrahydrofolate dehydrogenase
Sequence:
MASTEGANNMPKQVEVRMHDSHLGSEEPKHRHLGLRLCDKLGKNLLLTLTVFGVILGAVCGGLLRLASPIHPDVVMLIAFPGDILMRMLKMLILPLIISSLITGLSGLDAKASGRLGTRAMVYYMSTTIIAAVLGVILVLAIHPGNPKLKKQLGPGKKNDEVSSLDAFLDLIRNLFPENLVQACFQQIQTVTKKVLVAPPPDEEANATSAVVSLLNETVTEVPEETKMVIKKGLEFKDGMNVLGLIGFFIAFGIAMGKMGDQAKLMVDFFNILNEIVMKLVIMIMWYSPLGIACLICGKIIAIKDLEVVARQLGMYMVTVIIGLIIHGGIFLPLIYFVVTRKNPFSFFAGIFQAWITALGTASSAGTLPVTFRCLEENLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGVVLDGGQIVTVSLTATLASVGAASIPSAGLVTMLLILTAVGLPTEDISLLVAVDWLLDRMRTSVNVVGDSFGAGIVYHLSKSELDTIDSQHRVHEDIEMTKTQSIYDDMKNHRESNSNQCVYAAHNSVIVDECKVTLAANGKSADCSVEEEPWKREK
Protein: Xylose isomerase (EC 5.3.1.5) (Q9FKK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Xylulose kinase 2
- Sorbitol dehydrogenase
- Hexokinase-2
- Hexokinase-3
- Hexokinase-1
- Probable hexokinase-like 2 protein
- Hexokinase-like 1 protein
- Hexokinase-4
- Probable fructokinase-5
- Probable fructokinase-7
Sequence:
MKKVEFFMLLLCFIAASSLVSADPPTCPADLGGKCSDSDDWQGDFFPEIPKIKYEGPSSKNPLAYRWYNAEEEILGKKMKDWFRFSVAFWHTFRGTGGDPFGAATKYWPWEDGTNSVSMAKRRMRANFEFLKKLGVDWWCFHDRDIAPDGTTLEESNKNLDEVIELAKELQKGSKIKPLWGTAQLFLHPRYMHGGATSSEVGVYAYAAAQVKKAMEVTHYLGGENYVFWGGREGYQTLLNTDMGRELDHLARFFEAAVAYKKKIGFKGTLLIEPKPQEPTKHQYDWDAATAANFLRKYGLIDEFKLNIECNHATLSGHTCHHELETARINGLLGNIDANTGDAQTGWDTDQFLTDVGEATMVMMSVIKNGGIAPGGFNFDAKLRRESTDVEDLFIAHISGMDTMARGLRNAVKILEEGSLSELVRKRYATWDSELGKQIEEGKADFEYLEKKAKEFGEPKVSSAKQELAEMIFQSAM
Protein: Protein cps3 (Meiotically up-regulated gene 188 protein) (P41000)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Responsible for supersensitivity to the spindle poison, isopropyl N-3-chlorophenyl carbamate. Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MTKKNAFKNSEDMKKYHLSEFNSEATSLTRPSPKSLQHVPCKFFRQGTCTSGKNCIFSHDLELATEKTICKYFQKGNCKFGSKCALEHVLPDGRKVKTRAFAPSTTAMGSSSQNISAAPMANIISNNDKILPMTTMASATASEEKNRIKDEALVIKKEESNVAIPSEVTVAANAFSASTEDVYSIVGDSLSKKASVKDFSDVTGIETIPAYVEATNGSSTVRSPHAKRSLSSISVKSSTSPFSGSKFLSSSSYPHTPEAHLNSNHISPASFGSGIRTRNIFNPESMSLGLKPPILNRSYSASMAPGFSMNTFTATGNLGRPTKSPSVPTSVGSNKSRKFPGINGSTLTATPSSLENLYPLSSRRSVPNLISSLGTSPSTFSSQFLKSTDRTHSFTSKLQSFNPVGTSLLASSLGTSQEDSVNYDIPDEFANEEDFIPNSLQELLTPEELERKMSHGDEAVSSSSASRFMSKVSSNLNSGNPTPYNSYNGTPTSSRFVAFFDRHRQESEKATPPSLNKVSQEPLTATTPKNLGNLTAISETLENGQTLKSNMASSIEKSKTSTEVVASYDTTLDEETQFQMDEA
Protein: GTP-binding protein 8 (C9J8V5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVCFIGRSNVGKSSLIKALFSLAPEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPGYGFRAPEDFVDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKFVNMKTQGCFPQLFPVSAVTFSGIHLLRCFIASVTGSLD
Protein: Stress protein HSP70 (Q8UWM6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MSSAKGPSIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPNNTVFDAKRLIGRKFNDQVVQADMKHWPFKVVSDGGKPKVQVDYKGENKSFNPEEISSMVLVKMREIAEAYLGQKVSNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGMDKGKSRERNVLIFDLGGGTFDVSILTIEDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRALRRLRTACERAKRTLSSSSQASIEIDSLFEGIDFYTSITRARFEEMCSDLFRGTLEPVEKALGDAKMDKAQIHDVVLVGGSTRIPKVQKLLQDFFNGRELNKSINPDEAVAYGAAIQAAILSGDKSENVQDLLLLDVAPLSLGIETAGGVMTALIKRNTTIPSKQTQTFTTYSDDQPGVMIQVYEGERAMTKDNNLLGKFELSGIPPSPRGVPQIEVTFDIDANGILNVAAVDKSTGKENKITITNDKGRLSKEDIERMVQDADKYKAEDDAQREKMAAKNSLESYAFNMKSSVEDDNMKGKIRQEDKKKVMDRCNQTISWLENNQLGDKEEYEHQLKELEKVCQPIITKLYQQGGMPTGCCGDQARTSSGVSSQGPTIEEID
Protein: Telomeric repeat binding factor 2 isoform (F6KWE7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAGGGGSSDNGGRAANRRASRSGGRARRGRHEPGLGGAAERGAGEARLEEAVNRWVLKFYFHEALRAFRSSRYRDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTDSMVESSRRLVKEAAVIICIKNKEFEKASKILKKYMSKDPTTQKVRTDLLNIIREKNLAHPVIQNFSYEIFQQKMLRFLESHLDDTEPYLLTMAKKALRSESAASSTMKEEKHTEPVEKPLREPPRQPRNPPTTIGLRTVKAAFKALSTAQDSEAAFAKLDQKDLSIERQVEQP
Protein: Lysyl oxidase homolog 3 (EC 1.4.3.-) (EC 1.4.3.13) (Lysyl oxidase-like protein 3) (Lysyl oxidase-related protein 2) (Q9Z175)
Organism: Mus musculus (Mouse)
Function: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins. Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin. Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ). Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (By similarity). Also able to catalyze deacetylation of lysine residues on STAT3 (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:26954549}. Cytoplasm {ECO:0000250|UniProtKB:P58215}. Nucleus {ECO:0000250|UniProtKB:P58215}. Note=It is unclear how LOXL3 is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (LOXL2) also has intracellular and extracellular localization despite the presence of a signal sequence. {ECO:0000250|UniProtKB:P58215}.
Interaction partners:
- Zinc finger protein SNAI1
- Fibulin-5
- Transcription factor GATA-6
- Elastin
- Lysyl oxidase homolog 2
- Bone morphogenetic protein 1
- Lysyl oxidase homolog 4
Sequence:
MRAVSVWYCCPWGLLLLHCLCSFSVGSPSPSISPEKKVGSQGLRFRLAGFPRKPYEGRVEIQRAGEWGTICDDDFTLQAAHVLCRELGFTEATGWTHSAKYGPGTGRIWLDNLSCRGTEGSVTECASRGWGNSDCTHDEDAGVICKDQRLPGFSDSNVIEVEHQLQVEEVRLRPAVEWGRRPLPVTEGLVEVRLPEGWSQVCDKGWSAHNSHVVCGMLGFPGEKRVNMAFYRMLAQKKQHSFGLHSVACVGTEAHLSLCSLEFYRANDTTRCSGGNPAVVSCVLGPLYATFTGQKKQQHSKPQGEARVRLKGGAHQGEGRVEVLKAGTWGTVCDRKWDLQAASVVCRELGFGTAREALSGARMGQGMGAIHLSEVRCSGQEPSLWRCPSKNITAEDCSHSQDAGVRCNLPYTGVETKIRLSGGRSRYEGRVEVQIGIPGHLRWGLICGDDWGTLEAMVACRQLGLGYANHGLQETWYWDSGNVTEVVMSGVRCTGSELSLNQCAHHSSHITCKKTGTRFTAGVICSETASDLLLHSALVQETAYIEDRPLHMLYCAAEENCLASSARSANWPYGHRRLLRFSSQIHNLGRADFRPKAGRHSWVWHECHGHYHSMDIFTHYDILTPNGTKVAEGHKASFCLEDTECQEDVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVKPGNYILQVVINPNFEVAESDFTNNAMKCNCKYDGHRIWVHNCHIGDAFSEEANRRFERYPGQTSNQIV
Protein: Adipocyte-related X-chromosome expressed sequence 1 (C0HK79)
Organism: Mus musculus (Mouse)
Function: Plays a role in adipogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21177646}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Signal peptidase complex subunit 2
- Signal peptidase complex subunit 1
- Signal peptidase complex catalytic subunit SEC11A
- Signal peptidase complex catalytic subunit SEC11C
- Signal peptidase complex subunit 3
Sequence:
MNSLLSRANSLFAFTLSVMAALTLGCILTTAFKDRSAPVRLHVSRILLKKVEDFTGPRKKSDLGFITFHISADLEKTFDWNVKQLFLYLSAEYSTKSNAVNQVVLWDKILLRGENPKLNLKDVKSKYFFFDDGHGLKGNRNVTLTLSWQVIPIAGILPLVTGSGRVSVPFPDSYEIATTF
Protein: Protein LIN1 (P38852)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:12402242}. Note=Probably associated with chromatin.
Interaction partners:
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor 8
- Spliceosomal protein DIB1
- Pre-mRNA-splicing ATP-dependent RNA helicase PRP28
- Small nuclear ribonucleoprotein-associated protein B
- Pre-mRNA-splicing factor SNU114
- A1 cistron-splicing factor AAR2
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor 6
- Small nuclear ribonucleoprotein E
Sequence:
MKYTQYPNSSKLKRNSDRREHDEKLSDELHNQSTIYEDEELSRAEYDSDSDSSVEDSTDNENSGKEMDEKSYEKNEDHVEDHRKRKKSKIQLLDIAEFKKENLADLDYQIGNSESKVEKGVNIEPFNIDDEIKHGVFDKDGNYIKTENATENDQQDNEEWMNDVINTEEVNRLEKEQSVKTQNSRHYMVHEALNLLKFFLVDENETVLESLGRLNKLRKIAISKKNKSLKYVIHGIELLSDLINILEKKGFSEVYEYNRLKVQDAIEEEIFDDSSRIVNHKTKLWGFKWLNKLDEYHGLYTNYEMSYWQKSYFKNSVIVKFHSEPDRDENWIHVSCLSFM
Protein: F1F0 ATP synthase subunit g (Q59M30)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
- ATP synthase subunit d
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit 4
- ATP synthase subunit alpha
- ATP synthase subunit 5
- ATP synthase subunit beta
- ATP synthase subunit 9, mitochondrial
- Uncharacterized protein
- ATP synthase subunit a
- ATP synthase subunit gamma
Sequence:
MSSVITSIVTKTTGLANCAVYWAKVGAELSKAVYKGEGLKPPSSKEFELVYKNALKFIKTPSEQQKFLEQAKNFKPTKECAYKAGIYGIQLLAFFSVGEVIGRRQLTPYVPSHH
Protein: Enterobactin synthase component D (4'-phosphopantetheinyl transferase EntD) (Enterochelin synthase D) (Q9I4H2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Pyochelin synthetase PchE
- Pyochelin synthetase PchF
- Probable non-ribosomal peptide synthetase
- PvdJ
- Phosphoribosyl-dephospho-CoA transferase
- Pyoverdine synthetase D
- Pyochelin synthase PchD
- Pyrrole-2-carboxylic acid decarboxylase
- Probable acyl carrier protein
- PvdL
Sequence:
MRAMNDRLPSFCTPLDDRWPLPVALPGVQLRSTRFDPALLQPGDFALAGIQPPANILRAVAKRQAEFLAGRLCARAALFALDGRAQTPAVGEDRAPVWPAAISGSITHGDRWAAALVAARGDWRGLGLDVETLLEAERARYLHGEILTEGERLRFADDLERRTGLLVTLAFSLKESLFKALYPLVGKRFYFEHAELLEWRADGQARLRLLTDLSPEWRHGSELDAQFAVLDGRLLSLVAVGA
Protein: Ketimine reductase mu-crystallin (EC 1.5.1.25) (CDK108) (NADP-regulated thyroid-hormone-binding protein) (Q9QYU4)
Organism: Rattus norvegicus (Rat)
Function: Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- trans-L-3-hydroxyproline dehydratase
- Cystathionine beta-synthase
- Arginase-2, mitochondrial
- Guanidino acid hydrolase, mitochondrial
- Arginase-1
Sequence:
MRRAPAFLSADEVQDHLRSSSLLIPPLEAALANFSKGPDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNNAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKFLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASSVQGDVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMKQAVLYVDSREAALKESGDVLLSGADIFAELGEVVSGAKPAYCEKTTVFKSLGMAVEDLVAAKLVYDSWSSGK
Protein: Serine protease inhibitor A3F (Serpin A3F) (Q80X76)
Organism: Mus musculus (Mouse)
Interaction partners:
- Serine
- Haptoglobin
Sequence:
MAGVSPAVFGCPDVTLGRNTAVREVQENITSVDSLTLASSNTDFAFSLYKELVLKNPDENVVFSPFSICTALALLSLGAKSNTLKEILEGLKFNLTETPEPDIHQGFRYLLDLLSQPGNQVQISTGSALFIEKHLQILAEFKEKARALYQAEAFTADFQQPLEATKLINDYVSNHTQGKIKELISDLDKRTLMVLVNYIYFKGKWEMPFDPDDTCKSEFYLDENRSVKVPMMKINNLTTPYFRDEELSCTVVELKYTGNASAMFILPDQGKMQQVEASLQPETLRNWKDSLKPRLINELCLPKFSISTDYSLEHILPELGIRELFSTQADLSAITGTKDLRTSQVVHKAVLDVAETGTEAAAGTGYQNLQCCQGVIYSMKIYFDRPFLMIISDTNTHIALFMAKVSNPESDENFLNVEYAFPQVLEIMPEYRSVCTCCLPCLTRQ
Protein: Leucine-rich repeat protein kinase family protein (Leucine-rich repeat receptor-like protein kinase) (Putative receptor-like protein kinase) (O22138)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MVSPLTLFLILFFFFLSSALSSSSSELDILLDIKSSLDPEKRFLTSWTPDADPCSSGSFDGVACDGNRRVANISLQGMGLTGTIPPSIGLLTSLTGLYLHFNSLTGHIPKDISNLPLLTDLYLNVNNLSGEIPPLIGNLDNLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNLFGPVPVKLAGAPLLEVLDIRNNSFSGFVPSALKRLNNGFQYSNNHGLCGDGFTDLKACTGLNGPNPNRPDPTNPTNFTTVDVKPESADLQRSNCSNNNGGCSSKSLKSSPLGIVMGLIGSILAVAIFGGSTFTWYRRRKQKIGSSLDAMDGRISTEYNFKEVSRRKSSSPLISLEYASGWDPLGRGQSSNNNSALSQEVFESFMFNLEEIERATQSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYEFVPNGNLLQYLDVKDETGEVLEWATRVSIINGIARGIVYLHGENGNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVESGRLNEDFMDPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNLAADY
Protein: Receptor-like protein 1 (AtRLP1) (Receptor of eMax) (Q9LNV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plant defense. Confers resistance to the bacterial pathogen Xanthomonas through recognition of the microbe-associated molecular pattern (MAMP) eMax. Functionality seems to depend on the presence of the receptor kinase SOBIR1 as an adapter protein.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Tyrosine-protein phosphatase RLPH2
- Tyrosine-protein phosphatase At3g09960
- Endo-1,4-beta-xylanase 2
- Vacuolar protein sorting 55
- EPIDERMAL PATTERNING FACTOR-like protein 8
Sequence:
MRTDERRRWWVKPKKHITLVFITITMIIQFQMKGCVSCVETERMGLLQLKSYLKNLVDAEEEEEEGLSILKSWTHHEGDCCRWERVKCSDAINGHVIGLSLDRLVPVAFESQTRSLNLSLLHSFPQLQSLNLSWNWFTNLSDHFLGFKSFGTLDKLTTLDFSHNMFDNSIVPFLNAATSIRSLHLESNYMEGVFPPQELSNMTNLRVLNLKDNSFSFLSSQGLTDFRDLEVLDLSFNGVNDSEASHSLSTAKLKTLDLNFNPLSDFSQLKGLESLQELQVLKLRGNKFNHTLSTHVLKDLKMLQELDLSDNGFTNLDHGRGLEIPTSLQVLDFKRNQLSLTHEGYLGICRLMKLRELDLSSNALTSLPYCLGNLTHLRTLDLSNNQLNGNLSSFVSGLPSVLEYLSLLDNNFDGSFLFNSLVNQTRLTVFKLSSKVGVIQVQTESSWAPLFQLKMLYLSNCSLGSTMLGFLVHQRDLCFVDLSHNKLTGTFPTWLVKNNTRLQTILLSGNSLTKLQLPILVHGLQVLDISSNMIYDSIQEDIGMVFPNLRFMNFSSNHFQGTIPSSIGEMKSLQVLDMSSNGLYGQLPIMFLSGCYSLRVLKLSNNQLQGKIFSKHANLTGLVGLFLDGNNFTGSLEEGLLKSKNLTLLDISDNRFSGMLPLWIGRISRLSYLYMSGNQLKGPFPFLRQSPWVEVMDISHNSFSGSIPRNVNFPSLRELRLQNNEFTGLVPGNLFKAAGLEVLDLRNNNFSGKILNTIDQTSKLRILLLRNNSFQTYIPGKICQLSEVGLLDLSHNQFRGPIPSCFSKMSFGAEQNDRTMSLVADFDFSYITFLPHCQYGSHLNLDDGVRNGYQPKPATVVDFLTKSRYEAYQGDILRYMHGLDLSSNELSGEIPIEIGDLQNIRSLNLSSNRLTGSIPDSISKLKGLESLDLSNNKLDGSIPPALADLNSLGYLNISYNNLSGEIPFKGHLVTFDERSYIGNAHLCGLPTNKNCISQRVPEPPSVSTHAKEEENEEEGNVIDMVWFYWTCAAVYISTSLALFAFLYIDSRWSREWFYRVDLCVHHILQFKRSSVCN
Protein: Hig-anchoring scaffold protein, isoform A (Q8INW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNRLLLQCLVTTILVYKVISVPTSTMSTSIQTTSEIPQQDDDDDDWEEDDDSLESDDDGRVYKNPRNSPSTECPRDEEQATLLGQKCLRKCSSDEDCKSKKKKCLCDGVCGNSCIKPDRECPELAQPSLGQVTVAGRHFGARASYACPHGYHVVGLQSRLCQADGNWAGAEPACKQNIYCLKPPQIEHARNSALPEQETFDLDSTVQYHCHTGYVTNGFPRAKCLAIDNLASWYGPDIQCEPRSCGQPPDPAYGWHAGECYTYGCKITYNCGTGYELVGKHERYCQSDGSWTPKELPTCVLVTSVVCPTPENPKNGKATYTTLAYNSVVSYECRYGYTLVGESSSRCGADRKWSGTLPTCKEINCGHPGVLYNGWIENIEAGTGLGASIIFRCQPEMMINGLGSSVCQIDGRWRNALPECLAPCVVPTISQGNVYPIEIITDENGTTIVHPPTTTTQSPTQTQSIGGVEKVKHGTALEVKCDENYEFPVSLLSPPTCNNGTWSIIPRCVPARCKSMPRPPKHGMVMAPKTEHGMKARFKCKDGFKLVSPEGKDVTDPHDYVLTCSFGNWTGETPKCDEVFCSFPGYIPNGKVLLVGNMGLYDYRPYVKKIVNNKQIMYDCDKGYVLEVGPPGATCVGGKWRPLDLPQCLLGQHPRLRWNRRRRRSLQIRQLRSMYLLQRQRQLQRQLIDNQNYIKATDPVQPSVHRVKRSASPHPNSQPYASDVDRAYSKYYQKIKERYQRYVRKMLGRDRIYQRLHSQDAVGRVGNNLNTHDGGQVTMRGKSNFREFENGNNYLGSGGIGSGGVVGSGVVALPNINQASRNHQVHVNRTPKEELLSNGSPPIASRSLHLNATRSYIEQLKSQIVRRRRRRSSSIGQSPPPSGATIPDAEVDISDGGEAGKGGGGKRLRGPCEELEWDSFANVTTVRPGKVPGRNAVGIMLHLECNAGFKLNIKGENATARCIRGIWKPETPKCLSAPCLVPAVEHGQYYKVEPHTKQLSDKPSLTPLSTYEEIQSNEFITLECEDGFNIQGSAQLRCAHGSWSVNAFSECTSVPCTLPNIPGVIYDGGYRAGLTIGHGSSVSVRCELSTNANPIEMSCHKGILTPPSIPCESGLRKSREELEHATPTPHPKVEHNELDNDHDHHDNGTDEHDDMKMCGPPMLTDGALVYKNADHPELDGAYESGTEIFFNCIPNAAGDRQTWRIICDNGLWIGRSYNCENGTCVFRNNEANVVSFYNDLEIREDVVDFPPGATIISRCMDIGKFSFMGSHERTCIHSEWTNTKPVCSGLNQENDYAMEKAPTILFRHQNGPIAQSNDGKLIVYPGTTLHMECLWMRRFGNPKWNVSHTHKNYTEGWVTEADEGRDSTLEYRLSIVDAASDDSGFYSCMTPARHEHTVEVVVRAINCPEIPMRRGLIVNTNDTKLSTRALLSCANGNSLIGASELFCLPSGNWSAPLPVCESVECGDIPLGMGSNASSPRVSVLSREVGGRAAFSCASGYGLRGPAEAICNPTGEWSAPLPTCVEVQCDNPGAPQNGYAQGSAPYRAGDVVQFNCNPEYMMQGQPIIACQDNARWSGGLPKCVQACSYPGTVISGRMSSVKFYYAIGESITFTCDAGLDLRGSKVLKCLKNGKWSSAIPTCVTNEGPVGGGGGGGGGGGGGSGSVATNKHLATTMG
Protein: Transmembrane protein 225B (P0DP42)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLTLEDKDMKGFSWAIVPALTSLGYLIILVVSIFPFWVRLTNEESHEVFFSGLFENCFNAKCWKPRPLSIYIILGRVFLLSAVFLAFVTTFIMMPFASEFFPRTWKQNFVLACISFFTGACAFLALVLHALEIKALRMKLGPLQFSVLWPYYVLGFGIFLFIVAGTICLIQEMVCPCWHLLSTSQSMEEDHGSLYLDNLESLGGEPSSVQKETQVTAETVI
Protein: LIM and senescent cell antigen-like-containing domain protein 2 (LIM-like protein 2) (Particularly interesting new Cys-His protein 2) (PINCH-2) (Q7Z4I7)
Organism: Homo sapiens (Human)
Function: Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Plays a role in modulating cell spreading and migration.
Subcellular location: Nucleus {ECO:0000305}. Cell junction, focal adhesion {ECO:0000269|PubMed:12167643}. Cell membrane {ECO:0000269|PubMed:12167643}; Peripheral membrane protein {ECO:0000269|PubMed:12167643}; Cytoplasmic side {ECO:0000269|PubMed:12167643}.
Interaction partners:
- Scaffold protein ILK
- Alpha-parvin
- Ras suppressor protein 1
- Beta-parvin
- Gamma-parvin
Sequence:
MTGSNMSDALANAVCQRCQARFSPAERIVNSNGELYHEHCFVCAQCFRPFPEGLFYEFEGRKYCEHDFQMLFAPCCGSCGEFIIGRVIKAMNNNWHPGCFRCELCDVELADLGFVKNAGRHLCRPCHNREKAKGLGKYICQRCHLVIDEQPLMFRSDAYHPDHFNCTHCGKELTAEARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNALGKQWHVEHFVCAKCEKPFLGHRHYEKKGLAYCETHYNQLFGDVCYNCSHVIEGDVVSALNKAWCVSCFSCSTCNSKLTLKNKFVEFDMKPVCKRCYEKFPLELKKRLKKLSELTSRKAQPKATDLNSA
Protein: Mitochondrial exoribonuclease DSS-1 (TbDSS-1) (EC 3.1.13.1) (3'-5' exonuclease DSS1) (Q86MA2)
Organism: Trypanosoma brucei brucei
Function: 3'-5'exoribonuclease which is involved in the post-transcriptional processing, editing and degradation of mitochondrial RNAs, including mRNAs, rRNAs and guided RNAs (gRNA). As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors by catalyzing the processive 3'-5' degradation of uridylated gRNA precursors. Plays a role in the degradation of 12S rRNA processing intermediates and maturation by-products.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15470249, ECO:0000269|PubMed:19540236, ECO:0000269|PubMed:26833087}.
Interaction partners:
Sequence:
MTPRRVAKLVQFSGSYLNTEWARKFILGSLLQRYNPQSLTTVGSSAAGNSGEDASLDKELLHLQRSLSEVWSLPAQPLDAVSEGRILRLLARYATGEGVMSIEALNELSHVLSCIRGSPQRVEGPIDMEELLLAIGYAKPGDNLRRVAFAGELQYPPSALAHMRAHLRDDMERDGSDPFDILRVVTHNPAYAIDSASTSEVDDAIGVHKDPVTGEECFVVYVSDATVYCPFDSPLEQLTARLLTTTTYLPEGVFFMLPKPIVDAATLREDRPCRTFDIRFQIDEVTGELKNYSVGVGWLHKLRRITYDEVQALYDEEAQVGNQHHHTERESTQASPAKREEGKKGMVASGGTSSCRPSWMTVEDESILRRIYRAAQKRYETRQLRAGDRFIHADLPEPLIKVGAGAQVLSVEDQIIGTRDARLAVAEMMIAANEVCSRVAQENHLSIPFRGTRELSLDHVAAKSYREPHGVVSVQSLDPQYVFFAEAMQRSIRQLSGVTRAVYFHTPIYHAGLDTHNYTHSTSPLRRYADMLVHHQLKVWLWRTSHCSSGGGVLHSAQKSSPVLIEQPIAEHTMATLCSMISSKQEQSSILQESSQRYWLLKHIKQNILTKSPHHRFICLVGDTRSVKCAPEYARFVVECSHDSPSQPDGGVHRTVPWAGRWKQRHHEYLYVSDIYITELQFAHVVLHSLPDVVVGAVVECEVREVHPTQGYLSLAIVKVWSGGDERRFEPLWKKCLLPSLDS
Protein: Nucleolar protein 6 (A0A0C4DFX0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|RuleBase:RU364032}.
Interaction partners:
Sequence:
MVIVTPQDRKNSVWTQDGPSAQILQQLVVLAAEALPMLEKQLMDPRGPGDIRTVFRPPLDIYDVLIRLSPRHIPRHRQAVDSPAASFCRGLLSQPGPSSLMPVLGYDPPQLYLTQLREAFGDLALFFYDQHGGEVIGVLWKPTSFQPQPFKASSTKGRMVMSRGGELVMVPNVEAILEDFAVLGEGLVQTVEARSERWTV
Protein: Indole-3-acetate O-methyltransferase 1 (EC 2.1.1.278) (IAA carboxylmethyltransferase 1) (OsSABATH4) (S-adenosyl-L-methionine:(indol-3-yl) acetate carboxylmethyltransferase 1) (Q0J998)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the methylation of the free carboxyl end of the plant hormone indole-3-acetic acid (IAA). Converts IAA to IAA methyl ester (MeIAA). Regulates IAA activities by IAA methylation. Methylation of IAA plays an important role in regulating plant development and auxin homeostasis. MeIAA seems to be an inactive form of IAA.
Interaction partners:
Sequence:
MTMAMASMKGENVTVSAAAAPRMKKLASMLCMKGGNGDGSYLNNSQAQALHARRMLHFLEETLDAMMERSSSDKLFTAADLGCSCGSNSLFIVDVIVRRVSEAYESRGRDAPEFQVFFSDLPSNDFNTLFQLLPPLLAPVAGSLEECLAAGEGAATATRPYHAAGVPGTFYGRLFPGESIDVFTSTFSLHWLSQVPEEVGDSASPAYNGGRVFVHRATEAVAAAYKRQFQADLARFLRSRAREMKRGGAMFLACLGRSSGDPADQGGAGLLFGTHFQDAWDDLVQEGVVEGEKRDSFNIPVYAPSLQEFRDVVRADGAFAIDRLELVRGGSPLVVDRPDDAAEVGRAMANSCKAVAGVLVDAHIGERRGAQLFERLERRAARHARELVEKMHFFHVVCSLSLAP
Protein: Solute carrier family 5 member 12 (E9PLZ7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MVVMIVGFLTVLIQGSTHAGGFHNVLEQSTNGSRLHIFDFDVDPLRRHTFWTITVGGTFTWLGIYGVNQSTIQRCISCKTEKHAKLALYFNLLGLWIILVCAVFSGLIMYSHFKDCDPWTSGIISAPDQLMPYFVMEIFATMPGLPGLFV
Protein: Ribonuclease pancreatic (EC 4.6.1.18) (HP-RNase) (RIB-1) (RNase UpI-1) (Ribonuclease 1) (RNase 1) (Ribonuclease A) (RNase A) (P07998)
Organism: Homo sapiens (Human)
Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
Subcellular location: Secreted.
Interaction partners:
- Ribonuclease inhibitor
- Cytochrome c
- Myoglobin
- Ribonuclease T2
- Albumin
- Alpha-lactalbumin
Sequence:
MALEKSLVRLLLLVLILLVLGWVQPSLGKESRAKKFQRQHMDSDSSPSSSSTYCNQMMRRRNMTQGRCKPVNTFVHEPLVDVQNVCFQEKVTCKNGQGNCYKSNSSMHITDCRLTNGSRYPNCAYRTSPKERHIIVACEGSPYVPVHFDASVEDST
Protein: Glutathione peroxidase 3 (GPx-3) (GSHPx-3) (EC 1.11.1.9) (Plasma glutathione peroxidase) (GPx-P) (GSHPx-P) (P23764)
Organism: Rattus norvegicus (Rat)
Function: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
Subcellular location: Secreted.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Glutathione reductase
- Glutathione synthetase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX15B
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Superoxide dismutase
- Superoxide dismutase, mitochondrial
Sequence:
MARILRASCLLSLLLAGFVPPGRGQEKSKTDCHGGMSGTIYEYGALTIDGEEYIPFKQYAGKYILFVNVASYUGLTDQYLELNALQEELGPFGLVILGFPCNQFGKQEPGENSEILPSLKYVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTAELLGSPGRLFWEPMKIHDIRWNFEKFLVGPDGIPIMRWYHRTTVSNVKMDILSYMRRQAALGARGK