wanglab/gogpt-training-data huggingface dataset:
Protein: Protein PHR1-LIKE 2 (Myb family transcription factor PHL2) (Q94A57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator. Acts redundantly with PHR1 as a key component of the central regulatory system controlling transcriptional responses to Pi starvation. Binds in a sequence-specific manner to phosphate starvation-regulated promoters.
Subcellular location: Nucleus {ECO:0000269|PubMed:26586833}.
Interaction partners:
- SPX domain-containing protein 1
- SPX domain-containing protein 2
- Probable ubiquitin-conjugating enzyme E2 24
- Guanine nucleotide-binding protein alpha-1 subunit
- Sulfate/thiosulfate import ATP-binding protein, putative
- Purple acid phosphatase 10
Sequence:
MYSAIRSLPLDGGHVGGDYHGPLDGTNLPGDACLVLTTDPKPRLRWTTELHERFVDAVTQLGGPDKATPKTIMRTMGVKGLTLYHLKSHLQKFRLGRQAGKESTENSKDASCVGESQDTGSSSTSSMRMAQQEQNEGYQVTEALRAQMEVQRRLHDQLEVQRRLQLRIEAQGKYLQSILEKACKAFDEQAATFAGLEAAREELSELAIKVSNSSQGTSVPYFDATKMMMMPSLSELAVAIDNKNNITTNCSVESSLTSITHGSSISAASMKKRQRGDNLGVGYESGWIMPSSTIG
Protein: Dynein axonemal intermediate chain 7 (Cancer susceptibility candidate gene 1 protein) (Protein CASC1) (Cilia and flagella associated protein 94) (Lung adenoma susceptibility 1-like protein) (Protein phosphatase 1 regulatory subunit 54) (Q6TDU7)
Organism: Homo sapiens (Human)
Function: Via its association with the multisubunit axonemal dynein complex, is potentially involved in the regulation of cilia function. May also act as a cell cycle regulator.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q6TDU8}. Cytoplasm {ECO:0000250|UniProtKB:Q6TDU8}. Note=Colocalizes with microtubules in interphase. {ECO:0000250|UniProtKB:Q6TDU8}.
Interaction partners:
- Dynein axonemal intermediate chain 3
- Dynein axonemal intermediate chain 4
- Cilia- and flagella-associated protein 70
- Dynein axonemal heavy chain 2
- Dynein axonemal light chain 1
- Dynein axonemal heavy chain 1
- Dynein axonemal intermediate chain 2
- Outer dynein arm-docking complex subunit 1
- Dynein axonemal heavy chain 7
- Dynein axonemal heavy chain 5
Sequence:
MSGSKKKKVTKAERLKLLQEEEERRLKEEEEARLKYEKEEMERLEIQRIEKEKWHRLEAKDLERRNEELEELYLLERCFPEAEKLKQETKLLSQWKHYIQCDGSPDPSVAQEMNTFISLWKEKTNETFEEVIEKSKVVLNLIEKLKFILLETPPCDLQDKNIIQYQESILQLQELLHLKFGVATEILLKQASTLADLDSGNMEKVIKDENVTLYVWANLKKNPRHRSVRFSETQIGFEIPRILATSDIAVRLLHTHYDHVSALHPVSTPSKEYTSAVTELVKDDVKNVEKAISKEVEEESKQQERGSHLIQEEEIKVEEEQGDIEVKMSSAEEESEAIKCEREMKVLSETVSAAQLLLVENSSEKPDFFEDNVVDLCQFTTLGGVYHLDILELPPQCKPVKGWMIVEILKEGLQKYTYPPETTEEFETENAFPPIEVTLEVHENVIFFEDPVVVRWDAEGKHWRTDGISNVSYKPKERLVTFSLDTFGPVTLIQDAHINMPYQSWELRPLDVNKVLLTVTTVFTEIQIQIKENLCMLSSIKLKDKKHISILEGTWMTPIPFIIALKEAGLNIFPTRHSHFYVIINNKVPLVEVKAYRQMALLSSAFAFGWSKWNLLCNSTKVVFKVREHLTEACTENPNWALLMFSGDRAQRLKIKEESEAFSEALKEETEFHSTLYHMVKDFASEEAMEKVRSSNCQFVNSVCHMLLSTRLLSYS
Protein: MB2q1 protein (MB2q2 protein) (MB2q3 protein) (MB2q4 protein) (MB2q5 protein) (MB2q6 protein) (Q95602)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAALWLLLLVLSLDCMGAGGFVAHVESTCVLDDAGIPQDFTYCVSFNKDLLACWDPDVGKIVPCEFGVLSRLAEIISMILNEQESLIQRLQNRLQDCATHTQPFWDVLTHRTRPPSVRVAQTTPFNTREPVMLACYVWGFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDWTPGLSPIQTVKVSVSAATLGLGFIIFCVGFFRWRKSHSSSYTPLPGSTYPEGRH
Protein: Uncharacterized protein (A0A0L0V3D9)
Organism: Puccinia striiformis f. sp. tritici PST-78
Interaction partners:
- PLK/PLK1 protein kinase
- Protein phosphatase PP2A regulatory subunit B
- Autophagy-related protein
- Calmodulin
- EF-hand domain-containing protein
- GTP-binding protein ypt3
- RING-type domain-containing protein
- Serine/threonine-protein phosphatase
- Calcineurin-like phosphoesterase domain-containing protein
- Vacuolar membrane protein
Sequence:
MLRLNIYTAILSIIVFQVVAARDTPPLLAKRSVLGLNFCLARNNLEGCRGGDQGCCANFCHSHRVMIETEAAQQFCNPGKPIEKTPDPEPKPTPPPPPPAPIPTVVQVPPPPVYQVGPPPPVYYTQAPPPVAYSPYTPAPVLVQAH
Protein: Pre-mRNA-splicing factor CWC15 (Q389E7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRYIQHKESLPAQVGIKRYRTTAAEGATLASSTAHGGDTAELVDRGIESGVCHEHEESNGGNVQSVEKRTPSLEPTCADSDSSSENEDDYDELNKERLRLEQMQRDKKQTEDRKGSIGGSATGTFSPRSEKMGIAGNGNSAVGGVSSYNHDVLFRGGKWRDKNHEPAESESKKKKKEKWEAVVNDTQRSAAYQHFMKSYFK
Protein: Ankyrin (Q24241)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTLGDVRVENKIQTRSETCAINGMALDNKNGIIKQNDATISFLRAARSGDIKKVMDFLDCGEISDINSCNANGLNALHLAAKDGYVDICCELLRRGIKIDNATKKGNTALHIASLAGQHDVINQLILYNANVNVQSLNGFTPLYMAAQENHDNCCRTLLANGANPSLSTEDGFTPLAVAMQQGHDKIVAVLLENDVRGKVRLPALHIAAKKNDVNAAKLLLQHDPNADIVSKSGFTPLHIAAHYGNVDIATLLLNNKADVNYVAKHNITPLHVACKWGKLSLCTLLLCRGAKIDAATRDGLTPLHCASRSGHVEVIKHLLQQNAPILTKTKNGLSALHMAAQGEHDEAAHLLLDNKAPVDEVTVDYLTALHVAAHCGHVKVAKLLLDYKANPNARALNGFTPLHIACKKNRIKMVELLIKHGANIGATTESGLTPLHVASFMGCINIVIYLLQHEASADLPTIRGETPLHLAARANQADIIRILLRSAKVDAIVREGQTPLHVASRLGNINIIMLLLQHGAEINAQSNDKYSALHIAAKEGQENIVQVLLENGAENNAVTKKGFTPLHLACKYGKQNVVQILLQNGASIDFQGKNDVTPLHVATHYNNPSIVELLLKNGSSPNLCARNGQCAIHIACKKNYLEIAMQLLQHGADVNIISKSGFSPLHLAAQGGNVDMVQLLLEYGVISAAAKNGLTPLHVAAQEGHVLVSQILLEHGANISERTRNGYTPLHMAAHYGHLDLVKFFIENDADIEMSSNIGYTPLHQAAQQGHIMIINLLLRHKANPNALTKDGNTALHIASNLGYVTVMESLKIVTSTSVINSNIGAIEEKLKVMTPELMQETLLSDSDDESCDDLLDHNHYKYMATDDLKANYGQDQKNFDTTNTDHDLTDVSVLNKKEILPNEMSCIELTEIGHKPDNVVIARSQVHLGFLVSFLVDARGGSMRGYRHNGVRIIVPPKACAEPTRITCRYVKPQRVVNPPPLMEGEALVSRILEMSPVDGMFLSPITLEVPHYGTLRKNEREIIILRSDNGESWREHNLYKDIIGEDINQTEEFHSDRIVRIVTQNVPHFFAVVSRVRQEVHVIGPDGGTVFSTAVPQVKAIFPPHALTKKIRVGLQAQSVDLVECSKLLGQGVAVSPVVTVEPRRRKFHKAITLSIPAPKACTNSMVNACYGNGNSSSPTLRLLCSISGGQTRATWEDVTGSTPLSFVRDSVTFTTTVSARFWLIDCRNIIDAGRMATELYSHLAKVPFYVKFVIFAKRISQTEAKFSVFCMTDDKEDKTLEQQEYFTEVAKSRDIEVLQNQIVYLEFAGNIVPILKKGEQLYTKFQPFCENRLSFSAHIKDQEFPHGRICFMTYPMVGPDEVPLKPLCTLNISVDFKTITNHLERDNLHSLNDCINAHGKLNHNENIVFGVKEQQVKKIDITKACIMSSDIKLIHEADVILDDICSHLGSDWPLLANVLGVSQADIDLVKTEFLLNDSVKQSMAMLQLWLEHGGILTGNVLAEALYKIGRSDIVEKSFKNAEFGTHQPEKVLPTAGIGKDGDYEQ
Protein: Rifin (Q8I4N7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHCSKILLFLLPLNILVTSLSNVYSKNKSYITQRHTPRYTSRVLSECDIPSSIYDNDPDMKSVKGTFDRQTSQRFEEYDERMKGKRQKRKEERDKNIQEIIEKDRMDKSLAEKVEKCCLICGCGLGGVAASVGLIGGLTVNELKKAAMVVAIAGAQKSGALAGEVARIPAAIEAVISGIEREFGVSTDGVQGLKSLFTANTYNDVTMIARAINSEYNASSCLIGRSATDNSICPWVMTKQGAAPRIQGKAVSTYEVIETAVKSIVSDAPKAAETAVETATKEFIKASTDAVESTYASCQIAIIASVVAILIIVLVMIIIYLILRYRRKKKMKKKAQYTKLLNE
Protein: Protein arg11, mitochondrial [Cleaved into: N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) (N-acetyl-glutamate semialdehyde dehydrogenase) (NAGSA dehydrogenase); Acetylglutamate kinase (EC 2.7.2.8) (N-acetyl-L-glutamate 5-phosphotransferase) (NAG kinase) (AGK)] (P31318)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000305|PubMed:1313366}.
Interaction partners:
- Probable acetylornithine aminotransferase, mitochondrial
- Arginine biosynthesis bifunctional protein ArgJ
- Ornithine carbamoyltransferase, mitochondrial
- Probable argininosuccinate lyase
- Uncharacterized aminotransferase C417.11c
- Ornithine aminotransferase car2
- Argininosuccinate lyase
- Uncharacterized aminotransferase C27F1.05c
- Argininosuccinate synthase
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MLIELQQIVKSGLVRNGAKHCTKRSLLCSNASVIASKRFQGSFAPGQQQPLNPLAKPIEQDRDAIIRILSSIGSRREVEQYLRYFTSFEAQRFAIIKVGGAIITDELDTLAQSLAFLNHVGLYPIVVHGAGPQLNKILASRNVEPEYSDGIRITDAETLSVARKVFLEENAKLVDALEKLGTRARPITGGVFQAEYLDKEKYKYVGKIVKVNKAPIEHSIRAGTLPILTSMAETASGQLLNVNADITAGELARVLKPLKVVYLNEKGGLINGETKKKISSIYLDREYDGLMKQPWVKYGTKLKIKEIKELLDTLPRTSSVAIISTKDLQKELFTESGAGTLISRGFVINKHDSLDSIPDAALENLIIQKNSLAAPSESLKQFKDTLKDRKLRIYSDSFNESVAIVDTTDSSLPVLLAFGAADNNWLNNVVDSILTTLKADFPSLLWRLQPSAKNLEWFFSKSEGTLFANNFYYFWYGVKDLNKISKFIQSDKPFADAIIQTQSTKPPTASSTTNNPSSSQINQKRSYSTSSLFSKNKKMNRSLFLKGGKRFFSAEAQKTQKPLKAVSSKPAKVVLLGARGYTGKNLIGLINTHPYLELSHVSSRELEGTKLPGYTKKEIQYVNLSTDDVKKLEEEGAVDAWVMALPNGVCKPYVDALTSANGKSVIVDLSADYRFEPSWQYGLPELNDREALRNSKRISNPGCYATGSQVGLTPILSLIDGQPSIFGVSGYSGAGTKPSPKNDLNVLTNNLIPYSLTDHIHEREISYRLKQPVAFIPHVAQWFQGITLTINVPLKKSITSRELRNLYQDRYNGEPLIHVQGDVPLVKDNAHKHHVSVGGFGVHSSGKRAVIVVTIDNLLKGAATQALQNLNLSCGYDEYAGIHLD
Protein: Leucine-rich repeat neuronal protein 3 (Neuronal leucine-rich repeat protein 3) (NLRR-3) (Q9ESY6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Clathrin heavy chain 1
- Sodium channel and clathrin linker 1
- AP2-associated protein kinase 1
- Synergin gamma
- Vesicular acetylcholine transporter
- Sodium channel protein type 10 subunit alpha
- Clathrin light chain B
- Cation-independent mannose-6-phosphate receptor
- Epsin-2
- AP-2 complex subunit sigma
Sequence:
MKDAPLQIHVLLGLAITALVQAGDKKVDCPQLCTCEIRPWFTPRSIYMEASTVDCNDLGLLNFPARLPADTQILLLQTNNIARIEHSTDFPVNLTGLDLSQNNLSSVTNINVQKMSQLLSVYLEENKLTELPEKCLYGLSNLQELYVNHNLLSAISPGAFVGLHNLLRLHLNSNRLQMINSKWFEALPNLEILMLGDNPILRIKDMNFQPLLKLRSLVIAGINLTEVPDDALVGLENLESISFYDNRLNKVPQVALQKAVNLKFLDLNKNPINRIRRGDFSNMLHLKELGINNMPELVSIDSLAVDNLPDLRKIEATNNPRLSYIHPNAFFRLPKLESLMLNSNALSALYHGTIESLPNLKEISIHSNPIRCDCVIRWINMNKTNIRFMEPDSLFCVDPPEFQGQNVRQVHFRDMMEICLPLIAPESFPSILDVEADSYVSLHCRATAEPQPEIYWITPSGKRLLPNTLREKFYVHSEGTLDIRGITPKEGGLYTCIATNLVGADLKSIMIKVGGFVPQDNNGSLNIKIRDIRANSVLVSWKANSKILKSSVKWTAFVKTEDSQAAQSARIPSDVKVYNLTHLKPSTEYKICIDIPTIYQKSRKQCVNVTTKSLEHDGKENGKSHTVFVACVGGLLGIIGVMCLFGCVSQEGNCENEHSYTVNHCHKPTLAFSELYPPLINLWESSKEKPASLEVKATAIGVPTSMS
Protein: Endoplasmic reticulum lectin 1 (ER lectin) (Q9VKC7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- HMG-coA reductase degradation 3, isoform A
- Derlin
- E3 ubiquitin-protein ligase HRD1
- Derlin-1
- Argus, isoform A
- Transitional endoplasmic reticulum ATPase TER94
- Caspar, isoform A
- Fas-associated factor 2, isoform A
- LP20373p
- Endoplasmic reticulum chaperone BiP
Sequence:
MGKSYVIIARIALLLNLIIAAVSHEAKDFDDSILYKIDFEVPDLDVQPSLGNQLRTFYTPDKEKYDCLIPTLEHQKEEEKSDKPELSPITLLQPIFSALTCTYRIEAYWSYEICHGHHVRQYHEEREGKNVKFQEYYLGKWTDEKMEILTKAWQADIKAGVKPKYKSLKIDNTRYPYFEMEYSDGTMCDIINAPRTTMVRYVCYPHGKNDIYSFKETSSCNYEAIILSSALCPIRALHAEETKELSIQCFNSESKPHRPLSMLRSELKEWVESEADLLVFKEKATENLWPKTDGDLVTLNYGGDMEKVLLEHFRNGDLKVDGDFQQLLLSIAASETGPTPITDLTPLKDFISGKNCLTGGNGWWKYEFCYGRHVRQFHKDKTSEVELFLGYFSEEAHRAWSNANPDKGARRSGFTTSIWHHYGKGTHCEQIGVPREVDVKLTCTPVTNSGTAVSMYLLEPKTCQYILVVESPTICDLIHNADSQGLVKLENLDKILVTETDKSTTSSASAPAPAPTSSTDEENHP
Protein: Gasdermin-like protein rcd-1-2 (Regulator of cell death 1-2) (P0DW10)
Organism: Neurospora crassa
Function: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition). In N.crassa, the rcd-1 locus exists as 2 incompatible alleles, rcd-1-1 (AC Q7SBA0) and rcd-1-2 (this entry). During the allorecognition process, forms a heterooligomer with rcd-1-1, thereby forming a functional gasdermin-like complex that binds to membranes and forms pores, triggering cell death. Binds negatively charged phospholipids, such as cardiolipin and phosphatidylserine. Also binds to phosphoinositides, preferentially to phosphatidylinositol-3-phosphate (PtdIns-3-P), PtdIns-5-P and PtdIns-3,5-P2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32703806}. Cell membrane {ECO:0000269|PubMed:32703806}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P57764}. Note=Cytoplasmic in the absence of rcd-1-1 (PubMed:32703806). Forms a gasdermin-like pore that associates with the cell membrane in the presence of rcd-1-1 (PubMed:32703806). {ECO:0000269|PubMed:32703806}.
Interaction partners:
Sequence:
MDNEEWFPLKQTHYPPPTIPSMKTGHPTGPISIGHIIPDLRHLDNVINCKGFEPFPPNMDVFTAHYEQCHFGDHLNSEFVVQAKAAAPIKNIVPGVDVTGSAGLHHTNITSDRWEYDSVVEYAVYPTRQYIDRLLESKEVKQYIQKSKKLLGGWCVYMVTGIMVARGGGRNVVSEEKGAGVFGNVGFQVPGIGEXAPEVGWDTKTKTKVNAHHTTDFVCAIRLVKIAKSGLRSSWTMKKVTREF
Protein: Exopolygalacturonate lyase PelX (EC 4.2.2.9) (E0SDR9)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Pectate lyase D
- Pectate lyase E
- Pectate lyase A
- Pectate lyase B
- Pectate lyase C
- Pectinesterase A
- Oligogalacturonate lyase
- Pectate disaccharide-lyase
- Pectinesterase B
- Pectin acetylesterase
Sequence:
MKYAASGLLSVALNSFLLLGSNTAFAATQDTAPVWHSIAFGQSTDVNFATNVLPDKVGVNDVTINGKKLTVNDKVDLSAPITIESRGGKIANTHDGLTFFYTQLPANVNFTLQSDVTVDQFGPESDAKPNAQEGAGLLVRDILGVPRQEPLKEGYEEFPAASNMVMNAIMTQDKKSKTDVKMQLISRDGVTQPWGNTNAQITRTSYQEKINLEQTPTFRLKLERTDDGFITSYAPKGSDQWVSKTVKGADLVTHQDKNHYYVGFFASRNAKITISNASLTTSPANTKPSAPFKAEVNAPLLQVASSPLSASDTYPVQARVNYNGTIEVFQNGKSLGKPQQIRAGDYFSLTAKLTQPKSDFKLVYVPGEGEDKTAKETSFSVEKIKLADAKNLYVSPEGKADNNGSKNAPLDIKTAINALQAGGTLRLMDGDYSATVIPVSASGNANGIKTLMPAGKKAIFHGLQLNASYWKVKGVEITEKSFRIEGSYNQIERVLAHHCDNTGIQVSSNDSVGRPLWASHNLILNSESHSNQDPSKKDADGFAIKMRVGEGNVIRGAFSHDNVDDGFDLFNKIEDGPNGVVVIGNSISVNNTSNGFKLGGEGQPVAHQVKNSIAIGNHMDGFSDNFNPGALQVTNNIALDNVRFNFIFRPSPYYGPEKQGIFKNNVSLRTQPGKYDDAVVGRVDASNYFIKNNRALNSQGKEITTANYKSVTVPAVFNRDEKGNLQLGDFLKKK
Protein: Annexin (Q803A1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAGRGTVKPQSGFNANSDAEVLYKAMKGLGTDEDSILQLLTKRSNGQRQEIKAAYKTLHGKDLVNDLKSELGGKFEDLIVALMTPPIIYEVTCLRNAIKGAGTDEKVLIEILASRSPNEVNEIKSSYKREHDKDLEEDVTGDTGGHFERMLAVLLQASRQQGIQESLIQSDAQALFAAGEQKYGTDEGQFITILGNRSNAHLRRVFEEYRKLSGFEIEESIQRETSGSLQEILLAVVKCARSVPGYFADSLYAAMKGAGTDDQTLIRIMVTRSEVDLLDIRAEFRKRFATSLHKMIQSDTSGDYRKTLLLLCGGDDA
Protein: Proteasome subunit beta (Q585C1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit beta
- 26S proteasome regulatory subunit 4 homolog
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome alpha 7 subunit
- Proteasome subunit beta
- Proteasome regulatory non-ATP-ase subunit 10
Sequence:
MLRRPPGTLLHEPSYPLTLAHEPTANGPAQTAREYFQPDAAVLDPQLSEAVSLGTTIMAVSYKDGVVLAADSRTSTGAYVVNRASNKLTKLAKRIYCCRSGSAADTQALAEQTANYLESYETDISQPVNVATAANIFKKLCYMNKWNITAGIIVAGYDPLNGGSVYSIPTGGACVKLDYALGGSGSVFLYSFFDANYKPGMTKEECIRFCQRAVAHAYSRDGSSGGLIRTIALHQGEPEDVTVPWTMTPYCMEKDPKYAELAVQNPPYSSSAKVCQNLMTSQ
Protein: Sll0985 protein (P73148)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Sll0984 protein
- Sll0983 protein
- CheY subfamily
- Uncharacterized thylakoid-associated protein sll0982
Sequence:
MIIFMKFYSLPIVITSLWNLFVVRVLPTNRKNYIFRHQRLNLSQLIALTLLTLLLSLGFAQAQSAQTLLSQLPPQIDLVDPVKSDFPLQNKAFNLGFESDLSGRIGNLDYTTVRVDGEPIFLIAVPTGNASKEGDSSLSPIVYRQQRIESKFKEIVQRGFDPETLNVASSILNGAIIIQISDDKNLRPQILRTITKADADLYALTPEDLASETVDQVRNALMRARRERQPEALRRQIKVALVIVTIVVTVSLVVLFIYRWLGHRIHLLKMAINCLVKAEEEDPNFDYNYIDASIFKNIAAIPRYSFAFQILDRIAIFLYYLSAYSKTILFGNVGWGDSKKNPPLTFSLDNQKIFENILELFQGKDFYDFLKNRLKQVVFTRRILIFFLFIIWIRGSAFFLQVFPNTRRLGRQLSGTPISLTLIWLSAIILIKISDFLIESFFHTIENDYAILQTAKYTRRKIRINTVSSAVRGINLVVCIFTAFVFSLSLFDVPVATVLAGAGIIGFAVSFGSQNLIKDLIAGISNLMSDAFAINDFVLIGEFEGVVEDTNLFVTRIRCPNGDLVTIPNGAIGTVCNQTKDWSRVDYSVMVAADADPKKAIAVLQQVALGLYHDPWWHPKMLQAPELKGIEEVSHQGILIRIWLKTLPGEQWDVARELRLRVKVAFESQEIAIGVPQQQLLMTGTGTSPLYGDEKERASKDGEK
Protein: IFNc2 (Interferon alpha-1-like) (B7SVK1)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MALQTITWMSAFLCVAHVCSMPMPCQLQGQLVRITHNLLRDMGGNFPLDCLQENVFMAFPATAFASSGAPQLSSSGATAIYETLKNIDTLFGADDLPTQWDQQKLENFQNIVYRQIDESKCMMGSVDTSDYLIRTEGLNTYFGNIAAVLKEKNFSYCAWEVVRKELLYTLQFILEHNSDSLLWANRT
Protein: Insulin-like growth factor-binding protein 5 (IBP-5) (IGF-binding protein 5) (IGFBP-5) (xIGFBP-5) (Q90WV8)
Organism: Xenopus laevis (African clawed frog)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes anterior neural development by stimulating insulin growth factor (IGF) signaling via IGF receptors.
Subcellular location: Secreted {ECO:0000269|PubMed:11709186}.
Interaction partners:
Sequence:
MEMLLPMCLLLVSLCLGQCQALGSFVHCEPCDDKAMSMCPPTPVGCELVKEPGCGCCMTCALAEGHRCGVYTEHCAKGLRCLPEQGEEKPLHALLHGRGVCLNLKNHRDQSKIDRESREEDPTTSETEDIYQSKHRGKMRLSDQKAIALNTFRQKKHSQSRIVSVEKVQSPSTPEHSIEIDMGPCRRQVETLMQEMKLSHRVYPRAFYLPNCDRKGFYKRKQCKPSRGRKRGLCWCVDKYGLKLPGIDYVNGDLQCHSFDSSNTE
Protein: ER-derived vesicles protein ERV29 (P53337)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal di-lysine motif is required for exit from the endoplasmic reticulum. Required directly for packaging glycosylated pro-alpha-factor into COPII vesicles. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11157978}; Multi-pass membrane protein {ECO:0000269|PubMed:11157978}.
Interaction partners:
- Golgi SNAP receptor complex member 1
- Endosomal protein P24B
- Protein ERP1
- Endoplasmic reticulum vesicle protein 25
- Protein RER1
- ER-derived vesicles protein ERV14
- Protein ERP2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Protein transport protein SEC24
- ER lumen protein-retaining receptor
Sequence:
MSYRGPIGNFGGMPMSSSQGPYSGGAQFRSNQNQSTSGILKQWKHSFEKFASRIEGLTDNAVVYKLKPYIPSLSRFFIVATFYEDSFRILSQWSDQIFYLNKWKHYPYFFVVVFLVVVTVSMLIGASLLVLRKQTNYATGVLCACVISQALVYGLFTGSSFVLRNFSVIGGLLIAFSDSIVQNKTTFGMLPELNSKNDKAKGYLLFAGRILIVLMFIAFTFSKSWFTVVLTIIGTICFAIGYKTKFASIMLGLILTFYNITLNNYWFYNNTKRDFLKYEFYQNLSIIGGLLLVTNTGAGELSVDEKKKIY
Protein: E3 ubiquitin-protein ligase RNF181 (EC 2.3.2.27) (RING finger protein 181) (Q9P0P0)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Catalyzes monoubiquitination of 26S proteasome subunit PSMC2/RPT1.
Interaction partners:
- B-cell lymphoma/leukemia 10
- Ubiquitin-conjugating enzyme E2 D1
- Integrin alpha-IIb
- Ubiquitin-conjugating enzyme E2 D2
- Ubiquitin-conjugating enzyme E2 E1
- Polyubiquitin-B
- E2 ubiquitin-conjugating enzyme
- E3 ubiquitin-protein ligase UBR4
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MASYFDEHDCEPSDPEQETRTNMLLELARSLFNRMDFEDLGLVVDWDHHLPPPAAKTVVENLPRTVIRGSQAELKCPVCLLEFEEEETAIEMPCHHLFHSSCILPWLSKTNSCPLCRYELPTDDDTYEEHRRDKARKQQQQHRLENLHGAMYT
Protein: WW domain-containing protein (O16786)
Organism: Caenorhabditis elegans
Interaction partners:
- WW domain-binding protein wbp-11
- Thioredoxin-like protein
- Beta-catenin-like protein 1 N-terminal domain-containing protein
- Spliceosome-associated protein CWC15 homolog
- Cell division cycle 5-like protein
- Pleiotropic regulator 1
- Heat shock protein hsp-1
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SPF27
Sequence:
MPLPPALLARLQKRGIVKQEEEVIAENYEKEPEKKSFEENSAGAPGCPNKWNQYHVCLEFCYDHWGDGTPEYRLPERYVQNKNRMLAKFPLPENWVEVYDEGLAKYYFWNKTTDEVCWYSPRHPRAIISDPAPRIAREHATVLFGDSHASEEDNAARRRNFHNKKTSRGGNDDKQSRGNNAEKRKRRDPMTSQGPDSDEDELQEMTNKDRLKRAKRKGIDPMDPAAYGDAPVGKWSDGLRVDQVTGADVTAGGPLFQQRPYPAPGAILRKQKPQDEEDDQ
Protein: Dual specificity phosphatase 18 (F2Z2P2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTAPSCAFPVQFRQPSVSGLSQITKSLYISNGVAANNKLMLSSNQITMVINVSVERGDEAGPYFAALCCWCEPLSCPVPRLPHEVPRHVPAGRPHVDQVMPAHHPTQQRLLGAAHPL
Protein: Lysophospholipase D GDPD3 (EC 3.1.4.-) (Glycerophosphodiester phosphodiesterase 7) (Glycerophosphodiester phosphodiesterase domain-containing protein 3) (Q7L5L3)
Organism: Homo sapiens (Human)
Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines. Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylcholine (lyso-PC) and N-acylethanolamine lysophospholipids. Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q99LY2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99LY2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99LY2}. Endoplasmic reticulum {ECO:0000269|PubMed:27637550}. Note=Partially co-localized with CANX. {ECO:0000250|UniProtKB:Q99LY2}.
Interaction partners:
- Autotaxin
- Glycerophosphocholine cholinephosphodiesterase ENPP6
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Lysophospholipid acyltransferase LPCAT4
- Lysoplasmalogenase TMEM86B
- Lysophospholipase D GDPD1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Group 10 secretory phospholipase A2
- Cytosolic phospholipase A2
- Phospholipase A2, membrane associated
Sequence:
MSLLLYYALPALGSYAMLSIFFLRRPHLLHTPRAPTFRIRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHFAHGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLDNHGPAARTS
Protein: Filamin A (H0Y5F3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHV
Protein: Protein snet-1 (Suppressor of nep-2) (Q11099)
Organism: Caenorhabditis elegans
Function: Negatively regulates chemotaxis and olfactory plasticity which is the change from positive chemotaxis to dispersal after prolonged exposure to an odorant. May be down-regulated in response to pheromone exposure, resulting in promotion of olfactory plasticity.
Subcellular location: Secreted {ECO:0000303|PubMed:20929849}. Perikaryon {ECO:0000269|PubMed:20929849}. Note=May be transported to neurites in an unc-104-dependent manner and secreted from there. {ECO:0000303|PubMed:20929849}.
Interaction partners:
Sequence:
MARFTPLLMILLALVPLYYSLDCRKFSFAPACRGIMLKRSGGHPMIAEQQPMIDNAKAREVQMMELLIRNIEDEALIANSDCVSMSWLRDRLVNAKNEMPQ
Protein: Dehydrogenase/reductase 2 (H0YJG9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
EQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRQVGFGDLVVHVWLGRGS
Protein: Acetyltransferase Pat (EC 2.3.1.-) (GCN5-like enzyme) (GCN5-related N-acetyltransferase) (GNAT) (Protein acetyltransferase) (Pat) (O05581)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS). This acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.
Interaction partners:
- Universal stress protein Rv2005c
- Uncharacterized protein
- DUF5642 domain-containing protein
- pH-sensitive adenylate cyclase Rv1264
- Universal stress protein Rv2624c
- Universal stress protein Rv2319c
Sequence:
MDGIAELTGARVEDLAGMDVFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDGVAIIARALPGMIVGEIALLRDSPRSATVTTIEPLTGWTGGRGAFATMVHIPGVGERLLRTARQRLAAFVSPIPVRLADGTQLMLRPVLPGDRERTVHGHIQFSGETLYRRFMSARVPSPALMHYLSEVDYVDHFVWVVTDGSDPVADARFVRDETDPTVAEIAFTVADAYQGRGIGSFLIGALSVAARVDGVERFAARMLSDNVPMRTIMDRYGAVWQREDVGVITTMIDVPGPGELSLGREMVDQINRVARQVIEAVG