wanglab/gogpt-training-data huggingface dataset:
Protein: Kinesin-like protein KIF21B (Kinesin-like protein KIF6) (Q9QXL1)
Organism: Mus musculus (Mouse)
Function: Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10225949}. Cell projection, dendrite {ECO:0000269|PubMed:10225949, ECO:0000269|PubMed:24086586, ECO:0000269|PubMed:25172774, ECO:0000269|PubMed:27117409}. Cell projection, growth cone {ECO:0000269|PubMed:24086586}. Cell projection, axon {ECO:0000269|PubMed:10225949}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:F1M5N7}.
Interaction partners:
- Protein smoothened
- Kinesin-like protein KIFC2
Sequence:
MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDTVTSEEEQGIIPRAIAHLFRGIDERKRRAQEKGVTGPEFKVSAQFLELYNEEILDLFDSTRDPDARHRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRVCAQPDLVNETVTGLPDGAAPTGTEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELMEYKAGKRVIGEDGTEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARNPYSLGASPAGPAFGGSPATSMEDASEVIRKAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQAENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAEVSASTTSSEAESGARSVSSIVRQWNRKIDHFLGDRPTATVNGGRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMTGSSQNHLLLDALREKAEAHPELQALIYNVQHENGYASTDEEVSEFSEGSFSQSFTMKGSTSHDDFKFKGEPKLSAQMKAVSAECLGPPLDSSTKNITKSLASLVEIKEDGVGFSIRDPYYRDKVSRTVSLPTRGSTFPRQSRGATDTSPLTRRKSYDRGQPIRSTDMGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDKSDDSDSSLSEVLRGIITPIGGAKGARTAPLQCISMAEGHTKPILCLDATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSSSYIKVWDIRDSAKCIRTLTSSGQVISGDACIATSTRAITSAQGEHQINQMALSPSGSMLYVASGNAVRIWELNRFQPIGKLTGHIGPVMCLTVTQTSNQHDLVVTGSKDHYVKMFQLGDCVTGTIGPTHNFEPPHYDGIECLAIQGDILFSGSRDNGIKKWDLDQQELIQQIPNAHKDWVCALAFVPGRPMLLSACRAGFIKVWNVDNFTPIGEIKGHDSPINAICTNSKHIFTASSDCRVKLWNYVPGLTPCLPRRVLAIKGRAPPCPDLPPPPLTLPILPFPVFPPPRSELLLHVT
Protein: ZNF578 protein (Q3MI94)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
SCRPETHTPNNYGNNFFHSSLLTQKQEVHMREKSFQCNETGKAFNCSSFVRKHQIIHLGEKQYKFDICGKVFNEKRYLARHRRCHTSEKPYKCNECGKSFSYKSSLTCHRRCHTGEKPYKCNECGKSFSYKSSLTCHHRCHTGEKPYKCNECGKSFSYKSSLRCHRRLHTGIKPYKCNECGKMFGQNSTLVIHKAIHTGEKPYKCNECGKAFNQQSHLSRHHRLHTGEKPYKCNDCGKAFIHQSSLARHHRLHTGEKSYKCEECDRVFSQKSNLERHKIIHTGEKPYKCNECHKTFSHRSSLPCHRRLHSGEKPYKCNECGKTFNVQSHLSRHHRLHTGEKPYKCKVCDKAFMCHSYLANHTRIHSGEKPYKCNECGKAHNHLIDSSIKPCMSS
Protein: Large ribosomal subunit protein eL28 (60S ribosomal protein L28) (Q7SXI9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASPHLQWMVIRNSSSFLIKRNKQTYSTEPNNLKARNAFRFNGLIHRKTIGIEPAADGKGVVVVLKKRSGQRKPATSYGKITINKNSRATLASVRNIIRKNKYRRDLRMAALRRVSAILSSQKPVVVRKKRSRAPKSS
Protein: Epoxide hydrolase 1 (EC 3.3.2.10) (CEEH1) (G5EBI4)
Organism: Caenorhabditis elegans
Function: Catalyzes the hydrolysis of epoxide-containing fatty acids. Active against epoxyeicosatrienoic acids (EETs) including 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate (8,9-EET), 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate (11,12-EET) and 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate (14,15-EET) and the linoleic acid metabolites 12,13-epoxy-(9Z)-octadecenoate (12,13-EpOME) and 9,10-epoxy-(12Z)-octadecenoate (9,10-EpOME). These epoxides function as lipid signaling molecules, the enzyme can deplete the supply of the epoxide signal by transforming them into diol species that are more readily eliminated through excretion.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fatty acid synthase
Sequence:
MLFESIYIQCLNKFSKYKKFVCHTTCNCPNYKIIGYLLYFLCLCRPINCSLPLSRHDLAFGSFSYYLTMFLYRILVRLLQFYYFVKFSAILFLGFAVKGRSLFEKKQREKPNVLEGWDSRYIKLKKVRLHYVQTGSDDKPLMLFIHGYPEFWYSWRFQLKEFADKYRCVAIDQRGYNLSDKPKHVDNYSIDELTGDIRDVIEGLGYDKAIVVAHDWGGLVAWQFAEQYPEMVDKLICCNIPRPGSFRKRIYTSWSQFRKSWYMFFYQNEKIPEMLCSADDMKMLELCFRAKEIGIQNNKNFTDEDLEAWKYSFSMNGASFKYPINYYRNIFNAKKQQADLVLEMPTLIIWGTADGALDIEAAVDSLNTLKQGTMKKIEGASHWVQQDEPEMVNEHIKKFLNKYQ
Protein: Ammonium transporter Rh type A (Erythrocyte membrane glycoprotein Rh50) (Rhesus blood group family type A glycoprotein) (Q7T067)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPTYSTNMRLKFPILALILEIITIVLYALFVVYDTGDDKGHGDHHEKSNQTESPMTLYPMFQDVHVMIFIGFGFLMTFLKRYGFTSVGVNLLLAAFGLQWGLLLQNVWHMHGGKIRVSIDRMINADFSTATVLISFGAVLGKTSPVQLLIMTLLEITTFCINEYLVVEILGVSDVGASMTIHAFGAYFGLSVARVLYRPGLRNGHDNDGSLYHSHLFAMIGTVYLWMFWPSFNSAIATPGDHQLRAVVNTYFSLAACALAAYATSSLVEKKGKLDMVHIQNATLAGGVAVGTCADMDIQPFGAMLIGITAGIISTVGFKFLTPILASKLGIQDTCGVHNLHGMPGILGGVAGILAAALKRKEGVSPTYQAAGLASSLGFALVGGLITGLIMKIPFLGQPPDQNCFDDSIYWEVPEEEEETEERLTHGDYSKNKAEA
Protein: Isoleucine--tRNA ligase, mitochondrial (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS) (Q9NSE4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000305}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Glutamine--tRNA ligase
- Probable proline--tRNA ligase, mitochondrial
- Probable arginine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MRWGLRPRGPGAAALATARSLWGTPRLPCSPGWQGATKRLLVRSVSGASNHQPNSNSGRYRDTVLLPQTSFPMKLLGRQQPDTELEIQQKCGFSELYSWQRERKVKTEFCLHDGPPYANGDPHVGHALNKILKDIANRFHMMNGSKIHFVPGWDCHGLPIEIKVLSELGREAQNLSAMEIRKKARSFAKAAIEKQKSAFIRWGIMADWNNCYYTFDGKYEAKQLRTFYQMYDKGLVYRSYKPVFWSPSSRTALAEAELEYNPEHVSRSIYVKFPLLKPSPKLASLIDGSSPVSILVWTTQPWTIPANEAVCYMPESKYAVVKCSKSGDLYVLAADKVASVASTLETTFETISTLSGVDLENGTCSHPLIPDKASPLLPANHVTMAKGTGLVHTAPAHGMEDYGVASQHNLPMDCLVDEDGVFTDVAGPELQNKAVLEEGTDVVIKMLQTAKNLLKEEKLVHSYPYDWRTKKPVVIRASKQWFINITDIKTAAKELLKKVKFIPGSALNGMVEMMDRRPYWCISRQRVWGVPIPVFHHKTKDEYLINSQTTEHIVKLVEQHGSDIWWTLPPEQLLPKEVLSEVGGPDALEYVPGQDILDIWFDSGTSWSYVLPGPDQRADLYLEGKDQLGGWFQSSLLTSVAARKRAPYKTVIVHGFTLGEKGEKMSKSLGNVIHPDVVVNGGQDQSKEPPYGADVLRWWVADSNVFTEVAIGPSVLNAARDDISKLRNTLRFLLGNVADFNPETDSIPVNDMYVIDQYMLHLLQDLANKITELYKQYDFGKVVRLLRTFYTRELSNFYFSIIKDRLYCEKENDPKRRSCQTALVEILDVIVRSFAPILPHLAEEVFQHIPYIKEPKSVFRTGWISTSSIWKKPGLEEAVESACAMRDSFLGSIPGKNAAEYKVITVIEPGLLFEIIEMLQSEETSSTSQLNELMMASESTLLAQEPREMTADVIELKGKFLINLEGGDIREESSYKVIVMPTTKEKCPRCWKYTAESSDTLCPRCAEVVSGK
Protein: Hemocyanin C chain (P83172)
Organism: Cherax destructor (Common yabby crayfish)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
DGSGGASDAQKQHDVNYLLFKVYEDVNDENSP
Protein: Cytochrome b5 (A0A384ME44)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004131}. Microsome membrane {ECO:0000256|ARBA:ARBA00037877}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037877}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037877}.
Interaction partners:
Sequence:
MAEQSDEAVKYYTLEEIQKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDAREMSKTFIIGELHPDDRPKLNKPPETLITTIDSSSSWWTNWVIPAISAVAVALMYRLYMAED
Protein: Rho-GTPase-activating protein RGD2 (P43556)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts in signal transduction. Activates CDC42 and RHO5.
Interaction partners:
- GTP-binding protein RHO5
- RHO GTPase-activating protein RGD1
- Rho-GTPase-activating protein BAG7
- Rho-GTPase-activating protein LRG1
- GTPase-activating protein SAC7
Sequence:
MLSFCDYFWSEDLVSGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEAGMDNLKAVQEDEDEGVTVSRALRGILQEMSQEGTHHLTIASNIESLVLQPFSKWCIEHRERIQYSEKTLLTNVNNFRKSKKYVGKLEKEYFNKCRQLEEFKRTHFNEDELANAMKSLKIQNKYEEDVAREKDHRFFNRIAGIDFDYKTMKETLQLLLTKLPKTDYKLPLISYSLSNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKKFQYQWKNTAYMFANVPMPGSEEPTTGESLISRFNNWDGSSAKEIIQSKIGNDQGAAKIQAPHISDNERTLFRMMDALAASDKKYYQECFKMDALRCSVEELLIDHLSFMEKCESDRLNAIKKATLDFCSTLGNKISSLRLCIDKMLTLENDIDPTADLLQLLVKYKTGSFKPQAIVYNNYYNPGSFQNFGVDLETRCRLDKKVVPLIISSIFSYMDKIYPDLPNDKVRTSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIFDILSTSKLEPSTIASVVKIYLLELPDPLIPNDVSDILRVLYLDYPPLVETALQNSTSSPENQQDDDNEEGFDTKRIRGLYTTLSSLSKPHIATLDAITTHFYRLIKILKMGENGNEVADEFTVSISQEFANCIIQSKITDDNEIGFKIFYDLLTHKKQIFHELKRQNSKN
Protein: Serine/threonine-protein kinases PknA (EC 2.7.11.1) (Q8NU97)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- Protein serine/threonine phosphatases
- Cell division protein FtsI/penicillin-binding protein 2
- Oxoglutarate dehydrogenase inhibitor
- FHA-domain-containing proteins
- Cell division protein FtsZ
- FHA domain-containing protein
- Probable serine/threonine-protein kinase PknB
- Bacterial cell division membrane protein
- Cell division protein CrgA
- Thioredoxin-like fold domain-containing protein
Sequence:
MSQEDITGKDRLQELIGADYRLQWIIGHGGMSTVWLADDVVNDREVAIKVLRPEFSDNQEFLNRFRNEAQAAENIDSEHVVATYDYREVPDPAGHTFCFIVMEFVRGESLADLLEREGRLPEDLALDVMEQAAHGLSVIHRMDMVHRDIKPGNMLITANGIVKITDFGIAKAAAAVPLTRTGMVVGTAQYVSPEQAQGKEVTAASDIYSLGVVGYEMMAGRRPFTGDSSVSVAIAHINQAPPQMPTSISAQTRELIGIALRKDPGRRFPDGNEMALAVSAVRLGKRPPQPRTSAMMAQAEAPSPSESTAMLGRVARPATITQEAAPKRGSGIGIGLFIAALLAVIIGAVIYAGTTGILFNDTPEETTTPETITETYTPTVEETTSQWVPPTPPTRSTFTEPETTSHRPTTSEESTSEEPTTEAPTSSRTVPQIPTSTPRTSASVPVETNAPADDLIDAVNGLLDVGGAQ
Protein: Actin-2 (EC 3.6.4.-) (P10984)
Organism: Caenorhabditis elegans
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-related protein 2
- Actin-related protein 3
- Actin-1
- DNA-directed RNA polymerase II subunit RPB1
- Actin-related protein 2/3 complex subunit
- Probable actin-related protein 2/3 complex subunit 4
- Probable actin-related protein 2/3 complex subunit 3
- Probable actin-related protein 2/3 complex subunit 2
- Actin-related protein 10
- Tropomyosin isoforms a/b/d/f
Sequence:
MCDDDVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEALFQPSFLGMESAGIHETSYNSIMKCDIDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Envelope glycoprotein gp130 (Env polyprotein) [Cleaved into: Leader peptide (LP) (Env leader protein) (Elp) (gp18LP); Surface protein (SU) (Glycoprotein 80) (gp80); Transmembrane protein (TM) (Glycoprotein 48) (gp48)] (Q87041)
Organism: Simian foamy virus (isolate chimpanzee) (SFVcpz)
Function: The surface protein (SU) attaches the virus to the host cell by binding to the cell receptor. This interaction triggers the refolding of transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity).
Subcellular location: [Envelope glycoprotein gp130]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:23132852}. Note=The polyprotein has a highly unusual biosynthesis for a retroviral glycoprotein. It is translated as a full-length precursor protein into the rough endoplasmic reticulum and initially has a type III protein configuration with both its N and C-termini located intracytoplasmically (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Its N-terminus is located inside the viral particle. {ECO:0000250}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane; Peripheral membrane protein. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. {ECO:0000305}.
Interaction partners:
Sequence:
MAPPMTLQQWIIWNKMNKAHEALQNSTTVTDQQKEQIILEIQNEEVRPTRKDKIRYLLYTCCATSSRVLAWMLLVCVLLIVVLVSCFLTISRIQWNRDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYIEVNMTSIPQGVYYEPHPEPIVVTERVLGLSQVLMINSENIANNANLTQEVKKLLAEVVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFAHCYLVKYKTPKSWPTEGLIADQCPLPGYHAGLSYKPQSIWDYYIKVEITRPANWSSQAVYGQARLGSFYVPKGIRQNNYSHVLFCSDQLYSKWYNIENSIEQNEKFLLNKLDNLTTGSSLLKKRALPKEWSSQGKNALFKEINVLDVCSKPELVILLNTSYYSFSLWEGDCNFTKNMISQLVPECEGFYNNSKWMHMHPYACRFWRSKNEKEETKCRPGEKEKCLYYPYQDSLESTYDFGFLAYQKNFPAPICIEQQEIRDKDYEVYSLYQECKLASKVHGIDTVLFSLKNFLNHTGRPVNEMPNARAFVGLVDPKFPPSYPNVTREHYTSCNNRKRRSTDNNYAKLKSMGYALTGAVQTLSQISDINDENLQQGIYLLRDHVITLMEATLHDISVMEGMFAVQHLHTHLNHLKTMLLERRIDWTYMSSAWLQQQLQKSDDEMKVIKRIAKSLVYYVKQTYNSPTATAWEIGLYYELTIPKHVYLNNWNVVNIGHLVQSAGQLTHVTIAHPYEIINKECTETKYLHLKDCRRQDYVICDVVEIVQPCGNSTDTSDCPVWAEAVKEPFVQVNPLKNGSYLVLASSTDCQIPPYVPSIVTVNETTSCYGLNFKKPLVAEERLGFEPRLPNLQLRLPHLVGIIAKIKGLKIEVTSSGESIKDQIERAKAELLRLDIHEGDTPAWIQQLAAATKDVWPAAASALQGIGNFLSGAAHGIFGTAFSLLGYLKPILIGVGVILLIILIFKIVSWIPTKKKSQ
Protein: D-beta-hydroxybutyrate dehydrogenase, mitochondrial (EC 1.1.1.30) (3-hydroxybutyrate dehydrogenase) (BDH) (P29147)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:8515054}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q02337}.
Interaction partners:
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Dehydrogenase/reductase SDR family member 6
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Acetoacetyl-CoA synthetase
- Acetyl-CoA acetyltransferase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
Sequence:
MLAARLSRPLSQLPGKALSVCDRENGTRHTLLFYPASFSPDTRRTYTSQADAASGKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLLKDKGDAGVRELDSLKSDRLRTIQLNVCNSEEVEKAVETVRSGLKDPEKGMWGLVNNAGISTFGEVEFTSMETYKEVAEVNLWGTVRTTKSFLPLLRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMHPLGVKVSVVEPGNFIAATSLYSPERIQAIAKKMWDELPEVVRKDYGKKYFDEKIAKMETYCNSGSTDTSSVINAVTHALTAATPYTRYHPMDYYWWLRMQVMTHFPGAISDKIYIH
Protein: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC 2.4.1.102) (EC 2.4.1.148) (EC 2.4.1.150) (C2GnT-mucin type) (C2GnT-M) (hC2GnT-M) (Core 2/core 4 beta-1,6-N-acetylglucosaminyltransferase) (C2/4GnT) (O95395)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- C1GALT1-specific chaperone 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- C1GALT1-specific chaperone 1-like protein
Sequence:
MVQWKRLCQLHYLWALGCYMLLATVALKLSFRLKCDSDHLGLESRESQSQYCRNILYNFLKLPAKRSINCSGVTRGDQEAVLQAILNNLEVKKKREPFTDTHYLSLTRDCEHFKAERKFIQFPLSKEEVEFPIAYSMVIHEKIENFERLLRAVYAPQNIYCVHVDEKSPETFKEAVKAIISCFPNVFIASKLVRVVYASWSRVQADLNCMEDLLQSSVPWKYFLNTCGTDFPIKSNAEMVQALKMLNGRNSMESEVPPKHKETRWKYHFEVVRDTLHLTNKKKDPPPYNLTMFTGNAYIVASRDFVQHVLKNPKSQQLIEWVKDTYSPDEHLWATLQRARWMPGSVPNHPKYDISDMTSIARLVKWQGHEGDIDKGAPYAPCSGIHQRAICVYGAGDLNWMLQNHHLLANKFDPKVDDNALQCLEEYLRYKAIYGTEL
Protein: General transcription factor II-I repeat domain-containing protein 1 (Binding factor for early enhancer) (BEN) (XBEN) (GTF2I repeat domain-containing protein 1) (Williams-Beuren syndrome critical region 11-like protein) (XWBSCR11) (B7ZQJ9)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that activates a subset of organizer-specific genes. Binds to the distal element (DE) of the gsc promoter to regulate its expression. In the presence of pou5f1.1/oct-25, forms a repression complex on the promoter of the gsc and mix2 genes to inhibit their transcription.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UHL9, ECO:0000255|PROSITE-ProRule:PRU00484}.
Interaction partners:
Sequence:
MALAGKQYEGSLNNSRPNLWPSSIPGGKNEIITSLVTALDSMCTALSKLNTEVACIALHEESAFVVGTEKGRCFLNSRKELQADFQRFCIGAHKKDQENEVKRRNRDGIQNIQHVPLGPTSDIYLLRKMVEEIFEVLYSEALGKSNIVPVPYVKVMKEPGSVVVLGLPDGISFRKPAEYDLKSLMLILKHSHNIRFKLRIPTEESIREPKSCSELNSPPTSATKVIPETSQCHRLPIQEHPSSASNFPYSVSQPNQISLEPKQEVHSNMLGTNAVNQMLVQRPSAENNHDLSDCCGQQSPVAGSSLRQNVLASKHLLFSIVHDKTDKWDSFLRETEDINILRECVQILFNSRYAGALGLDHMVPVPYRKIACHPEAVEINGFPDKIPFKRPCTYGVPKLKRILEERHNIHFTIKSMFDQRIFDGTTFTKETTKSDSSSLGEEACSENQKAAALDMLGFPTGSRSEKSSISDECEPGTSSETTGVKLIKLEAEDPDIMQIAVPGTSSETSGVKIIKLESEDPDLIQITVPGTSNETSGVKPKLESEDPDLIQIAVPDRLAECVKNHLAPEDPSYVLDTGKVCDDRPCGVLRNENKHLDGIGDIIRQLRKHVENLFNRKYAKAIGASGPVKVPYAKFLMYPEDLFVLGLPEGVAFRRPNCFGITKLRRILEYSDGIQFVVKRPELISEGLEDCVVGSPGTLGFNDKSNEVILDETNTRPSFQESFDARLSRIDIANTLREQVQVLFNKKYGEALGIKYPVQVPYKRIKNNPGSVIIEGLPPGIPFRKPCTFGSQNLERILAVADKIRFTVTRPFQGLIPRPDDEDANRLGEKVILREQVKELFNEKYGKALGLDQPALIPYKLIRDNPDAVEVRGMPNDIPFRNPNSYDLHRLENILKAQDQIQMVVIKQLEPFPEICSEPPKIKNGNTGPKRKRKRVSEGNSISSASSNCSSSSSSSSNMDPISSAHHVSLVQWPMYMLDYGGLNMQLPGPINY
Protein: Transcription elongation factor TFIIS (Protein REDUCED DORMANCY 2) (Q9ZVH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites (Probable). Involved in the control of seed dormancy and germination.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000269|PubMed:19150360}.
Interaction partners:
- Transcription elongation factor SPT4 homolog 2
- Transcription initiation factor IIB-1
- Transcription elongation factor SPT6 homolog
- DNA-directed RNA polymerase II subunit 4
- FACT complex subunit SPT16
- DNA-directed RNA polymerase II subunit 2
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases II, IV and V subunit 11
- FACT complex subunit SSRP1
- Mediator of RNA polymerase II transcription subunit 6
Sequence:
MESDLIDLFEGAKKAADAAALDGVTSSGPEVSQCIDALKQLKKFPVTYDTLVATQVGKKLRSLAKHPVEDIKSVATDLLEIWKKVVIEETAKAKKTEGTNGCKEAKVNKMDVEKPSNPAPVKVQKLQRGDSAKSIKVERKEPDNKVVTGVKIERKVPDIKVTNGTKIDYRGQAVKDEKVSKDNQSSMKAPAKAANAPPKLTAMLKCNDPVRDKIRELLVEALCRVAGEADDYERESVNASDPLRVAVSVESLMFEKLGRSTGAQKLKYRSIMFNLRDSNNPDLRRRVLTGEISPEKLITLSAEDMASDKRKQENNQIKEKALFDCERGLAAKASTDQFKCGRCGQRKCTYYQMQTRSADEPMTTYVTCVNCDNHWKFC
Protein: Uncharacterized protein (Q582T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
- STI1 domain-containing protein
Sequence:
MANAALEENFVKAASLVREGNHIAAIGLYKTISSDEHITVAQKIRAFSNMSACYAAREQFAEALSAAKEALQMDDRNSKVHGRMAAAYHGLKHYEEASRHYARAYELDPNTILYKEQHQLVLELMRSGRGVASKDTLDSYYYRKGIEQGKEAMTKGEYLSAVRHFSKAIELHTKCASNGESNRGNGGGSVAADMAVLLCNRSAAYARAGRWSESLKDGMRAIEVHPTYARAFFRVGCAQHQLKRPQESCTALRRCLELDPSHGEAKNLMVEVEKLVAEACKTTEEREREREIQVREILERQNAEGATHAVGSRGRAHATSYVLCSYCNDGGHTREECPLLRRKRSRTS
Protein: Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase) (Q6FTL6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MTKDTIFTLTGKCALDNILDANRQWAQAMHRSQPQLFPTNGQGQDPHTLFIGCSDSRYNEDCLGVLPGEIFTLKTVANICHTDDHSLLATLEFAILNLKVNRIILCGHTDCGGIKTCLLGRESIKESCPHLYEHLDDIEDLVESHESELNQLDNICSKSKLMSHRNVERQLQRLLQIPVVQDALRNSNQDHEFNIFGLVYNVDSGLVDVVREVYGNQQK
Protein: Maleylacetoacetate isomerase (MAAI) (EC 5.2.1.2) (O43123)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Fumarylacetoacetase
- Homogentisate 1,2-dioxygenase
- homogentisate 1,2-dioxygenase
- homogentisate 1,2-dioxygenase
- Fumarylacetoacetase
- Fumarylacetoacetase
- glutathione transferase
- Condensation domain-containing protein
- Glutathione S-transferase
Sequence:
MSTNSDLRVTLYTYFRSSCSARLRIALALRSISYTSVPINLLKGEQSSTKNTAVNPSATVPTLIIEHVDRSQSPITITQSLAALEYLDEAFPDNPNPLLPPISNPQQRALVRSLASIIACDIQPVTNLRILQRVAPFGVDRAAWSKDLIEAGFAAYEAIARDSAGVFSVGDTITMADVCLIPAVWGAERAGVNLGQYPTIKRVAEALEKENAVKEGHWRTQQDTPTEFRC
Protein: Bomanin Bicipital 1 (Bomanin-23) (Immune-induced peptide 23) (DIM-23) (DIM23) (Q9V8F5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Secreted immune-induced peptide induced by Toll signaling. Has a role in resistance to bacterial and fungal infections.
Subcellular location: Secreted {ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738, ECO:0000269|Ref.5}.
Interaction partners:
- Bomanin Short 1
- Daisho1
- Bomanin Short 2
- GNBP-like 3
- Bomanin Short 3
- Bomanin bicipital 2, isoform A
- demerged
- Bomanin bicipital 3, isoform A
- Bomanin Tailed 2
- Bomanin Short 5
Sequence:
MKCLILSFAIFVVLASQATAGNVIIGGVCQDCSPPVAENVVVGGQSYRTGRPGQGTVYINSPGAYLGALDGPIRRTGAGGGGGGGAQYPDGYSGRLPGGTYLHNKDCVGCSISGGGD
Protein: Probable peptidase (O07178)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable aldehyde dehydrogenase
- DUF779 domain-containing protein
- Probable protease II PtrBa [first part]
- Conserved hydrophobic protein
Sequence:
MTFEPAPDGADPYLWLEDVTGAEALDWVRARNKPTTAAFCDAEFERMRVEALEVLDTDARIPYVNRRGNYLYNFWRDAANPRGLWRRTTLDSYRTDSPGWDVLIDVDELGRADDQKWVWGGAGVIEPDYTRALIGLSPGGSDASIVREFDMLTREFVEDGFQLPPAKSQITWEDPDTVLLGTDFGGDSLTTSGYPRVIKRWRRGKPLADAETIFEGAGTDVRVNASADRTPGFERTLLGRALDFWNEEVYELRGSELIRIEAPTDASVSIHRDWLLIELRTDWTVATTRYTAGSLLAAEYDEFLAGSAELQVVFEPDEHTALYQYAWTRDRLLIVTLADVASRVEIATPGSWRREPLSGIPAATNTVIVSADSHGDEFFLDSSGFDTPSRLMRGTDDGRLAEIKSAPAFFDAENMAVTQYFATSDDGTSIPYFVVRRTDADNPGPTLLNGYGGFETSRTPTYDGVLGRLWLARGGTYALANIRGGGEYGPGWHTQAMREGRDKVAQDFAAVATDLVTRGITTAEQLGARGGSNGGLLMGIMLTGYPEKFGALVCDVPLLDMKRYHLLLAGASWMAEYGDPDNPDDWKFISEYSPYQNISANRKYPPVLMTTSTRDDRVHPGHARKMTAALQAAGHPVWYYENIEGGHAGAADNAQIAFKSALSFAFLWRMLAG