wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 90 kDa subunit homolog) (eIF3 p90) (Translation initiation factor eIF3 p90 subunit homolog) (Q5AGV4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit H
- JAB1/MPN/MOV34 metalloenzyme domain-containing protein
- Eukaryotic translation initiation factor 2 subunit gamma
- Eukaryotic translation initiation factor 3 subunit C
- Translation initiation factor eIF5
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 2 subunit alpha
Sequence:
MSINEEDYLQLEKEIKLDDIDFSDLEEKYEVNIGLDNYIIVDGAPIAPEAKVPVLIKVLRKLFSQVGEIVEGDEGIYMPLENGKSKGYLFIQFKSTESADLAIKKLHGKKLDQNHRLLVNKLSDMEKYGVDGAVNEEFIEPEIEPFQSHGYLKSWLQDEQGRDQMVLHFSETVGVYWNKKSADPEPVIEPRKGFTSKYAKFSPKGTYLFSIHPQGIQSWGGANFNSIKRFFHQQVRLVDFSPNEKFMVTLSPIPISLPDSTVDRAQFPFGPESEGHKLVIWNMITGEPVRTFALPPHLEGQKEMPWPLVKWSYDDKYCARQGPDALAIYETESNFQLLDKKLVKVDGIQDFEWAPAGVKLHNSKAVDGKHVLSYWTPESTNQTARVALMQIPSREILRTVNLFQVSDCKMHWQSNGKLLCVKVDRHTKSGKTIFSNLEFFKTNERDIPVEKLELKDVVVNFAWEPNTERFITISRLDDGNPNPAIPKNTISFYAPEVTKGGVNHNSKKKGGAAIAAAVAAAAINNQSSTKYKAYTKIENKHSNTIFWSPKGRYVVVATISRTSGELEFFDVSFDDETNKKSLPANVKLLKTDKFSGMTNISWDPSGRFVAAWSTSWLHAIENGYRLYEFTGNLLRDDSIDQFKDFVWRPRPPSLLTNSDKKKVRSNLREYSAQFEEADAMEADAAVKEIILARRKALEEWRKYRAKHISKQGNSKNEVQAEIIEEIKEEIIEEKEEIVE
Protein: Spikar (Zinc finger, MYND-type containing 8) (A8C4G9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Integrator complex subunit 6.
- Integrator complex subunit 3
- Integrator complex subunit 1
- Integrator complex subunit 5
- Zinc finger protein 592
- Drebrin
- Zinc finger protein 687
Sequence:
MDISTRSKDPGSTERTAQKRKVPSPPHSSNGHSPQDSSTSPIKKKKKPGLLNSSSKDQSELRHGPFYYMKQPLTTDPVDVVPQDGRNDFYCWVCHREGQVLCCELCPRVYHAKCLRLTSEPEGDWFCPECEKITVAECIETQSKAMTMLTIEQLSYLLKFAIQKMKQPGTDAFQKPVPLEQHPDYAEYIFHPMDLCTLEKNAKKKMYGCTEAFLADAKWILHNCIIYNGGNHKLTQIAKVVIKICEHEMNEIEVCPECYLAACQKRDNWFCEPCSNPHPLVWAKLKGFPFWPAKALRDKDGQVDARFFGQHDRAWVPVNNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRKKFGVFNYSPFRTPYTPNSQYQMLLDPSNPSAGTAKTDKQEKVKLNFDMTASPKIILSKPLLSGGAGRRISLSDMPRSPTSTNSSVHTGSDVEQDPEKKAPSSHFSASEESMDFLDKSTASPASTKTGQAGSLSGSPKPFSPQAPTPIMTKPDKTSTATTGSILNLNLDRSKAEMDLKELSESVQQQSAPVPLISPKRQIRSRFQLNLDKTIESCKAQLGINEISEDVYTAVEHSDSEDSEKSESSDSEYVSDEEQKPKNEPEDPEDKEGSRVDKEAPAIKRKPKPSNQVEVKEEVKSNSPVGEKVDPAPAKDKASPEPEKDFAEKAKPSPHPTKDKLKGKDETDSPTVHLGLDSDSESELVIDLGEDPSGREGRKNKKEPKVPSPKQDAIGKPPPPTPAGNQSPPETPVLTRSATQAPAAGVTVAATTSTMSTVTVTAPATAAVTGSPVKKQRPLLPKETVPAVQRVVWNASSKFQTSSQKWHMQKIQRQQQQQQQQQQQQQSQQQQPQSSQGTRYQTRQAVKAVQQKEVTQSPSTSTITLVTSTQPAALVSSSGSASTLASVINADLPIATASADVAADIAKYTSKMMDAIKGTMTEIYNDLSKNTTGSTIAEIRRLRIEIEKLQWLHQQELAEMKHNLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKKKQWCANCKKEAIFYCCWNTSYCDYPCQQAHWPEHMKSCTQSATAPQQEADAEANQETGNKTSQGSSSNTQSAPSEPASTPKEKETSSSSSNSSSTEKSKDSNSTLDLSGSRETPSSILLGSNQGSDHSRSSKAGLWSSSEEKRGSSRSEHSAGTSTKNLMPKESRESRLDTFWD
Protein: [tau protein] kinase (EC 2.7.11.26) (Q9YH61)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Axin-1
- Catenin beta-1
- Axin-2
- Low density lipoprotein receptor-related protein 5
- Casein kinase I isoform alpha
- ETS domain-containing protein Elk-4 isoform 1
- Protein Wnt
Sequence:
MSGSGRPRTSSFAEPPGVPGAAAAAAGSAVAGGSSSGKTGGAQASGGSSSGFGNLKLGRDSGKVTTVVATPGQGPDRPQEVSYTDIKVIGNGSFGVVYQARLIDSQEMVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDFVPETVYRVARHFNKSKTTIPIIYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSNIDIWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKPRTPPEAISLCSRLLEYTPVTRLSPLEACAHAFFDELRQPNARLPNGRELPQLFNFSPVELSIQPQLNSILIPPHARSQTTPASHEGSGSDGPAQSSSAPGPLSNNT
Protein: Lanosterol synthase (EC 5.4.99.7) (2,3-epoxysqualene--lanosterol cyclase) (Oxidosqualene--lanosterol cyclase) (OSC) (P84466)
Organism: Bos taurus (Bovine)
Function: Key enzyme in the cholesterol biosynthesis pathway. Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. Through the production of lanosterol may regulate lens protein aggregation and increase transparency (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P48449}; Peripheral membrane protein {ECO:0000250|UniProtKB:P48449}.
Interaction partners:
- Squalene monooxygenase
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Sterol-C5-desaturase
- Delta
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Isopentenyl-diphosphate Delta-isomerase 1
- Chromosome 14 open reading frame 1 ortholog
- Squalene synthase
Sequence:
MTEGTCLRRRGGPYKTEPATDLSRWRLSNQVGRQTWTYSQEEDPVREQSGLEAHLLGLDTKSFFKDLPKAHTACRGALNGVTFYAALQTEDGHWAGDYGGPLFLLPGLLITCHVANIPLPAGYREEIIRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNLLHKKGGAVFIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWMPAHPSTIWCHCRQVYLPMAYCYSTRLSAEEGPLVQSLRQELYLEDYSCIDWAAHRNSVAPDDLYTPHSWLLHVVYAILNLYERHHSTSLRQWATQKLYEHIAADDRFTKCISIGPISKTINMLVRWHVDGPASAVFQEHVSRIPDYLWLGLDGMKMQGTNGSQIWDTAFAIQALLEARAQHRPEFWSCLRKAHEYLRISQVPDNFPDYQKYYRHMSKGGFSFSTLDCGWIVADCTAEALKSILLLQEKCPFVSNHVPRERLFDTVAVLLSLRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKTFHKQFPDHRAGEIRETLEQGLQFCRQKQRPDGSWEGSWGVCFTYGAWFGLEAFACMGHTYHNGVACAEISRACDFLLSRQMADGGWGEDFESCKQRRYVQSAQSQIHNTCWALMGLMAVRHPDVAALERGVSYLLEKQLPNGDWPQENISGVFNKSCAISYTSYRNVFPIWTLGRFSRLHPDPALAGHP
Protein: 1-aminocyclopropane-1-carboxylate synthase 1 (ACC synthase 1) (OsACS1) (EC 4.4.1.14) (S-adenosyl-L-methionine methylthioadenosine-lyase 1) (Q10DK7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants. Involved in defense response by producing ethylene at early stage after fungal pathogen infection. Involved in several phospate deficiency-induced adaptive responses, such as lateral root elongation.
Interaction partners:
- Os06g0573900 protein
- 1-aminocyclopropane-1-carboxylate oxidase 1
- 1-aminocyclopropane-1-carboxylate oxidase 1
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 5
- 1-aminocyclopropane-1-carboxylate synthase 2
- Os05g0149300 protein
- 1-aminocyclopropane-1-carboxylate oxidase
- Os05g0221800 protein
- 1-aminocyclopropane-1-carboxylate oxidase
Sequence:
MVSQVVAEEKPQLLSKKAGCNSHGQDSSYFLGWQEYEKNPFDPVSNPSGIIQMGLAENQLSFDLLEEWLEKNPHALGLRREGGGASVFRELALFQDYHGLPAFKNALARFMSEQRGYKVVFDPSNIVLTAGATSANEALMFCLADHGDAFLIPTPYYPGFDRDLKWRTGAEIVPVHCASANGFRVTRPALDDAYRRAQKRRLRVKGVLITNPSNPLGTASPRADLETIVDFVAAKGIHLISDEIYAGTAFAEPPAGFVSALEVVAGRDGGGADVSDRVHVVYSLSKDLGLPGFRVGAIYSANAAVVSAATKMSSFGLVSSQTQYLLAALLGDRDFTRSYVAENKRRIKERHDQLVDGLREIGIGCLPSNAGLFCWVDMSHLMRSRSFAGEMELWKKVVFEVGLNISPGSSCHCREPGWFRVCFANMSAKTLDVAMQRLRSFVDSATGGGDNAALRRAAVPVRSVSCPLAIKWALRLTPSIADRKAER
Protein: 39 kDa FK506-binding nuclear protein (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase) (P54397)
Organism: Drosophila melanogaster (Fruit fly)
Function: PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nucleolar protein 58
- Ribosome biogenesis protein BOP1 homolog
- H/ACA ribonucleoprotein complex subunit 4
- Transgelin
- Ribosome production factor 2 homolog
- rRNA 2'-O-methyltransferase fibrillarin
- Probable ATP-dependent RNA helicase pitchoune
- Putative rRNA methyltransferase
- RING-type E3 ubiquitin transferase
- Pescadillo homolog
Sequence:
MSMFWGLNMKPERKYSQTIIKSFHISGVALDKGQEAKLYLAAEKQEYIVATVTKAIPQVALDLNFSKGDRIMFYTAGDASVSLLGYLHDIDSEDDEDDDQMTIENLLNSKAIKNSKKSEDDEDENESGEEDEEDTDDDSQIIEEYESFLENGEEEDDDDVDEDNEESGEEDEQDSDDSEAEEEQPKAKVAKLSPGASAKKSGKEQNGVAKKEEAKQQQKKKEKPEAKKEQPKAKEPAKQQPASKDPRTITGGVKIVDQVVGKGEEAKQGKRVSVYYIGRLQSNNKTFDSLLKGKPFKFALGGGEVIKGWDVGVAGMKVGGKRVITCPPHMAYGARGAPPKIGPNSTLVFEVELKAVH
Protein: Early growth response protein 1 (EGR-1) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor Zif268) (Zinc finger protein Krox-24) (P08046)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes. Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation. Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy. Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia. Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary. Regulates the amplitude of the expression rhythms of clock genes: BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription. Regulates the rhythmic expression of core-clock gene BMAL1 in the suprachiasmatic nucleus (SCN).
Subcellular location: Nucleus {ECO:0000269|PubMed:11100120, ECO:0000269|PubMed:15958557, ECO:0000269|PubMed:8336701}. Cytoplasm {ECO:0000250|UniProtKB:P18146}.
Interaction partners:
- Protein c-Fos
- Transcription factor Jun
- Mitogen-activated protein kinase 3
- NGFI-A-binding protein 1
- Protein FosB
- NGFI-A-binding protein 2
- Mitogen-activated protein kinase 1
- Early growth response protein 3
- Nuclear receptor subfamily 4 group A member 1
- Transcription factor JunB
Sequence:
MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGTPEGSGGNSSSSTSSGGGGGGGSNSGSSAFNPQGEPSEQPYEHLTTESFSDIALNNEKAMVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPTSSSSAPSPAASSSSSASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPATKGGFQVPMIPDYLFPQQQGDLSLGTPDQKPFQGLENRTQQPSLTPLSTIKAFATQSGSQDLKALNTTYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASPAASSLSSYPSPVATSYPSPATTSFPSPVPTSYSSPGSSTYPSPAHSGFPSPSVATTFASVPPAFPTQVSSFPSAGVSSSFSTSTGLSDMTATFSPRTIEIC
Protein: Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death) (O54918)
Organism: Mus musculus (Mouse)
Function: Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent.
Subcellular location: Membrane {ECO:0000269|PubMed:9430630}; Peripheral membrane protein {ECO:0000269|PubMed:9430630}. Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic membranes.
Interaction partners:
- Bcl-2-like protein 2
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- Induced myeloid leukemia cell differentiation protein Mcl-1 homolog
- Apoptosis regulator BAX
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-related protein A1
- Beclin-1
- Dynein light chain 1, cytoplasmic
- Bcl-2 homologous antagonist/killer
Sequence:
MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMVILQLLRFIFRLVWRRH
Protein: Lysosomal protective protein (EC 3.4.16.5) (Carboxypeptidase C) (Carboxypeptidase L) (Cathepsin A) (Protective protein cathepsin A) (PPCA) (Protective protein for beta-galactosidase) [Cleaved into: Lysosomal protective protein 32 kDa chain; Lysosomal protective protein 20 kDa chain] (P16675)
Organism: Mus musculus (Mouse)
Function: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.
Subcellular location: Lysosome.
Interaction partners:
- Sialidase-1
- Beta-galactosidase
- Cathepsin D
- Cathepsin B
- Sialidase-4
- N-acetylgalactosamine-6-sulfatase
- Elastin
- Cathepsin Z
Sequence:
MPGTALSPLLLLLLLSWASRNEAAPDQDEIDCLPGLAKQPSFRQYSGYLRASDSKHFHYWFVESQNDPKNSPVVLWLNGGPGCSSLDGLLTEHGPFLIQPDGVTLEYNPYAWNLIANVLYIESPAGVGFSYSDDKMYVTNDTEVAENNYEALKDFFRLFPEYKDNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLASYEQNDNSLVYFAYYHGLLGNRLWTSLQTHCCAQNKCNFYDNKDPECVNNLLEVSRIVGKSGLNIYNLYAPCAGGVPGRHRYEDTLVVQDFGNIFTRLPLKRRFPEALMRSGDKVRLDPPCTNTTAPSNYLNNPYVRKALHIPESLPRWDMCNFLVNLQYRRLYQSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVDYGESGEQVAGFVKECSHITFLTIKGAGHMVPTDKPRAAFTMFSRFLNKEPY
Protein: Cytosolic sulfotransferase 9 (AtSOT9) (EC 2.8.2.-) (Sulfotransferase 4c) (AtST4b) (Q9FX55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor. No activity with brassinosteroids.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Plasma membrane-associated cation-binding protein 2
- Lysine-specific demethylase JMJ32
- Plasma membrane-associated cation-binding protein 1
Sequence:
MDEKDILRNLREEEEEEEENQSEETKILISSLPWEIDYLGNKLFKYQGYWYYEDVLQSIPNIHSSFQPQETDIVVASFYKSGTTWLKALTFALVQRSKHSLEDHHHPLLSHNPHEIVPYLELDLYLNSSKPDLTKFLSSSSSSSSPRLFSTHMSLDALKLPLKKSPCKVVYVCRNVKDVLVSLWCFLNANKGVEWGDFSQNEKIIRAENYSFKAIFESFCNGVTLHGPFWDHAQSYWRGSLEDPKHFLFMRYEELKAEPRTQVKRLAEFLDCPFTKEEEDSGTVDKILELCSLSNLSSLEINKTGSLGGVDYKTYFRKGQVGDWKSYMTSEMVNKIDMIVEEKLKGSGLKF
Protein: TM2 domain-containing protein amaretto (TM2D2) (Q9VY86)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- TM2 domain-containing protein biscotti
- AT06125p
Sequence:
MRIFYGLLAFLVARQHDAQAIQARSDKEQPQTVVSGTAVQSVVPVQAQLGSGMGPSSSSSSASSASGGAGNSAFYPLGPNVMCSFLPRDFLDCKDPVDHRENATAQQEKKYGCLKFGGSTYEEVEHAMVWCTVFADIECYGNRTFLRAGVPCVRYTDHYFVTTLIYSMLLGFLGMDRFCLGQTGTAVGKLLTMGGVGVWWIIDVILLITNNLLPEDGSNWNPYV
Protein: Large ribosomal subunit protein uL11 (60S ribosomal protein L12) (P61866)
Organism: Caenorhabditis elegans
Function: Binds directly to 26S ribosomal RNA.
Interaction partners:
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Plectin/eS10 N-terminal domain-containing protein
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL39
Sequence:
MPPKFDPTEIKIVYLRCVGGEVGATSALAPKVGPLGLSPKKIGEDIAKATQDWKGLKVTCKLTIQNRVAKIDVVPSAASLIVKELKEPPRDRKKVKNVKHNGDLTVDTIIKIARIMRPRSMAKKLEGTVKEILGTAQSVGCTIDGQHPHDIIESIANGEIEIPAQ
Protein: Sialic acid-binding Ig-like lectin 8 (Siglec-8) (Sialoadhesin family member 2) (SAF-2) (Q9NYZ4)
Organism: Homo sapiens (Human)
Function: Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells. Preferentially binds to alpha-2,3-linked sialic acid. Also binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. Recognizes simultaneously epitopes having a terminal N-acetylneuraminic acid (sialic acid) and an underlying 6-O-sulfated galactose. Preferentially binds to Gal-6-sulfated sialyl-Lewis X glycan epitopes.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-5 receptor subunit alpha
Sequence:
MLLLLLLLPLLWGTKGMEGDRQYGDGYLLQVQELVTVQEGLCVHVPCSFSYPQDGWTDSDPVHGYWFRAGDRPYQDAPVATNNPDREVQAETQGRFQLLGDIWSNDCSLSIRDARKRDKGSYFFRLERGSMKWSYKSQLNYKTKQLSVFVTALTHRPDILILGTLESGHSRNLTCSVPWACKQGTPPMISWIGASVSSPGPTTARSSVLTLTPKPQDHGTSLTCQVTLPGTGVTTTSTVRLDVSYPPWNLTMTVFQGDATASTALGNGSSLSVLEGQSLRLVCAVNSNPPARLSWTRGSLTLCPSRSSNPGLLELPRVHVRDEGEFTCRAQNAQGSQHISLSLSLQNEGTGTSRPVSQVTLAAVGGAGATALAFLSFCIIFIIVRSCRKKSARPAAGVGDTGMEDAKAIRGSASQGPLTESWKDGNPLKKPPPAVAPSSGEEGELHYATLSFHKVKPQDPQGQEATDSEYSEIKIHKRETAETQACLRNHNPSSKEVRG
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTG9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Homoaconitase, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- aromatic-amino-acid transaminase
- Histidine biosynthesis trifunctional protein
- homocitrate synthase
- 3-isopropylmalate dehydratase
- Saccharopine dehydrogenase [NADP
- Candida glabrata strain CBS138 chromosome H complete sequence
- Tryptophan synthase
- 2-oxoglutarate dehydrogenase, mitochondrial
Sequence:
MLRGSATRLTAMRGFSSTRLAQKALTIGLIPGDGIGKEVIPAGKQILEKVGPKFDLDFKFIDLHAGWETFQNTGKALPDETVEVLRRDCQGALFGAVQSPTTKVEGYSSPIVALRKAMGLFANVRPVKAVEGTNDRPVDMVIVRENTEDLYIKIEKTYTDPATGTRVAEATKRISEVATRRIATIALDIALQRLQSRGHATLTVTHKSNVLSQSDGLFREICKDVYESNKDKYGKIQYNEQIVDSMVYRMFREPECFDVVVAPNLYGDILSDGAAALVGSLGVVPSANVGPEIVIGEPCHGSAPDIAGRGIANPIATIRSTALMLEFLGYPEAAQPIYKAVDSNIRENQIKTPDLGGKSTTQQVVDDILSKI
Protein: Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25) (Bifunctional phenylalanine ammonia-lyase) (Bifunctional PAL) (Q8VXG7)
Organism: Zea mays (Maize)
Function: Catalyzes the non-oxidative deamination of L-phenylalanine and L-tyrosine to form trans-cinnamic acid and p-coumaric acid respectively with similar efficiencies. Facilitates the commitment step in phenylpropanoid pathways that produce lignins, coumarins and flavonoids.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Arginase 1, mitochondrial
Sequence:
MAGNGAIVESDPLNWGAAAAELAGSHLDEVKRMVAQARQPVVKIEGSTLRVGQVAAVASAKDASGVAVELDEEARPRVKASSEWILDCIAHGGDIYGVTTGFGGTSHRRTKDGPALQVELLRHLNAGIFGTGSDGHTLPSEVTRAAMLVRINTLLQGYSGIRFEILEAITKLLNTGVSPCLPLRGTITASGDLVPLSYIAGLITGRPNAQAVTVDGRKVDAAEAFKIAGIEGGFFKLNPKEGLAIVNGTSVGSALAATVMYDANVLAVLSEVLSAVFCEVMNGKPEYTDHLTHKLKHHPGSIEAAAIMEHILDGSSFMKQAKKVNELDPLLKPKQDRYALRTSPQWLGPQIEVIRAATKSIEREVNSVNDNPVIDVHRGKALHGGNFQGTPIGVSMDNARLAIANIGKLMFAQFSELVNEFYNNGLTSNLAGSRNPSLDYGFKGTEIAMASYCSELQYLGNPITNHVQSADEHNQDVNSLGLVSARKTAEAIDILKLMSSTYIVALCQAVDLRHLEENIKASVKNTVTQVAKKVLTMNPSGELSSARFSEKELISAIDREAVFTYAEDAASASLPLMQKLRAVLVDHALSSGERGAGALRVLQDHQVRGGAPRGAAPGGGGRPRGVAEGTAPVANRIADSRSFPLYRFVREELGCVFLTGERLKSPGEECNKVFVGISQGKLVDPMLECLKEWDGKPLPINIK
Protein: Protein O-glucosyltransferase 1 (H7C5H0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XCGAALPPAPQRGICSSKWKVFIDQINRSLENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRKLGTHYQITKNRLYRENDCMFPSRCSGVEHFILEVIGRLPDMEMVINVRDYPQVPKWMEPAIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPIYPTGLGRWDLFREDLVRSAAQWPWKK
Protein: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial (PDP 2) (EC 3.1.3.43) (Pyruvate dehydrogenase phosphatase catalytic subunit 2) (PDPC 2) (Q504M2)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O88484}.
Interaction partners:
- Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- [Pyruvate dehydrogenase
- Pyruvate dehydrogenase protein X component, mitochondrial
- [Pyruvate dehydrogenase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Sequence:
MSSTVSYWIFNSARNRIALLRGGRRLYSRAATSRNLLKWRPFSPALASSALKCGSPPGGFALRKAYRHTSTEEEDFHLQLSPEQVSDLLRAGESSHKVLDFNNGVPNSVLRFESNQLAANSPVEDRQGVATCVQTNGMMFGIFDGHGGHACAQAVSERLFYYMAVSLMSHQTLEQMEEATENMKPLLPILRWLKHPGDSIYKDVTSVHLDHLRVYWQELLDLHMEMGLSIEEALMYSFQRLDSDISLEIQAPLEDEVTRNLSLQVAFSGATACMAHVNGVHLHVANAGDCRAILGVQEENGAWSCLPLTCDHNAWNEAELSRLKREHPESEDRTLIIDDRLLGVLMPCRAFGDVQLKWSKELQRNVLARGFDTEALNIYQFTPPHYYTPPYLTAKPEVTYHRLRRQDKFLVLASDGLWDMLGNEDVVRLVVGHLSKVGRHKPDLDQRPANLGLMQSLLLQRKASGLHAADQNTATHLIRHAIGSNEYGEMEPERLAAMLTLPEDVARMYRDDITVMVVFFNSDSIDTYCKEG
Protein: Iron-regulated transcriptional activator AFT1 (Activator of iron transcription protein 1) (P22149)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transcription factor that activates the genes for FRE1, FRE2 and FET3 in response to iron deprivation. Also required for the expression of LSO1. Iron could interact directly with AFT1 and inhibits its activity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Iron transport multicopper oxidase FET3
- Monothiol glutaredoxin-3
- Monothiol glutaredoxin-4
- Ferric/cupric reductase transmembrane component 1
- Ferric/cupric reductase transmembrane component 2
- mRNA decay factor CTH2
- Ferric reductase transmembrane component 6
- Copper-transporting ATPase
- Plasma membrane iron permease
- Ferric reductase transmembrane component 3
Sequence:
MEGFNPADIEHASPINSSDSHSSSFVYALPKSASEYVVNHNEGRASASGNPAAVPSPIMTLNLKSTHSLNIDQHVHTSTSPTETIGHIHHVEKLNQNNLIHLDPVPNFEDKSDIKPWLQKIFYPQGIELVIERSDAFKVVFKCKAAKRGRNARRKRKDKPKGQDHEDEKSKINDDELEYASPSNATVTNGPQTSPDQTSSIKPKKKRCVSRFNNCPFRVRATYSLKRKRWSIVVMDNNHSHQLKFNPDSEEYKKFKEKLRKDNDVDAIKKFDELEYRTLANLPIPTATIPCDCGLTNEIQSFNVVLPTNSNVTSSASSSTVSSISLDSSNASKRPCLPSVNNTGSINTNNVRKPKSQCKNKDTLLKRTTMQNFLTTKSRLRKTGTPTSSQHSSTAFSGYIDDPFNLNEILPLPASDFKLNTVTNLNEIDFTNIFTKSPHPHSGSTHPRQVFDQLDDCSSILFSPLTTNTNNEFEGESDDFVHSPYLNSEADFSQILSSAPPVHHDPNETHQENQDIIDRFANSSQEHNEYILQYLTHSDAANHNNIGVPNNNSHSLNTQHNVSDLGNSLLRQEALVGSSSTKIFDELKFVQNGPHGSQHPIDFQHVDHRHLSSNEPQVRSHQYGPQQQPPQQLQYHQNQPHDGHNHEQHQTVQKDMQTHESLEIMGNTLLEEFKDIKMVNGELKYVKPED
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q9VAW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD43819p
- Pre-mRNA-splicing factor CWC22 homolog
- Cytosolic Prostaglandin E synthase
- Pre-mRNA-processing factor 17
- Peptidyl-prolyl cis-trans isomerase
- Stress-induced-phosphoprotein 1
- Serine/arginine repetitive matrix protein 1
- Pre-mRNA-processing factor 39
- LD23779p
- RNA helicase
Sequence:
MTVNKRDAGATRPRCFFDISLGGLGMGRIVFELFNDVAPKTAENFRALCTGEKGFGLITGKKLQYKGVIFHRVVKDFMVQAGDFSAGNGTGGESIYGGTFEDESFEKKHDRPFLLSMANRGKNTNGSQFFITTQPAPHLDNIHVVFGQVISGQELVRQLEGLPVDRNSRPLQDAAIANCGELVRQTKAKKEKKHKRRSTATEDSNSEESEAEAKVVRKAKKKKRSRKDTKSQSDSEDNETSRGNGKHDQTPQDDDEDREEGELHPLVTITKIDPNEIPEVSNKFLMRAERSKSLDREERGARGQDRDRGKDQDRDRSRNNFGWSKKQAPPTSRSGRIVKGRGVFRFRTPSRSRSRSTTPPHWKHAQKRTIKLSDLERIEEESKMREEEMKRREHERKRRHEEATKNPKQSFFELSHASTYGGKITPDRFSPEHKAKSKDTADRGKAKEREKAGEKDKARDVTPVKRRKSMDMNALDYEQQTESEVESEDEEQLKVKPPSKQDIRVEPSTSKDRNAKRDERKPTEEKAKPKRSRSRSPRRQSPARRQQRSPARRPGQNYNQNQNQNQNQNQNQNQLNRGNRRNPFADRDRRRRSRSQDNEYRNRYPLSPIRGRGSPSGDRRRQQRSRSQNRRQDSPSQRRQLSPGRKRQDSPSKKRPNSTERKWRDSPERKRDDSHDRKREASPNWKRDDSPARKRKDSANRKREDSQDKKIQDSKRQEDSAGKKREDSPSKKRKDSDKKRQDSPVKRQESPGRKRQDSPERKRRDSPDRRRKDSPARRRQESSGRRRQDSDGRRRRESSGNRRSRSRGRWHSSSRSRSPSTSRSRRRRSRSPLPKLTSALPMSEEREKAAREKMQKRAEAAMLMKEHMRNEIAKEEERRMEKQRQDDLDKERTTRELNELERLKAETLRKLHEEDSVDPDAAASAGSASKTDATSTGAKSKRDSSSENRHREKKRKHKKSKKSSGRSDND