wanglab/gogpt-training-data huggingface dataset:
Protein: B9 domain-containing protein 1 (MKS1-related protein 1) (Q9UPM9)
Organism: Homo sapiens (Human)
Function: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:19208769}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19208769}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000250}.
Interaction partners:
- Tectonic-1
- B9 domain-containing protein 2
- Transmembrane protein 231
- Coiled-coil and C2 domain-containing protein 2A
- Meckelin
- Tectonic-2
- Transmembrane protein 216
- Tectonic-3
- Tectonic-like complex member MKS1
- Centrosomal protein of 290 kDa
Sequence:
MATASPSVFLLMVNGQVESAQFPEYDDLYCKYCFVYGQDWAPTAGLEEGISQITSKSQDVRQALVWNFPIDVTFKSTNPYGWPQIVLSVYGPDVFGNDVVRGYGAVHVPFSPGRHKRTIPMFVPESTSKLQKFTSWFMGRRPEYTDPKVVAQGEGREVTRVRSQGFVTLLFNVVTKDMRKLGYDTGPSDTQGVLGPSPPQSFPQ
Protein: Caveolin (Q6YLH8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|RuleBase:RU000680}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|RuleBase:RU000680}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU000680}; Peripheral membrane protein {ECO:0000256|RuleBase:RU000680}. Membrane, caveola {ECO:0000256|RuleBase:RU000680}; Peripheral membrane protein {ECO:0000256|RuleBase:RU000680}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}.
Interaction partners:
Sequence:
MDNDSINEKTLQDVHTKEIDLVNRDPKHLNDDVVKVDFEDVIAEPAGTYSFDGVWKASFTTFTVTKYWCYRLLTALVGIPLALVWGIFFAILSFIHIWAVVPCVKSYLIEIHCISRVYSICVHTFCDPLFEAMGKCFSNVRVTATKVV
Protein: DNA-binding protein StpA (H-NS homolog StpA) (P0ACG3)
Organism: Shigella flexneri
Function: A DNA-binding protein that acts in a fashion similar to H-NS, repressing gene transcription. A subset of H-NS/StpA-regulated genes require auxillary proteins for repression; these auxillary proteins (Hha and other similar proteins) may also modulate oligomerization of the H-NS/StpA complex (By similarity).
Subcellular location: Cytoplasm, nucleoid {ECO:0000250|UniProtKB:P0ACG1}.
Interaction partners:
- OriC-binding nucleoid-associated protein
- Hemolysin expression-modulating protein Hha
Sequence:
MSVMLQSLNNIRTLRAMAREFSIDVLEEMLEKFRVVTKERREEEEQQQRELAERQEKISTWLELMKADGINPEELLGNSSAAAPRAGKKRQPRPAKYKFTDVNGETKTWTGQGRTPKPIAQALAEGKSLDDFLI
Protein: 6-cysteine protein (C0H478)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNRGWHVVFYFILLLMNKSLGGEEKLTKFDPVMIKEGELFGEVSYDCEYSGFLEIENDDILYYCFFVGEDDHNGLLLRKFHMDDMVWGIPMEVLITRKKINLYILTVDYILSKLILIYSFDEKIRITVFNNYMEESVMSEKISINYEILYKANMISYITYFYKNKKSLCVCGMNRNENILCTFSFDYGLTMKDDHTIEFFLKKKIPLGHYKMQVTFKETEVYFNLYNDLNETNFYELKCVKKQDEYICDIMNKIRETQEYNYKRYTYPSSEHNKYYNDHHNKQPQGKQGQQGGAPLPNLGEEENNFIYKHIVRNKYFQMIVFQKDQKCYLAWSFNSLNINDEITKEISSVPCSNVASYYRQERLIVTLKKNQLGSRNHFFLIYEKLTEKGVGCEFGVGGSLYVTKTFMNNTCDMDINNMNVSTTNYDEINFSLIIPLSFQLNYSTCFIWEENVDNNEERSSLYYLEEYTNEKEDIKVYTFYFYKYILIYKNFKKSTCTFESKNNEKLYISFRGDTYYKEYNCNILLDSCDFFLHTQSKINITYDDDVWQVSEELYDGFVMYNGTYVSLYDVLSRSNAHGLIYIDGKENNTSINLNNIKNNNNNNNNNNNNNNTSNNNNISNNSNSNNSFGEHEKVITIIIPYGIPSTRTIKIEFLNKQNNEEKRWAYLRLQKNEYIMKKVIGINSSDIFDLSYKYYKYNQEKIKFILNDFSETTYLGFICQTKEEIKKSLCTISLVDHSHKNMAINNLFKTNNHILPFLYDQSPPRKIQPYNQIISEFRFVLFKNFHLFLQENKINYILLKCMCSSSSSYINTQKNIELSYLITNEQVSHDFIHTPGILIRPRTNISHNDYQKNNKGNHKGNNKSNNKSNDKDSNNNSNNNSNKNGNNHNDNNNNNQNKDIDINSNYSIHNNNEKVKRTKKKINDAPYDKQDEELPSYDFNDLLHEKKNGTSVFDFNFVLFLFICITFF
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-gamma-2) (Phospholipase C-gamma-2) (PLC-gamma-2) (Q8CIH5)
Organism: Mus musculus (Mouse)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling.
Subcellular location: Membrane raft {ECO:0000269|PubMed:23478294}.
Interaction partners:
- B-cell linker protein
- Tyrosine-protein kinase BTK
- Tyrosine-protein kinase SYK
- Proto-oncogene vav
- Lymphocyte cytosolic protein 2
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Linker for activation of T-cells family member 1
- Protein kinase C beta type
- Epidermal growth factor receptor
- SH3 domain-binding protein 2
Sequence:
MTTMVNVDTLPEYEKSQIKRALELGTVMTVFNARKSTPERRTVQMIMETRQVAWSKTADKIEGFLDIMEIKEIRPGKNSKDFERAKAVRHKAECCFTILYGTQFVLSTLSLATDSKEDAVKWLSGLKILHQEAMSASTPTMIESWLRKQIYSVDQTRRNSISLRELKTILPLVNFKVSGIKFLKDKLVEIGAQKDELSFEQFHLFYKKLMFDQQKSILDEFKKDSSVFILGNTDRPDASAVYLQDFQRFLLHEQQELWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENSIWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSTEAYIRCLRAGCRCIELDCWDGPDGKPIIYHGWTRTTKIKFDDVVQAIRDHAFVTSSFPVILSIEEHCSVEQQRHMAKVFKEVLGDMLLTKPTEASADQLPSPSQLREKIIIKHKKLGPKGDVDVNVEDKKDEHKPQGELYMWDSIDQKWTRHYCAIADAKLSFGDDIEQAVEEEPVQDTPPTELHFGEKWFHKKVESRTSAEKLLQEYCAETGAKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMENGVMKYYLTDNLTFNSIYALIQHYREAHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDMLMRIPRDGAFLIRKREGTNSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYYEKHALYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDYKAKRSDELTFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISAGDAEEMEKQIIEDNPLGSLCKGILDLNTYNVVKAPQGKNQKAFVFILEPKKQGDPPVEFATDRVEELFEWFQSIREITWKMDTKENNMKYWERNQSIAIELSDLVVYCKPTSKTKDHLENPDFREIRSFVETKADSIVRQKPVDLLRYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTPDKYMQMNHALFSLNGRTGYVLQPESMRSEKYDPMPLESQRKILMTLTVKVLGARHLPKLGRSIACPFVEVEICGAEYDSNKFKTTVVNDNGLSPVWAPTQEKVTFEIYDPNLAFLRFVVYEEDMFSDPNFLAHATYPIKGIKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSCRQLRRRQEELNNQLFLYDTHQNLRGANRDALVKEFNVNENQLQLYQEKCNRRLREKRVSNSRFYS
Protein: PH, RCC1 and FYVE domains-containing protein 1 (Protein Praf4) (Q947D2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to phosphatidic acid and to phosphoinositides such as PtdIns3P, PtdIns(3,4)P(2), PtdIns(3,4,5)P(3) and PtdIns(4,5)P(2). Catalyzes guanine nucleotide exchange on specific Rab proteins.
Interaction partners:
- Probable disease resistance protein At1g52660
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- At1g61690
- RING/FYVE/PHD-type zinc finger family protein
- RING/FYVE/PHD-type zinc finger family protein
- Translocon-associated protein subunit alpha
- Lysine-specific demethylase JMJ29
- 30-kDa cleavage and polyadenylation specificity factor 30
Sequence:
MADLVTYSNADHNLEQALITLKKGTQLLKYGRKGKPKFYPFRLSSDEKSLIWISSSGEKRLKLASVSKIVPGQRTAVFQRYLRPEKDYLSFSLLYNGKKKSLDLICKDKVEAEIWIGGLKTLISTGQGGRSKIDGWSGGGLSVDASRELTSSSPSSSSASASRGHSSPGTPFNIDPITSPKSAEPEVPPTDSEKSHVALDNKNMQTKVSGSDGFRVSVSSAQSSSSHGSAADDSDALGDVYIWGEVICDNVVKVGIDKNASYLTTRTDVLVPKPLESNIVLDVHQIACGVRHAAFVTRQGEIFTWGEESGGRLGHGIGKDVFHPRLVESLTATSSVDFVACGEFHTCAVTLAGELYTWGDGTHNVGLLGHGSDISHWIPKRIAGSLEGLHVASVSCGPWHTALITSYGRLFTFGDGTFGVLGHGDKETVQYPREVESLSGLRTIAVSCGVWHTAAVVEIIVTQSNSSSVSSGKLFTWGDGDKNRLGHGDKDPRLKPTCVPALIDYNFHKIACGHSLTVGLTTSGQVFTMGSTVYGQLGNLQTDGKLPCLVEDKLASEFVEEISCGAYHVAALTSRNEVYTWGKGANGRLGHGDLEDRKVPTIVEALKDRHVKYIACGSNYTAAICLHKWVSGAEQSQCSTCRLAFGFTRKRHNCYNCGLVHCHSCSSKKAFRAALAPSAGRLYRVCDSCYVKLSKVSEINDTNRRNSAVPRLSGENRDRLDKSEIRLAKFGTSNMDLIKQLDSKAAKQGKKTDTFSLGRNSQLPSLLQLKDAVQSNIGDMRRATPKLAQAPSGISSRSVSPFSRRSSPPRSATPMPSTSGLYFPVGIADNMKKTNEILNQEIVKLRTQVDSLTQKCEFQEVELQNSVKKTQEALALAEEESAKSRAAKEAIKSLIAQLKDVAEKLPPGESVKLACLQNGLDQNGFHFPEENGFHPSRSESMTSSISSVAPFDFAFANASWSNLQSPKQTPRASERNSNAYPADPRLSSSGSVISERIEPFQFQNNSDNGSSQTGVNNTNQVEAEWIEQYEPGVYITLVALHDGTRDLRRVRFSRRRFGEHQAETWWSENREKVYEKYNVRVSEKSTASQTHRDRDEEEEDIPH
Protein: Tyrosine-protein phosphatase non-receptor type 5 (EC 3.1.3.48) (Neural-specific protein-tyrosine phosphatase) (Striatum-enriched protein-tyrosine phosphatase) (STEP) (P54829)
Organism: Homo sapiens (Human)
Function: May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 14
- Receptor-type tyrosine-protein phosphatase R
- Tyrosine-protein phosphatase non-receptor type 7
- Dual specificity protein phosphatase 3
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 8
Sequence:
MNYEGARSERENHAADDSEGGALDMCCSERLPGLPQPIVMEALDEAEGLQDSQREMPPPPPPSPPSDPAQKPPPRGAGSHSLTVRSSLCLFAASQFLLACGVLWFSGYGHIWSQNATNLVSSLLTLLKQLEPTAWLDSGTWGVPSLLLVFLSVGLVLVTTLVWHLLRTPPEPPTPLPPEDRRQSVSRQPSFTYSEWMEEKIEDDFLDLDPVPETPVFDCVMDIKPEADPTSLTVKSMGLQERRGSNVSLTLDMCTPGCNEEGFGYLMSPREESAREYLLSASRVLQAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLSHQSPE
Protein: Zinc-regulated GTPase metalloprotein activator 1 (EC 3.6.5.-) (P53729)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase MAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of MAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1 to the zinc binding site in the peptidase domain of MAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active MAP1.
Interaction partners:
- Methionine aminopeptidase 1
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein bL33m
- General negative regulator of transcription subunit 2
Sequence:
MSALRNIKFNEEEDGELPCLVTGEENNLQEILENVSYDGGNIVSDAKVERVNKQVENTSAGATDVHEKKRIPVSIITGYLGSGKSTLLEKIALKGADKKIAVILNEFGDSSEIEKAMTIKNGSNSYQEWLDLGNGCLCCSLKNIGVKAIEDMVERSPGKIDYILLETSGIADPAPIAKMFWQDEGLNSSVYIDGIITVLDCEHILKCLDDISIDAHWHGDKVGLEGNLTIAHFQLAMADRIIMNKYDTIEHSPEMVKQLKERVREINSIAPMFFTKYSDTPIQNLLDIHAYDSVRISDILDSGSGNGTIHDDRMGTIMLTFRPLKNEEEYNNKFIKQFLQPLLWKNFGAMTVLGGRRRDDGRDWEVQRTKGLILIEGENPIARVIQGVRDTYDVFPGKYDGSNKECKIVLIGKYLEKESIEELLRKTLE
Protein: Nuclear receptor subfamily 6 group A member 1 (Germ cell nuclear factor) (GCNF) (xGCNF) (P70033)
Organism: Xenopus laevis (African clawed frog)
Function: Probable orphan nuclear receptor. Binds to a response element containing repeats of the motif 5'-AGGTCA-3'. Required for anterior-posterior patterning during organogenesis. Acts with chordin to play a role in patterning the midbrain-hindbrain. Isoform Em is required for integrin-mediated cell matrix interaction during neurulation and for the morphogenetic movements leading to formation of the neural tube. Also mediates the effect of retinoic acid on primary neurogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10349627, ECO:0000269|PubMed:9025060}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:10349627, ECO:0000269|PubMed:9025060}.
Interaction partners:
Sequence:
MDTWEDDRVDQRACLICGDRATGLHYGIISCEGCKGFFKRSICNKRVYRCSRDKNCVMSRKQRNRCQYCRLLKCLQMGMNRKAIREDGMPGGRNKSIGPVQISDEEVERIMSGQEFEEEANTSWSNNGDSDHSSPGNAVSESNQPSPVSTPSSSRSMELNGFSSLRDQYLGTPGPTHYQYLPHLFSFSAHPTIIPAQSRSLDPQSHTLINQLLTAEDIEPLNTPMLIEDGYKVTQSELFALLCRLADELLFRQITWVKKLPFFCDLSIKDYTCLLSTTWQELILLSSITTYSKQIFGDLTDVTSKYSPSEDELHRFSEDGMEVMERLIYLFRKFSQLKVSNEEYVCMKAINFLNQDIQGISSASQVEQLNKRYWYVCQDFTEYRYPHQPNRFPDLMMCLPEVRYIAGKLVNVPLEQLPLLFKAFLHSCKTIVTKE
Protein: RNA-binding protein, putative (Q382W9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAAVTQQGNDTRKLRCNVYVASLPLDFDDDQLFDLFSPYGRISSARIMRSKGARQSRGYGFVLFRHASSAEKAIDSLVGYVIGGSRIQVRLAHPEASVAYSGQRGSRSGNSTPGALPEKTLPAASGVITPPPPSSAIISHPNDSGMMVQTYPITTMYPTMYPSVVPQIIAQPQAPVPAAMQQVVFLPQYAQQSNQSTPPTFYMMVPDAMQAVPPTLS
Protein: 3',5'-bisphosphate nucleotidase AHL (EC 3.1.3.7) (3',5-bisphosphonucleoside 3'-phosphohydrolase) (3'-phosphoadenosine-5'-phosphate phosphatase AHL) (PAP phosphatase) (PAPase) (DPNPase) (Halotolerance protein) (PAP-specific phosphatase HAL2-like) (AtAHL) (Q38945)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Prevents both the toxicity of PAP on RNA processing enzymes as well as the product inhibition by PAP of sulfate conjugation.
Interaction partners:
- 5'-adenylylsulfate reductase 1, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- Bifunctional adenosine 5'-phosphosulfate phosphorylase/adenylylsulfatase HINT4
- Assimilatory sulfite reductase
- At3g27906
- Probable eukaryotic translation initiation factor 5-1
- Adenylyl-sulfate kinase 1, chloroplastic
- ATP sulfurylase 1, chloroplastic
- ATP-sulfurylase 3, chloroplastic
Sequence:
MAVDSLETEIDTAVRVVHLASSLCVKVQEKLHLPNGGHVKSKDDDSPVTVADFGVQAIVSWVLAEVFGDQNLSIVAEEDTETLSEADSLGLLGAVSNAVNEALSEAQNYGLPKPVKPLGSSEILKAISRCNSVGGPKGRHWVLDPVDGTLGFVRGDQYAVALALIENGKVLLGVLGCPNYPVKKECLSNGCNQAMKTKAVAGSVSKGCVMYAKRGSGQAWMQPLIVGGIPESATLLKVSSVDDPVLATVCEPVERANSNHLFTAGLANSMGVRKQPMRVYSMVKYAAIARGDAEVFMKFAQSSYKEKIWDHAAGVVIVEEAGGVVTDAGGRNLDFSKGVYLEGLDRGIIACSGQVLHEKIIGAVYASWESSSL
Protein: Spon2b protein (Spondin-2b precursor) (Q0V935)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
METMTSLRVNCWLTMTLALLSGVPAMPVDVDRMCTAPSTAKYRLTFTGQWTQTAFPKHYPLYRPPAQWSPLIGVTHSSDYHLWQRNEYASNGVREFSERAEAWTLIKEVEAAGERIQSVYGLFSAPAVVAGTGHATTEFEVFARHSLLSFIVRIVPSPDWFIGVDSLNLCEGDHWKENISLELYPYDAGTDSGFTFSSPNFETIPQDKVTQITSSFPSHPANSFYYPRLKHLPPIAKVSLTKIKNNQIFSLPIQPTQSNQIPSGNEIDGPLINTPLDCEVSVWSPWGLCKGQCGEKGVKHRTRYIHTHPANNGAPCPSLEEKRLCIPDNCV
Protein: Synaptotagmin-1 (Synaptotagmin I) (p65) (P41823)
Organism: Aplysia californica (California sea hare)
Function: Acts as inhibitor of neurotransmitter release. Overexpression leads to a decrease in the amplitude of the excitatory postsynaptic potential in dissected cholinergic and glutaminergic neurons while depletion with antisense oligonucleotides leads to an increase. Overexpression of isoform 1 blocks the reversal of synaptic depression by serotonin in sensory neurons.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Synapse. Note=And vesicle-like structures.
Interaction partners:
Sequence:
MDSLLARVKRAADADALNPAQEGVTGGPDAAGLPDVSTSSPGGGGAGDKLKEKMDEYKDKLINEIENLPIWAIVLIIAGSLLFLVCCVYCVCRRSCRKRKKKEGKKGLKGAVDLKSVQLLGNSYKEKVQPDLDELPVNMEDNEDAESTKSEVKLGKLQFSLDYDFQKGELSVNVIQAADLPGMDMSGTSDPYVKVYLLPDKKKKYETKVHRKTLNPVFNESFTFKVPYAEVGSKILTFAVYDFDRFSKHDQIGQVQVPLNSIDLGRVVEDWKDLQSPDTESEKENKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIALLQGTKRLKKKKTTIKKNTLNPYFNESFGFEVPFEQIQKVTLIITVVDYDRIGTSEPIGRCVLGCNSSGTELRHWSDMLANPRRPIAQWHTLQEVPEKN
Protein: Enoyl-[acyl-carrier-protein] reductase [NADH] (ENR) (EC 1.3.1.9) (Trans-2-enoyl-CoA reductase [NADH]) (TER) (EC 1.3.1.44) (Q2P9J6)
Organism: Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Function: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It can also use crotonyl-CoA.
Interaction partners:
Sequence:
MIIHPKVRGFICTTTHPLGCERNVLEQIAATRARGVRNDGPKKVLVIGASSGYGLASRITAAFGFGADTLGVFFEKPGTASKAGTAGWYNSAAFDKHAKAAGLYSKSINGDAFSDAARAQVIELIKTEMGGQVDLVVYSLASPVRKLPGSGEVKRSALKPIGQTYTATAIDTNKDTIIQASIEPASAQEIEETITVMGGQDWELWIDALEGAGVLADGARSVAFSYIGTEITWPIYWHGALGKAKVDLDRTAQRLNARLAKHGGGANVAVLKSVVTQASAAIPVMPLYISMVYKIMKEKGLHEGTIEQLDRLFRERLYRQDGQPAEVDEQNRLRLDDWELRDDVQDACKALWPQVTTENLFELTDYAGYKHEFLKLFGFGRTDVDYDADVATDVAFDCIELA
Protein: Thioredoxin (Q7D8E1)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTTRDLTAAQFNETIQSSDMVLVDYWASWCGPCRAFAPTFAESSEKHPDVVHAKVDTEAERELAAAAQIRSIPTIMAFKNGKLLFNQAGALPPAALESLVQQLKAYEVEAGEATTQNGRAQQA
Protein: Basonuclin 2 (Zinc finger protein basonuclin-2 isoform 2) (A0A2R8QKL6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSEETELDVRGGVVWRERDRERARESTARASSRSSSSSSGAGGGGGEEGESSMQFSTRPASAEPGFMGTWTQQSTDSNLLFRMSQQAIRCTLVNCTCECFQPGKIHLRTCDQCKHGWVAHALDKLSTQHLYHPTQVEIVQSNVVFDISSLMLYGTQAVPVRLKILLDRLFSVLKQEEVLHILHGLGWTLRDYVRGYILQDAAGKVLDRWTIMSREEEIITLQQFLRFGETKSIVELMAIQEKEGQAVTVPSSKTDSGIRTFIESNNRTRSPGLLSHLENNSPSSIHHFENIPNSLAFLLPFQYINPMSAPMLGLPPNGLSIEQSGLRMREPNLPNQSDPVEASESEVSLSPFHSGQSPSRGVMGTLPNAIEPKTEPNRASPISPTPSTLQSQQPQTPTQQTQGQQQSSSLNNHQIHHHFEKNEQSKTITHSSFSSKMHRIRRMGATSRKGRVCCNSCGKTFYDKGTLKIHYNAVHLKIKHRCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMLRNNRDKDLIRSSSGTATPVISSTKSGFNLTSPGRPPLSFATPPLEPMIQSPLQSPLVFPSLKSVQPVQPVPPFYRTLLSPADLVSPPVSLPTSPILPTTANSTSLTDQQQMLAVSSLSMHVSETSPFSHRLPTNHSTQDSIILDPMPKKKPRKSSMPVKIEKEVIDVADDYDDKDEDDDDGDSCHHHHHQPSSIHNVNGNCNNNNNGSSSSSHHCGGSGHESPSHDEMSPSQALRGMLHPEQEECTGSHGGRGHGDLRCIDSFTSEDQDHERDFENESETSESKMLYRDELMDTDINQTALGKNMDKEHQGTEDDQHLRKDLDEHSHSPPSQHQPVIKIKEEINDPTYDMFCMGQYSLYNGGMAAAAAAAASMAALHESFISSMSYGTSTPKFPSQSPEGDLCSSPDPKICYVCKKSFKSSYSVKLHYKNVHLKEMHVCTVSGCNAAFPSRRSRDRHSSNINLHRKLLTKELDDIVLDPQLTTLPKQLRAEFLSKIYADHHTGLEGVGGFDNGPPQSRGHEGMRSQVAREYSHSNGYCHGPNDDYVVLDLSTASSVQSSGSVQSSHESDEGSDEGILLDDLEDASDTEDCTPSTGAQRLSMEGKNREEAGKEEREGETDERILHYDPSVSPSILASSGGNGTGGILCTICHKLYSNKGTLRVHYKTVHLREMHKCKIPGCNMMFSSVRSRNRHSQNPNLHKKAPYTTMID
Protein: Cellulose synthase-like protein B1 (AtCslB1) (EC 2.4.1.-) (O80898)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein trichome birefringence-like 43
- Protein trichome birefringence
- At2g23910
- Protein trichome birefringence-like 35
- Uncharacterized protein F7J8_130
- Leucine-rich repeat protein kinase family protein
- Protein trichome birefringence-like 3
- Calcium-binding EF hand family protein
Sequence:
MADSSFSLPPLCERISYTNYFLRAVYLTVLGLFFSLLLHRIRHTSEYDNVWLVAFFCESCFFLVCLLITCLKWSPADTKPFPDRLDERVHDLPSVDMFVPTADPVREPPIMVVDTVLSLLAVNYPANKLACYVSDDGCSPLTYFSLKEASKFAKIWVPFCKKYNTRVRAPSRYFLKPISVATEDYEFNRDWEKTKREYEKLRRKVEDATGDSHMLDVEDDFEAFSNTKPNDHSTLVKVVWENKGGVGDEKEIPHIIYISREKRPNYVHNQKCGAMNFLARVSGLMTNAPYILNVDCDMYANDADVVRQAMCILLQESLNMKHCAFVQFRQEFYDSSTELIVVLQSHLGRGIAGIQGPIYIGSGCVHTRRVMYGLSPDDFEVDGSLSSVATREFLVKDSLARRFGNSKEMMKSVVDAIQRNPNPQNILTNSIEAAREVGHCQYEYQTSWGNTIGWLYDSVAEDLNTSIGIHSRGWTSSYISPDTPAFLGSMPAGVPEALLQQRRWATGWIEILFNKQSPLRGLFSKKIRFRQRLAYLCIITCLRSIPELIYCLLPAYCLLHNSTLFPKGLYLGITVTLVGIHCLYTLWEFMSLGYSVQSWLVSQSVWRIVATSSWLFSIFDITLKLLGISETVFIITKKTVAGTKSALGSGPSQGEDVGPNSDLFKFEFDGSLCFLPGTFIVLVNIAALAVFSVGLQRSSYSHEGGGSGLAEACGCVLVMMLFLPFLMGLFKKGKYGTPLSTLSIAGFLAVLFVVFSV
Protein: Aspartyl aminopeptidase (EC 3.4.11.21) (C9J1E2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKG
Protein: High mobility group 20B (K7EJR8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
QNKAREAELRRLRKMNVAFEEQNAVLQRHTQSMSSARERLEQELALEERRTLALQQQLQAVRQALTASFASLPVPGTGETPTLGTLDFYMARLHGAIERDPAQHEKLIVRIKEILAQVASPLNPEKALAARYTQKNLTAEGAPPRRTATRYTGSPGHPQDTGQTKPTPSTRQDPPNYSLRGAVP
Protein: Rhomboid protease GlpG (EC 3.4.21.105) (Intramembrane serine protease) (P44783)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:17210913}; Multi-pass membrane protein {ECO:0000269|PubMed:17210913}.
Interaction partners:
- Probable N-acetylmuramoyl-L-alanine amidase AmiB
- Glycerol-3-phosphate regulon repressor
Sequence:
MKNFLAQQGKITLILTALCVLIYLAQQLGFEDDIMYLMHYPAYEEQDSEVWRYISHTLVHLSNLHILFNLSWFFIFGGMIERTFGSVKLLMLYVVASAITGYVQNYVSGPAFFGLSGVVYAVLGYVFIRDKLNHHLFDLPEGFFTMLLVGIALGFISPLFGVEMGNAAHISGLIVGLIWGFIDSKLRKNSLE
Protein: Ribonucleotide reductase regulatory TP53 inducible subunit M2B (A0A8I5YCI9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGDPERPEAARPEEGEGLHCDFACLMFQYLVNKPSEERVMEIIVDAVKIEQEFLTEALPVGLIGMNCVLMKQYIEFVADRLLGELGFSKIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
Protein: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase (EC 1.1.1.127) (2-deoxy-D-gluconate 3-dehydrogenase) (2-keto-3-deoxygluconate 5-dehydrogenase) (2-keto-3-deoxygluconate oxidoreductase) (KDG oxidoreductase) (20-ketosteroid reductase) (EC 1.1.1.-) (P37769)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH (Ref.4). To a lesser extent, can also reduce 5-keto-D-gluconate and oxidize D-gluconate and 1,2-propanediol. Together with KduI, seems to play a role in the catabolism of hexuronates under osmotic stress conditions, substituting for the regular hexuronate degrading enzymes UxaABC and UxuAB whose expression is repressed in these conditions. In vitro, also exhibits NADH-dependent 20-ketosteroid reductase activity against eukaryotic steroid hormone 11-deoxycorticosterone (11-DOC), which is converted into the product 4-pregnen-20,21-diol-3-one. In addition to 11-DOC, five other C21 steroid compounds (11-deoxycortisol, cortisol, corticosterone, cortisone, and 21-hydroxypregnenolone) are reduced by KduD, but steroids lacking the hydroxyl group at C21 position, such as pregnenolone, testosterone propionate, cortisone acetate, or progesterone, cannot be used as substrate.
Interaction partners:
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
- 2-dehydro-3-deoxygluconokinase
- Altronate dehydratase
- Mannonate dehydratase
- Starvation-sensing protein RspA
- Ribose-5-phosphate isomerase B
- Ribulose-phosphate 3-epimerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- 2-keto-3-deoxygluconate permease
- Ribose-5-phosphate isomerase A
Sequence:
MILSAFSLEGKVAVVTGCDTGLGQGMALGLAQAGCDIVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLDRAVAEFGHIDILVNNAGLIRREDALEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPIVFLASSASDYVNGYTIAVDGGWLAR