wanglab/gogpt-training-data huggingface dataset:
Protein: Tensin homolog (EC 3.1.3.48) (C1 domain-containing phosphatase and tensin homolog) (Suppressor of vhp-1 deletion lethality protein svh-6) (H2L045)
Organism: Caenorhabditis elegans
Function: Probable phosphatase which regulates axon regeneration after injury by linking the svh-2 and integrin signaling pathways.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:31109965}. Note=Localizes to punctate structures along the axon in motor neurons. {ECO:0000269|PubMed:31109965}.
Interaction partners:
- Integrin beta pat-3
- START domain-containing protein
- Probable clathrin heavy chain 1
- Receptor tyrosine-protein kinase let-23
- Protein nipi-4
- Inactive tyrosine-protein kinase kin-32
- RICTOR_N domain-containing protein
Sequence:
MAAAALCCASRKSNKYNNEAGYEVYTISEDQLRLKQKMKDRKEGVQVEYITSRLIVLSCTSETSERKFVESLLKASQQIQNAHNKHIRVWNVSQRRHDISSSLDAIPFGWPSETAPSLEKLCTICKNLDQWMLEHPLNIAVIFCKGGLERCAIVVNAFMRFNAISATDDSVDDRFSMQRFSERFLGPDGPPSYKRYLGYFSSLLSGRISVNSDPLYLHNIILTFFEPINVFLKIYERLVPVYQSKTVALNKSSKFEMDGSLKLRGDIFFKCIVAASSPGSSTRCLFTCQLNTCALELHPINSEGYSVVRLHKEELDLIFNDKKIDNRVTVELVVSHTSGPTTIATAAVQSVHSLLPRNNSYETFELAQDDETNRSRLEVEYSEIRKKSTKSSKSANPINNNQEEEMPVGPPVPPKPSTPIMNGERLGEYGVGGHIGNGDVVPERRGILPASLREKINQKKELEGRATPSIEPDLVGRDRYDKASRCFSYVPAKSMQEAFERPRRTSFSRAIEKRENSVENVSQEEVARTEIPQSYQQNDISTPAKWDEQVEDAKQSALLEELARAPSAMQHNYWGNGEVDNVQVVDQAQRAVITPTSTLQRRPKPPARSGSYRTLNDDAYCSDMDELCDPEYYLNYNSNTAPLPPPRRQEQHAGTRSVQLPRKKMNFDAVTDPLDDVLESTKRLGSAYSVGDVRGGQQQQQEQHNASNDFNFSNTLNNTPTDYRQHYRNRNCQSVTTPRNHHFSTPSREQEADAADTWLSGKLKKVRSKRDIDPDIVRRRTQEKMLLEELKDSAANNDENQHNLPNGHARGAGLQNIDPLAEFRREEERLRNTRSPYGEERWRGRMRGKPPTPPPRESSASPVNSLPRGTPAHHMDRQRHNQSVPLPMHHRQFDEDFDVNSLFNFSHDPRQQSTTLERGGRSLSRGARIQDAYYASQQDLSANNRFNSGQERVAAAIYRAETAHRDMYASGTINRAETPGRYFPENSAVLERSSTPSFPVSRATPLPFHPLLYNNGERGGSGHAAGGGGGGHNGYSTMNNRSASPRLFGGSSTLSRRSSVNSVDTSEIIHHHPLFVKDTSKYWYKPTISREQAINMLRDKPPGTFVVRDSNSFPGAFGLALKVSTPPPGVNPGDGSELVRHFLIEPSPKGVKLKGCNNEPVFGSLSALVYQHSITALALPTKLVLPDFDPAATPEHLSATQALLEQGAACNVVYVGSVDVESLTGNECVKRSIATCSQRAINGDSRAVSVHFKVSSQGVTLTDNTRKVFFRRHFNVQSVIFAGMDPIERRFENTRALGFHDGCIAQARLFAFVARIPSSSENACHVFAELEPEQPGSAVVNFINKVMLAQKNRS
Protein: Protein YIP5 (YPT-interacting protein 5) (Q9UTD3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Possible role in vesicle-mediated transport. May be involved in proper membrane localization of Rab GTPases (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein YIP4
- Protein transport protein yip1
- Golgi apparatus membrane protein tvp23
- PRA1-like protein
- Protein transport protein yif1
Sequence:
MAHEIEIDSEADLGRTTFEAEDLYKQRTPITKPPAPRLQSRRASMQETPWTIKDSFNVETKDVVQRCIHTLIPTVNFFDVVDDRPDLYGPFWITTTVIQALFFSNSITEYARYATGHGTSGYSIKKLISAASIIYGYTTIIAVLLWGILVWNKCNPKLLDCLCLYGYANIVWLPVSLATPPFGLLSTLASHIVKYVLTGIGLLISIVFLTRNLYPICQQAGSNLCKLLLFGIIVFHCLLALSLQLIFFS
Protein: Probable cytosolic iron-sulfur protein assembly protein Ciao1 (Q7K1Y4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
Interaction partners:
- MIP18 family protein galla-2
- MMS19 nucleotide excision repair protein
- MIP18 family protein galla-1
- Probable cytosolic Fe-S cluster assembly factor CG17683
- ADP/ATP translocase
- General transcription and DNA repair factor IIH helicase subunit XPD
- GH12701p
- Pyridoxal-dependent decarboxylase domain-containing protein 1
- Lipoyl synthase, mitochondrial
- Cytosolic Fe-S cluster assembly factor Nubp2 homolog
Sequence:
MGRLILEHTLQGHKGRIWGVAWHPKGNVFASCGEDKAIRIWSLTGNTWSTKTILSDGHKRTIREIRWSPCGQYLASASFDATTAIWSKSSGEFECNATLEGHENEVKSVSWSRSGGLLATCSRDKSVWIWEVAGDDEFECAAVLNPHTQDVKRVVWHPTKDILASASYDNTIKMFAEEPIDNDWDCTATLTSHTSTVWGIDFDADGERLVSCSDDTTIKIWRAYHPGNTAGVATPDQQTVWKCVCTVSGQHSRAIYDVSWCKLTGLIATACGDDGIRIFKESSDSKPDEPTFEQITAEEGAHDQDVNSVQWNPVVAGQLISCSDDGTIKIWKVTE
Protein: UPF0057 membrane protein C04G6.5 (Q17638)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- CaeNaCin
Sequence:
MATDADVIIEVILCIFLPPLAIWWHTKECDINVLIDIIFCLLFWLPGILYAVYICFFRK
Protein: Uncharacterized protein (Q386U1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial SSU ribosomal protein
- Mitochondrial glycoprotein-like protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- 30S ribosomal protein S8, putative
- Uncharacterized protein
- Small ribosomal subunit protein mS41
- Uncharacterized protein
Sequence:
MPSASSGYTFADFLRRLERSPDSHMAPLYHEHRELFVRRHDMFARVISSVTWSKGVALVAAAGYTQAVNVTIYRALLARMLLHNRHVRQCGAGSVVPWSAALRTYSEAIATHGNAVPTRMTLSALRLCTPARQWVAAISLLMLSQANDKLTLPMLIDAAGCCATPAAWEKAMTLLGRFHAQSLQVLPDSIQSLRPVGTSASTVDAAAHALLPRSEGPTPEQKHILTVINKVVSAVPWQVALSNEMCRSYLTHLVASTTLRPTEKTASLTTAVQQLPWEAFVTLMKTVTATVQEGSQGVLGSRSTPQLPPPQDGMERGDVAKSLLSNSIIREGVNLLQSEPETAIPFITTILHKLPSAEAAALFLSEATSAYRNSSSAVVAAAIRHPVVVGALLKRCADSNSWYLAASIFKSTSPTAIPCDVASDLVIQMRRANQAPLVVDVLQKYIVPSRTKLTEEAIEAALLCVLVHNRALAKASAVVAGTSPDNRTGKPNGIGVANGVHWISALSWATDLLEEGVESRILQTGTTPSVGGVNHEDPTVLLRKKTLSPRILSLLIYICVNAGSPRGGLFALGYARTVSKTELELSEEITALLYCMMYDRPREAESIIQHAVKKHGEYKGKYLGRLLVASQEAKGSALRNQT
Protein: Zinc finger protein GIS (Protein GLABROUS INFLORESCENCE STEMS) (Q84WI0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor required for the initiation of inflorescence trichomes in response to gibberellin (GA). Mediates the induction of GL1 expression by GA in inflorescence organs and is antagonized in its action by the DELLA repressor GAI. Acts upstream of the trichome initiation regulators GL1 and GL3, and downstream of the GA signaling repressor SPINDLY (SPY). Does not play a significant role in the cytokinin response. Controls trichome branching through GA signaling. Acts downstream of the key regulator STICHEL (STI) in an endoreduplication-independent pathway. Controls trichome cell division indirectly by acting downstream of a key endoreduplication regulator SIAMESE (SIM).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9SLB8}.
Interaction partners:
- Transcription factor TRY
- Transcription initiation factor IIF subunit alpha
- C2H2-type zinc finger family protein
- MYB-like transcription factor TCL1
- Protein SCAR3
- Trichome differentiation protein GL1
- Plant UBX domain-containing protein 2
Sequence:
MDEATGETETQDFMNVESFSQLPFIRRPKDKNPKPIRVFGKDFTGRDFSITTGQEDYTDPYQTKNKEEEEEEDQTGDNSTDNNSISHNRRFECHYCFRNFPTSQALGGHQNAHKRERQLAKRGVSSYFYHPDNNPYSYRHYPSWTNGPLTAARSYGGFSSGPKPSGYYTRPSYGSQLGLWRLPPRVQGVYNSNAAFTSNGSSSSSNSTLPLLTRSQTQLSSQVGGSAAQNRMSSYGYGLSPNVQDHVSLDLHL
Protein: GDP-mannose 4,6-dehydratase (EC 4.2.1.47) (Q8IAX4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- GDP-L-fucose synthase
- mannose-1-phosphate guanylyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- Phosphoacetylglucosamine mutase, putative
- UTP-monosaccharide-1-phosphate uridylyltransferase
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A, putative
Sequence:
MRVALIFGITGQDGSYLSELLLEKNYHVHGVIRRCSSFNTKRIDHIFDKLILHYGDLLDSSNICSLICEIKPNEIYNLAAQSHVKVSFEMPEYTTEATALGTLRILEGIRISKVKNIKFYNASTSELFGKVQCPIQNENTPFYPVSPYAIAKLYAHYITINYRESYNMFCINGILFNHESPRRGETFVTRKITRGIAKIQKKLETSIILGNIDTYRDWGHAKDYVYAMYLMLQQNEADDFVICSNEQHSVREFCEISFSFVNIHIKWIGKGIQEIGVDQNNNVLIKKHEKYFRNCEVNTLLGDCSKAKNILKWEPTYTFTQLVYEMLKCDMQDYNLSMDDYDTCMKKYDTYKMGKKQ
Protein: Folic acid synthesis protein FOL1 [Includes: Dihydroneopterin aldolase (DHNA) (EC 4.1.2.25) (7,8-dihydroneopterin aldolase) (FASA) (FASB); 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) (EC 2.7.6.3) (2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (PPPK) (FASC); Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase) (FASD)] (P53848)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes three sequential steps of tetrahydrofolate biosynthesis.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15169867}.
Interaction partners:
- GTP cyclohydrolase 1
- Dihydrofolate synthetase
- Probable folylpolyglutamate synthase
- Folylpolyglutamate synthase
- Aminodeoxychorismate lyase
- Aminodeoxychorismate synthase
- Repressible alkaline phosphatase
- Dihydrofolate reductase
- Serine hydroxymethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, mitochondrial
Sequence:
MSKLFSTVNSARHSVPLGGMRDYVHIKKLEMNTVLGPDSWNQLMPQKCLLSLDMGTDFSKSAATDDLKYSLNYAVISRDLTNFVSKKKNWGSVSNLAKSVSQFVMDKYSGVECLNLEVQADTTHIRSDHISCIIQQERGNPESQEFDVVRISELKMLTLIGVFTFERLKKQYVTLDIKLPWPKKAELPPPVQSIIDNVVKFVEESNFKTVEALVESVSAVIAHNEYFQKFPDSPLVVKVLKLNAITATEGVGVSCIREPREIAMVNIPYLSSIHESSDIKFQLSSSQNTPIEGKNTWKRAFLAFGSNIGDRFKHIQMALQLLSREKTVKLRNISSIFESEPMYFKDQTPFMNGCVEVETLLTPSELLKLCKKIEYEELQRVKHFDNGPRTIDLDIVMFLNSAGEDIIVNEPDLNIPHPRMLERTFVLEPLCELISPVHLHPVTAEPIVDHLKQLYDKQHDEDTLWKLVPLPYRSGVEPRFLKFKTATKLDEFTGETNRITVSPTYIMAIFNATPDSFSDGGEHFADIESQLNDIIKLCKDALYLHESVIIDVGGCSTRPNSIQASEEEEIRRSIPLIKAIRESTELPQDKVILSIDTYRSNVAKEAIKVGVDIINDISGGLFDSNMFAVIAENPEICYILSHTRGDISTMNRLAHYENFALGDSIQQEFVHNTDIQQLDDLKDKTVLIRNVGQEIGERYIKAIDNGVKRWQILIDPGLGFAKTWKQNLQIIRHIPILKNYSFTMNSNNSQVYVNLRNMPVLLGPSRKKFIGHITKDVDAKQRDFATGAVVASCIGFGSDMVRVHDVKNCSKSIKLADAIYKGLE
Protein: N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC 2.1.1.244) (Alpha N-terminal protein methyltransferase 1A) (Methyltransferase-like protein 11A) (X-Pro-Lys N-terminal protein methyltransferase 1A) (NTM1A) [Cleaved into: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed] (Q8R2U4)
Organism: Mus musculus (Mouse)
Function: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by NTMT2-mediated monomethylation. Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1) (By similarity). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BV86}. Note=Predominantly nuclear. {ECO:0000250|UniProtKB:Q9BV86}.
Interaction partners:
- EEF1A lysine methyltransferase 2
Sequence:
MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISNIDLNSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEIYHVYSFALR
Protein: Sorbose reductase sou1 (EC 1.1.1.289) (Sorbitol utilization protein sou1) (Q9Y6Z9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the NADP dependent reduction of L-sorbose to D-glucitol.
Interaction partners:
- Uncharacterized oxidoreductase C22A12.17c
- Uncharacterized oxidoreductase C1739.08c
Sequence:
MTSMFSLKGKTTLITGGSGGIGFSIAKAFAAAGSNVGLLYGRNKKALEYAAELRDKHGVQAKAYSCPIENRSAVIETTNQAVEELGGRLDVMIANAGIAIPHLSLEDKNEDIWTKVVGINLNGAYYTAQAAGHHFKKQGKGSLIFTASMSGHIANWPQQWASYHATKAAVKHLARALAVEWAPFARVNSVSPGYIDTDLTLYADENLRKKWKEYTPQARIGLPDELPGAYLYLASDASSYCTGSDIIVDGGYCSR
Protein: Alpha-1,2-mannosyltransferase MNN24 (EC 2.4.1.-) (Q5AD72)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Alpha-1,2-mannosyltransferase required for cell wall integrity. Responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides. Addition of alpha-1,2-mannose is required for stabilization of the alpha-1,6-mannose backbone and hence regulates mannan fibril length; and is important for both immune recognition and virulence.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Mannan polymerase complex subunit MNN9
- Alpha-1,6-mannosyltransferase
- Putative alpha-1,3-mannosyltransferase MNN1
- Alpha-1,6-mannosyltransferase
- Anp1p
- Alpha-1,6-mannosyltransferase
- Glutamyl-tRNA
Sequence:
MFSIPVSSKTVRLILVSLLLITLINILAAFQRSTLSSWFPSSRHIINKFTDLRLALSSQESVLRDEEGEIYSLVGYHHDFDSNLVVVQKQYLLEKTPNEDTTEHFWNFLQSNFETKSEYDLNLIDGYNYKKLIKHLNEQNELQLSHSFVEQYKMENQFIQSFQNFFVQLIDTIEDCKPDLDPINNDNHYPNGDKIVKYYELRNKIPSENMKQFNIERLIHRNGRIPIYGGHLREQYKDELIRNKEFLSMYLTLSDSEISALKKSHTKFLETMMENWPENLFKFNKFNNFMKGDGIVYLGGGKYNQLVLLSIKILRENGSRLPVEVIIPYKNDYDIQFCDRVLPTLNGKCKLMTDYLPQTFVDKISGFQLKNIALLISSFERILYLDADNIPIRNPDVLFTNAPFTTKHLVVWPDLWRRSTSPHYYTIAGIEVDPNFKVRNSYVDGDERGKYTDSMYYSYHDCKGSIPEASSETGQLLINKKIHFQTLILAMYYNYYGPDYYYPLFSQGAAGEGDKETFIAAAHKLDLPYYQVGEFNREFGPINDNTRKHEFYGMGQYDPIIDYYMSTITTTQKDTKKKINYNSPLPEKYAANDEDDTCSNYDFHLFQSSSLFFLHANWPKYYIEKLFLYSYDEDRGPVTNDGDKRRLYGNELKKELGGYDFELNIMKNLHWCFCEEPLIDLIGIPVVGSKTRTDVCIAIKNHIEFLEIS
Protein: BEL1-like homeodomain protein 8 (BEL1-like protein 8) (Protein POUND-FOOLISH) (Q9SJJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for specifying floral primordia and establishing early internode patterning events during inflorescence development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein KNATM
- Protein LEAFY
- Homeobox protein knotted-1-like 2
Sequence:
MDMIKPDFQQIRRDKFRVEQMNDFPNTWTQQQHQNIRIPNNLDLIGILQNQISVPVQTDLYQDSAATFMNMPQSIHRDPQGPSNWRISDLSQPSTVNHGYDQAGIRPNNVADLLSDHFSSRNQILDRPLYVGRDSIPQSSMIRRSEVSCLDDNQKGCVTVACSGTGNEILRSSYDQGSSSGSYRGEFSFLPSLENQSVAHNASNWNHGPVNVTATSHTNSKKGFPLSLLSDIPPSRDVGNAAVLSTMNIHGPLGPFTGYASILKSSRFLEPAQKMLEEFCISYASKIISRSESTSMEDDDDDDDNLSGFSSSSEPLEPKNRLKKAKLLFLQEEVCKWYKLYNHQLQTVMSSFNTVAGLNTATPYISLALKRTSRSFKALRTAIAEHVKQISSHSSNGNNNNRFQKRQRSLIGNNVGFESQQQHIWRPQRGLPERAVAVLRAWLFDHFLHPYPTDSDKQMLATQTGLSRNQVSNWFINARVRLWKPMVEEIHTLETKAIKNADTSHNIEPSNRPNTVSSPSHEQTLTGLSGTKRSRLEYMDMVGFNRGNVSLTLELRRGVDNVIQTQTQDHQFGTGSQMFHDFVG
Protein: SH3 domain-containing protein (O18250)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSQPIARRSDYRTGSEQMTPRSDHRGPSMGYGNGGSVDQRVDDVTPSYYVEHLATFAVGRQFGLTFPADGIRKLKQMEKNSAIWAQPLILRFRHNAVTVEDDNGELVEQFPLELIEQPTAHVSNDSRETYNNVLLFVVREDRKRMSTPTEMHIFQCIRVSATDVAEDLKNYVQGQFRRVRNGRRTAAPTHLQAQQQQMPFYPPDDASISSETSEMFERDVNTLNRCFDDIERFVARIQSAALAQREIEQQNHRYRTANRRDKKNQQPPDPNGILFMRAQLPLESEFVDILKKFKLSFNLLAKLKNHIHEPNAPELLHFLFTPLAVILEACHWGLGRNVAPTVASPLLSLEARELMQNCLTSHESDIWMSLGEAWRTPPEDWTKPLPPPYRPIFNDGFAPYGVADRAMATPNQIHRGHSAPPEHFRQPPPRERNMVDTLEFDRLTLERERLEFEKAKIMERESRLRHEEKQIEDEKRRMHAEKDLITKETTQPVPPPAAVVTHQPITKRYDPPISISPPPQRNNYSHVKVTVDSDTSPRQQAFIDDIVAKGGKLAVVTYDRGGQNTKELTVHKGEYLEVIFDERNWWECKNMHQRVGYVPHTILSMVPFEQQQYASPNHHNNSSSTGGYNNGHHQGPAQNVYRPPPPPLVSDAGVQVEIRREHVAPPPPPVVIPPPPPPVRTPTMEELLRMQQQQQQKQRKPPVEEPVYQPQPAQRAGLEIWRRNQNPQLIQEVTETVGQHSGDILRPAMQRATRVAINEKSSPEDVTRWLQEKGFSPRVIDLLDGQDGANLFSLSKLHLQQACGRDEGGYLYSQLLVQKKRSGFRTHTGDELKAILNHRRTHVELSNEAAADEPVFTINPIL
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (G5ECR5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKTRVVLILALSVCIEAASEVIRARAYIFKAEAGKIPTELIGTIDFDQSGSFLKLNGSVSGLAAGKHGFHIHEKGDTGNGCLSAGGHYNPHKLSHGAPDDSNRHIGDLGNIESPASGDTLISVSDSLASLSGQYSIIGRSVVIHEKTDDLGRGTSDQSKTTGNAGSRLACGTIGIVEERILETTTASLPPVTQSQPIGSSSYYYSTFYLPIILYFLLSRIL
Protein: C2H2-type domain-containing protein (Q9XWK6)
Organism: Caenorhabditis elegans
Interaction partners:
- C2H2-type domain-containing protein
- SUPpressor
- Ubiquitin-conjugating enzyme E2 ubc-18
- TIR domain-containing protein
- F-box C protein
- DUF38 domain-containing protein
- F-box domain-containing protein
- Heterogeneous nuclear ribonucleoprotein A1
Sequence:
MAHTFACPRGDCGLFSLSKLDDHLTADHHLEHMCSECEESFGSAEEAKEHTLLAHENAQTFDDPKIRNTRIVDSIIAAVRVSGDVIEEFNSVIMRAVIRHWGNTSTEKLIAVVDSPMITRDFYIDCFEALKMRYDSGEKSIDLLCRLAKLCTKIGNFVEKEKRKDIIIKGKMYATEAWNTDSYNILAAHWAAVMSGKAIEYLEGDEKNLEMRHCRQYLDRAISIQAGKNAMYNNILGRWALSALEIWESDRQQLIHHYATPYDAIDDAIYQFRSAFDLIPYWIDNIVHLGKALLYNENKEAAIGMFQLALKMDPSNDIEKELLADALDLCSI
Protein: Degenerin mec-4 (Mechanosensory abnormality protein 4) (P24612)
Organism: Caenorhabditis elegans
Function: Subunit of an amiloride-sensitive cation channel (degenerin channel complex) permeable for sodium, potassium, lithium and N-methylglucamine, and required for mechanosensory transduction (touch sensitivity). Negatively regulates the turning step of male mating behavior.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:12478294}. Note=Co-localizes with mec-6 in touch neuron axons. {ECO:0000269|PubMed:12478294}.
Interaction partners:
- Mechanosensory protein 2
- Degenerin mec-10
- Mechanosensory abnormality protein 6
- Kunitz/Bovine pancreatic trypsin inhibitor domain protein
- MEC-5
- Tubulin beta-1 chain
- Band 7 domain-containing protein
- Band 7 domain-containing protein
- Ion transport domain-containing protein
- Acid-sensing ion channel 1
Sequence:
MSWMQNLKNYQHLRDPSEYMSQVYGDPLAYLQETTKFVTEREYYEDFGYGECFNSTESEVQCELITGEFDPKLLPYDKRLAWHFKEFCYKTSAHGIPMIGEAPNVYYRAVWVVLFLGCMIMLYLNAQSVLDKYNRNEKIVDIQLKFDTAPFPAITLCNLNPYKASLATSVDLVKRTLSAFDGAMGKAGGNKDHEEEREVVTEPPTTPAPTTKPARRRGKRDLSGAFFEPGFARCLCGSQGSSEQEDKDEEKEEELLETTTKKVFNINDADEEWDGMEEYDNEHYENYDVEATTGMNMMEECQSERTKFDEPTGFDDRCICAFDRSTHDAWPCFLNGTWETTECDTCNEHAFCTKDNKTAKGHRSPCICAPSRFCVAYNGKTPPIEIWTYLQGGTPTEDPNFLEAMGFQGMTDEVAIVTKAKENIMFAMATLSMQDRERLSTTKRELVHKCSFNGKACDIEADFLTHIDPAFGSCFTFNHNRTVNLTSIRAGPMYGLRMLVYVNASDYMPTTEATGVRLTIHDKEDFPFPDTFGYSAPTGYVSSFGLRLRKMSRLPAPYGDCVPDGKTSDYIYSNYEYSVEGCYRSCFQQLVLKECRCGDPRFPVPENARHCDAADPIARKCLDARMNDLGGLHGSFRCRCQQPCRQSIYSVTYSPAKWPSLSLQIQLGSCNGTAVECNKHYKENGAMVEVFYEQLNFEMLTESEAYGFVNLLADFGGQLGLWCGISFLTCCEFVFLFLETAYMSAEHNYSLYKKKKAEKAKKIASGSF
Protein: Serine protease 29 (EC 3.4.21.-) (Implantation serine proteinase 2) (ISP-2) (Strypsin-2) (Strypsin-related protein) (Tryptase-like proteinase) (Q99MS4)
Organism: Mus musculus (Mouse)
Function: Involved in embryo hatching and implantation.
Subcellular location: Secreted {ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15349836}. Note=Secretion into the glandular and uterine lumen may occur as a consequence of progesterone-induced epithelial differentiation.
Interaction partners:
Sequence:
MLIQLCLTLFFLGCSIAGTPAPGPEDVLMGIVGGHSAPQGKWPWQVSLRIYRYYWAFWVHNCGGSIIHPQWVLTAAHCIRERDADPSVFRIRVGEAYLYGGKELLSVSRVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGAVSTHRSLPPPYRLQQVQVKIIDNSLCEEMYHNATRHRNRGQKLILKDMLCAGNQGQDSCYGDSGGPLVCNVTGSWTLVGVVSWGYGCALRDFPGVYARVQSFLPWITQQMQRFS
Protein: Golgin subfamily A member 7B (Q2TAP0)
Organism: Homo sapiens (Human)
Function: Play a role in cell adhesion by regulating the plasma membrane localization of the palmitoyltransferase ZDHHC5. May be involved in protein transport from Golgi to cell surface.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31402609}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- Palmitoyltransferase ZDHHC5
- Palmitoyltransferase ZDHHC9
Sequence:
MATEVHNLQELRRSASLATKVFIQRDYSDGTICQFQTKFPPELDSRIERQLFEETVKTLNGFYAEAEKIGGSSYLEGCLACATAYFIFLCMETHYEKVLKKISRYIQEQNEKIFAPRGLLLTDPVERGMRVIEISIYEDRCSSGSSSSGSSSGSGSSSGGGGGAGAR
Protein: Scratch-a transcription factor (Transcriptional repressor scratch 2) (Q6YI50)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPRSFLVKKIKLDDFSSSPVSNHHHHHHNDRHMDDSFSRSRSSLGVRLCENGYIKDYISSSEYTEEKQADMKLNSELLYSPVSSGGGEYCQPDLEHPDSPQSGLTARGYFSSESESLSEGYTMDAFFISDGRSRRKGEVSEAAKADEVEKEVVGVNNGGARHTCNECGKTYATSSNLSRHKQTHRSLDSKMARKCPTCDKVYVSMPALAMHILTHDLKHKCHVCSKAFSRPWLLQGHMRSHTGEKPFACAHCGKAFADRSNLRAHMQTHSAFKHYSCKRCNKTFALKSYLNKHYESACFRGSGDEDESGSEN
Protein: Secretory carrier-associated membrane protein (Secretory carrier membrane protein) (Q9VXV6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363122}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363122}.
Interaction partners:
- RE23381p
Sequence:
MSGSGLDENPFGEPNLDNPFADPAIQQARRLQSGAALVSLEDYNPFEEQAKPQLQINSTNTAAVVQPLSQNIPPPQTSSLGASAPSTSIQITSEELQRRQEELDRKAAELDRREQQLQGNVPQLNNWPPLPDNFCVKPCFYQDFEVEIPPEFQKLVKRLYYIWIFYTMTLLANVIGGLILLFHAGEFETFFLAIFYTMLFSPASYVCWFRPAYKAFRNDSSFNFMVFFFIYFFQTLYSIVQAVGFNKMGYCGFITAIGQFDGQASGIIVGILLLNVAFCFTAVAVANVLMITKIHSIYRSTGASMAKAQAEFTTEFLRNQHVQEAASSAVNTAINSQFNNSRY
Protein: Metal transporter CNNM3 (Ancient conserved domain-containing protein 3) (Cyclin-M3) (Q8NE01)
Organism: Homo sapiens (Human)
Function: Probable metal transporter.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein tyrosine phosphatase type IVA 2
- Protein tyrosine phosphatase type IVA 3
- Cystathionine beta-synthase
- Cystathionine beta-synthase-like protein
- Protein tyrosine phosphatase type IVA 1
- GMP synthase
Sequence:
MAAAVAAAGRLGWLFAALCLGNAAGEAAPGPRVLGFCLEEDGAAGAGWVRGGAARDTPDATFLLRLFGPGFANSSWSWVAPEGAGCREEAASPAGEWRALLRLRLRAEAVRPHSALLAVRVEPGGGAAEEAAPPWALGLGAAGLLALAALARGLQLSALALAPAEVQVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYRAAGQRAVPAVLGSAGLVFLVGEVVPAAVSGRWTLALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGGDPYSDLSKGVLRCRTVEDVLTPLEDCFMLDASTVLDFGVLASIMQSGHTRIPVYEEERSNIVDMLYLKDLAFVDPEDCTPLSTITRFYNHPLHFVFNDTKLDAVLEEFKRGKSHLAIVQKVNNEGEGDPFYEVLGLVTLEDVIEEIIRSEILDESEDYRDTVVKRKPASLMAPLKRKEEFSLFKVSDDEYKVTISPQLLLATQRFLSREVDVFSPLRISEKVLLHLLKHPSVNQEVRFDESNRLATHHYLYQRSQPVDYFILILQGRVEVEIGKEGLKFENGAFTYYGVSALTVPSSVHQSPVSSLQPIRHDLQPDPGDGTHSSAYCPDYTVRALSDLQLIKVTRLQYLNALLATRAQNLPQSPENTDLQVIPGSQTRLLGEKTTTAAGSSHSRPGVPVEGSPGRNPGV
Protein: Probable FAD-binding monooxygenase AlmA (EC 1.14.13.-) (Q6F7T9)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Is able to catalyze the degradation of n-alkanes with C chain lengths of 32 and 36. Probably allows Acinetobacter baylyi strain ADP1 to grow on the long-chain n-alkane dotriacontane (C32H66) as a sole carbon source.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative monooxygenase
Sequence:
MEKHIDILIVGAGISGIGIAAHLSKDAPQRQFEIIERRENIGGTWDLFRYPGIRSDSDMSTFGFNFKPWQSPNVLASGSSIKGYLSEVVDEYDLKKKIHFKHRVLAANYDTASKKWYVEIEDAAQKKQTWIANFIVGCTGYYNYDQGFEPDFPNKDAFKGQFIHPQHWPENLDYVGKKVVIIGSGATAITLVPAMSKGGAEHVTMLQRSPTYIASIPSIDFVYDKMRKVLPEDLAYKLTRARNIGVQRGIYTLSQKQPKLVRKFLLKSIEMQLKGKVDMKHFTPSYNPWDQRLCVVPDGDLFKILRSGQASVETDQIEKFTETGIQLKSGKHLDADIVVSATGLEIQILGGIKGTIDGQPLDTSKSMLYQGVMVSDVPNMAMIIGYINASWTLKVDVAADYICRLLNYMDKQGYDEVIPEGDQTELMEDTVMGSLTSGYIARAANVMPKQGKHAPWKVTNNYLADRKALKNARFDDGVLHFDKKTDTVERKTKPKLVS
Protein: Glyoxylase I 4 (AtGLXI-like;4) (AtGLYI4) (Q9XI31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the detoxification and scavenging of methylglyoxal (MG), a cytotoxic aldehyde produced in response to primary metabolism alteration observed during biotic and abiotic stresses. Modulates cross-talk between salicylic acid (SA) and jasmonic acid (JA) signaling pathways during defense responses to pathogens such as Botrytis cinerea.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31652571}. Cytoplasm {ECO:0000269|PubMed:31652571}. Note=Localized at the plasma membrane during methylglyoxal (MG) accumulation, but translocates to the cytoplasm upon jasmonate (MeJA) stimulus. {ECO:0000269|PubMed:31652571}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g71460
- Trimethylguanosine synthase
- Lactoylglutathione lyase GLX1
- Zinc finger protein CONSTANS-LIKE 8
- Lactoylglutathione lyase
- Aspartate-glutamate racemase family
- Hydroxyacylglutathione hydrolase 1, mitochondrial
- Probable lactoylglutathione lyase, chloroplastic
- Defensin-like protein 206
- Hydroxyacylglutathione hydrolase 2, mitochondrial
Sequence:
MKEDAGNPLHLTSLNHVSVLCRSVDESMNFYQKVLGFIPIRRPESLNFEGAWLFGHGIGIHLLCAPEPEKLPKKTAINPKDNHISFQCESMGVVEKKLEEMGIDYVRALVEEGGIQVDQLFFHDPDGFMIEICNCDSLPVVPLVGEMARSCSRVKLHQMVQPQPQTQIHQVVYP