wanglab/gogpt-training-data huggingface dataset:
Protein: Enoyl-CoA hydratase, mitochondrial (mECH) (mECH1) (EC 4.2.1.17) (EC 5.3.3.8) (Enoyl-CoA hydratase 1) (ECHS1) (Short-chain enoyl-CoA hydratase) (SCEH) (P14604)
Organism: Rattus norvegicus (Rat)
Function: Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-CoA) to the corresponding 3(S)-3-hydroxyacyl-CoA species through addition of a water molecule to the double bond. Catalyzes the hydration of medium- and short-chained fatty enoyl-CoA thioesters from 4 carbons long (C4) up to C16. Has high substrate specificity for crotonyl-CoA ((2E)-butenoyl-CoA) and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA) and methacrylyl-CoA ((2E)-2-methylpropenoyl-CoA). Can bind tiglyl-CoA (2-methylcrotonoyl-CoA), but hydrates only a small amount of this substrate (By similarity). Plays a key role in the beta-oxidation spiral of short- and medium-chain fatty acid oxidation. At a lower rate than the hydratase reaction, catalyzes the isomerase reaction of trans-3-enoyl-CoA species (such as (3E)-hexenoyl-CoA) to trans-2-enoyl-CoA species (such as (2E)-hexenoyl-CoA), which are subsequently hydrated to 3(S)-3-hydroxyacyl-CoA species (such as (3S)-hydroxyhexanoyl-CoA).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:9480773}.
Interaction partners:
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Peroxisomal acyl-coenzyme A oxidase 1
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
Sequence:
MAALRALLPRACNSLLSPVRCPEFRRFASGANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSGKFLSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKANFKDH
Protein: Diaminobutyrate--2-oxoglutarate transaminase (EC 2.6.1.76) (Diaminobutyric acid transaminase) (E1V7V7)
Organism: Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
Function: Involved in the degradation of ectoine, which allows H.elongata to utilize ectoine as both a carbon and a nitrogen source for growth. Probably catalyzes the conversion of L-2,4-diaminobutyrate (DABA) to L-aspartate beta-semialdehyde (ASA) by transamination with 2-oxoglutarate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Aspartate-semialdehyde dehydrogenase
- N-alpha-acetyl-L-2,4-diaminobutyric acid deacetylase
- L-2,4-diaminobutyric acid acetyltransferase
- Aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- Diaminobutyrate--2-oxoglutarate transaminase
- Ectoine hydrolase
- L-threonine dehydratase family protein EutB
- FAD-dependent oxidoreductase
Sequence:
MTTHKDLIDRDRKVTFHASTHLRDFAHGDAPGRVITGGKGIKIVDKDGREFIDGFAGLYCVNIGYGRSEVAEAIYQQALEMSYYHTYVGHSNEPQIALSEKILELAGPGMSKVYYGMSGSDANETQLKIVRYYNNVLGRPQKKKVISRMRGYHGSGIASGSLTGLKAFHDHFDLPIETIRHTEAPYYYHRAAEQEGMTEREFSKHCAAKLEEMILAEGPDTVAAFIGEPVLGTGGIVPPPEGYWDEIQAVLTKYDVLLIADEVVCGFGRTGSDFGSHHYGIKPDLITIAKGLTSAYQPLSGVIVGDRVWEVLEQGTGEYGPIGHGWTYSGHALGCAAGLANLAIIEREGLTANAAETGAYLQERMKAAFADHPVVGQVRGVGMMAALEFSVDPAARRHFDPSLKVGPRMSAAALEEDLIARAMPQGDILGFAPPLTTTREEVDEIVARTERAVNKVTDALTREGAIQAA
Protein: Dynamin-like protein C (EC 3.6.5.5) (Q55AX0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in cytokinesis. May hydrolyze GTP.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Dynamin N-terminal domain-containing protein
- Uncharacterized protein
- Rac guanine nucleotide exchange factor B
- Guanylate-binding protein
- Protein SEY1 homolog
Sequence:
MSHQQQQAHFDISSNSTLTTNTIATTTNASVSSSPQLNKAQMAIAEAMALKMHEEEKKKREEKKRKRDNEELLSKQVRTKLENERKKLDDSESINASTNQELYSLFNDLQMISHDHNISFDTPELVVVGMQSDGKSSFIESLLGFQFNIVETNIGTRRPLIIQMINNPSKQQPSCRFKKEDYSNSYGGSSSSTSTTSGNSNHNTDKQQNVSSSQGGGGGSNNLNEDKWEEYETPVNELTEEIIRRTNERTGRAGDRVSSIPIFLRVEFAHCSNLNIYDTPGFRKGGDERLKYEISEMVKKLIEPKNRIIVCLEQSNVEWANTISRPLVKKIDPDFSRTILVNTKFDNRVKELRNRESAHKYLEGEGIIAQKKPFFISLPLKRNLETHRFKDAMKETFLDDYRKLLEIGFDENRFGGQIGIYKVRQYVENLLHEKYQQNLLPSMLQLESICKKTEADIVRVKKELSDNNIVTLKEKVMRFVSNFNGQIERLLEGSVVGDPDEFGQTLLQEKENCSVQPWPGYNFDFDIQNSNYSLYGGAQYERLLNEFEFVIHSKEFPETSINEVASAIGVSKSHNSPIYELAATNIFQTKSKKVLLPLIDIVLQRSSYIMKRLFDISVSILGKDENESSHTVSLYEHFLKELQSQYEKFIQTIESECKSRLKDDFEMFTKIVDWNLLSGLTEIKPYNYLKVSPEETKQRVISIMDCKKLEDEPLSRSRNIDDDTYQKVCMIAGRLFSGIRFFFSKLIRNKLNAFFLDPMFQKLGSFVTDYFSKLNDQKYEEMFQLGLKELENKLHKLEFQLIDCKKNRDKFKDVYNRMKQSLNQNQNQNSSSSSNSASSSNNNVIIKHQQSLNGKFSTPDKNSLTMSPFTSPFTQSNYHQHNNNNYQINQQPLDINNDHYFDQN
Protein: RH35718p (Q8MYV4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVLDMESDDSHASSASNSSESRSNSPTNDKDEVVADHGGESPGGGGDPILDRSDRAPSTSSSSSNSSSSSNRSDLSKKQKKSSSSSSGSGSGSGSSSSSGSSSEDEGDQEPEQEVQRLSEQQREQQQHSPINERESESAAGTPVNADQPGSPNAKSQPSSFLSSVRSRSVSPQLYNQAAVDLNISHDDLSDVSDIEGEEKRTSSKNSMRPADENEDGAISNDSLPTLGEEDEVEQKQSTPNGKASSGDEKEPFAKETHTDDASNGLAPATALQEDLVKTHDDDALDFEAEEGECPEQAKEPSPMESTANETNQTKSTTKVSQDEGDDDGEVDKDGDDKDGDDKDTRKDGAGNGCLEDGAGNDSRKDDAGNGCLEEGEEEKDIVSVSTSSSQEKVEEGELEEGEVSDEDEKRPEETEPKPVCRFYTRGQCTWGMSCRFLHPGVTDKGNYTMFDNVIRPVPMQGGSTGASAPAAPSSTAAPRAGGSAYSSHASATADYHDYRTERPLHHRPPLLHAPSIYGAPVHDARTLLPDGAPVVVENAWERGLRTAKEMMRKANKRKEQDMDFEDKKMNLTLSPDEMEKDSYYLKDRGGSSARSPPPPSANVREQPLNPLSMPLSMHPHAVAHANPRALLPLQYSVYGPPPDRYGRPQYMPPQYDDVDAYGRMTRYRELPPHRMPHYEDDRRSRPTREVIVQRVEAAGRGDEWSDLWMRSKSVGRGSYEREDRRRRDRRSYSSNSSYSTSNSSQSDSSSDSSRSSSPSDHKRRYGSHKLATATATSRRHGGRAARSPSQIPRRPRRTSKGSLSPSYKRPAVDKRGVGHSPSSKRKKLSSPAPKKFDKLRRRRSSSSSDSDSSDTSYSDSESGSSSSDSSSGSRETPQKRVRATDKALNERKLISKPAEQSTKKRSPISIEIKKTSNMVGVSALASASNSADSDAEKDHDNGKDKEKDHVKEKDKDCKEKDKDKDGMKDKEGKKSRREELLKQLRAVEDAIAKKRSKLN
Protein: Ribonuclease H2 subunit B (Ribonuclease HI subunit B) (A0A2R8YEC1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKNGLMFVKLVNPCSGEGAIYLFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKGNPEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKMAAQRQKRGK
Protein: CCDC28A protein (Q7Z6N9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPKKNAIPVSKSTGFSNPASQSTSQRPKLKRVMKEKTKPQGGEGKGAQSTPIQHSFLTDVSDVQEMERGLLSLLNDFHSGKLQAFGNECSIEQMEHVRGMQEKLARLNLELYGELEELPEDKRKTASDSNLDRLLSDLEELNSSIQKLHLADAQDVPNTSAS
Protein: Short transient receptor potential channel 4-associated protein (Trp4-associated protein) (Trpc4-associated protein) (Protein TAP1) (Rabex-5/Rin2-interacting protein) (TNF-receptor ubiquitous scaffolding/signaling protein) (Protein TRUSS) (Q9JLV2)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRPC4AP) complex specifically mediates the polyubiquitination and subsequent degradation of MYC as part of the DesCEND (destruction via C-end degrons) pathway. The DesCEND (destruction via C-end degrons) pathway recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The DCX(TRPC4AP) complex specifically recognizes proteins with an arginine at the minus 3 position (R-3 motif) at the C-terminus, such as MYC, leading to their ubiquitination and degradation (By similarity). Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome. Involved in JNK activation via its interaction with TRAF2. Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEL6}.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- Cullin-4B
- DDB1- and CUL4-associated factor 4
- DDB1- and CUL4-associated factor 5
- DDB1- and CUL4-associated factor 6
- DDB1- and CUL4-associated factor 8
- DDB1- and CUL4-associated factor 12
- DNA damage-binding protein 2
- E3 ubiquitin-protein ligase RBX1
Sequence:
MAAAPAAAGAGASRGRRLAATAAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKLSKWSGIPQLLLKLYATSHLHSDFVECQSILKEISPLLSMEAMAFVTEDRKFTQEATYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQELEEWYTWLDNALVLDALMRVANEESEHNQAPTVFPSLGTSEEGGLPHTSARAQLPQSMKIMHEIMYKLEVLYVLCVLLMGRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQELNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGLLEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFENQVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKKYPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE
Protein: Chaperone protein DNAJ, putative (Q57VQ3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP-dependent protease ATPase subunit HslU1
Sequence:
MSYGKWAGVYSPHFLMSHVTMCRRVAHILWRRPSCSPQRSRSDTESPFGYVETLVSRPRAYARSTPLMTSAALLRSGLTARTGIRFATLPPAWPQVTARRFASAGQRAPTYDEVRDACSVLGVDVDSDPKHLKKIYRGLVQKHHPDAGGDAAAMSRITVAYNRLKDLSKLEREQFKAQQATYRGGSYHYSSRAGSSGNGTPSYDTSGRYAAQGSHDAGTSYDYRGASNADYFKQTANPRRGFYTYKQSDRSFTDNPFSTSNPFSMHAQVRRAWNMPMSSILLRAIVAYLGICVLFLLAYRRYRDWMHDDGWKMAESFARHERLAELQRLRQEMNDRIQSSREAAAAERLDAQRYSLARGFGGQSGTDYNVVTTSKERELRALERARRQRIENNTIARGWPFIPEEKGRLVVRAHHPPGVVFFEPSRREEQLRQLTNMQRGRAWSDANQSLAEGAAVNPQSVVSDELNAVRAIRTILNGIHDGGQAENRVL
Protein: Transcription factor TCP7 (Q9FMX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Two-component response regulator-like APRR1
- Transcription factor TCP21
- Transcription factor TCP5
- Transcription factor TCP13
- Transcription factor TCP17
- Transcription factor TCP3
- Anthocyanin acyltransferase-like protein
- Transcription factor TCP24
- Transcription factor TCP2
- Transcription factor TCP4
Sequence:
MSINNNNNNNNNNNDGLMISSNGALIEQQPSVVVKKPPAKDRHSKVDGRGRRIRMPIICAARVFQLTRELGHKSDGQTIEWLLRQAEPSIIAATGTGTTPASFSTASVSIRGATNSTSLDHKPTSLLGGTSPFILGKRVRADEDSNNSHNHSSVGKDETFTTTPAGFWAVPARPDFGQVWSFAGAPQEMFLQQQHHHQQPLFVHQQQQQQAAMGEASAARVGNYLPGHLNLLASLSGGSPGSDRREEDPR
Protein: Large ribosomal subunit protein bL19m (39S ribosomal protein L19, mitochondrial) (L19mt) (MRP-L19) (Q9VHN6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P49406}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- GM03767p
- Large ribosomal subunit protein uL29
- FI01658p
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL5
Sequence:
MNLSTRVMLNRLTQQCVYKRIVTFSTKTAEHVIENQEEQKKEAPPTTPTSPVNRKTIIPANYRFVYPEFLPDPKVEWRNLVREKLERLDMLDRRKQIDLPEFYVGSVLAVTSSDPHAAGKTSRFVGICINRDRCGLRARFILRNVIDHQGMEVVYELYDPTILKIEVLRLEKRLDDSLFYLRDALPEYSTFDENMEAEPLEEGAPVPVNDIKVVLRPRPWLERWERQNLRGVANIDEYLKDKHRLSAAKVQKPWEKYDMMKDYRSSIPEEEQTEIFAEVHTELHALELQRKRNKRKRTFIKPKQLA
Protein: Transcription factor bHLH3 (Basic helix-loop-helix protein 3) (AtbHLH3) (bHLH 3) (Transcription factor EN 34) (bHLH transcription factor bHLH003) (O23487)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor MYB10
- Transcription factor MYB1
- Anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
- Dihydroflavonol 4-reductase
- Protein TRANSPARENT TESTA GLABRA 1
- Naringenin,2-oxoglutarate 3-dioxygenase
- Leucoanthocyanidin dioxygenase
- Transcription factor MYB75
- Transcription factor TT2
- Transcription factor MYB114
Sequence:
MGQKFWENQEDRAMVESTIGSEACDFFISTASASNTALSKLVSPPSDSNLQQGLRHVVEGSDWDYALFWLASNVNSSDGCVLIWGDGHCRVKKGASGEDYSQQDEIKRRVLRKLHLSFVGSDEDHRLVKSGALTDLDMFYLASLYFSFRCDTNKYGPAGTYVSGKPLWAADLPSCLSYYRVRSFLARSAGFQTVLSVPVNSGVVELGSLRHIPEDKSVIEMVKSVFGGSDFVQAKEAPKIFGRQLSLGGAKPRSMSINFSPKTEDDTGFSLESYEVQAIGGSNQVYGYEQGKDETLYLTDEQKPRKRGRKPANGREEALNHVEAERQRREKLNQRFYALRAVVPNISKMDKASLLADAITYITDMQKKIRVYETEKQIMKRRESNQITPAEVDYQQRHDDAVVRLSCPLETHPVSKVIQTLRENEVMPHDSNVAITEEGVVHTFTLRPQGGCTAEQLKDKLLASLSQ
Protein: Probable nucleoredoxin 1 (AtNrx1) (EC 1.8.1.8) (O80763)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase required for pollen tube growth and pollen function in the pistil. Seems not to be required for in vitro pollen tube growth. May be involved in the generation of lipid signaling molecules in pistil.
Interaction partners:
- Non-specific lipid transfer protein GPI-anchored 4
- GDSL esterase/lipase At2g31550
- WAT1-related protein At1g70260
- Cation/H
Sequence:
MAETSKQVNGDDAQDLHSLLSSPARDFLVRNDGEQVKVDSLLGKKIGLYFSAAWCGPCQRFTPQLVEVYNELSSKVGFEIVFVSGDEDEESFGDYFRKMPWLAVPFTDSETRDRLDELFKVRGIPNLVMVDDHGKLVNENGVGVIRSYGADAYPFTPEKMKEIKEDEDRARRGQTLRSVLVTPSRDFVISPDGNKVPVSELEGKTIGLLFSVASYRKCTELTPKLVEFYTKLKENKEDFEIVLISLEDDEESFNQDFKTKPWLALPFNDKSGSKLARHFMLSTLPTLVILGPDGKTRHSNVAEAIDDYGVLAYPFTPEKFQELKELEKAKVEAQTLESLLVSGDLNYVLGKDGAKVLVSDLVGKTILMYFSAHWCPPCRAFTPKLVEVYKQIKERNEAFELIFISSDRDQESFDEYYSQMPWLALPFGDPRKASLAKTFKVGGIPMLAALGPTGQTVTKEARDLVVAHGADAYPFTEERLKEIEAKYDEIAKDWPKKVKHVLHEEHELELTRVQVYTCDKCEEEGTIWSYHCDECDFDLHAKCALNEDTKENGDEAVKVGGDESKDGWVCEGNVCTKA
Protein: Acyltransferase easC (EC 2.3.1.-) (Emericellamide biosynthesis protein B) (C8VPT2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics. The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain. EasB produces several polyketides that can be further processed by the downstream enzymes. The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD. The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA. EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues. A last step of cyclization leads to the production of emericellamides.
Interaction partners:
- Acyl-CoA ligase easD
- Nonribosomal peptide synthetase easA
Sequence:
MEETNVKLSVPLSEDVIKLSALDQQIMRFYAKAVFIFERDSSKTSIDIVHHLKQGLAVTLSEIPDLAATIAPVPNSHRKDLELRIGPNSGVPFKVVDQTKQESWVYGTYPDLAAKHFPTSDIPHDILFIPQPQPSADGLPAAFLQVNIIDGGVIIAISWHHSVCDARGISILIDAWARHTATSLANGKPDLPATPAEGSRDRWRLDHGLREVTIDQLPEYTIDSSAREDPSGSYLLDRENPVTVPYSVSTWYFSASSLKALRDALAQVENDESTQFTKVEAVSALVWKHMSIARQLDRSNPDGSSLFTTRLDFRARTKPPFPDTFIGNINEPTARVRLPIAEICRASTPESLTTLAEAVRAATENTTEQSMRTLIGLVNDAPAVTDVAWKYNYFPGPDLGVTDISNIDAMKKNWGAGLGTPTCVRSYSRETGLLYLFPQDDDGGFEIQVQCEVEAVERLKADETFTRYCEFKRASAYNA
Protein: Metallothionein-3 (MT-3) (Growth inhibitory factor) (GIF) (Metallothionein-III) (MT-III) (P37361)
Organism: Rattus norvegicus (Rat)
Function: Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro (By similarity).
Interaction partners:
- Metallothionein
- Metallothionein 2, pseudogene 1
- Metallothionein-2
- Probable proton-coupled zinc antiporter SLC30A3
Sequence:
MDPETCPCPTGGSCTCSDKCKCKGCKCTNCKKSCCSCCPAGCEKCAKDCVCKGEEGAKAEKCSCCQ
Protein: PH domain-containing protein DDB_G0275795 (Q1ZXL0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSSVRAQFAEVQEQLNQVHSLVDSNTPSDLNKAATILKSLLPVYKDLSGNEESKRPENLEILKEIKSRLTEETQRVMSKKEEAKSLQIQQQQQQQQLLQQQQQQQILESTTRNRQASQQELPKPPILSGYLKKQGDKGLVRSFKKRWFLQRDTKLFYYEKEGDSEPYGFVNLPEMINVKTVDSGFELATPSRVYVFQVFKPSDLTYWTEGLKEFKKYYQSLQNSQKFGANANGNGNSSPNMSSSGSYSDFRKYSESSQQPLNSSTGAINTTPQRGTPIKDRRGTVSGGTTEYSHSSSSTAPDSPTLSSSYVPPPSSSNLNPQDEELKRRENEIIRKHQEKLKQQDDQQQDDKQQQQQQSQEPPQQQQQQQEQLQSQPSQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPPQTSPQNSRHGSTNYSQLQQQQQQPQQQPQQQSSPQVIISNNNSPRFESQQQQNNFHNNGSNINLESFRQSIEDELNKKFLKEKQDLMEFEIKKRLEIESEIKKLQLQLDQTKTDAEEKQNKSSNELKKKKAEIEDYEARVTIITKRNEEMDAKIKELESSRPVETFPHEFLWTEEVNSRDLLIASQSKRILELEEQLKLKDNAVTVIKRENEMLRQETEKKDKYINELLEKGGGSGIHTNSNNNNNSNNNNNNSNNNSNTDKIKESMVAHQTQNAFLLQEIQRLETQSQFKLDIKIQQIEELENQLEQQLYQFHRFREAIIGTMSNEYCVKIEKENLDVKKEYFQSLGVSIKLHRVKEGYFANIDINSLFDKVIKENVHYRNWPEWISNQFNQA
Protein: Gasdermin-A (Gasdermin-1) [Cleaved into: Gasdermin-A, N-terminal (GSDMA-NT); Gasdermin-A, C-terminal (GSDMA-CT)] (Q96QA5)
Organism: Homo sapiens (Human)
Function: This form constitutes the precursor of the pore-forming protein and acts as a sensor of infection: upon infection by S.pyogenes, specifically cleaved by S.pyogenes effector protein SpeB in epithelial cells, releasing the N-terminal moiety (Gasdermin-A, N-terminal) that binds to membranes and forms pores, triggering pyroptosis.
Subcellular location: [Gasdermin-A]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17471240}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5Y4Y6}.; SUBCELLULAR LOCATION: [Gasdermin-A, N-terminal]: Cell membrane {ECO:0000269|PubMed:35110732, ECO:0000269|PubMed:35545676}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.
Interaction partners:
- Gasdermin-E
- ORM1-like protein 3
- Caspase-1
Sequence:
MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVRTDYTLLDVLEPGSSPSDPTDTGNFGFKNMLDTRVEGDVDVPKTVKVKGTAGLSQNSTLEVQTLSVAPKALETVQERKLAADHPFLKEMQDQGENLYVVMEVVETVQEVTLERAGKAEACFSLPFFAPLGLQGSINHKEAVTIPKGCVLAFRVRQLMVKGKDEWDIPHICNDNMQTFPPGEKSGEEKVILIQASDVGDVHEGFRTLKEEVQRETQQVEKLSRVGQSSLLSSLSKLLGKKKELQDLELALEGALDKGHEVTLEALPKDVLLSKEAVGAILYFVGALTELSEAQQKLLVKSMEKKILPVQLKLVESTMEQNFLLDKEGVFPLQPELLSSLGDEELTLTEALVGLSGLEVQRSGPQYMWDPDTLPRLCALYAGLSLLQQLTKAS
Protein: Sucrase-isomaltase, intestinal [Cleaved into: Sucrase (EC 3.2.1.48); Isomaltase (EC 3.2.1.10)] (P14410)
Organism: Homo sapiens (Human)
Function: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.
Subcellular location: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border.
Interaction partners:
- Pancreatic alpha-amylase
- demerged
- Alpha-amylase 2B
- Alpha-galactosidase A
- Lysosomal alpha-glucosidase
- Probable maltase-glucoamylase 2 pseudogene)
- Neutral alpha-glucosidase C
- Hexokinase HKDC1
- Hexokinase-1
- Hexokinase-2
Sequence:
MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDSGKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMTTTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEFTGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISTRLPSDYIYGIGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSNAMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRWNYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQKYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNPNCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMYSKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAHWLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSRNHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHEFYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDMYLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDTIQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMNAHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGCVWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRVEVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRSSGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPPGYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGPTPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDIDYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVFVKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVDFYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEAEQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGDNYARWDNMDKSIIGMMEFSLFGMSYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNIANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKPTWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDTINLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLYLSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNEDTTNMILRIDLTTHNVTLEEPIEINWS
Protein: Homeobox protein Hox-A9 (Homeobox protein Hox-1G) (P31269)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15657436}. Cytoplasm {ECO:0000269|PubMed:15657436}.
Interaction partners:
- Pre-B-cell leukemia transcription factor 1
- Homeobox protein Meis1
- Nuclear pore complex protein Nup98-Nup96
- Pre-B-cell leukemia transcription factor 3
- Homeobox protein Hox-A7
- Homeobox protein Hox-A10
- RNA-binding protein Musashi homolog 2
- Histone-lysine N-methyltransferase 2A
- Protein AF-9
- Pre-B-cell leukemia transcription factor 2
Sequence:
MATTGALGNYYVDSFLLGADAADELSVGRYAPGTLGQPPRQAATLAEHPDFSPCSFQSKATVFGASWNPVHAAGANAVPAAVYHHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPGALSFAGLPSSRPYGIKPEPLSARRGDCPTLDTHTLSLTDYACGSPPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE
Protein: FI09243p (GEO12728p1) (Listericin) (A1Z8G7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD31543p
Sequence:
MKQYLVLALVFAAILAMISGHPLEEQKITLEDAEAQPGIDDGTGVRAARHFGGGFGRGGYCCGGGGGFRRGGFGGGGYGGGGYGGGGYPGGGFGGYPRGGFGGGSASASASASASSSWGRK
Protein: Asparagine synthetase [glutamine-hydrolyzing] 2 (EC 6.3.5.4) (Glutamine-dependent asparagine synthetase 2) (Q9LV77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for nitrogen assimilation, distribution and remobilization within the plant via the phloem.
Interaction partners:
- Aspartate aminotransferase, cytoplasmic isozyme 1
- Aspartate aminotransferase 3, chloroplastic
- Isoaspartyl peptidase/L-asparaginase 1
- Aspartate aminotransferase, chloroplastic
- Probable isoaspartyl peptidase/L-asparaginase 2
- Aspartate aminotransferase, cytoplasmic isozyme 2
- Aspartate aminotransferase, mitochondrial
- Adenylosuccinate synthetase, chloroplastic
- Argininosuccinate synthase, chloroplastic
- Aspartate carbamoyltransferase, chloroplastic
Sequence:
MCGILAVLGCIDNSQAKRSRIIELSRRLRHRGPDWSGLHCYEDCYLAHERLAIIDPTSGDQPLYNEDKTVAVTVNGEIYNHKILREKLKSHQFRTGSDCEVIAHLYEEHGEEFIDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWGLDGSVWFASEMKALSDDCEQFMSFPPGHIYSSKQGGLRRWYNPPWYNEQVPSTPYDPLVLRNAFEKAVIKRLMTDVPFGVLLSGGLDSSLVAAVALRHLEKSEAARQWGSQLHTFCIGLQGSPDLKAGREVADYLGTRHHEFQFTVQDGIDAIEEVIYHIETYDVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEILGGYLYFHKAPNKKEFHEETCRKIKALHQFDCLRANKSTSAWGVEARVPFLDKEFLNVAMSIDPEWKLIKPDLGRIEKWVLRNAFDDEERPYLPKHILYRQKEQFSDGVGYSWIDGLKDHANKHVSDTMLSNASFVFPDNTPLTKEAYYYRTIFEKFFPKSAARATVPGGPSIACSTAKAVEWDATWSKNLDPSGRAALGVHVAAYEEDKAAAAAKAGSDLVDPLPKNGT