wanglab/gogpt-training-data huggingface dataset:
Protein: Putative amidase C869.01 (EC 3.5.1.4) (Q9URY4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein CPT2R1.02
- Glutamyl-tRNA
- Putative aldehyde dehydrogenase-like protein C922.07c
- Putative amidase PB8B6.03
- Putative amidase C550.07
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Uncharacterized isomerase C186.06
- ATP-dependent DNA helicase tlh2
Sequence:
MKLQLLFLTLAQLAKHGLAIPLLQSSKTTTNSTLVASQEVNFTTYVYPDTNSTNIFPMPKCQNITLEDATIDQLQNYMENGILTSTDIVHCYLDRYLQVNPYVNGILQLNPDVLTIASELDDERANGIIRGPLHGIPFIVKDNFATKDKMDTTAGSYALLGSIVPRDAYVVKQLREAGAVLFGHATLSEWADMRSNDYSEGYSARGGQSRCPFNLTVNPGGSSSGSAISVASNMIAFALGTETDGSIIDPAMRNGVVGLKPTVGLTSRYGVIPESEHQDTTGPIARTVRDAVYVFQSMWGIDENDIYTLNQTGKTPEDGDYMKFLSNKTSLEGARFGLPWKRLWQNAKADEIDRLLEVVKQIEEAGAIVYNNTNFYNLDVISNDGWNWELGSVNESEYTVVKVDFYNNIKSYLSEVKNTEIHSLEDIVEYNNKYMGTEGGKPNIVPAFSSGQDGFLASLEWGGVKNETYWQAVEYVRRTSQDEGIDYALNYTDPKTNDSFILNGLLVPSGTSITYQQAAKAGYPMITLPIGVKTNGRPFGLGIMHSAWQEPQLIKYGSAIEDLLQYKAKPKFYEYVAKNVPVW
Protein: F-box protein KIB4 (Protein KINK SUPPRESSED IN BZR1-1D 4) (Q9SRV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Required for brassinosteroid (BR) signal transduction. Mediates ASK7/BIN2/SK21 inactivation both by competing with substrate binding (e.g. BZR1) and by promoting its ubiquitination and subsequent proteasomal degradation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9SU05}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9SU05}.
Interaction partners:
Sequence:
MSDSNKKTCNDAKQPILVLDLVRLVLERLSFVDFHRARCVSSVWYSASKSCIGGTNPTAPWIILFPNEHVKTNNDSCKSIDPRDHSSYTIRDLGFDMVRSRCLASSGSWFLMLDHKTDFHLLNLFTRERIPLPSLESIDGLQMKFVRTGDCGFEMSMYYKAHGLISYGKNSDLRISDAVLWVDEKNGDYFVVWFHHSTFAYHKKGGDNNSWKVFQPSKHQGCINMVFKEGKLYVLNPARNISVFDFSGGHSPVEYATPPSPNDDYYVRNLAVTLSGEVLIISSNPKKCFVKLYKIDPKSSEWRLIKSIGDEALILDLGITVAAKDGVMRNCIYFSHHELLRYKGVSLCNDDKYGICIYHIKTKKKVQEFEHLTTSSPILFKDARWFFPTFGGN
Protein: AP-4 complex subunit epsilon (Q583N8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- AP complex subunit sigma
- AP complex subunit sigma
- AP complex subunit beta
- Mu-adaptin 4, putative
- AP-3 complex subunit beta
- AP complex subunit sigma
- Clathrin heavy chain
- AP complex subunit beta
- Mu-adaptin 1, putative
- Mu-adaptin 3, putative
Sequence:
MSKLYKAQTEMVHTWEFTAFIRAVGEARSKQEEDEIIQRDLGNLRKSFETAHVEDWLLKEYVVRVLYAEMLGHPAKFAHIHCVNLSASPDLLVKRTGYLGTWLTIAPQEDIMILIVSNLLRDMNSCNFLHTAAALTAASKVVRRDLICAIKPEVVKLLDHSAPLVRKKAVIALHALYRNTADLIDYKNFFLRALGDPNPAVEAAALSPLLDIVQTNPELCRDLTETFIKVLEKVVSRRLSGDYEYQRVPGPWFQIQVMRILAALVCDSRELAAKCEYVLTEVITRADTGSTIGYAVACEAISLITRIPTIPSLIELSVETTAKMFATRNVNLRYTAIQALSNLACINTDYLRRHQEDILECLGDGDEMIRRKTTFLLLSMCNEGNVDIIVKKLIKYLNSQIDKYVLQELTQSICRTVERFSMRRLWYISTMNRLLLCAAEHVPYSSIQGMLKLIVEGGESGDEASDVAFRLRCVEDYFGLISCSQKKMPDALCRVAAWVVGEYGFLATAINRRLMVDGLCDLFARTDSGDARDWIIMAVMKIVASDGVVPENVKELIERFKDSRIATTQQRCYEFSRLTQMLPLMKRSLPLDRCCEEVDIEETLSFLNPFVQKALLGGAKPYEKRPVCREVRMEIPLCIEKYETPQLKTSEASLTCEVCDTEAKPPELAIRPSTRRWGAKTGNAAAMVNTGLAPDSHMREVGGGERITLSAQVARTGATLDEPCGVFGPQCDQSLPATPPTLGTKCSKNKKLLEDIFDASVQLKKYPHVAQQVPDLFEAVEVENKKNLAGENGSALSVHMEHVREERAVGITLFIVGNVTVNDLVVNVLPPSNCTLHVTSHSVQSAKLTGSTTITMETLKVNQSLEVVMQLLLTGFPNDMHVRVKVVYRRSEPFDMIDVGKSESKTATMTLQVGDFLRPASSMTTDTFGEMWLKYIGEYKTTLHGTAALTLESISQLLMERASLRVVEMIGNELIVAAVLPGTDQLLLGHVVLVDHHCANATFRAQDKRLAEFVVRSLDSAIPLS
Protein: Protein O-mannosyl-transferase TMTC4 (EC 2.4.1.109) (Transmembrane O-mannosyltransferase targeting cadherins 4) (Transmembrane and tetratricopeptide repeat-containing 4) (Q8BG19)
Organism: Mus musculus (Mouse)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q5T4D3}.
Interaction partners:
Sequence:
MVELDADLDHIVPSVLPPFWAKLVVGFVSLLCFARSYDGDFVFDDSEAIVNNKDLQSDTPLGDLWHHDFWGSKLSSNTSHKSYRPLTVLTFRINYYLSGGFHPVGFHVVNILLHGSISILMLDVFSVLFGGLQYTGKGQRVHLAPRASLLATLLFAVHPVHTECVAGVVGRADLLCALFFLLSFLGYCQAFKETGNKEGTHSSTFWVLLSIFLGAVAMLCKEQGITVLGLNAVFDILVIGKLDILAAVRKVLHKDKSQENAGMFKNGGLLFRIALLTIGGTSMLYIRWKIMGTGPPAFTEVDNPASFADSMLVRAINYNYYYSLNAWLLLCPWWLCFDWSMGCIPLIKSVGDWRVIALAALWLCLIGLIFQALCSEDSCKRRILTLGLGFLVIPFLPASNLFFRVGFVVAERVLYLPSAGYCVLLTFGFGALSRHTKKKKPVAAIILGILLINALRCVIRSGEWRSEEQLFRSALSVCPLNAKVHYNIGKNLADQGNQTAAIKYYREAVRLNPKYVHAMNNLGNILKERNELQEAEELLSLAVQIQPDFAAAWMNLGIVQNSLKRFEEAEQSYRTAIKHRRKYPDCYYNLGRLYADLNRHVDALNAWRNATVLKPEHSLAWNNMIILLDNTGNLAQAEAVGREALQLIPNDHSLMFSLANVLGKSQKYKESEALFLKAIKANPNVASYHGNLAVLYHRWGHLDSAKKHYEISLQLDPVAVGTKENYSLLRRKLEQTQKKDV
Protein: Tequila, isoform G (EC 3.4.21.-) (Q9VSU2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMAKWLLGLWLAILLVDRPGAKAYRSGSGYHSEQSEPVGLSATGNAHSSYGGDQQQPIYHRDSACPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVVCPSAESASTRLGRLRQLDSEPKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHKDLAKCGSGTGAVRDDTSGTGYPALPFDDLGCPPGTRGLRPHPHDVHKYLRCGIGVKPQVEQCPRGHIFDGSSSVCVYSDSPRTSSSSFTSAEIQVNYLLCPVGAVGQFVHPFDQTKFLSCKDGKSAVQNCQPNYVFSISRRYCQLKAQLAFTDYVTLIISEISYEYSLILNACPGNINGIFLYPYDAKKYVQCSSGGRMSILSCGPQMAFSVSQRSCLPSHQVHISDRVQFWQEVQVQTTYTSQDLRGNVQSQLSSLRSCPPNVQKNYPYPFHAGHYVRCQYGALEIICCPTGQLYSLSQRQCVPRSLLSAHDYLDYSYISAELSTEFMVDRSTLSCPPQAQGLYLHPFDCTKYVRCWNQQTFIESCTPGEIFSFSNQKCVPKEQCKGPTDHVEYLIETTTVTTYDSDGPESASSLAKTGDISCPPGASGNHAHPFDCTKFLECSNGQTFVKNCGPGTAFSTAKHICDHANQVDCSGRNSLPEQSQVTQNNIATSYPTKPLDILPILKTSPPSYPHAEHLTDLLCPSGVNGQFVHPFDQTKFLLCQAGKLAVQSCQSGYVFSISKSICQPKTQLVYSDYVTYKVSVISIDQTMILSACPDGTNGLHLYPYDAGKYVRCSDGGKMSIQSCENQMAFSLSQRACRPSRLLSTEDRVRFREELQIQTTYSSQDIQIQQSPLKECPSVLRGNYPYPFHAGHFVNCQNGHLQIVSCPPTALYSLSQRECVVRQLLSPHDYLDYAYISVQLSTNIIHDTTALSCPPQAQGYYLHPFDCTKYIVCWEKQTHIESCPQGEAFSISQQKCVARDKITQAYDRVEYLEDTQHELSHEEAEEEEQTEPESNLSLDGGNQPPGKYQAPYYSNGGYPTPSQNNGGYQTPSQNNGGYQAPFQNNGGYQPSYQGNGGYTPTYQNPFEGYHQPNQSSYQTNGGYQPPLPPHGGYQPPSQTYGGFQQPNRTYEDFHNPSQTVGGFQPPYSVKGGYQPHNQLNGGYNQPNQSSSFQANGGYQPPSQVNRGYQTSFESNGGYQPPLETNKGHQVPSQINGGYQPRVDGNRGYQPPNELNGGYQPPNELNGAYPAPSQLNGGYQPPLEGNLGYRPLSQQNSGYQPPQPSTGGYQPPFQSTGSGHYPGQDAPYAIPTPLLCPEKISGLFPNPFDATGYLTCIDGHTLPRQCQPLDVFSVSQGYCLPEQHVNKTDRVPFERTQTYQDNSLDCPRDFLGFVVYPFDCSKYLSCGPSGMKLLNCPGEQHYSISHGFCKPVDQVQREDRLYTINELHIIFEWTQKMMIVGAVTACPEGITGTLPHPRVPTKYLRCGPGQAEMYDCPSQQIFSVSRRVCVLDDKLSSYDRTDYLVRGVNSGWMDPSNDNRQSKSYETSGRDQFGNRYTTRTTTTTRVIGDRWTDMNMQRPSGVGVEQNPHHHHHGYNPGWSGQETSYVQRGPTQSTLYVEGSLQPNRNYPTNKTPLAPMAPTNTGGVYYGQPVEDKQNVPSRQNYSRRIDYGSPGNGWKPMPPLDPLGGQQPLNLDYSPHSPGAKEPQSQDSLPGQKPINLDYDEEPIPQYLHNGLPPYPGSPPRFYPDQLPSGSKPIGRQQPVESSPDASGYPDQQKPLDPDNGLHGSKVPPRHSPNPGYPLYNESNLYGGLLPPKPDSPVNTTPTPTPNPSSSQAPTPQLANRLHTFPIYPPVDNKTSLRNPIQPHYSPSYAGIAHSRDAPWAKVPVTSTTPAQDPDPFNPELDEPFYDDVDFLTTTVRNVLVPPPFDHKFYSPQSTNPSINRNQSASGPNSQAAIKEALKLMLRPYFNHSGNAQEQLAQQAESAIVSVISKPSTTTTTTPRPTSKTPKTDPDFDAELIKAGEQESLDSVDDDYVFPDARETSRTEQTLDPSTTYASTNFQRSTRRAELDPDTLTATTMKTNWHAPGHSRDYHRRHPNLPDPFTEHHPNSSPHQHHHHHRHPHEHSADFHIRHPELPNPFPLKNETPQHQDLNDDWDLLPNSNAEEVTPKLATRSSFNTQCDFDCGNGQCLKKEEICDGKKNCPNGKDEANCPPSDYEVRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFYAPPNQDFNYLMDEVECHGNETKLGQCAFKGWGVHNCGVDEVAGVTCKVPVMKCPNNYWLCHTSKECIPPAFVCDNTPDCADKSDECAAVCQAPVQYRLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNIFGNSNGPIWLDQVMCFGNETSIDQCNHWNWGEHNCNHTEDVALHCSAGPPPRSQRYSQTQIKGGRSLGRETTPKTYSQIGLWERSSKAVHTPRRCGIFKDDLTDEYAHREERVVRGNVAQRGRHPWQATIRTRGRGGISSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENWYLHENFRKGTHMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADHVCKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEKINESLLRF
Protein: Inactive protein-arginine deiminase type-6 (Peptidyl arginine deiminase-like protein) (Peptidylarginine deiminase VI) (hPADVI) (Protein-arginine deiminase type VI) (Protein-arginine deiminase type-6) (Q6TGC4)
Organism: Homo sapiens (Human)
Function: Catalyzes the deimination of arginine residues of proteins (By similarity). May be involved in cytoskeletal reorganization in the egg and early embryo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27545678}. Nucleus {ECO:0000250|UniProtKB:Q8K3V4}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q8K3V4}. Note=Predominantly cytoplasmic (oocyte cytoplasmic sheets), also nuclear. Released extracellularly during the cortical reaction, and remains associated with the blastomeres surfaces as a peripheral membrane protein until the blastocyst stage of development. {ECO:0000250|UniProtKB:Q8K3V4}.
Interaction partners:
- Oocyte-expressed protein homolog
- Transducin-like enhancer protein 6
- 14-3-3 protein sigma
- NACHT, LRR and PYD domains-containing protein 5
- KH domain-containing protein 3
- NACHT, LRR and PYD domains-containing protein 2
- Zinc finger BED domain-containing protein 3
Sequence:
MVSVEGRAMSFQSIIHLSLDSPVHAVCVLGTEICLDLSGCAPQKCQCFTIHGSGRVLIDVANTVISEKEDATIWWPLSDPTYATVKMTSPSPSVDADKVSVTYYGPNEDAPVGTAVLYLTGIEVSLEVDIYRNGQVEMSSDKQAKKKWIWGPSGWGAILLVNCNPADVGQQLEDKKTKKVIFSEEITNLSQMTLNVQGPSCILKKYRLVLHTSKEESKKARVYWPQKDNSSTFELVLGPDQHAYTLALLGNHLKETFYVEAIAFPSAEFSGLISYSVSLVEESQDPSIPETVLYKDTVVFRVAPCVFIPCTQVPLEVYLCRELQLQGFVDTVTKLSEKSNSQVASVYEDPNRLGRWLQDEMAFCYTQAPHKTTSLILDTPQAADLDEFPMKYSLSPGIGYMIQDTEDHKVASMDSIGNLMVSPPVKVQGKEYPLGRVLIGSSFYPSAEGRAMSKTLRDFLYAQQVQAPVELYSDWLMTGHVDEFMCFIPTDDKNEGKKGFLLLLASPSACYKLFREKQKEGYGDALLFDELRADQLLSNGREAKTIDQLLADESLKKQNEYVEKCIHLNRDILKTELGLVEQDIIEIPQLFCLEKLTNIPSDQQPKRSFARPYFPDLLRMIVMGKNLGIPKPFGPQIKGTCCLEEKICCLLEPLGFKCTFINDFDCYLTEVGDICACANIRRVPFAFKWWKMVP
Protein: BcDNA.GH06032 (Q9Y139)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MTEAAGATNPGGAAGDAESYGKEMALQSGRPKEPTKLDDLVQYVSLHVRIPTPLTGVVLPFVPLYLSAFYLWINVTGGQENDTTNNDVITADNQTTTDNITTWNDVGFIGVLAIAFLHILTLLFCYWSVHVLAFLTCRRVKLPGANVLAKVVPTPNNGNSKIVPIRSSKLEDGSTQYYFVFQKTKYVWNEDRKTFRAVEFPVNGLLSTYSSSRGLETEEDIKRATQTYGNNEMEMVVPEFHELFIERATAPFFVFQVFSVGLWCMDDYWYYSLFTLFMLIAFECTIVKQQLRNMSEIRKMGNKPYLIYAFRQNKWRHLGSDELLPGDLVSITRSQNDNIVPCDLVILRGSCIVDESMLTGESVPLMKKSLESLDNLDVEMDAEGDGKLFVLFGGTKVVQHTAPTKESLRAPDGGCIGYVIRTGFNTSQGKLLRTILFGANRATENNVETFAFIAFLMVFAVAAASYVWVKGSEDPERNRYKLFLECTLILTSIIPPDLPIELTLAVNTSLIQLTKLFVFCTEPFRIPFAGKVQICCFDKTGTLTTDNLMVEGIAGLAPNGACVPIEKAEGNTVQVLACCHSLALLDDGLVGDPLEKATLAAVDWTLTKMDSVIPKRPQFKPLKIIQRYHFSSALKRMSVLAGHLIPYSNEVKHIGAVKGAPEVIQKMLREVPADYEKVYLEYARRGARVLALGIKDLGTLGAQRVREMKREEVECDLTFAGFLIISCPMKPDSKSVIKELIQSSHKVVMITGDSPLTACHVARELRFTRKKLIILTPPEEDRKNNWSWVSIDGDQSYELDTKPGSKKLSHLLATHDLCITGEGLQYLQQNQPQYMRQLLPQITVCARFAPKQKELVITQLKQLGYCTLMCGDGTNDVGALKHANVGVSLLTSAPVKRKRTEEEQQQAAANAAAIAAQAQANANQQLTTRERALRRRQEHLNQTQARLQNALRDMEEQTMVKLGDASIAAPFTSKSSSIMCVNHIIKQGRCTLVTTLQMFKILALNALIQAYCQSVLYIDGIKFSDTQATMQGIFIAACFLFITRAKPLKTLSKVAPLPNIFNFYTISTILSQFAVHFGTLYYLTSQANILAPPREGKVKLYIDMDAEEKTKYDPNIVSSTVYIICLSLQVATIAVNYKGYPFMESLRSNRMLMYAIGASAALVILLSTGLAPELTEFFEIIDFPTDFRKTLLGVLVLDIVGAFLLDRICSFLFGETRRKSKVLNC
Protein: Apidaecin 1+ [Cleaved into: Apidaecin 1-] (C0HKX8)
Organism: Pimpla disparis (Parasitic wasp) (Coccygomimus disparis)
Function: Antimicrobial peptide active against many Gram-negative enterobacterial and plant-associated bacterial species. Not active against other bacterial species like H.pylori, P.mirabilis, B.pertussis or N.gonorrhoeae.
Subcellular location: Secreted {ECO:0000269|PubMed:7929322}.
Interaction partners:
Sequence:
GKPNRPRPAPIQPRPPHPRL
Protein: Zinc finger-containing transcription factor, putative (B9WGE7)
Organism: Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
Interaction partners:
Sequence:
MLPIAGGPQNTNHEMGDANEVQVEFSRNKIPETLIKNLPVDGKVITHGYVHGHIHKHKDHTHIHGHIHNHDHSTDLNTQINDRSIQPISKEYNQPNFNFSCPELDDLDFCKDVFCNDLDDCFYLSCGDSKNSNTCDVNCCDSRVDEICCTNDQCVEPNSVQPSSCEKSDHLECCADPRCESYDICHSNLGDQSSVCTDPNCSEIDTCCSSLPQPTLPSHSENNLCQPQLSKRPIFEDLITNVHLSCKQTQSQKTNNVYPPKKKIKCESDFDIHFPHECHQDYKKPSTTTTTNHQLHQSCFHTTIPDRKNTSLEYDEKLMSDFDFVIQFNNFNQLLNTAPKHEPQQEQPNQFSKTTDFNEESTTRPMSYSCQWENCFKRLNNNTFLNHVIEDHLEKEEIVKTENSNYQCEWNECNFTDNDFNSLINHLKSHQPSNQIETSSGSSLLNHVTNNYALTPLSCSISNDASPVVALQSPQAPDLNITSVKIVPKSKKSCKPKVKKEEKDVDLEFTCNWQVGTDDNGDPLYCNIKHQSPGELHSHLLDVHIGSGKHEYYCCWRGCERHNGKVFTQKQKLIRHIHIHTNFKPCKCDICGASFAVESVLQQHYRVHSGEKPFKCPICDKTFATSSSLSIHTRVHTGERPLACKWPGCNKRFSESSNLAKHMKIHTKKFNCEICGQSFDKKASFNRHVLEHSTEK
Protein: Leptin (Obesity factor) (Q0D250)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Leptin receptor.
- Appetite-regulating hormone isoform X1
- Leptin b.
- Adiponectin, C1Q and collagen domain-containing, b.
- Pro-opiomelanocortin protein
- Agouti-related neuropeptide.
- Melanocortin receptor 4
- Glucagon b
- Proopiomelanocortin b.
- Insulin
Sequence:
MRFPALRSTCILSMLSLIHCIPVHQHDRKNVKLQAKTIIVRIREHIDGQNLLPTLIIGDPGHYPEIPADKPIQGLGSIMETINTFHKVLQKLPNKHVDQIRRDLSTLLGYLEGMDCTLKESTNGKALDAFLEDSASYPFTLEYMTLNRLKQFMQKLIDNLDQLKIC
Protein: Beta-glucan synthesis-associated protein (A0A1D8PKB6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Kre9p
- Kre5p
- Protein ROT1
Sequence:
MASQRDLTSNNPHFHISSSRNNTNDDFNSDHNPRNPFGDEPEEEEELDSASFSSSSQNNQPHHPFATSNQTSSTNNLHSTNSIRNEAEYGKPFQAYSGYYSNGGSSSYLNQEGVISDESRLLSSGNNNNNNNNNRDVSSVGGGGGSGDNRLNPTSPAEFDRYPSMAGSRVVSSTSLVSFNNPSNMMRNHHQHQPHLGSSSSPTSSSMNNDSISDKSTSPFPNDFSPFGGYPASSFPLSIDEKEPDDYLHNPDPVQDAEYEKNRFMHDLKNMDKRSLGGLIGFIILFIAALAVFIILPALTYSGATNPYHPESYEVLTKYSYPMLSAIRMNLVDPDTPESAYKKKAKDGSEWVLVFSDEFDAEGRTFYEGDDQFFTAPDIHYDATKDLEWYDPDAVTTANGTLNLRMDAYKNHNLFYRSGMVQSWNQLCYTQGHLEISARLPNYGNVTGLWPGLWSMGNLGRPGYLGSTDGVWPYSYDSCDAGITPNQSSPDGISYLPGQRLNKCTCPGELHPNRGVGRGAPEIDVIEGEVMTDSSGKKENCGVASQSLQLAPMDIWYIPDYNWVEIYNFSVSTMNTYTGGPFQQALSATTMLNVTWYEFGDNAHNFQTYGYEYLNDPETGYLRWFVGDDPTLTVYSQALHPDGNIGWRPLSKEPMSLILNLGISNNWAYIDWPSISFPVTFRIDYVRVYQPPDQINVGCDPTDFPTYDYIQQHLNLYENANITSFEDGGYKFPKNSLIGC
Protein: Vesicle-fusing ATPase 1 (EC 3.6.4.6) (N-ethylmaleimide-sensitive fusion protein 1) (NEM-sensitive fusion protein 1) (Protein comatose) (Vesicular-fusion protein NSF1) (dNsf-1) (NSF-1) (P46461)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Subcellular location: Cytoplasm.
Interaction partners:
- Alpha-soluble NSF attachment protein
- Syntaxin-1A
- LYR motif-containing protein 4 homolog
- Synaptosomal-associated protein
- Synaptosomal-associated protein 25
Sequence:
MAYILKATKCPTDELSLTNRAIVNVGDFPEEIKYADISPAPGQHFIFALEKTVEVPSGYVGFSLVQRKWAMVSINQELEVRPYRFDASSDVITCVSFETDFLQKKTVSQEPYDSDQMAKEFIMQFAGMALTVGQSLVFNFKDKKLLGLAVKSLEAIDPKSLGEGKDTAMRNVRFGRILGNTVVQFEKAENSSLNLQGKSKGKVVRQSIINPDWDFGKMGIGGLDKEFNSIFRRAFASRVFPPELVEQLGCKHVKGILLYGPPGTGKTLMARQIGTMLNAREPKIVNGPQILDKYVGESEANVRRLFAEAEEEEKRLGPNSGLHIIIFDEIDAICKQRGSVAGNSGVHDTVVNQLLTKIDGVDQLNNILVIGMTNRRDMIDEALLRPGRLEVQMEISLPNEQGRVQILNIHTKRMREFNKINDDVDNKEIAALTKNFSGAELEGLVRAAQSSAMNRLIKADAKVTVDPEAMEKLKVNRDDFLHSLEHDIKPAFGTAQEILDNMLARGVINWGAPVSNLLEDGMLYVQQAKAPESSGLVSVLVAGAPNSGKTALAAQLAKMSDFPFVKVCSPEDMVGYTESAKCLHIRKIFDDAYRSMLSCIVVDNVERLLDYGSIGPRYSNMTLQALLVLLKKQPPKGRKLLILCTSSRREVLEEMEMLTAFTSVLHVPNLSKPDHVLAVLENTDIFSKGEIQAIGKKMAGKRVFIGIKKLLGLIDMARQTEQSQRAIKFLSKMEEEGGLDMVARQ
Protein: Serum paraoxonase/arylesterase 2 (PON 2) (EC 3.1.1.2) (EC 3.1.1.81) (Aromatic esterase 2) (A-esterase 2) (Serum aryldialkylphosphatase 2) (Q15165)
Organism: Homo sapiens (Human)
Function: Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis.
Subcellular location: Membrane {ECO:0000269|PubMed:11579088}; Peripheral membrane protein {ECO:0000269|PubMed:11579088}.
Interaction partners:
- Probable ATP-dependent RNA helicase DHX40
Sequence:
MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDIDILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNPHGISTFIDNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYCEL
Protein: Coxsackievirus and adenovirus receptor (CAR) (hCAR) (CVB3-binding protein) (Coxsackievirus B-adenovirus receptor) (HCVADR) (P78310)
Organism: Homo sapiens (Human)
Function: Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15533241}; Single-pass type I membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:11316797, ECO:0000269|PubMed:12021372, ECO:0000269|PubMed:12297051, ECO:0000269|PubMed:15364909}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:11734628, ECO:0000269|PubMed:12297051}. Cell junction, adherens junction {ECO:0000269|PubMed:12297051}. Note=In epithelial cells localizes to the apical junction complex composed of tight and adherens junctions (PubMed:12297051). In airway epithelial cells localized to basolateral membrane but not to apical surface (PubMed:11316797). {ECO:0000269|PubMed:11316797, ECO:0000269|PubMed:12297051}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:14978041}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000269|PubMed:14978041}.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted {ECO:0000269|PubMed:14978041}.
Interaction partners:
- Junctional adhesion molecule-like
- E3 ubiquitin-protein ligase LNX
- Membrane cofactor protein
- Complement decay-accelerating factor
- Occludin
- Tight junction protein 1
- Cytochrome P450 2B6
- Desmoglein-2
Sequence:
MALLLCFVLLCGVVDFARSLSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPPSNKAGLIAGAIIGTLLALALIGLIIFCCRKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTPQSPTLPPAKVAAPNLSRMGAIPVMIPAQSKDGSIV
Protein: hypoxia-inducible factor-proline dioxygenase (EC 1.14.11.29) (Q8I0C2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNQYGLSVVDDFLGMETGLKILNEVRSMYNAGAFQDGQVVTNQTPDAPAVRGDKIRGDKIKWVGGNEPGCSNVWYLTNQIDSVVYRVNTMKDNGILGNYHIRERTRAMVACYPGSGTHYVMHVDNPQKDGRVITAIYYLNINWDARESGGILRIRPTPGTTVADIEPKFDRLIFFWSDIRNPHEVQPAHRTRYAITVWYFDAKEREEALIRAKLENSKTNNLAAQAQAQQAEPDSTTTPPAAPASSASSLPVSMSTGTGALNANVSSNSCATSSEICT
Protein: AQP7 protein (Aquaporin 7) (Q6P5T0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFRWHHLPGLHWLHHPTGAPEIGGFCGV
Protein: Egg-laying defective protein 27 (Q09228)
Organism: Caenorhabditis elegans
Function: Transcription factor which promotes stress survival and delays aging. Required for cell cycle progression and development of the mesodermal and endodermal embryonic lineages. Required for normal T-cell polarity, for correct migration of QL neuroblast descendants and other cells, for embryonic patterning and for the embryonic expression of hlh-8. Also required for the transdifferentiation of the Y rectal epithelial cell to the PDA motor neuron during larval development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10226007, ECO:0000269|PubMed:22493276, ECO:0000269|PubMed:9927605}.
Interaction partners:
- Spalt-like protein sem-4
- Homeobox protein ceh-6
- Histone deacetylase 1
- Probable histone-binding protein rba-1
- Protein let-418
- Probable histone-binding protein lin-53
- DIOX_N domain-containing protein
- Helicase ARIP4
- Transcription factor dcp-66
- Putative histone deacetylase 2
Sequence:
MSRFDSQCSSEDVNKEDECVPSSSEDSQDGVSSPMENDDEPEFSQKHYDIEPCYYSLTGKSDRNCRGIVYRYRQDSDLKGFQSHDGTLYRLRDSVFVEVSQNEPYVIAAICGFKYTKRDHVVVKLTRYFRADDIPEISLNLMKQERAELEINPHLCPQSLNRELFNSELQITQPVSCLRGKCIVEYVKDVRHARTVADFSLDNDTFFFCLHYNQDSTKLASTHYAIRVGTSFQATLPPMAECSVGDDSDRDELLYRPNSIESGEEEDYIKLARCYRTYTLSGNHMLDSQKNARSLQVSDLLMDEAIIQLHRSGYKIDDALSELNANDIILTTDVDNMTQDDAKKFAKGIKQLGKNFSRIHRELLPHHSREQLVSYYYLWKKTPEATKPKQAARRVNPTSIKRPTKEKVKASRPTSTEYLDFDSASESDVENNGPSGRACHHCYGAESKDWHHANGLLLCTDCRLHYKKYGQLRQIANRPSQVPACLFKRSNSDEEESGVRTRAGKKEQRRRTPSSMSETPDRRSPSTVSNGAPNLTAEETPTKKLNGSVKRAPKRPLHNGVINNVEKSNSSEEPASPTTPPPTLTNGLTNGHGPESSTPNGETISKRMKVEPSYDDDDDEEEGKMTIDEGDDDPMPVLNGFKKEESVEEIKLELNGTIKKENGVETDPTTPTCSMEAENEVCETPAVVSVEIRDETNGETNSDLKDDENVEPDSPEDTFELGSNVEFETKNAMFVRSIVRSCGPRCARTDLIFKIKVGGVWEKSIKEKEERKKVHLQNQRIQDSEKVAIQQNQIKKEQQQSQPTPQQIHQQQAQQNAQHLQQLQQAVMLGHLPPEVLRQMMPPQFGVDPTAILMQQMMAGQQSQGVNAAFQHQMALQQQLEAHQVQFQLMMAHQHQQKMIAEQQQQQRHAAAQQLREREQREQRERERERQHQQQAQQALHQQQQQHAAAAANQLNPAMMQMMALMANSAASQQDIARLMEMAAQQQQQQQQAAQAQAQRDQERERREREAREREAAREREREQAAREAAARDQAAREHAQAVQAAAAAAQQAQALTPDMQHMHLLQQLMLNPALMMQLQQAQAQQQQQQPQVTNPLQMLQHGMAAQSANQAEMMRRIHPEPAMRPQHQ
Protein: Corrinoid adenosyltransferase (EC 2.5.1.17) (Cob(II)alamin adenosyltransferase) (Cob(II)yrinic acid a,c-diamide adenosyltransferase) (Cobinamide/cobalamin adenosyltransferase) (Q50EJ2)
Organism: Limosilactobacillus reuteri (Lactobacillus reuteri)
Interaction partners:
Sequence:
MKIYTKNGDKGQTRIIGKQILYKNDPRVAAYGEVDELNSWVGYTKSLINSHTQVLSNELEEIQQLLFDCGHDLATPADDERHSFKFKQEQPTVWLEEKIDNYTQVVPAVKKFILPGGTQLASALHVARTITRRAERQIVQLMREEQINQDVLIFINRLSDYFFAAARYANYLEQQPDMLYRNSKDVFR
Protein: Fas apoptotic inhibitory molecule 1 (Q9NVQ4)
Organism: Homo sapiens (Human)
Function: Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MTDLVAVWDVALSDGVHKIEFEHGTTSGKRVVYVDGKEEIRKEWMFKLVGKETFYVGAAKTKATINIDAISGFAYEYTLEINGKSLKKYMEDRSKTTNTWVLHMDGENFRIVLEKDAMDVWCNGKKLETAGEFVDDGTETHFSIGNHDCYIKAVSSGKRKEGIIHTLIVDNREIPEIAS
Protein: Strongylocin 2 (EeStrongylocin 2) (A0A144LVM3)
Organism: Echinus esculentus (Sea urchin)
Function: Has antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria with minimum inhibitory concentration (MIC) between 0.78 uM and 3.13 uM.
Interaction partners:
Sequence:
MNIRTASFTFIVVMMILSQTMADRFFNEPEEDDHLVESWNPFKKIAHRHCYPKNECITTNGKKTCKDYSCCQIVLFGKKTRSACTVVAQ