wanglab/gogpt-training-data huggingface dataset:
Protein: Soluble guanylate cyclase 88E (EC 4.6.1.2) (Q8INF0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Heterodimers with Gyc-89Da and Gyc-89Db are activated in response to changing oxygen concentrations, alerting flies to hypoxic environments. Under normal oxygen concentrations, oxygen binds to the heme group and results in low levels of guanylyl cyclase activity. When exposed to reduced oxygen concentrations, the oxygen dissociates from the heme group resulting in activation of the enzyme.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Head-specific guanylate cyclase
- Guanylate cyclase soluble subunit beta-1
- Soluble guanylate cyclase 89Da
- Soluble guanylate cyclase 89Db
- Inosine triphosphate pyrophosphatase
- Bis
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
- SD08423p
Sequence:
MYGLLLENLSEYIKSVYGEEKWEDIRRQAGIDSPSFSVHQVYPENLLQKLAKKAQQVLGVSERDFMDQMGVYFVGFVGQYGYDRVLSVLGRHMRDFLNGLDNLHEYLKFSYPRMRAPSFICENETKQGLTLHYRSKRRGFVYYTMGQIREVARYFYHKEMHIELVREEILFDTVHVTFQLTFDNRAFTLASLAMTREEKHLPISAHVLFEIFPFCMVFGADMVVRSIGNSLMVILPELLGKKITAWFDLVRPLIAFKFQTILNRTNNIFELVTVDPVTERFDVQNEDLLQHEDGSEPEKSLRLKGQMVYMENWRMIMFLGTPVMPDLTSLITTGLYINDLSMHDFSRDLMLAGTQQSVELKLALDQEQQKSKKLEESMRLLDEEMRRTDELLYQMIPKQVADRLRRGENPIDTCEMFDSVSILFSDIVTFTEICSRITPMEVVSMLNAMYSIFDKLTERNSVYKVETIGDAYMVVAGAPDKDANHAERVCDMALDMVDAITDLKDPSTGQHLRIRVGVHSGAVVAGIVGLKMPRYCLFGDTVNTASRMESTSIAMKVHISESTKVLIGPNYKIIERGEIDVKGKGTMGTYWLEERENRLPLQLTAALQVHPLSPVPPTPTPKTKAIMPPVSKPLTPMMPVSVSLAASMPTSNVPAVDVMASSSSISGLALTAAAAAHMSLHHQAVVAEALTGASVEVALPSVASGATGAAAGGGAPSDDRNSRIYSPVTFKDVARRSVANSPVRSCAQPDQERRRESRSNSTGHVFMRTPSEIFGSLILDTEEFLEDLQISRSSLANNNNNQSPCGFSPTPPFRIGSAPPKPRPSNPDKFTPEELAAMDQLTPPSTAPARETASCSSASLDRDKATKLKKITFSNSSSLDATTPTALAAVVCPMRTKSPPMAVAPVMHMVQASTSKGDGQRPGSKDSVSSISLHSPPPHRSNSAPARPHSMSKAARKAFLAAKQTKAMEKLDKMIEEVQEVESQSVAKAANMRLALYGHDGGGDLAAGGCPLFLPPPPQQQQQQQQSLMPSSISDSGLCSHGHSHAPSCHHMDPKMTNSQSFQHSPRGGITHQCCSGFGHGNGRHSHRMHSNACRIL
Protein: FI18611p1 (Zinc/iron regulated transporter-related protein 89B) (Q9VEX1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- IP18018p
- FI23527p1
- Zinc transporter 63C, isoform F
- LD23375p
- Zinc transporter ZIP11
- RING finger protein vilya
- Zinc/iron regulated transporter-related protein 102B, isoform E
Sequence:
MNQTQVNNFLKCFLQIDEPSNRWTSRHDGEDLDDNDHDHDHDDDNDDDESGVLVAKVTAMVVLFCASAICGSIPFLLNRCYRWTENQTNARSAIVVKCLLYFGGGVLLATTFLHLLPEVQEVVEELQECGIIGELTFPLAELLMCCGFFLMYFIEEAMHTYVHHHQKDEAGAAFERGHSIRNSHLLKPTEGNATTPTAPPAPLAGTAELGTLSVQNLLQNDLEQQKFATKPQQQANGHGHSHGHGHGHSHLPVIADDADAGDMLASSLRGLFIVSALSLHELFEGMAIGLESSASSVWFMFGAVSAHKLVLAFCVGVELIVARTRMLLAVLYVLTFAVVSPLGIGIGILINHGEETSGPSLVSAILQGFACGTLIYVVFFEILSKNRSGLRAYLALFVGFLVMFGLQQLTSIGGHGHSHSHSSCSTSEHTHNHQETETETRSASGHTHGHQHDHDHPHHHNHAEELATVHNYEQQLQLLRQVTQKLLEAHPKKDA
Protein: Down syndrome cell adhesion molecule 1, isoform Z (Q0E9J1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVNQYYEAEVVSEYVIRGNTAVLKCTIPSFVADFLRVEAWVASDGTEYAPEEDFDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGTVSPKISTGEDFKHLKGKSSQDLSILCPAQAYPQPFFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPQIQAFDFGSEAANTGEMAGGFCMVPKGDLPMEIRWTLNSAPIITGEHGFSLSRLNPRTSSLSIDSLEARHRGLYRCIASNKAGSAEYSAELHVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Probable E3 ubiquitin-protein ligase ATL45 (EC 2.3.2.27) (RING-H2 finger A3b) (RING-H2 finger protein ATL45) (RING-H2 zinc finger protein RHA3b) (RING-type E3 ubiquitin transferase ATL45) (Q9ZT49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that possess E3 ubiquitin ligase activity in vitro and mediates protein monoubiquitination (Ref.10). Triggers the monoubiquitination of phosphorylated BIK1 in response to pathogen-associated molecular pattern (PAMP) detection (Ref.10). May be involved in the early steps of the plant defense signaling pathway (Probable).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable E3 ubiquitin-protein ligase ARI9
- Probable E3 ubiquitin-protein ligase ARI5
- U-box domain-containing protein 26
- U-box domain-containing protein 25
- Probable E3 ubiquitin-protein ligase ARI7
- E3 ubiquitin-protein ligase UPL4
- Serine/threonine-protein kinase PBL13
- Interferon-related developmental regulator family protein / IFRD protein family
Sequence:
MTRSSRFLGTASPPPPEEILAAETDMVVILSALLCALVCVAGLAAVARCAWLRRLTGVNPAAVGEAPPPNKGLKKKALQALPKSTYTASASTAAAADDLPCSSVGDGDSSTECAICITEFSEGEEIRILPLCSHAFHVACIDKWLTSRSSCPSCRRILVPVKCDRCGHHASTAETQVKDQPPHHQHPSQFTSAIIPAFLP
Protein: Protein translocase subunit SecA, chloroplastic (EC 7.4.2.4) (Q41062)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane. Facilitates the transport of precursor proteins from the chloroplast stroma to thylakoid lumen.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:7989297}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:7989297}; Peripheral membrane protein {ECO:0000305}. Note=A minor fraction is associated with the chloroplast thylakoid membrane. {ECO:0000269|PubMed:7989297}.
Interaction partners:
Sequence:
MATSSLCSSFTSQTCNPHSRPHRKTLTLPGSVFLCRQFHLNSPSVSKTRRIRTRQSGPVASLGGLLGGIFKGTDTGEATRKQYAAIVNTINGLEPKISALSDSELRDMTFASRERAQKGESLDSLLPEAFAVVREASKRVLGLRPFDVQLIGGMVLHKGEIAEMRTGEGKTLVAILPAYLNALVGKGVHVVTVNDYLARRDCEWVGQVPRFLGMKVGLIQQNMTSEQKKENYLCDITYVTNSELGFDFLRDNLATSVEELVIRGFNYCVIDEVDSILIDEARTPLIISGPAEKSSDQYFKAAKIADAFERDIHYTVDEKQKSVLLSEQGYEDAEEILAVKDLYDPREQWASFVINAIKAKELFLRDVNYIIRGKEVLIVDEFTGRVMQGRRWSDGLHQAVEAKEGLPIQNETVTLASISYQNFFLQFPKLCGMTGTAATEITEFESIYKLKVTIVPTNKPMIRKDESDVVFRATTGKWRAVVVEISRMNKTGRPVLVGTTSVEQSDSLSQQLKEAGILHEVLNAKPENVEREAEIVAQSGRLGAVTIATNMAGRGTDIILGGNAEFMARLKLREIMMPRVVKLVAEGEFVSVKKPPPSKTWKVNEKLFPCQLSNQNTELAEKAVQLAVKTWGKRSLTELEAEERLSYSCEKGPAQDEVIAELRNAFLEISKEYKVFTEEERKKVVAAGGLHVVGTERHESRRIDNQLRGRSGRQGDLGSSRFFLSLEDNIFRIFGGDRIQGLMRAFRVEDLPIESQMLTKALDEAQKKVENYFFDIRKQLFEYDEVLNSQRDRVYTERRRALQSVNLQSLLIEYAELTIDDILEANIGSDAPKESWDLDKLIAKIQQYCYLLTDLTPDLLLNECSDYEGLRSYLRLRGKEAYLQKRDIVEQQAPGLMKEAERFLILSNIDRLWKEHLQALKFVQQAVGLRGYAQRDPLIEYKLEGYNLFLEMMAQIRRNVIYSIYQFKPVLLKQDQDKMENQKSGKRNARPPTDTNPDPVGTVEPSTSASS
Protein: Oxalate oxidase 1 (EC 1.2.3.4) (Germin) (P45850)
Organism: Hordeum vulgare (Barley)
Function: Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry. May play an important role in several aspects of plant growth and defense mechanisms.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250, ECO:0000303|PubMed:8509360}. Secreted, cell wall {ECO:0000250, ECO:0000303|PubMed:8509360}.
Interaction partners:
Sequence:
SDPDPLQDFCVADLDGKAVSVNGHTCKPMSEAGDDFLFSSKLTKAGNTSTPNGSAVTELDVAEWPGTNTLGVSMNRVDFAPGGTNPPHIHPRATEIGMVMKGELLVGILGSLDSGNKLYSRVVRAGETFVIPRGLMHFQFNVGKTEAYMVVSFNSQNPGIVFVPLTLFGSDPPIPTPVLTKALRVEAGVVELLKSKFAGGS
Protein: Glucokinase regulatory protein (Glucokinase regulator) (Q07071)
Organism: Rattus norvegicus (Rat)
Function: Regulates glucokinase (GCK) by forming an inactive complex with this enzyme. Acts by promoting GCK recruitment to the nucleus, possibly to provide a reserve of GCK that can be quickly released in the cytoplasm after a meal. The affinity of GCKR for GCK is modulated by fructose metabolites: GCKR with bound fructose 6-phosphate has increased affinity for GCK, while GCKR with bound fructose 1-phosphate has strongly decreased affinity for GCK and does not inhibit GCK activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10456334, ECO:0000269|PubMed:10518020, ECO:0000269|PubMed:16542652}. Nucleus {ECO:0000269|PubMed:10456334, ECO:0000269|PubMed:10601273}. Mitochondrion {ECO:0000269|PubMed:16542652}. Note=Under low glucose concentrations, GCKR associates with GCK and the inactive complex is recruited to the hepatocyte nucleus. {ECO:0000269|PubMed:10456334}.
Interaction partners:
- Hexokinase-4
- N-acetylglucosamine-6-phosphate deacetylase
- Kynureninase
- Pro-glucagon
- Transmembrane 6 superfamily member 2
Sequence:
MPGTKRYQHVIETPEPGEWELSGYEAAVPITEKSNPLTRNLDKADAEKIVKLLGQCDAEIFQEEGQIVPTYQRLYSESVLTTMLQVAGKVQEVLKEPDGGLVVLSGGGTSGRMAFLMSVSFNQLMKGLGQKPLYTYLIAGGDRSVVASREQTEDSALHGIEELKKVAAGKKRVVVIGISVGLSAPFVAGQMDYCMDNTAVFLPVLVGFNPVSMARNDPIEDWRSTFRQVAERMQKMQEKQEAFVLNPAIGPEGLSGSSRMKGGGATKILLETLLLAAHKTVDQGVVSSQRCLLEILRTFERAHQVTYSQSSKIATLMKQVGISLEKKGRVHLVGWQTLGIIAIMDGVECIHTFGADFQDIRGFLIGDHSDMFNQKDELTNQGPQFTFSQDDFLTSILPSLTETDTVVFIFTLDDNLTEVQALAERVREKCQNIQALVHSTVGQSLPAPLKKLFPSLISITWPLLFFDYEGTYVQKFQRELSTKWVLNTVSTGAHVLLGKILQNHMLDLRIANSKLFWRALAMLQRFSGQSKARCIESLLQAIHFPQPLSDDVRAAPISCHVQVAHEKEKVIPTALLSLLLRCSISEAKARLSAASSVCEVVRSALSGPGQKRSTQALEDPPACGTLN
Protein: MxiN (Q6XVX6)
Organism: Shigella flexneri
Interaction partners:
Sequence:
MKVCNMQKGTLPVSRHHAYDGVVIKRIEKELCKTIKDRDTESKKKAICVIKDATKKAESLRIDAVCDGYQIGIQTAFEHIIDYICEWKLKQNENRRNIEDYITSLLSENLHDERIISTLLEQWLSSLRNTVTELKVVLPKCNLALRKKLELDLHKYRSDVKIILKYSEGNNYIFCSGNQVVEFSPQDVISGVKIELAEKLTKNDKKYFKELAHKKLRQIAEDLLKENPVND
Protein: Receptor tyrosine kinase (Q7KA88)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MESTTIVFVTLLTIITQRKHCAAVDVYFPTTSVKFNLPINEESESIFSKIPLAQFQVLRMEDNRLASDYLYSLEQNPLLRINSSSGEIYMRTDYRSPNSSATFLVTAFPRDQPDHELLNVSHLSLEVTPQPLEEYCSELEHICFWSSAQYTIAESHGPYRRKDFFEPVLIGALNSRAAKYLCPHVSLEYSLNAGSSHFVLKQNRLYTRQTLDHDELNGLNAKAGQLQARITCTVKLSSRDQRKFSRILDIKLLDRNDNGPKLQESSSKFDFYLEQPYFQADEEAGKKVIYVDKDTLEANAHLVYAVHNDSHGLFRPDCHAYEADHTGRPHTIVSCQLRFSRNGVFRETPYCVSLEARDLTIVSRVDAMSATANVCYHINLSKLHESEQELPQALPLRARQHRIFESEEFNGDSAGRSLSPPTVDYDKDVSVYRSAASNFRVVQPDSFLDLMRLRSIRFDIVEDKLGAFGITSTSGIVFVKNPQVLEEAPETIYFLNVTWIDQQRLSHVRVINVHLVHGRPENTSCELKVKSRSQTCAQIKYQSQCVRYCGLATGGGSCQWRGSNSAMFGTRYGSCVPESRYCPDHVCDPLEELNPMACPQDCTPAGRIVGPHSSNENKRGIYSASGTCICEDNGKCSCAPLDEEPKMKKPRKRKNETEAEPLLGVRRGTPPNQPLQDPMLLGVLNVAGFECDRSCMFFVITCPLLFVLLLLCLLIAQRKMLQRRLGKQSMTTSSKQALPESGGGDFALMPLQSGFRFESGDAKWEFPREKLQLDTVLGEGEFGQVLKGFATEIAGLPGITTVAVKMLKKGSNSVEYMALLSEFQLLQEVSHPNVIKLLGACTSSEAPLLIIEYARYGSLRSYLRLSRKIECAGVDFADGVEPVNVKMVLTFAWQICKGMAYLSELKLVHRDLAARNVLLADGKICKISDFGLTRDVYEDDAYLKRSRDRVPVKWMAPESLADHVYTSKSDVWSFGVLCWELITLGASPYPGIAPQNLWSLLKTGYRMDRPENCSEAVYSIVRTCWADEPNGRPSFKFLASEFEKLLGNNAKYIDLETNAVSNPLYCGDDSALITTELGEPESLQHLWSPPKIAYDIHDQATSYDQSEEEMPVTSTAPPGYDLPRPLLDATANGQVLRYENDLRFPLNIRKSSCTPSYSNMTSEPPATTSLPHYSVPVKRGRSYLDMTNKSLIPDNLDSREFEKHLSKTISFRFSSLLNLSETKEVSPGWQAEDAV
Protein: Uncharacterized protein (Q582A5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGLFIQQQRRWGIRGLFFHAPRVDSRRFIHLGCSQNALLRPSIAPFATNSFPLTHQKQHQHHSQTQSQYQPHHYHHKQQHHHSQTQHQTHQHQHQYSKQQQQQQQQQQLGRFSVLRPFRSGWNRFCSQCRGRKCLIVAAACILGCCSYVVLCLALWWRQQEAVGRLFSPLEEHPLEEWSLVEPTLREGDIILMMGTGEISSKITAAQYVYSGMRAAALRYSHVAVVVEPAHFDRLRSRRTSFAYDIRNNSDNGSSRSNNNSVDGNIADSVNAEYGGMLLTRPLSAGIMGEGQSLFERRPRRGAVIMEAIDNIDVNAPDVNGHVRHNCVQLVEASRRLFGRHDEKWCYRRFAVRRLKGFEWTPQRKRLLREFINENVGRPLDTNSALMLSYIHPRLYEWVGGRPHGNEISCGELIVDLYKHCGVIRRRERPITNSGVMTSGLLSPTPVTSAVALTTSLEDGVEGNKEREKECVEEYYARPSIQTAPYQFAEGEEVGVLDFAEGISLGPEVRMCHPYATQQS
Protein: Glycoprotein 3-alpha-L-fucosyltransferase A (EC 2.4.1.214) (Core alpha-(1,3)-fucosyltransferase) (Q9VUL9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes alpha-1,3 glycosidic linkages of N-glycans. Plays a role in neuronal development by promoting ventral nerve cord formation, possibly by promoting interactions between migrating cells and the extracellular matrix or by promoting neural activity.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
Interaction partners:
- Alpha-
- Probable beta-hexosaminidase fdl
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- Uncharacterized protein, isoform F
- Uncharacterized protein, isoform E
- Kekkon 6, isoform B
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Sequence:
MRRPKISLKKYFYLTLICALLLIFGFSLKEREIWKTLSPRSSQITTQQQQHQHLHQLQSMDEEHPMATSSTPPPIAATLLPEVADNLVEEPEQTVLEEEESEADRLQEPPAEKAWFFKNGEYYPKPAKTYSNRKARKRHAPRLLPHQDPYSDRIINQLMYVPHNYEEIKSSGKLKTILLYNGLGPWNVKKGRDVFLKAKCPVDTCELTANRDLASTADMILYKDHYIPTGIRRPSNSKQVSMLYYLECPYHTQNVKVPDAINWTATYRRDSTIVAPYEKWQYYDTKVQQQEQDINYSVNKTKKVAWFVSNCGARNGRLQYAHELQKYIEVDIYGACGNFKCSRSTADKCFEILDNDYKFYLAFENSNCKDYITEKFFVNALNRRVLPIVMGARPEDYEVSAPRRSYIHVDEFSSPKELAEYLRILDHDDELYNSYFKWKGTGEFINTYYWCRVCATLHNEEQLRKPRWYTDLNDWWRGPGVCTTRSWRNFKARKDVISDSSDD
Protein: Growth hormone receptor (A0A087X162)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRKEN
Protein: Peroxisomal biogenesis factor 3 (Peroxin-3) (Peroxisomal assembly protein PEX3) (P56589)
Organism: Homo sapiens (Human)
Function: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:10848631, ECO:0000269|PubMed:11390669, ECO:0000269|PubMed:21768384}; Multi-pass membrane protein {ECO:0000269|PubMed:11390669}.
Interaction partners:
- Peroxisomal biogenesis factor 19
- Peroxisomal membrane protein PEX16
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 2
- Peroxisomal ATPase PEX6
- Peroxisome assembly protein 26
- Peroxisome biogenesis factor 10
- Peroxisomal targeting signal 1 receptor
Sequence:
MLRSVWNFLKRHKKKCIFLGTVLGGVYILGKYGQKKIREIQEREAAEYIAQARRQYHFESNQRTCNMTVLSMLPTLREALMQQLNSESLTALLKNRPSNKLEIWEDLKIISFTRSTVAVYSTCMLVVLLRVQLNIIGGYIYLDNAAVGKNGTTILAPPDVQQQYLSSIQHLLGDGLTELITVIKQAVQKVLGSVSLKHSLSLLDLEQKLKEIRNLVEQHKSSSWINKDGSKPLLCHYMMPDEETPLAVQACGLSPRDITTIKLLNETRDMLESPDFSTVLNTCLNRGFSRLLDNMAEFFRPTEQDLQHGNSMNSLSSVSLPLAKIIPIVNGQIHSVCSETPSHFVQDLLTMEQVKDFAANVYEAFSTPQQLEK
Protein: Probable serine/threonine-protein kinase abkD (EC 2.7.11.-) (Q54P00)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKILKFSLLSKLKHKDFIVTSFRNNIINSIKNNNTNNNGLLKFSNNKYNFLNNNNNNNNNNVNKINNVYYINNNFKNVMENKIKPSSIQFFSSLSNKYNLNSFTTTKPQPCQAKPPSSKQQQQQQQQQQQQQQQQQQQQSKKKTSKDRLRDILKKTVITPQEFLNVLQRFAKNYKKTIASILAAIALIIYSYETPDSYFGSMMNVIVRFYRAMKCATKIMINYKILSYTPEKSSEYLEKSKICHQESADLILDLCLTNGGLYIKAGQYIASLNHILPIQYTKTLSVLQDQAPWRDFYEVESVFLKDLGNAPNHYFSDFDRLPIAAASLAQVHRAITKEGEEVAVKVQYVDLQRNFDGDIFTHNVLLTLVNMAFPDFEFNWMAEEMKNVLIKELDFSQEADNAERAAQDLSSNNNAYIPKVFRPYSSKRILTTEFIHGCKINNVQAIRSMGLSEKTVSQRFMEIMCEQIFIHAFVHVDPHAGNVLVRQHPNHPNQPQIVLLDHGLYREYDEEFRLNFCNLYKNLVLCNNKKVEKYSKALGVQNWKLFSTMILMRNFEGSSVGLSNSISSEELEKLLSGAIERLKDINLLMKAMPRHLLLILRNNNLLRSINMELGSPVNRFSIMARYAAKGLNSNSSKNSGIIRLVKSVEEKVSLEVMLKGYELYYYFVNRILSILIRLHIINPEKLIKDQMKKLG
Protein: Chromatin modification-related protein YNG2 (ING1 homolog 2) (Q5AHB8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Enhancer of polycomb-like protein 1
- Chromatin modification-related protein EAF6
- Histone acetyltransferase ESA1
- Chromatin modification-related protein EAF3
- Protein AF-9 homolog
- Histone acetyltransferase
- SWR1-complex protein 4
- Chromatin modification-related protein EAF1
- Chromatin modification-related protein EAF7
- Actin
Sequence:
MDTSTVLEKYTQDLSNLPLEVRHLLEEIKSKDVQVSEARKRYQTRDHQLHKFIRTNGTLTKHPKEDQLYSKIEEDMKLVQKLQKEKILLANTALFLISKHLYHFETDIAKLERDELLPPLEHPIELTEVSKDEYAKSLNGFSDSASATPTPRNGSSATPVAETVKKIQKKKLSVKGASSSSAQSSSASRQVKRLRSEEIEDPLPYEGGSLAFNGNVAMSINSAADANGPNGEDADNNLYCFCQRVSFGEMIGCDNEDCKYEWFHWSCVGITSPPKDDEIWYCPDCASKMEKRKKKRKN
Protein: D-aspartate oxidase (DASOX) (DASPO) (DDO) (EC 1.4.3.1) (Q99489)
Organism: Homo sapiens (Human)
Function: Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:1991137, ECO:0000269|PubMed:37805834}. Cytoplasm, cytosol {ECO:0000269|PubMed:37805834}. Note=Active in the peroxisomal matrix. {ECO:0000269|PubMed:37805834}.; SUBCELLULAR LOCATION: [Isoform DDO-1]: Peroxisome matrix {ECO:0000269|PubMed:33650155}.; SUBCELLULAR LOCATION: [Isoform 3]: Peroxisome matrix {ECO:0000269|PubMed:33650155}.
Interaction partners:
Sequence:
MDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL
Protein: Protein YIP (Q8GWB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000256|RuleBase:RU361264}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361264}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protein YIP
- Golgi apparatus membrane protein-like protein ECHIDNA
- Protein YIP4a
- Prohibitin-4, mitochondrial
- Secretory carrier-associated membrane protein 1
- Protein YIP
- E3 ubiquitin-protein ligase
- E3 ubiquitin-protein ligase
- Protein YIP
- Transcription factor
Sequence:
MMSGGNYTTIDSQKVSGSVPSVPDPGHTTVKFAESNLQTFPPSATQGKISGGSNPPRDADDSFSGHGNGSTDEPQSGGWLHKFTVGAYKPFFDVDTSDVVERLKESLFPFRGTFTEKTADKPDLYGPFWICTTLIFVAASIGTFVTYIAHKWKKQEWNYDINLVTWSAGVFYGYVTIVPLALYVVLKYFSAPSGLVQLFCLYGYSLFVFIPALCLSVVPVEIFRWVIAGVAGFMSATFVALNLKAHINSAGERSILIIASIFLLQLALAVVLKLYIFNVKV
Protein: Gamma-glutamylcyclotransferase 2-2 (AtGGCT2;2) (EC 4.3.2.7) (EC 4.3.2.9) (Gamma-glutamyl cyclotransferase 2;2) (Q84MC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and plays a significant role in glutathione (GSH) homeostasis. Converts GSH to 5-oxoproline and cysteine-glycine (Cys-Gly) dipeptide in vitro. Possesses low activity towards gamma-glutamyl-L-alanine. Has no activity towards gamma-glutamyl-L-cysteine.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8GY54}.
Interaction partners:
- Leucine aminopeptidase 1
- 5-oxoprolinase 1
- Leucine aminopeptidase 3, chloroplastic
- Glutathione hydrolase 2
- Glutathione hydrolase 1
- Putative inactive glutathione hydrolase 4
- Glutathione hydrolase 3
- Glutathione synthetase, chloroplastic
- Gamma-glutamylcyclotransferase 2-3
- Gamma-glutamylcyclotransferase 2-1
Sequence:
MVMWVFGYGSLVWNPGFHYDEKVLGFIKGYKRVFDLACIDHRGTPEHPARTCTLEKAEEAICWGTAFCVRGGPEKERLAMEYLERRECEYDLKTSVDFYKEDDPLKPAVTGVIVFTSTPDKVSNKYYLGPAPLEDMARQIATANGPCGNNRDYLFLLEKAMHDIGHEEDYVIELANEVRKVLAESSTKKVTPVKESRASRVANKSKNNVPTAHQILPHHPEAVATTI
Protein: Coiled-coil domain-containing protein 50 (Protein Ymer) (Q8IVM0)
Organism: Homo sapiens (Human)
Function: Involved in EGFR signaling.
Subcellular location: Cytoplasm. Note=Associated with microtubules of the cytoskeleton and mitotic apparatus. {ECO:0000250}.
Interaction partners:
Sequence:
MAEVSIDQSKLPGVKEVCRDFAVLEDHTLAHSLQEQEIEHHLASNVQRNRLVQHDLQVAKQLQEEDLKAQAQLQKRYKDLEQQDCEIAQEIQEKLAIEAERRRIQEKKDEDIARLLQEKELQEEKKRKKHFPEFPATRAYADSYYYEDGGMKPRVMKEAVSTPSRMAHRDQEWYDAEIARKLQEEELLATQVDMRAAQVAQDEEIARLLMAEEKKAYKKAKEREKSSLDKRKQDPEWKPKTAKAANSKSKESDEPHHSKNERPARPPPPIMTDGEDADYTHFTNQQSSTRHFSKSESSHKGFHYKH
Protein: Chaperone Ric-8 (Synembryn) (Q9W358)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins independently of G-protein coupled receptors. Acts by exchanging bound GDP for free GTP. Plays a key role in asymmetric spindle positioning, a step for asymmetric cell division that generates cell diversity during development by activating G(i) alpha protein independently of G-protein coupled receptors. In addition to its GEF activity, it plays an essential role in cortical subcellular localization of heterotrimeric G proteins, suggesting it acts as a facilitator of G-alpha function through control of its membrane targeting and/or assembling of associated components rather than a GEF. Also required during gastrulation and sensory organ precursors (SOP) formation.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:16228010, ECO:0000269|PubMed:16228011}. Presynapse {ECO:0000269|PubMed:25074811}. Cytoplasm {ECO:0000269|PubMed:25074811}. Note=Detected in both type Is boutons and Ib boutons in close proximity to synaptic active zones. {ECO:0000269|PubMed:25074811}.
Interaction partners:
- G protein alpha i subunit subunit alpha 65A)
- G protein alpha o subunit subunit alpha 47A)
- Delta-1-pyrroline-5-carboxylate synthase
- Guanine nucleotide exchange factor MSS4 homolog
- G protein alpha s subunit subunit alpha)
- G protein beta subunit 5
- Guanine nucleotide-binding protein subunit alpha homolog
- LP21163p
- Regulator of G-protein signaling loco
- G protein alpha q subunit subunit alpha)
Sequence:
METEHLKRLEAKEADHIPAILDEFNTKNADLLVFDSFRTDNLWHELWLAIFGILDDQRLSHLHTQCLNTVRILTRDEFSLQTNYIEQEVNTLLKLARIEAGSLKLPATPDELKQEEREEPQLEPSQAQSEVIAEALKCLCNLVYQSSDCRRQCLRQHCLDAILKRVASSMRHPCALEYYDMKLLFLLTALEPAARSRLQIDLNGLTYMTKWLDDKLGEDSVGEEQLNIICELLKVMFNVTSAPDKSPNEYEIQSLHLTGVLRELLLRFGDLATEKDRAVVTHAINLLTNISGSCLTELTLRCSNAELESHKEREQDNEKEKDTEAGAGAKPRECCSQCFEKRNVRSLDVLLRYLRQSLAQQEAEASSHELLSPVLTVLVKCARSDRVMRHYLRQEILPPLRDVSQRPEVGQELRNHLCRFLTLPAMILRDLSAELLFVLCKENVGRMIKYTGYGNAAGLFAKRGILDCRRVEGTDYSSDSEDSDTEEYKQQQQGINPVLGCVEPRSKSHLDDISEEQKEYEAMQLVNLIEQLRQGGIVKPAMIDKDGRPQPLEHILQLQEELPQQQLDQKRKT