wanglab/gogpt-training-data huggingface dataset:
Protein: Cysteine protease CP14 (Low-temperature-induced Cysteine proteinase-like) (T2BRA8)
Organism: Nicotiana tabacum (Common tobacco)
Interaction partners:
- UPF0235 protein At5g63440 isoform X1
- UPF0235 protein At5g63440 isoform X1
- Mitochondrial succinate-fumarate transporter 1-like
- Developmentally-regulated G-protein 3-like
- DNA polymerase epsilon subunit
- Mitochondrial succinate-fumarate transporter 1
- DNA polymerase epsilon subunit
- Developmentally-regulated G-protein 3
- UPF0235 protein C15orf40 homolog
- UPF0235 protein C15orf40 homolog
Sequence:
MGSIQIPYRHFLLLPLFLILAALYSQVSAFTTDFPILDRPTEFLSEERVFQLFQEWKQRHGKVYKNEKEEEMRLDKFKRNVKYIVEKNSKKKSDSDHFVGLTKFADMSNEEFRQVHTSNIKIPFNKRKTIQMRSVERKPSTASCDVPPSKDWRKHGAVTEVKNQDQCGACWAFSACGAMEGINAIATGELISLSEQELINCDNSYNTGCDGGLMDPAFEWVMNNSGINSEADYPYTASQGRCNYDKVNHKVVIIDGYQDVPEDENALLCAVGQQPVSVGIDGSSLDFQLYRGGIYDGECSSNPDDLSHAVVIVGYGSEGDDDYWIIKNSWGTSWGMEGYAYIRRNTYLPYGVCAINSLASYPTKEASSAPSPYPSPAVPPPPPPSPPPPPPPSPKPSECGEFYYCPEDQTCCCELYFFGICFIQGCCPYENGVCCHGSEFCCPADYPICDVYEGLCLKDYRDNIGVAARKRRMAKHKLPWRANTEATEERDQTLKWKRNHVAAMR
Protein: Precursor of CEP12 (PCEP12) [Cleaved into: C-terminally encoded peptide 12 (CEP12)] (P0DN99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that may regulate primary root growth rate and systemic nitrogen (N)-demand signaling.
Subcellular location: [C-terminally encoded peptide 12]: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}. Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
Interaction partners:
- F-box protein At2g43440
- F8M12.2 protein
- Primary amine oxidase 1
- Precursor of CEP9
- Amine oxidase [copper-containing] gamma 1
- Amine oxidase
- Amine oxidase [copper-containing] alpha 2, peroxisomal
- Protein GOLVEN 8
- Amine oxidase [copper-containing] gamma 2
- Amine oxidase [copper-containing] zeta, peroxisomal
Sequence:
MVNRDNSIVALSFFMLFLLVLHLHFETTTAARKPVRVFGPPSSIEWSPPSPPKDDFEWFEINIYKNIEQTAFRPTGQGPSQGIGHKDPPGAP
Protein: Synaptotagmin-like protein 4 (Exophilin-2) (Granuphilin) (Q8VHQ7)
Organism: Rattus norvegicus (Rat)
Function: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:12058058}; Peripheral membrane protein {ECO:0000269|PubMed:12058058}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12058058}; Peripheral membrane protein {ECO:0000269|PubMed:12058058}. Note=Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles.
Interaction partners:
- Ras-related protein Rab-27A
- Syntaxin-binding protein 1
- Ras-related protein Rab-27B
- Ras-related protein Rab-3A
- Ras-related protein Rab-8A
- Unconventional myosin-Va
- Syntaxin-1A
- Syntaxin-binding protein 2
Sequence:
MSEILDLSFLSEMERDLILSVLQRDEELRKADEKRIRRLKNELLEIKRKGAKRGSQHYSDRTCARCQEGLGRLISKSNTCVGCNHLVCRECRVLESNGSWRCKVCSKEIELKKATGDWFYDQKVNRFAYRTGSDIIRMSLRRKPAVNKRETVGQSLLQQTQMGDIWPGRRIIQEQQKEQSVLFEVPKLKSGKSALEAESESLDSYTADSDSTSRRDSLDKSGLFPEWKKMSAPKSQVEKEIAPGNQNAVCGDEGDMIFKKNTRKVLRPSEYTKSVIDLRPEDVAQESGILGDRSKSVPGLSVDMEDEEEEEEDIDHLVKLHRQKLARGSMQSGSSMSTIGSMMSLYSEAGDFGNVSVTGKIAFSLKFEQKTQTLVIHVKECHQLAYADEAKKRSNPYVKTYLLPDKSRQGKRKTSIKRDTINPLYDETFRYEISESLLAQRTLQFSVWHHGRFGRNTFLGEAEVHMDSWKLDKKLDHCLPLHGKISTESSPGLPAHKGELVVSLKYIPASKLPVGGDRKKSKGGEGGELQVWIKEAKNLTAAKSGGTSDSFVKGYLLPMRNKASKRKTPVMKKTLNPHYNHTFVYNGVRLEDLQHMCLELTVWDREPLASNDFLGGVRLGVGTGISSGEVVDWMDSTGEEVSLWQKMRQYPGSWAEGTLQLRSSMVKQKLGV
Protein: Uncharacterized protein C9G1.07 (O14303)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C16C6.04
- Meiotically up-regulated gene 113 protein
- Uncharacterized protein C1494.08c
- Uncharacterized protein C56F8.02
- Uncharacterized protein C14G10.04
Sequence:
MDDLLNSVSFSNASNPHNAWGSENISNSNSAIPSITNDVSFSMEASVWKENALNLDTFNLKDINEKLDYTFGVVKPPKRISLASKDYIGITATSETNFRQLIRLGYNEKSLGELKQGTISRLLKEHMTLWNQERSNVNRKSNVLFCWSTAYQKQKRKTASYTNSPVTPPINDKNILLPEQSPLSNFSTTKISSINVPSDILDFSNLSSNEIPKDYSSSTALLNNTVAVKQDHKLSANTFLSSPVKLIERESNSCSTISINKEDEVVPKSPLSLDRKKVDEVEEHSSIAKLDSEEKIRETKKKNSSTSLSPDPTSDNFEWGSWVSSQDTSKNSSNLASASVDDVSEESQVEPNTLIFQNFSSPSTSLSAPKDTPAVIQSINTSFLNNERAGRGNIKTVDQNQLINRIVDKLPDLSYLVD
Protein: Uncharacterized membrane protein YFL051C (P43552)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane; Single-pass membrane protein.
Interaction partners:
- Putative uncharacterized protein YNL150W
- Uncharacterized membrane protein YNL033W
- Uncharacterized membrane protein YFL067W
- Uncharacterized membrane protein YNL019C
- VEL1-related protein YOR387C
Sequence:
MSIPHSVFSALLVFVALATTTLASTEACLPTNKREDGMNINFYEYTIGDQTTYLEPEYMGYEYSNTKKLGSVSGQTNLSIYYSPPCESTPTCVTYAVLKRDEDGYDPCGPLYETKKRDTEYCDPNTAYWSSDLFGFYTTPTNVTVEMTGYLIWSMGNRRR
Protein: Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (Neolactotriaosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.275) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1] (P15291)
Organism: Homo sapiens (Human)
Function: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
Subcellular location: [Isoform Long]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903, ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Cell surface {ECO:0000269|PubMed:1714903}. Cell projection, filopodium {ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of Golgi but is mainly localized at the plasma membrane (PubMed:1714903). B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:1714903}.; SUBCELLULAR LOCATION: [Isoform Short]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Note=Found in trans cisternae of Golgi. {ECO:0000269|PubMed:1714903}.; SUBCELLULAR LOCATION: [Processed beta-1,4-galactosyltransferase 1]: Secreted {ECO:0000303|PubMed:2120039}. Note=Soluble form found in body fluids. {ECO:0000303|PubMed:2120039}.
Interaction partners:
- Alpha-lactalbumin
- Beta-galactoside alpha-2,6-sialyltransferase 1
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6
- Beta-1,3-galactosyltransferase 1
- Beta-1,3-galactosyltransferase 2
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5
- Alpha-
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- Beta-1,3-galactosyltransferase 5
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
Sequence:
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPLQGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVPHTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Protein: Probable 6-phosphogluconolactonase 2 (6PGL2) (EC 3.1.1.31) (Q8LG70)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24008768}.
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 3, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Gluconokinase
- Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic
- Inactive glucose-6-phosphate 1-dehydrogenase 4, chloroplastic
- Glucose-6-phosphate 1-dehydrogenase 3, chloroplastic
- Glucose-6-phosphate 1-dehydrogenase 5, cytoplasmic
- Glucose-6-phosphate 1-dehydrogenase 6, cytoplasmic
- Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic
Sequence:
MAPVKRRVFKTNNEMAVELAKYTADLSSKFCKERGVFTVVLSGGDLIAWLWKLLEAPYIDSIEWSKWHIFWVDERVCAWDHADSNYKLAYDGFLSKVPVPAENIYAIDNGLGAEGNAELAAERYEECLKQKVNQNIIRTYKSSGFPQFDLQLLGMGPDGHMASLFPGHAQINEKVKWVTSITDSPKPPSKRITLTLPVINCASYNVMAVCDKEQADSVAAALNHTKDLPAGRLTADVEVVWFLDQAAASKLPHGWCSIL
Protein: ARM repeat superfamily protein (F4JR52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATSADARAVKSLNTSEGRKRFVFKSASQRTNDIDNISNYRNLDKVKAEPSEGSTFFRDCLIEWRELNTAEDFILFYEEMLPSVQSLSLIIMQKERIFSNLVSRLQMKARLSLEPILRLIAALSRDLLNDFIPFLPQIVNSFVTLLNNGAHNDPEIIQQVFTSWASIIVSLQKYLVCDIEGILRDTLELRYYPKDNISEFMSESMSFLLRKAQDEQLEKGMKMILSEVAHPSKKAGGVGVLYNVMRGTYGRLHSKAGRVLSFLLKDSTLSFLDNFPQGPCTVVEVVSLVLQRICEDLEAEKLSAMWEYLYKKINKSISNKKSVHLSRLLSVLMAVVKIKEGRKVHDIPSLIGIVSRIVSTFFTSSETAVEGDNLSAVLDEVLELILCTINTVNEMETVASLWAPIFALKSSSLLTFLREFLKKDQSVVKAFTKNILCAINNMIWESSEEVIPLLLTLCEEHKTQQTSHDVVNSISQTFESRYERIHEFLEAKIKKVQQNIENAGLAQINEAELAAIWGVVKCYPYFKVDSSLLICFKKTLRQHLAVSDDTCSGPELMWQSLLGTTLRSCYKMTGINHSDLEEALSFAKDYKSCEQVLSPVADVLEFMHRPALAHGRSKPYPELQANKAGDAFEIFSENLRHPNKNIRLMTLRILCHFETLSSDPSFEEHPPKKKMKTEKNVLQLLLLFEETAPTVDTSRMLAGYISTIQDNLSAGRIHSAYVKLVLNGMLGILHISYRPLCVQASECLAVLVRKYTGAVWSDFVCYLGQCQLKFETLHDHSENANQSMSERHACNLNLNGRFNLFLFPPSAITPTATVSDVVSQLLQTLQKASSVAQSRASEILPLLLKFLGYNSENPGSVGSYNGRVCKGEDWKTVLVQWLTLLKLMKNPRSFCFSQFLNDILQNRFLDDNDAEIQTNVLECLLLANDFLLPHRQHLLNLIKPKELREELTTWNLSENIGEPHRSYIFSLVIRILMPKVRTLKNSASRKHTSIRHRKAVLCFISQLDVNELALFFALLIKPLNIISEETMDSFWSSGKSSLDYFQNSNFLKYFTVDTISTLSRNQKFGFLHVIQHILEVFDELRVRPFLDFMMGCVVRLLVNYAPNVDEEMNIDSLALRNVTAAPSTSDDKENASINHDQAGTAFKQFKELRSLCLKIIAHVLDKYEDCDLGSEFWDLFFSAVSPLIKSFKQEGSSSEKPSSLFSCFLSMSKSRNLVNLLCREESLVPDIFSILTVTTASEAIKSSALKFIENLLCLDNVLGEDENMIRGFVDPYIEALINSLHSLFIGDILKRKSVKYHGEREIKILKLLSKRMQDRSHVMKYLDVLLSFLNKSVKDPDIRREALLAIQDIIAYLGMESTSKIINTVSPLLVDAELDVRLCICDLLESLAKIDFSLDDVAKRVRDMNAISAMEVDDLDYEKIVNAYVEINADFFIKSSEQHTMIILSQSSILCREAPAHSEFGKEVKNADVSWTGDRVLCILRNFILKHIGDAINRGGIIIKEWILLIREMVTKLPDAANLSAFRPLCSEDENVDFFKAIVHIQAHRRARAISRFSSVVKDSSLPEGVVRKLLVSVFFNMLLEGQDGKDNNVRNACTEALASISAHMSWTSYYALLNRCFREMNKHTKKGKILLRLICLILDKFHFAKDGYPHEAEEIRTCLQKIVFPRMQKLMNSDSDNVNVNSSVAALKVLKLLPEDVLDSNLSSIVHKIASFLKNRLESTRDEARLALVACLKELGLEYLQVVVNILRAILKRGSEVHVLGYTLNSILSKCLSNPTCGKLDHCLVDLLAVVETDILGEVAEQKEVEKFASKMKETRKRKSFETLKLIAENVTFRSHGLKLLSPVTAQLQRHLTPKIKTNLEKMLKQIAAGIEGNTSVDQGDLFLFIYGLVDDGINNRSGLGDQVSLPPSKKKKKSRDLKETSGLCFGPKSCPHLITVFALDLFYNRMKKLRLDNTDEELLSKCFTSLVKFPLPSLTSEADELKTALLTIAQSAVSSSSPLVQSCLKLLTTLLKNINITLSSEQLKMLIQFPIFIDLESDSSFVTLSLLKAIMNRKLVVPEIYDIAIQVSKLMVNSQLESIRKKCKHILLQFMVHYTLSEKRLEQHVNFLLENLRYEFPTGREAVLDMLHALILKFSEPNLGKQSVLDQQSQKLFIQLTVCLSNETDRKVLPLVGAVIEVLIGRMSKDQVDSSLLYCLCWYKQQNLSAAAAQVLGFFISAMKKTFRKHIYNTVEDARTILESAISASSLQLQDTVEEASLPFWKEAYYSLVMIEKMLEQFPDLRFGKDLERSPARKITALALSASITTLDLDIWKMVFKFLLHPHAWLRNKSCRLLNLYFEALAGRKRPECRTLVADSLLEKPSSLFMVAVSLCFQLKEQPTTGNIDVDLLTANIVFAVSSLHSLIGQFDQATHNRFWSSLGEDEQVVFLKAFEVLDAGKGRSTFLALTSGKRTENGDDDVRNVMIGSLLKRMGKIALDMESVQMRVMFNVYKSFASQLNQEECRLYAYKILLPLYKVCEGYTGKIVTDELKQLAEEVRDSIRDKSLGNKMFVEVYSEIRNSLRTKRDKRKREEKLMAVVNPERNAKRKLRLASKNKANKKRRMTSMKLSRWACS
Protein: Thiamine diphosphate dependent-3-acetyloctanal synthase PigD (ThDP-dependent enzyme PigD) (EC 2.2.1.12) (Q5W251)
Organism: Serratia marcescens
Function: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the decarboxylation of pyruvate, followed by the modification of the resulting two-carbon fragment acetaldehyde at the C3 position of the 2-octenal (1,2-addition of acetaldehyde) giving 3-acetyloctanal. In vitro, it can act on a number of alpha,beta-unsaturated carbonyl compounds, including aldehydes and ketones, and can catalyze both 1,2-addition and Stetter-type 1,4-addition depending on the substrate.
Interaction partners:
Sequence:
MRAATAACRDRRGLCRAEFARLAEAVTPFWLHKELIMTTLTGQARLTNSAAYEQVWQAERQACRTDADPDTLTVGVVVVTRNPAFFQTGLSVLNDIRDYVFNRVHIQSEMPLKLLDLAADSLYLAAREKALHFLKGQNKAINVRIIQCASLAEATGKIIYTHALEQRPEFHLGMLFYDQTTPAGVDDSIEQIDRDLDAFYSALQRSGIPAFYTTFSTVAFIRQLRSPFRYLPQQYREIVRSEDPAIFQTELLCLWMDFFEMNYTNRRVKPIGALALHNTLGEQLIQFFERTAAERWLVSYYTGSIISNLIGYLDRHAEARGALILRGPNEHAIACGAMANWQLYRMPFLGVVTSGMMDEFKGTLANLKETAAQGIIVAAENRGNQWYSFQGTLTPTEDMREVLIARRIPFVYIDDVEMIGAGLTEAFRLYHQGQGPVVILATQNVLESTLSLEGAVCDPSPIPVLSADDPLPMSESLAQAIALINRGPERLVWQLGPVSDDEYALIHDIADAAGIALVDSLAHPGSAPKYYQGRRNPHYLGTLAIYGYSPRVYNFLHTNDKLNAMSEQSLFMIKSRVAQITTPFSDGRLERKVHLVQLTHDDRHLSAYADLHLHMNCLAFLRTVKAHLDVDPALRERRRALIAAYLDSPSDVVSQLPSLPMSANYFFCQLNRVIEELIETEGFDFTGVYDVGRCGISAARNVAKTRRGFSGWYGRALMGDALLATGYLAYTSPSHVMAFIGDGAKGIVPDILPAFIDNILTHPQLLNKSITVFYLCNGGLSVINTYQERILFNRTSRQMRLVNVEQPDVEQTVNNFHIQSKTLTHFDEDVIRQALTTSHRLNLFSVVLGHNNEGDGISPGHRQRLAALIRADHDALQERKAWAAQQPESTSTAFDQDPTQEATS
Protein: Protein ZNRD2 (Autoantigen p27) (Protein zinc ribbon domain type 2) (Sjoegren syndrome/scleroderma autoantigen 1) (Zinc ribbon domain-containing protein 2) (O60232)
Organism: Homo sapiens (Human)
Function: Might play a role in mitosis. Antigenic molecule. Could be a centromere-associated protein. May induce anti-centromere antibodies.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32170109}.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
Sequence:
MALNGAEVDDFSWEPPTEAETKVLQARRERQDRISRLMGDYLLRGYRMLGETCADCGTILLQDKQRKIYCVACQELDSDVDKDNPALNAQAALSQAREHQLASASELPLGSRPAPQPPVPRPEHCEGAAAGLKAAQGPPAPAVPPNTDVMACTQTALLQKLTWASAELGSSTSLETSIQLCGLIRACAEALRSLQQLQH
Protein: Cysteine/Histidine-rich C1 domain family protein (T5A14.16 protein) (Q9ZVU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEPPPPHFSRAKPPCRLSDPAQPHKLCRRRRPSYPPLSICFTCKGKQLRSSAYYYYCATCNLEFHRGCHIFLPVIRSSFHPSHPLTFFSSDPKFDVSIIPKYWRDSSATEESSDESINQLTIEYLGDVSDDDGEDSHSDHDLGASEDDGEDSHSDHDLGASDDDGEDSHSDHDLGARDDDGNGNGAGDVHADGEASLSDGNHLKCKCCGVPLQMTYYHCSICKFNLNLDCSMRQPPPIISHLKSHEHTLTLFPIRLPLPCDACGLSLNDTEDLVYSCLPCSRMVHRSCIYLPRVIKITRHQHRLSHTSSLQPGDFSCGVCRQTVDVNYGQYSCNKECHYAVHSKCATRNDVWDGKDLDGVPEEPDEFIEPPFLKIDEETIQHFSHHHYLKLHEKKTIYKRDKFCEACTLPVMISQRFYGCMQCDFVLDETCASLPRKKNHPLHKHPLNLHTLPLGESAMINKGATSKDIFKCIGCGRIGCGFYYKCDEKNCDEFLLDVRCASLPDPFVHDCHPHDHPLFFNLTKGNCMGCGSDSCSSYFLECIKCKSFLGIKCATLPCEAHYTHDRHPLTLCYEEEEDTTSGQYWCEICEFKLDPKTWFYTCDYCMITLHVNCLLGKDIYLKPCHIFKVGLFYKEVEIARNDGNSRLFCYICRLRCGQTLVFKWLGRRKSFCTLRCIGKYVKDTRGYYDAVAMGYFESYPTNLVTSPEASDSSVIKSAFDFLFRD
Protein: FI01543p (Rebuf) (A1Z8Q9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uninflatable, isoform C
Sequence:
MISRRKIISRSLDNLDAIGQEEQEEDVWHDREKLFRDHINEVLSKWEQIDDEIWAKIIVFEKNRRVAKAYARSSVITINGSKNGFDGVRIGLNGFDNPMRDAETKVIKKSIGDGFKIKMDDTGNIFIKRYGKSSIYVNSTSQGNEETVIGGDIIQMPQMSLTAATSARLFDMKKFQTNINREFARTYPERGRLERQCLSAVSLVKSNNNLINSPVWILVVNVVAMDMLRSRLQTIPKSLDAMGMRVPLTNSSEDPYSTIESQVGLIYPTPAASDDSQNSQHSSNSSKGRRSIFSAAFLNEGPYVPKPDYESGGSLTPIYADKKRQKSSGSQQRKKQDDPYYCGLLARIPNFIKSSKQPCPGGASKPKKEPKISRKISAQHQQQQFLQPAQPIPIATFHHSYFPYKLYPPQHRLSQSQMSLWDARSLISAHE
Protein: Sorting nexin (Q803H8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTSISEDSDKEKARSVSVDLNNDASLLIDIPDALCERDKVKFTVHTKTTLSPFQKPDFSVPRQHEDFIWLHDAIVETEEYAGLIIPPAPPKPDFEGPREKMHKLGEGESSMTKEEYAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSFSKDRNFHIFLEYDQDLSVRRKNAKEMFGGFFKNMVKTADEVLISGVKEVDEFFEQEKIFLLDYSNKIKDSTAKAEKMTRSHKNVADDYNHISGALNSVAADNNSAFKKHLEKCVEVFEKLRKVEDRVASDQELKLTELLRYYTRDIQAAKDLLYRRARALADYENSNKALDKARLKGKDVPQAEENQKQCLQKFDRLSESGKKELTSFKARRVVAFRKNLIEMTELEIKHAKNSMSTLQGSIELLKSN
Protein: Protein TIC 100 (Protein EMBRYO DEFECTIVE 1211) (Translocon at the inner envelope membrane of chloroplasts 100) (AtTIC100) (Q8LPR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope. Plays an important role during embryogenesis and chloroplast biogenesis.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:23372012}.
Interaction partners:
- Protein TIC 56, chloroplastic
- Protein TIC 214
- Protein TIC 20-I, chloroplastic
- Protein TIC 40, chloroplastic
- Protein TIC110, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic
- Translocase of chloroplast 159, chloroplastic
- Protein TOC75-3, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic
- Protein TIC 22, chloroplastic
Sequence:
MANEELTESQQQEDPSQQLPNADEEKGSDSDSNSDSDASSQSSGDDFYISESENEAEGDNTIFNYVRPSDIPPDPNANPETNIRRFNRVLDGKRVKRMQEEEEDKYTFYEDLFDFPRDPERWKEQDLREIWADGPLEMTKPGWDPAWADEDDWDVVNDEIQEGRDPGIQPFYVPYRKPYPAIPDNHYDIENAKGVVEELDRIEEFLQWVSYIFPDGSSYEGTVWDDLAQGKGVYIAENGLVRYEGEWLQNDMEGHGVIDVDIPDIEPIPGSKLEAKMRAEGRIIKRDYMTPEDRKWLEMDVEDSVALTDGNFQVPFYENEEWVTQFGEKPEKGRYRYAGQWKHSRMHGCGVYEVNERILYGRFYFGELLEEEHGCTVDICALHSGLAEVAAAKARMFVNKPDGMIREERGPYGDPQHPYFYEEDDVWMAPGFINQFYEVPEYWETYVGEVDQEREMWLNSFYKAPLRLPMPAELEHWWENVEVTPEFVLLNKEPEPDPNDPSKLVQKEDPVILHTPTGRIINYVEDEKHGIRLFWQPPLEEGEEVDPSKVEFLPLGFDEFYGKEVVVKKEHPIKSFVLGIEKSVKPMLDGLEKWTEEKKKAYEERKEMIQQELELVEAEICLEEAIEDMDEELKKKEQEEEKKTEMGLTEEDEDVLVPVYKEEKVVTAKEKIQENKQEEKYKDDDDEDDDDGDDDDDDDDDDDLGPSSFGSADKGRRNSPFSSSSLSFASCTLFPAVQSRLESSFLAWKQHRAEPSKVNTGIIKGADTASASIHFPPLSSNNARLKMGKVANRGCVQRSYGSSRSQSQLMSLSRLLSCNASSSSSPPDSSSSEYLKDSGLWETPVGDMSVVLSLQIQTKCSDLFAETPAVS
Protein: Ras-related protein RABC1 (AtRABC1) (Ras-related protein Rab18) (AtRab18) (O23657)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Kinesin-like protein KIN-1
- At3g14910
- Syntaxin-32
- Protein COLD-REGULATED 15A, chloroplastic
- Rab3 GTPase-activating protein catalytic subunit
- Rab3 GTPase-activating protein catalytic subunit
- Vesicle-associated membrane protein 711
- Vesicle transport v-SNARE 12
Sequence:
MGSSSGQPEFDYLFKVLLIGDSGVGKSSLLLSFTSNTFDDLSPTIGVDFKVKYLTIGEKKLKLAIWDTAGQERFRTLTSSYYRGAQGIIMVYDVTRRDTFTNLSDIWAKEIDLYSTNQDCIKMLVGNKVDKESERAVSKKEGIDFAREYGCLFLECSAKTRVNVEQCFEELVLKILETPSLTAEGSSGGKKNIFKQNPAQTTSTSSSYCCSS
Protein: Oxygen sensor protein DosP (EC 3.1.4.52) (Direct oxygen-sensing phosphodiesterase) (Direct oxygen sensor protein) (Ec DOS) (Heme-regulated cyclic di-GMP phosphodiesterase) (P76129)
Organism: Escherichia coli (strain K12)
Function: Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate. Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.
Interaction partners:
- Diguanylate cyclase DosC
- Diguanylate cyclase DgcM
- Cyclic di-GMP phosphodiesterase PdeH
- Probable diguanylate cyclase DgcE
- Probable diguanylate cyclase DgcC
- Signal transduction histidine-protein kinase BarA
- Diguanylate cyclase DgcP
- Diguanylate cyclase DgcZ
- Diguanylate cyclase DgcN
- Probable diguanylate cyclase DgcJ
Sequence:
MKLTDADNAADGIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI
Protein: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (hPNGase) (EC 3.5.1.52) (N-glycanase 1) (Peptide:N-glycanase) (Q96IV0)
Organism: Homo sapiens (Human)
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15358861}.
Interaction partners:
- UV excision repair protein RAD23 homolog B
- Transitional endoplasmic reticulum ATPase
- UV excision repair protein RAD23 homolog A
- E3 ubiquitin-protein ligase AMFR
- Derlin-1
- 26S proteasome regulatory subunit 4
- UBX domain-containing protein 1
- Ubiquitin thioesterase otulin
- Cytosolic endo-beta-N-acetylglucosaminidase
- TRAF-type zinc finger domain-containing protein 1
Sequence:
MAAAALGSSSGSASPAVAELCQNTPETFLEASKLLLTYADNILRNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIERSSRLDGSNKSHKVKSSQQPAASTQLPTTPSSNPSGLNQHTRNRQGQSSDPPSASTVAADSAILEVLQSNIQHVLVYENPALQEKALACIPVQELKRKSQEKLSRARKLDKGINISDEDFLLLELLHWFKEEFFHWVNNVLCSKCGGQTRSRDRSLLPSDDELKWGAKEVEDHYCDACQFSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRAVGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYVIAFSKDEVVDVTWRYSCKHEEVIARRTKVKEALLRDTINGLNKQRQLFLSENRRKELLQRIIVELVEFISPKTPKPGELGGRISGSVAWRVARGEMGLQRKETLFIPCENEKISKQLHLCYNIVKDRYVRVSNNNQTISGWENGVWKMESIFRKVETDWHMVYLARKEGSSFAYISWKFECGSVGLKVDSISIRTSSQTFQTGTVEWKLRSDTAQVELTGDNSLHSYADFSGATEVILEAELSRGDGDVAWQHTQLFRQSLNDHEENCLEIIIKFSDL
Protein: Phosphodiesterase YaeI (EC 3.1.4.-) (P37049)
Organism: Escherichia coli (strain K12)
Function: Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP).
Interaction partners:
- Prophage antitermination protein Q homolog QuuQ
Sequence:
MISRRRFLQATAATIATSSGFGYMHYCEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVLFDMSLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFGERHIYTTRGVGSLYGLRLNCRPEVTMLELV
Protein: Cell division activator CedA (P0AE60)
Organism: Escherichia coli (strain K12)
Function: Activates the cell division inhibited by chromosomal DNA over-replication.
Interaction partners:
- Uncharacterized protein YdjO
Sequence:
MKKPLRQQNRQIISYVPRTEPAPPEHAIKMDSFRDVWMLRGKYVAFVLMGESFLRSPAFTVPESAQRWANQIRQEGEVTE
Protein: Nuclear export factor-a isoform 2 (Q99JG5)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
GQFTEDGELGVVKVTVPCGRKYDKTQLMNSIHSLCSVPFTPVDFHCDKHRIQFFVPDFRIASALKDISYKIHNEYFQKIPIFVNPSVAPYSVQNRFTKEEMEQLKLAMRKRYDVSQHALCLKKLRFDPDLMKNNIHMILNHRSCMAATLQIIQENFPKLLSLNLSSNKLFQLDSLIDVVKKAPQLKILNLSKNMLRTVWELEKMKGLKLEQLWLEGNPLCSTFPDRSSYIRAVLECFPELSYPDGRKLLPPTVMNTQERKLMKPCKDIFMGSEVIKNQVHRFLREYYLMYDSEERQGLLNIYHDQACFSLTIPFNPNDPDLNSMYVYFKDENDMKNFKEFHIQRQLLKYTKQDIVECLRGFPQTLHAFSSFQVNICFQMETMLCFSVCGLFKEEGTPKECVRAFMRIFIALLGSSNMYIVNDQLFVRNPSSEEINSAFVIPSPTSYSNFKLVLSQEQQRMVQAFSTQSGMKLEWSQKCLEDNKWDYARAAEVFTMLQTKCKIPKEFFKQ