wanglab/gogpt-training-data huggingface dataset:
Protein: Type 3 secretion system ATPase (EC 7.4.2.8) (Q9Z7J8)
Organism: Chlamydia pneumoniae (Chlamydophila pneumoniae)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Flagellar motor switch Domain/YscQ family
- Flagellar assembly protein FliH
- Type III secretion inner membrane protein SctU
- Pathogenicity-related ORF2
- Flagellar Secretion Protein
- Uncharacterized protein CPn0706 Homolog
- Low calcium response D
- Flagellar assembly protein FliH
- Outer membrane secretion protein Q
- Uncharacterized protein CPn0708 Homolog
Sequence:
MDQLTTDFDTLMSQLGDVNLTTVVGRITEVVGMLIKAVVPNVRVGEVCLVKRNGMEPLVTEVVGFTQSFAFLSPLGELSGVSPSSEVIPTGLPLHIRAGNGLLGRVLNGLGEPIDVETKGPLQNVDQTFPIFRAPPDPLHRAKLRQILSTGVRCIDGMLTVARGQRIGIFAGAGVGKSSLLGMIARNAEEADVNVIALIGERGREVREFIEGDLGEEGMKRSVIVVSTSDQSSQLRLNAAYVGTAIAEYFRDQGKTVVLMMDSVTRFARALREVGLAAGEPPARAGYTPSVFSTLPRLLERSGASDKGTITAFYTVLVAGDDMNEPVADEVKSILDGHIVLSNALAQAYHYPAIDVLASISRLLTAIVPEEQRRIIGKAREVLAKYKANEMLIRIGEYRRGSDREIDFAIDHIDKLNRFLKQDIHEKTNYEEAAQQLRAIFR
Protein: RIC3 acetylcholine receptor chaperone, isoform T (A0A0B4KFX1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGCCDVVLDREQFLNATKKDTVEPFGPHLYRKQINVYTGEISLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLGAATATAAAKKPAAKDTEKELYNASVSATEVASSLSASLKSHQQLKEAEQLMEIEKLRQKLESTERAMAQLVAEMNTDQYEAKMIALKFLKRQPNF
Protein: Ethylene-responsive transcription factor CRF6 (Protein CYTOKININ RESPONSE FACTOR 6) (Q9M374)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cytokinin signaling pathway involved in cotyledons, leaves, and embryos development. Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16832061}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:16832061}. Note=Relocalization from the cytoplasm into the nucleus is induced by cytokinins.
Interaction partners:
- Two-component response regulator ARR10
- Two-component response regulator ARR12
- Histidine kinase 3
- Two-component response regulator ARR1
- Two-component response regulator ARR2
- Two-component response regulator ARR7
Sequence:
MERRTRRVKFTENRTVTNVAATPSNGSPRLVRITVTDPFATDSSSDDDDNNNVTVVPRVKRYVKEIRFCQGESSSSTAARKGKHKEEESVVVEDDVSTSVKPKKYRGVRQRPWGKFAAEIRDPSSRTRIWLGTFVTAEEAAIAYDRAAIHLKGPKALTNFLTPPTPTPVIDLQTVSACDYGRDSRQSLHSPTSVLRFNVNEETEHEIEAIELSPERKSTVIKEEEESSAGLVFPDPYLLPDLSLAGECFWDTEIAPDLLFLDEETKIQSTLLPNTEVSKQGENETEDFEFGLIDDFESSPWDVDHFFDHHHHSFD
Protein: Iron-sulfur cluster assembly enzyme ISCU (NifU-like N-terminal domain-containing protein) (NifU-like protein) (Q9D7P6)
Organism: Mus musculus (Mouse)
Function: Mitochondrial scaffold protein, of the core iron-sulfur cluster (ISC) assembly complex, that provides the structural architecture on which the [2Fe-2S] clusters are assembled. The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5. Exists as two slow interchanging conformational states, a structured (S) and disordered (D) form. May modulate NFS1 desulfurase activity in a zinc-dependent manner. Modulates the interaction between FXN and the cysteine desulfurase complex.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9H1K1}.
Interaction partners:
- Cysteine desulfurase
- Frataxin, mitochondrial
- LYR motif-containing protein 4
- Molybdenum cofactor sulfurase
- Selenocysteine lyase
- Ferredoxin-2, mitochondrial
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Adrenodoxin, mitochondrial
Sequence:
MAAATGAGRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQESKKEEPEKQ
Protein: Rik1-associated factor 1 (Cryptic loci regulator 8) (De-localization of swi6 protein 1) (O74910)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me. ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. Has a role in both mitotic and meiotic chromosome segregation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:18345014}.
Interaction partners:
- Rik1-associated factor 2
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Cullin-4
- Chromatin modification-related protein rik1
- RING-box protein pip1
- DNA damage-binding protein 1
- Ubiquitin-conjugating enzyme E2 4
- Cell division cycle protein cdt2
- Anaphase-promoting complex subunit 13
- Meiotic chromosome segregation protein P8B7.28c
Sequence:
MTNSSPRVKRRTDTQYLHSVSSKLPKVDFDTNNEEFFEEEFEIYDPFYRAELPCPKPSLSISKHSIAKVPSNVNKRLELQLLLTSGTFLPNSRPYLSERVRKHTHLLSNSITGDDKPSLIHVDFTPEECFILQEAKLKFGPVNSVQFNDAYSTHISPKLPGRAYEDCQKFEIDNPSLSPVDKHGAIILRTYKKNKKLLPDYLKSFYNAGSSYFQREQVHQLMDGESVFFLKPWKHFNETSGDTVCVAYNPLCEKFALGSTAQDGAYNRLGNLWIGDFHSETIQSLESHYKLNQVGEKEYSTISDLCFSKGNLFLYTGAFDNAVKVWDMEGNLCGIFNAPTDYIHKLALSDDDLLAVACKNGYGYLLSTDNSTGEILTSANLIYPEALEKGYSASLIEFSNFLGRSSDKVIIGYDSFHTSNNRGCLALFDASTASFVQKFNTADEAFTSLYMHPSQVGFVASSNTLSNGRVYYLDTRMYKVCLNFTTTQKDINHATISNSGILVTSSGTDNQTFVWDSRKPDKPLSLLKHGKTKMIHFDGANEEEVDAGINMAQWQPKGNLFVTGGSDGIVKVWDLRLNNPFIQNFTEMNSAITYGGFSEDASKLTVCCVGGDVNMYSLGNDNGNKFGEFRIIENRLLT
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Inositol polyphosphate 3-phosphatase) (Q9U470)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MANTISLMSNVIRNVVSKKRIRYKEKGYDLDLTYINDNIIAMGYPAPDKLEGLFRNRLEDVFKLLEENHAQHYKIYNLCSERSYDVAKFRGRVAVYPFDDHNPPTIELIQRFCSDVDMWLKEDSSNVVAVHCKAGKGRTGTMICAYLVFSGIKKSADEALAWYDEKRTKDRKGVTIPSQRRYVQYFSKLVCSSVPYSKVSLNVCEIRFSESSCVQNLGMVECSISVLHDSATENAKPDRLKTLPIDFQKSFVLTIKPSIPVSGDVKFELTKKSPDKIICHFWLNTFFVRNYSPCESDGTVNKYIHTLSKSEIDDVHKDSEHKRFSEEFKISIVFEAENFSNDVQAEASEKERNENVLNFERSDYDSLSPNCYAEKKVLTAIVNDNTTKSQTIETLDHKDIVTKIQYDTSTNSKNTSTACKRKQPNSKTLLPSLNDSTKEEIKRNHIFNQPSIKKTDLIKWQNSEVHITRSINENKNINYNSYITCKQSSPKFNCGTEDGEEDWESE
Protein: Dual specificity protein phosphatase 5 (EC 3.1.3.16) (EC 3.1.3.48) (MAP-kinase phosphatase CPG21) (O54838)
Organism: Rattus norvegicus (Rat)
Function: Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 1
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Protein c-Fos
Sequence:
MKVTSLDGRRLRKMLRKEAEARCVVLDCRPYLAFAASSVRGSLNVNLNSVVLRRARGGAVSARYVLADEAARARLLQEGGGGVAAVVVLDQGSRHWQKLREESAARVVLTSLLACLSAGPRVYFLKGGYETFYSQYPECCVDAKPISQEKLEGERGLLSQCGKPILSVAYRPAYDQGGPVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRTSEACTTHLHYKWIPVEDSHTADISSHFQEAIDFIDCVREEGGKVLVHCEAGVSRSPTICMAYLMKTKQFRLKEAFEYIKQRRSVVSPNFGFMGQLLQYESEILPSTPTPQPPSCQGEAASSTFIGHLQTLSPDMQGAYCTFPTSVLAPVPTHATVAELHRSPVATATSC
Protein: Jupiter microtubule associated homolog 2 (H3BU16)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKPPGGESSNLFGSPEEATPSSRPNRMASNIFGPTEEPQNIPKRTNPPGGKGSGIFDESTPVQTRQHLNPPGGKTSDIFGSPVTATSRLAHPNKPKDHVFLCEGEEPKSDLKAARSIPAGAEPGEKGSARKAGPAKEQEPMPTVDSHEPRLGPRPRSHNKVLNPPGG
Protein: O-GlcNAcase BT_4395 (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Hexosaminidase B) (N-acetyl-beta-glucosaminidase) (Q89ZI2)
Organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Function: Can hydrolyze the glycosidic link of O-GlcNAcylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates (in vitro).
Interaction partners:
- Beta-N-hexosaminidase, glycosyl hyrolase family 20
- Transposase
Sequence:
MKNNKIYLLGACLLCAVTTFAQNVSLQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKELLSGKQSSKKGMLISIGEKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVLAGNDERGTYYALQTFAQLLKDGKLPEVEIKDYPSVRYRGVVEGFYGTPWSHQARLSQLKFYGKNKMNTYIYGPKDDPYHSAPNWRLPYPDKEAAQLQELVAVANENEVDFVWAIHPGQDIKWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQKQAELLNYIDEKFAQVKPDINQLVMCPTEYNKSWSNPNGNYLTTLGDKLNPSIQIMWTGDRVISDITRDGISWINERIKRPAYIWWNFPVSDYVRDHLLLGPVYGNDTTIAKEMSGFVTNPMEHAESSKIAIYSVASYAWNPAKYDTWQTWKDAIRTILPSAAEELECFAMHNSDLGPNGHGYRREESMDIQPAAERFLKAFKEGKNYDKADFETLQYTFERMKESADILLMNTENKPLIVEITPWVHQFKLTAEMGEEVLKMVEGRNESYFLRKYNHVKALQQQMFYIDQTSNQNPYQPGVKTATRVIKPLIDRTFATVVKFFNQKFNAHLDATTDYMPHKMISNVEQIKNLPLQVKANRVLISPANEVVKWAAGNSVEIELDAIYPGENIQINFGKDAPCTWGRLEISTDGKEWKTVDLKQKESRLSAGLQKAPVKFVRFTNVSDEEQQVYLRQFVLTIEKK
Protein: 10-epi-juneol synthase (EC 4.2.3.172) (Tau-cadinol synthase) (EC 4.2.3.173) (Terpene synthase 1) (IhsTPS1) (A0A1L2D3T3)
Organism: Inula hupehensis (Inula helianthus-aquatilis subsp. hupehensis)
Function: Sesquiterpene synthase that catalyzes the formation of sesquiterpenes and sesquiterpenoid alcohols. Converts farnesyl diphosphate (FPP) to 10-epi-juneol. Converts FPP to tau-cadinol. 10-epi-juneol is the major product.
Interaction partners:
Sequence:
MATQKSTTALDAKSKMTTDLVRPLANFPSSIWGDRFMSLSIDKSELKTYDKVIEKQKQELRRLIIDPSMDSNKKLSLINSVYRLGLTYLFEEEIEGQLDKLFKEIDMQEACNEADLYTISVNFQVFRQHGYKLSCNVFNKFKDYTSDHKFKEYIMADVRGMLGLYESTQLRIRGETILEEAFAFTESQLKGVLDTLEGNIARQVKHALTSPFHRGLRTVEARIYFSNYEEECSTYDSLQKLANAHFNYLQLQHKEELASVIKWGEDMDFKTITPYARDRIPDLYLWGLGLFSEPHYSQARILISKMAQLICVLDDTYDAYATIDELHLLTNAINRWELSATEQLPEYMKPLYKVLLNEHVELEKQLSSKGKSNFVNASKKAFQELAMGYLQEAEWRHNGKVPSFQEYLKNGLITSTYNVFAKSSLICMSDIVTEEACTWYDSDPIILQATGLLGRVYNDISTFQFERKRAQQQITSIEAYMKTFGVPENVALEELKKMVEIAWNDINKGCLNTNEISKKLLAPIVNLARMTDVIYRYNDKFTFPEKTIEEYITLLFCESIPKN
Protein: Pumilio RNA binding family member 2 (C9JW01)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGASHHSMSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPH
Protein: Inhibin beta chain (Activin beta chain) (dAct) (dActivin) (O61643)
Organism: Drosophila melanogaster (Fruit fly)
Function: Controls several aspects of neuronal morphogenesis; essential for optic lobe development, EcR-B1 expression in larval brains, mushroom body remodeling, dorsal neuron morphogenesis and motoneuron axon guidance. Ligands Actbeta and daw act redundantly through the Activin receptor Babo and its transcriptional mediator Smad2 (Smox), to regulate neuroblast numbers and proliferation rates in the developing larval brain.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase receptor
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- Follistatin, isoform A
- Mothers against decapentaplegic homolog
- Synaptotagmin 7, isoform A
Sequence:
MRFAFDSNHSQSGAPFKGSRCFFNCQCICCRQGCCVVVVKCCCCFNLNCCNSLGSRKSFPQPAAMRKKVADLEVLRVSRFVAVILVLARWVTAVATLLTSCILLDIFSVPGQSGVADRSQASSRTVHVSVPTTPNETPSSTSETKLKLLYGYTSYDINNDQQVKSNNLCRVLCKSRNRKRQRRRRRRRNHRRRRHRYTKRLHHLMQDNMSGFEQRLNFSDAKCQSLETNYGTNYDLVQGGKLFSQSERSLLVSPLREIEAPWPAIHGSMRNCSKIKRNRANLIWLLIGLVWFEVKLINCNGISSSNYYASNLESHKGCTLCHESGKPNIYTDKDNPHTDYNIYNKYHSNNNFNKKTNQPHNNIAPSDEVRLESIKRQILTKLGLSHKPNVSHPLPKQFIWETIYRVDGGRMIPNNAFGSSGKNLDQKTIKLRAFASPGSHLFNGRGGRTDQRSERDPSHHKYRSPFDFTFNISKNNVYGKVLRNRSLERIDKKNSFLNGWTENRQLKINSQIASMPIELKSHHNSSPKELKSGAVRKVNGINGTQMNENALKKSTYPIDINHSIDNKTHTGKNGEMSHNDYEYFNDYSVQTHDKNRYHEGRSSIGYQPAIHNIEYENQKGHHESFADDHENIDHEDFFGNTQEIITFAEEGTQYRQYRILEFSAQNRRVPSQKLSIRSAQIHIRIDKPHSLWIEKAKSLPEKHLLNTKRKWGANKPHHRIKIWVFQLSTSINITEKGIDKAIIFRASFQVDPKNLGWQKFDLTDTIREWYGHTSHEKLRLLIDCTGCGGRYSLHLFQTSKLRGNSSDYLSTNPNRPFLVLHTESSRTRRVRRRAVDCGGALNGQCCKESFYVSFKALGWDDWIIAPRGYFANYCRGDCTGSFRTPDTFQTFHAHFIEEYRKMGLMNGMRPCCAPIKFSSMSLIYYGDDGIIKRDLPKMVVDECGCP
Protein: V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 67 kDa subunit) (Vacuolar proton pump subunit alpha) (P31406)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17255}; Cytoplasmic side {ECO:0000250|UniProtKB:P17255}.
Interaction partners:
- V-type proton ATPase subunit c
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B
- V-type proton ATPase subunit a
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- V-type proton ATPase subunit F
- V-type proton ATPase subunit H
- V-type proton ATPase subunit c'
Sequence:
MAGGIELAKKAIRSLKNYDEHENRYGSIFSVSGPVVVAANMLGCSMYELVRVGHEELVGEVIRIHQDKCTIQVYEETSGLTVGDPVQRTGKPLSVELGPGLAETIYDGIQRPLKQIFDKSQSIYIPRGINTESLNREHKWDFTPNKDLRIGDHVSGGDVFGSVFENSLFNDHKIMLPPRARGTVTYIAEAGSYHVDEKLLEVEFNGKKHSFSMLHTWPVRAARPVADNLTANQPLLTGQRVLDALYPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDLIVYVGCGERGNEMAEVLMDFPELTIDINGKPEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYYRDQGKNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGAKLASFYERAGRARCLGSPDREGTVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINTSLSYSKYINALQPWYEERVPGFNTLRDQIKQIIQQEDSMLEIIQLVGKSALSETDKVTLDIAGIIKNDFLQQNGYSDYDRCCPLYKTYHMMRNMIAYYTKAKSAVETGSVPWSKIKESTSDIFYELTSMKFENPNEGEKEIVEHYETLHKKIEDKFHTLTE
Protein: Transcription factor E2-alpha (Transcription factor 3) (K7ENH8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XTSQWPRAGAPGALSPSYDGGLHGLQSKIEDHLDEAIHVLRSHAVGTAGDMHTLLPGHGALASGFTGPMSLGGRHAGLVSAGRGWSWAVGGDPAPPDAPVSPRLQVGGSHPEDGLAGSTSLMHNHAALPSQPGTLPDLSRPPDSYSGLGRAGATAAASEIKREEKEDEENTSAADHSEEEKKELKAPRARTSSTDEVLSLEEKDLRDRERRMANNARERVRVRDINEAFRELGRMCQMHLKSDKAQTKLLILQQAVQVILGLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQMVLSAPHPGLSEAHNPAGHM
Protein: 4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase (HMG/CHA aldolase) (EC 4.1.3.16) (EC 4.1.3.17) (4-hydroxy-2-oxoglutarate aldolase) (Oxaloacetate decarboxylase) (OAA decarboxylase) (EC 4.1.1.112) (Q9AQI0)
Organism: Pseudomonas straminea
Function: Catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway. Has a broad substrate specificity and catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate, 4-hydroxy-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate, and the decarboxylation of oxaloacetate. Preferentially cleaves the L-isomer of 4-carboxy-4-hydroxy-2-oxoadipate, and has lower activity towards 4-hydroxy-4-methyl-2-oxoglutarate and 4-Hydroxy-2-oxoglutarate. Does not cleave 4-hydroxy-2-oxovalerate, citrate, 4-hydroxy-2-oxobutyrate, 2-oxoglutarate or fructose-1,6-bisphosphate.
Interaction partners:
Sequence:
MYELGVVYRNIQRADRAAADGLAALGSATVHEAMGRVGLLKPYMRPIYAGKQVSGTAVTVLLQPGDNWMMHVAAEQIQPGDIVVAAVTAECTDGYFGDLLATSFQARGARALIIDAGVRDVKTLQEMDFPVWSKAISSKGTIKATLGSVNIPIVCAGMLVTPGDVIVADDDGVVCVPAARAVEVLAAAQKRESFEGEKRAKLASGVLGLDMYKMREPLEKAGLKYID
Protein: Vesicle-associated membrane protein 712 (AtVAMP712) (Q9SIQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}. Prevacuolar compartment membrane {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}.
Interaction partners:
- Putative SNAP25 homologous protein SNAP30
- SNAP25 homologous protein SNAP29
- Syntaxin-23
- Syntaxin-22
- Syntaxin-21
- Syntaxin-52
- Syntaxin-123
- Syntaxin-112
- SNAP25 homologous protein SNAP33
- Syntaxin-125
Sequence:
MSILYALVARGTVVLAELSTTSTNASTIAKQILEKIPGNGDSHVSYSQDRYVFHVKRTDGLTVLCMADEDAGRRIPFSFLEDIHQRFVRTYGRAIHSAQAYAMNDEFSRVLNQQIEYYSNDPNADTISRIKGEMNQVRDVMIENIDNILDRGERLELLVDKTANMQGNTFRFRKQTRRFNNTVWWRNCKLTLLLILVLLVIIYIGVAFACHGPTLPSCV
Protein: Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase 4 kDa subunit (OTase 4 kDa subunit) (Oligosaccharyl transferase 4 kDa subunit) (Q96VG2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost5
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
- Uncharacterized protein C553.06
Sequence:
MTDVQLQNIVTTFGISMMLLIILYHYLSRPQA
Protein: Carnitine O-Acetyl-Transferase, isoform A (EC 2.3.-.-, EC 2.3.1.7) (Carnitine O-Acetyl-Transferase, isoform D) (LD01568p) (Q9VI16)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Choline/carnitine acyltransferase domain-containing protein
- Choline/carnitine acyltransferase domain-containing protein
- Peroxisomal multifunctional enzyme type 2
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Vesicular acetylcholine transporter
- Acyl-coenzyme A oxidase
- Isocitrate dehydrogenase
- Congested-like trachea protein
Sequence:
MLINRSKTRVSPTSERILEKTEAEMKFRGNGKLLWNLTKNSLAQQSPNGIAKKVLPASSYSTVQKTIPLEQPNLLKYHVLPLEETLNRFMTTVEPLLTPEEFQRQKGITSEFLKKQGRELQLLLEETGSKEKNWLAHRWLKAAYLTYRDPVTVFVSPGMTFPKQNFRDSRAFVDYTARVIYGLGEFNDMVHANKIPIVKMGKNELDNSQFGKVFGTCRIPRRGTDEIVYNPDSDYVVVIYKNHFYQLKIYSKEGKLIAAPCLAAQLENIVLKETQVGVPYGILTTDSRDNWAEAYEYLVETPGNRDALKTIQGALFTVSLDEGTILKEGEETDELILSLIHGSGSKINSGNRWMDKTIQLVVNPNGNVGFTYEHSPAEGQPIAMMMDYVVQKMKEDPSFGQSGSQDFAPAQKIQFSSSNKSLEKSLNVAQENVDKLADALQMKVLKFNGFGKDFIKKQRLGPDSFVQMALQLAFYKMHSEPPAQYESAHLRIFDGGRTETIRSCSNESLAFSRAMQDPNVTDQERAAKLREAVVSHQTYAKLALQGKGVDRHLLGLKLMALEHSKPIPEFFKSPGFVKSSHFRMSTSQVATKYDAFMGYGPATDDGYACCYNPRDNDIILAISAWRHCPITDHLKFVKTLEQSFFEMKNVLEKNPPETKSKL
Protein: BK channel (H8ESE3)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGEIYSPSQSKGFNQPYGYPMNCNLSRVFMEMTEEDRKCLEERKYWCFLLSSITTFCASMILVVIWRVVTHLCCQRREKEFVEPIPAPEAVQINMNGSKHAPSETDPFLKQQEEKHLGWMTEAKDWAGELISGQSLTGRFLVLLVFILSIGSLIIYFYDASFQNFQVETCIPWQDSPSQQIDLGFNIFFLVYFFIRFIAASDKVWFLLEMYSWIDFFTIPPSFVAIYLQRNWLGFRFLRALRLMTVPDILQYLNILKTSSSIRLTQLVTIFVAVCLTGAGLVHLLENSGDFFKGFINPHRITYADSVYFVLVTMSTVGYGDIYCTTLCGRLFMIFFILFGLAMFASYVPEIADLIGNRQKYGGEYKGEHGKKHIVVCGHITYDSVSHFLQDFLHEDRDDVDVEVVFLHRVVPDLELEGLFKRHFTKVEFFTGTVMDSLDLSRVKIGDADACLVLANKYSTNPDAEDAANIMRVISIKNYSSDIRVIVQLMQYHNKAYLLNIPSWDWKRGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSQTTPDWLNLYLCGAGMEMYTDTLSHSFVGMTFPEAVDLLFNRLGLLLLAIELKDEENKECNIAINPGPHIVIQPQTQGFFIAQSADEVKRAFFWCKQCHDDIKDVSLIKKCKCKNLALFRRNTKHSTAARDYSDFDALFYQNDARATDVLQQFQPQAPAGPMGHLGQQVQLRMINQQSSTSDTHLNTKSLRFAYEIKKLMPSSGGRRNSMSIPPDGRGVDFSKDFEQQFQDMKYDSTGMFHWCPSRNLEDCVLERHQAAMTVLNGHVVVCLFADQDSPLIGLRNFIMPLRSSNFHYHELKHVVIVGDLEYLRKEWKTLYNLPKISILNGSPLSRADLRAVNINLCDMCVIISARVPNTEDTTLADKEAILASLNIKAMQFDDTLGFFPMRHQTGDRSPLGSPISMQKKGAKFGTNVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAISVLDSLMSTTYFNDSALTLIRTLVTGGATPELELILAEGAGLRGGYSTPETLSNRDRCRIAQISLQDNPYDGVVHNTTYGAMFTIALRRYGQLCIGLYRLHDQDNPDSMKRYVITNPPAELRIKNTDYVYVLEQFDPGLEYEPGKRHF
Protein: Meiotic drive suppressor wtf5 (Q8TF80)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons (By similarity). Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity).
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEESTLPPYSDHALVNNPPNTHRENHSYGTTDNSSPLLIILLISFTSIILFNAPEVCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWTKAVKVTVISLAKCVKVTAIFLAQCVKACGKGIKHFLKKWENMPMAFSEVFLFNILVGSPRMNLRYIFGDRWGLKCSLADHIIFVVLSILVFIAETVKPGSIRVNLIRKMGYEAKQQVNEYTAVPLREMNSESEA