wanglab/gogpt-training-data huggingface dataset:
Protein: General transcription factor IIH subunit 1 (A0A0G2JWQ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- General transcription factor IIH subunit 2
- General transcription factor IIH subunit 3
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 4
- General transcription and DNA repair factor IIH helicase subunit XPD
- Cyclin-H
- General transcription factor IIE subunit 1
- CDK-activating kinase assembly factor MAT1
- Cyclin-dependent kinase 7
- General transcription factor IIF subunit 2
Sequence:
MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATESSTSSHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAETVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPMLDLTALEDKPLDEGYGISSVPSTSNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQQAQNGQNGEPSSVDGNSGDTDCFQPAVKRAKLQESIEYEDLGNNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAVNQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNVSSSW
Protein: NADH--cytochrome b5 reductase 1 (EC 1.6.2.2) (Q9ZNT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reductase transferring electrons from NADH to cytochrome b5. Required for the NADH-dependent electron transfer involved in the desaturation and hydroxylation of fatty acids and in the desaturation of sterol precursors. No activity with NADPH as electron donor.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:21896887}; Single-pass membrane protein {ECO:0000269|PubMed:21896887}.
Interaction partners:
- Cytochrome b5 isoform E
- Cytochrome b5 isoform B
- Cytochrome b5 isoform A
- Cytochrome B5 isoform D
- Cytochrome B5 isoform C
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase
- NADH-cytochrome b5 reductase-like protein
- Uridine 5'-monophosphate synthase
- Cytochrome B5-like protein
Sequence:
MDTEFLRTLDRQILLGVFVAFVAVGAGAAYFLTSSKKRRVCLDPENFKEFKLVKRHQLSHNVAKFVFELPTSTSVLGLPIGQHISCRGKDGQGEDVIKPYTPTTLDSDVGRFELVIKMYPQGRMSHHFREMRVGDHLAVKGPKGRFKYQPGQFRAFGMLAGGSGITPMFQVARAILENPTDKTKVHLIYANVTYDDILLKEELEGLTTNYPEQFKIFYVLNQPPEVWDGGVGFVSKEMIQTHCPAPASDIQILRCGPPPMNKAMAANLEALGYSPEMQFQF
Protein: Suppressor of cytokine signaling 5 (SOCS-5) (Cytokine-inducible SH2 protein 6) (CIS-6) (Cytokine-inducible SH2-containing protein 5) (O75159)
Organism: Homo sapiens (Human)
Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits for instance EGF signaling by mediating the degradation of the EGF receptor/EGFR. Involved in the regulation of T-helper cell differentiation by inhibiting of the IL4 signaling pathway which promotes differentiation into the Th2 phenotype. Can also partially inhibit IL6 and LIF signaling.
Interaction partners:
- Interleukin-4 receptor subunit alpha
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK1
- Signal transducer and activator of transcription 1-alpha/beta
- Cullin-5
- Suppressor of cytokine signaling 6
- Suppressor of cytokine signaling 3
- Elongin-C
- Signal transducer and activator of transcription 3
- RING-box protein 2
Sequence:
MDKVGKMWNNFKYRCQNLFGHEGGSRSENVDMNSNRCLSVKEKNISIGDSTPQQQSSPLRENIALQLGLSPSKNSSRRNQNCATEIPQIVEISIEKDNDSCVTPGTRLARRDSYSRHAPWGGKKKHSCSTKTQSSLDADKKFGRTRSGLQRRERRYGVSSVHDMDSVSSRTVGSRSLRQRLQDTVGLCFPMRTYSKQSKPLFSNKRKIHLSELMLEKCPFPAGSDLAQKWHLIKQHTAPVSPHSTFFDTFDPSLVSTEDEEDRLRERRRLSIEEGVDPPPNAQIHTFEATAQVNPLYKLGPKLAPGMTEISGDSSAIPQANCDSEEDTTTLCLQSRRQKQRQISGDSHTHVSRQGAWKVHTQIDYIHCLVPDLLQITGNPCYWGVMDRYEAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYNRSLHARIEQWNHNFSFDAHDPCVFHSSTVTGLLEHYKDPSSCMFFEPLLTISLNRTFPFSLQYICRAVICRCTTYDGIDGLPLPSMLQDFLKEYHYKQKVRVRWLEREPVKAK
Protein: calcium/calmodulin-dependent protein kinase (EC 2.7.11.17) (F1QW17)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATIVTCTRFTDEYQLYEELGKGAFSVVRRCVKKSTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSIAEEGFHYLVFDLVTGGELFEDIVAREYYSESDASHCINQILESVSHIHQHDIVHRDLKPENLLLASKMKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSVGRQHTSPATPTTSTAALAQEACKSLLNKKSDGVKPQTNNNKNSVVSSSTKDSSISSTAPMEPQTTVVHNPADGTKGSTESCNTTEEEDMKGRKADPPHDVKNVAWSSSGQSSCPDLEPAVPAPASTTAGGSSVNRQQSRKQEIIKITEQLIEAINNGDFEAYTRICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPVHTTILNPHVHLIGEDAACIAYIRLTQYIDGQGRPRSSQSEETRVWHRRDAKWLNIHFHCSGAPAAPLQ
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (EC 7.1.1.2) (Complex I-49kD) (CI-49kD) (NADH-ubiquinone oxidoreductase 49 kDa subunit) (Q91WD5)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. Redox-sensitive, critical component of the oxygen-sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction. Plays an important role in carotid body sensing of hypoxia. Essential for glia-like neural stem and progenitor cell proliferation, differentiation and subsequent oligodendrocyte or neuronal maturation.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase iron-sulfur protein 5
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MAALRALRCLRGVGAPVLRPGSGIRLPSQPSRGARQWQPDIEWAEQFSGAVMYPSKETAHWKPPPWNDVDILKEKAVTNMTLNFGPQHPAAHGVLRLVLELSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSIAVEKLLNIQPPPRAQWIRVLFGEITRILNHIMAVTTHALDIGAMTPFFWMFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLLDDIYEFSKNFSLRIDEVEEMLTNNRIWRNRTVDIGVVTAEDALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPIGSRGDCYDRYLCRVEEMRQSLRIIEQCLNKMPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEIDR
Protein: Sll0638 protein (P72963)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Slr1661 protein
Sequence:
MKTTTHSRAMGQSASGDRRGLSRSLLNKLMAVGMGLTLASFSMAPAFAQTLSEKIVAMEKAREQEFAAYFGESLAEVTQTPEDIALTLQKITAETGKKPAVLWIIPEKEFLHLVLVTPDLDPIVVDLHDVPEAVLRPVVSTFQRELQLSQTVNRREASQQLYQWIIAPYAETLEAQGIDTLLFCLGNGVRGLPMAALFDGEEYLLEKYSLTNIPAFNLIDSNYKPLQPGNILAMGASEFADQSPLPAVPVELENIVWEMAINRPAADRWQAETFLNQDFTVDRLQKELEQKRPSIVHLATHSSFRSGKPANSYIEFWNDKLALNKVSQINWQSSAVELLVLSACQTALGDDQAELGFAGLALKAGVKSAVASFWNVDDAATLVLMTEFYRQLGQTSTKAEALRQAQLKMLRGELTAGLEQSGISRGAIALPPSLINLGQTNFSAPYYWASFTMLSSPW
Protein: NAD(+)-dependent glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2) (NAD-specific glutamate dehydrogenase) (A3MUY9)
Organism: Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)
Function: Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Is strictly specific for NAD(+)/NADH as the acceptor/donor, since it cannot use NADP(+)/NADPH. May function in vivo in the catabolic direction. Also catalyzes at low rates the oxidative deamination of L-norvaline, L-2-aminobutyrate, L-valine and L-isoleucine, and the reductive amination of 2-oxovalerate and 2-oxobutyrate.
Interaction partners:
- Sulfide dehydrogenase
- isocitrate dehydrogenase
- L-glutamine synthetase
- Aminotransferase
- Aminotransferase
- Carbamate kinase
- Citrate synthase
- Citrate synthase
- Phosphoribosylformylglycinamidine synthase subunit PurQ
- Dihydrolipoyl dehydrogenase
Sequence:
MSTTYIVSDFLINTLLTIKRGVELAGLPPEFYEALEKPKRILVVNIPVKMDDGKIKYFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSRLVGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIVGKTAAVQGLGNVGRWAAYWLEKMGAKVVAVSDVNGVVYRERGLDVDLIRETKAKGPQLLEMISQKNGVEIVKNPDQIFSLDVDILVPAAIENVVREDNVDGVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI
Protein: Membrane protein Rv1476 (O53167)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-
- Carboxylesterase/lipase Culp6
- Protein Rv3035
- Putative lipoprotein LprB
- Uncharacterized protein Rv0479c
- Probable conserved membrane protein
- Probable arabinosyltransferase A
- Terminal beta-
- Possible lipoprotein LprC
- Possible protease
Sequence:
MTGPYFPQTIPFLPSYIPQDVDMTAVKAEVAALGVSAPPAATPGLLEVVQHARDEGIDLKIVLLDHNPPNDTPLRDIATVVGADYSDATVLVLSPNYVGSYSTQYPRVTLEAGEDHSKTGNPVQSAQNFVHELSTPEFPWSALTIVLLIGVLAAAVGARLMQLRGRRSATSTDAAPGAGDDLNQGV
Protein: Transforming growth factor beta (A5YM40)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MKMHLQRALVVLALLNFATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNRTNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (Q7JAI4)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 2
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH-ubiquinone oxidoreductase 23 kDa subunit, mitochondrial, putative, expressed
- Os05g0509200 protein
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Os07g0585800 protein.
Sequence:
MNNQSIFQYSWEILPKKWVHKMKRSEHGNRFYTNTDYLFPLLCFLKWHTYTRVQVLIDICGVDYPSRKRRFEVVYNLLSTRYNSRIRVQTSADEVTRISSVVSLFPSAGWWEREVWDMFGVSFINHPDLRRILTDYGFEGHPLRKDFPLSGYVEVRYDDPEKRVVSEPIEMTQEFRYFDFASPWEQRSDG
Protein: Short transient receptor potential channel 4-associated protein (Trp4-associated protein) (Trpc4-associated protein) (Protein TAP1) (TNF-receptor ubiquitous scaffolding/signaling protein) (Protein TRUSS) (Q8TEL6)
Organism: Homo sapiens (Human)
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. Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome (By similarity). Involved in JNK activation via its interaction with TRAF2 (By similarity). Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1 (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:26038816}.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- Cullin-4B
- DET1- and DDB1-associated protein 1
- DDB1- and CUL4-associated factor 5
- DDB1- and CUL4-associated factor 4
- E3 ubiquitin-protein ligase RBX1
- DDB1- and CUL4-associated factor 12
- DDB1- and CUL4-associated factor 6
- DDB1- and CUL4-associated factor 8
Sequence:
MAAAPVAAGSGAGRGRRSAATVAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKQSKWSGIPQLLLKLHTTSHLHSDFVECQNILKEISPLLSMEAMAFVTEERKLTQETTYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQELEEWYTWLDNALVLDALMRVANEESEHNQASIVFPPPGASEENGLPHTSARTQLPQSMKIMHEIMYKLEVLYVLCVLLMGRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQELNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGLLEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFENQVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKKYPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE
Protein: LexA repressor (EC 3.4.21.88) (Q92PW3)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
Sequence:
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYAGASQVRRGFSPSVIEGSLGKPAAPPPAPKPAPPAEAASVAVPVMGRIAAGVPISAIQNNMHDISVPVEMIGSGEHYALEIKGDSMIEAGILDGDTVIIRNGSTASPGDIVVALIDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKIQGRLVGLIRRYH
Protein: Interleukin-26 (IL-26) (Protein AK155) (Q9NPH9)
Organism: Homo sapiens (Human)
Function: May play a role in local mechanisms of mucosal immunity and seems to have a pro-inflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin.
Subcellular location: Secreted {ECO:0000269|PubMed:18483078}.
Interaction partners:
- Interleukin-10 receptor subunit beta
- Interleukin-20 receptor subunit alpha
- Interleukin-22 receptor subunit alpha-1
- Interleukin-20 receptor subunit beta
- Interleukin-19
- Interleukin-22
- Signal transducer and activator of transcription 3
- Interleukin-17A
- Interleukin-24
- Signal transducer and activator of transcription 1-alpha/beta
Sequence:
MLVNFILRCGLLLVTLSLAIAKHKQSSFTKSCYPRGTLSQAVDALYIKAAWLKATIPEDRIKNIRLLKKKTKKQFMKNCQFQEQLLSFFMEDVFGQLQLQGCKKIRFVEDFHSLRQKLSHCISCASSAREMKSITRMKRIFYRIGNKGIYKAISELDILLSWIKKLLESSQ
Protein: Mitochondrial import inner membrane translocase subunit TIM13 (P53299)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10469659}; Peripheral membrane protein {ECO:0000269|PubMed:10469659}; Intermembrane side {ECO:0000269|PubMed:10469659}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM8
- Mitochondrial import inner membrane translocase subunit TIM12
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial import inner membrane translocase subunit TIM23
- Mitochondrial import receptor subunit TOM40
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM54
Sequence:
MGLSSIFGGGAPSQQKEAATTAKTTPNPIAKELKNQIAQELAVANATELVNKISENCFEKCLTSPYATRNDACIDQCLAKYMRSWNVISKAYISRIQNASASGEI
Protein: LP15256p (RH11839p) (Tropomodulin, isoform K) (Tropomodulin, isoform O) (C7LAH8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MADTAKDKDVIDQEDVEVEEQEETTTTTTTTKKTSQWHKTRTTKTSATTKTTTLTTPAKLYGKDLSEYDDVDVESLLAQLSPEEITILAKEVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQPEFEPFVQGKVRGKKWVPPPRDARDIEAEEQIAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQDQYHASLLNKGQPVGLGWDGITKSTQQKLFPMDPPNNTDVEESIKRVKDDDSKLIDLNLNNIKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFRASNQRSAVLGNKIEMEITDLVEKNSSLLRLGLHLEFNDARHRVAAHLQRNIDRIRKDLELRLQFRFFNNLHRKSTRIQ
Protein: Transcription factor TCP21 (Protein CCA1 HIKING EXPEDITION) (Protein CHE) (Q9FTA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the regulation of the circadian clock. Acts as a repressor of CCA1 by binding to its promoter. No binding to the LHY promoter.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701, ECO:0000269|PubMed:19286557}.
Interaction partners:
- Two-component response regulator-like APRR1
- Transcription factor TCP7
- Transcription factor TCP13
- Transcription factor TCP3
- Transcription factor TCP10
- Transcription factor TCP5
- Transcription factor TCP17
- Transcription factor TCP4
- Transcription factor TCP2
- Protein CCA1
Sequence:
MADNDGAVSNGIIVEQTSNKGPLNAVKKPPSKDRHSKVDGRGRRIRMPIICAARVFQLTRELGHKSDGQTIEWLLRQAEPSIIAATGTGTTPASFSTASLSTSSPFTLGKRVVRAEEGESGGGGGGGLTVGHTMGTSLMGGGGSGGFWAVPARPDFGQVWSFATGAPPEMVFAQQQQPATLFVRHQQQQQASAAAAAAMGEASAARVGNYLPGHHLNLLASLSGGANGSGRREDDHEPR
Protein: Homeobox protein DLX-6 (P56179)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein DLX-5
- Runt-related transcription factor 2
- Putative protein SEM1, isoform 2
- Bone morphogenetic protein 2
- Methyl-CpG-binding protein 2
- Tumor protein 63
Sequence:
MSHSQHSPYLQSYHNSSAAAQTRGDDTDQQKTTVIENGEIRFNGKGKKIRKPRTIYSSLQLQALNHRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKRSKFKKLLKQGSNPHESDPLQGSAALSPRSPALPPVWDVSASAKGVSMPPNSYMPGYSHWYSSPHQDTMQRPQMM
Protein: GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (Glutamine amidotransferase) (Q9CAD1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- Guanylate kinase 3, chloroplastic
- Guanylate kinase 1
- Guanylate kinase 2
- Adenine phosphoribosyltransferase 1, chloroplastic
- Adenine phosphoribosyltransferase 5
- Adenine phosphoribosyltransferase 4
- Adenine phosphoribosyltransferase 2
- Adenine phosphoribosyltransferase 3
Sequence:
METPTMKPDTVLILDYGSQYTHLITRRIRSLNVFSLVISGTSSLKSITSYNPRVVILSGGPHSVHALDAPSFPEGFIEWAESNGVSVLGICYGLQLIVQKLGGVVVEGESKEYGKMEIEVKGKSEIFGSESGGEKQMVWMSHGDEAVKLPEGFEVVAQSAQGAVAALESRKKKIYGLQYHPEVTHSPKGMETLRHFLFDVCGVSADWKMEDLMEEEIKVINKTVASDEHVICALSGGVDSTVAATLVHKAIGDRLHCIFVDNGLLRYKEQERVMDTFERDLHLPVTCVDASERFLSELKGVVDPETKRKIIGREFINIFDQFAQELEKKHGKKPAFLVQGTLYPDVIESCPPPGTDRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRELGRILNVPVGFLKRHPFPGPGLAVRVLGDVTQGNALEVLRQVDEIFIQSIRDAGLYDSIWQAFAVFLPVRSVGVQGDKRTHSHVVALRAVTSQDGMTADWFNFEHKFLDDVSRKICNSVQGVNRVVLDITSKPPSTIEWE
Protein: Plasma membrane ammonium transporter (Ato3), putative (AFU_orthologue AFUA_5G01140) (Q5ATJ0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSDITDKPSDETINLNRMKTAESVFLPISRETFEKLYLTPKHPSVQTDLRKKFGNPTPICLMGFLIASTPHACMLMGWRGAGGNGSALVPTYIFFGGIVQILGGIGEWIIGNTFSCAIFFTYGTFWLVQGGGLMPFFASGMNYSPTGNSFEGQQTGEYAATIAFYYVFLGLLTFIYLICSIRTNVCLFSALFLLVITFSLVAGAFFQLANGAHELAEKLLVAGGAFNFALCVPVWHIFLTQILEAVDFPISVPVGDLSSIVPGRSQKVKRAED
Protein: Accessory gland protein 98AB (O46201)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for physiological and behavioral changes in mated female flies.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Accessory gland protein Acp63F
- Accessory gland protein Acp36DE
- Accessory gland-specific peptide 95EF
- Accessory gland protein Acp53Ea
- Accessory gland protein Acp32CD
- Accessory gland-specific peptide 26Aa
- ACP53C14A
- Accessory gland protein Acp76A
- Ductus ejaculatorius peptide 99B
- Accessory gland peptide Acp33A
Sequence:
MKLLILFLAALGAASARIRGHTIKG
Protein: Protein VP3 [Includes: 2',5'-phosphodiesterase (EC 3.1.4.-); mRNA guanylyltransferase (EC 2.7.7.50); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56)] (B1NKT1)
Organism: Rotavirus A (strain RVA/Human/United States/P/1974/G3P1A[8]) (RV-A)
Function: Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04128}. Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04128}.
Interaction partners:
Sequence:
MKVLALRHSVAQVYADTQTYLHDDSKDEYENAFLISNLTTHNILYLNYSLKTLKILNKSGIAAVEVQSPDELFALIRCNFTYDYENNIIYLHDYSYYTNNEIRTDQHWITKTDIIDYLLPGWKLTYVGYNGKNTRGHYNFSFSCQNAATDDDIIIEYIYSNELDFQNFLLRKIKERMTTSLPIARLSNRVFRDKLFPSIVNIYKKVINVGPRNESMFTFLNFPTIKQFSNGAYIVKHTIKLKQEKWLGKRVSQFDIGQYKNMLNVVTTIYYYYNLYHSKPIIYMLGSAPSYWIHDIKQYSDFTFETWDPLDTPYSTIHHKELFFDKDVNKLKDNSVLYIDIRTDRKNMDWKEWRKVVEQQTVNNLNIAYKYLSTGKAKVCCVKLTAMDLELPITAKLLHHPTTEVRSEFYAILDAWDIITIKRFIPKGVFYAFINNITTENVFIQPPFKLKASPTDYIVALYALSNDFNSRQDVINLINKQKQSLITVRMNNTFKDEPKVNFKNIYDWTFLPTDFELKDSIITSYDGCLGMFGLSISLSSKPTGNNHLFIINGTDKYYKLDQYANHMGISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNVENSVSGHVYNALIYYRYNYAFDLKRWIYLHSIGKVTVEGGRYYEHAPIELIYACRSAKEFAILQDDLTVLRYANEIEGYINKVYSITYADDPNYFIGIKFNSIPYEYDVKVPHLTLGVLFISDNMIHDVVTVLKKMKTELFKTEISTSYTYMLSDNIYVANASGVLSTYFKLYNMFYRNHITFGQSRMFIPHITLSFSNKQTVRIESTRLKINSIYLRKIKGETVFDMSE