wanglab/gogpt-training-data huggingface dataset:
Protein: L-erythrulose-1-phosphate isomerase (EC 5.3.1.33) (A0R756)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the isomerization of L-erythrulose-1P to D-erythrulose-4P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source.
Interaction partners:
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Enolase
- Glucose-6-phosphate isomerase
- D-erythrulose-4-phosphate isomerase 2
- Fructose-bisphosphate aldolase class 1
- Fructose-bisphosphate aldolase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Tagatose-1,6-bisphosphate aldolase GatY
- Pyruvate kinase
Sequence:
MPDARALGAAQLWIGTSWKMNKGLAESRGYARELAEYVAAKPPAGVQPFIIPSFTALTTVRDALGDDSPVLLGVQNAHWEDHGAWTGEVSVAQAKDAGAQIVEIGHSERREHFGETVETTRLKVAAALHHGLVPLLCIGESAENKQAGESSRFILEQAAGALEGLTDEHLARVLIAYEPIWAIGENGRPATVEELRQPFDDLAREYGCRTMGLLYGGSVNTDNAEDLLGIDHVTGLFIGRAAWQLPGYVRILEMAAAHPKAKA
Protein: Protein Wnt-9b (Protein Wnt-14b) (Protein Wnt-15) (O14905)
Organism: Homo sapiens (Human)
Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway. Required for normal embryonic kidney development, and for normal development of the urogenital tract, including uterus and part of the oviduct and the upper vagina in females, and epididymis and vas deferens in males. Activates a signaling cascade in the metanephric mesenchyme that induces tubulogenesis. Acts upstream of WNT4 in the signaling pathways that mediate development of kidney tubules and the Muellerian ducts. Plays a role in cranofacial development and is required for normal fusion of the palate during embryonic development (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
Interaction partners:
- Protein-serine O-palmitoleoyltransferase porcupine
- Wnt inhibitory factor 1
- Palmitoleoyl-protein carboxylesterase NOTUM
- Glypican-3
- Cerberus
- Frizzled-4
- Frizzled-5
- Low-density lipoprotein receptor-related protein 6
- Low-density lipoprotein receptor-related protein 5
- Frizzled-7
Sequence:
MRPPPALALAGLCLLALPAAAASYFGLTGREVLTPFPGLGTAAAPAQGGAHLKQCDLLKLSRRQKQLCRREPGLAETLRDAAHLGLLECQFQFRHERWNCSLEGRMGLLKRGFKETAFLYAVSSAALTHTLARACSAGRMERCTCDDSPGLESRQAWQWGVCGDNLKYSTKFLSNFLGSKRGNKDLRARADAHNTHVGIKAVKSGLRTTCKCHGVSGSCAVRTCWKQLSPFRETGQVLKLRYDSAVKVSSATNEALGRLELWAPARQGSLTKGLAPRSGDLVYMEDSPSFCRPSKYSPGTAGRVCSREASCSSLCCGRGYDTQSRLVAFSCHCQVQWCCYVECQQCVQEELVYTCKH
Protein: FI24227p1 (Sterile20-like kinase, isoform E (EC 2.7.11.-)) (Q59E61)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFITNLKKVFHLGGGEAKKKRLYNNIKMDTDPAEFWEMVGELGDGAFGKVYKAQHKEQKRFAAAKMCQLEDEENLSDHMVEIDILSEIKHPNIVELYEAFSIDDKLWMLIEYCDGGALDSIMVELEKPLTEPQIAYVCKHMTEGLTFLHRNKVIHRDLKAGNVLLTMEGGVKLADFGVSAKNKHTMQKHDTFIGTPYWMAPELVLCETFRDNPYDHKVDIWSLGITLIELAQMEPPNSEMSPMRVLLKIQKSEPPKLEQPSRWSKEFNDFLKKSLVKDPQVRPTTDVLMQHAFINRNLDAKPIKDLLLEYKAEVVEEVVDDETEEPRNSALQLDLDDDSASLQSQDIDKLPGTPTSILRDAKEQSQPSSSLPIAAAATAAAAATTTTKATTPDRPNHTKDDNAEAAAQQPPHTKVPAPAPPSSQQTPPPQVQQPPTPPAQPTAAVLQKKPEDVAAVAETSEKTESDKKHFVKKGKAPPPPSPLGLANAKPAASDSQTSPKKLATPEPTSPVTTAIEVAIGQEAMEPKPQPPSPTASSIVSVQSVASSSSSGSVSNAVLSSSTSLITINSDPPTPHHHQPLPPQPQHLILPNSLESVSQITVVTSTHPPVIIDNSVMPPQNEVIIVSNDMNKSTHLHESSTDDDFPSLDDSLGDATTPPHKQSSMILAVNEPAGVVPAPPSQPQTSSTVHARKLDESEVLIVSPSYADDDSAYNTASGSHSHDHSDHLMDTSHVSVVTVGDEGVKVKDSSNELVKRQPNGVGIVPEDVNIIVNRFKQEKRSPDSSLSENGSVRGRRGIEVLVGGSGGSDVDSIGTNTSQESRHETDHNNKQQYPAAALMPPPPPSLTNNHNHETIDEEEEVVIRPKARVPAVVKSANAQGLTKEEIELRNLRKKTRKRTRKFEIDGVQMTTTTSRVIYGDDENGRIYDDHDFRKQELRELKLLQKQEKKQQTELHLKEQQAKEQQDRRFEQERSSLEKTYEADMDMLARQHKQLVEKTEQTQENELRSSSKRIRSEQEQELKIFRENLKQEIRLLKQEVDLFPKDKRKDEFKQRRSAMELDHEEKERAFLDSLKERHELLLRRLSEKHRDHLATINRNFLQQKQNAMRTREALLWELEEKQLHERHQLSKRHVKELCFMQRHQMIIRHEKELDQVKRMLQRKEEDMVKKQTMEKRALPKRIRAERKARDLMFRESLRISTNLDPEIERDRLKKFQEQEKKRYMQEERRFEVKHQKQLEELRATRESAIKELEQLQNEKRRALVEHEHSKLSEIDERLKGELREWREQLVPRKQRLEETFAQQLDEMETLYGGALIVSMPSDTLQRDHFTGSTRSSLSSYSEG
Protein: E3 ubiquitin-protein ligase RNF34 (EC 2.3.2.27) (Caspase regulator CARP1) (Caspases-8 and -10-associated RING finger protein 1) (CARP-1) (FYVE-RING finger protein Momo) (Human RING finger homologous to inhibitor of apoptosis protein) (hRFI) (RING finger protein 34) (RING finger protein RIFF) (RING-type E3 ubiquitin transferase RNF34) (Q969K3)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells. Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15069192}; Peripheral membrane protein {ECO:0000305}. Endomembrane system {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus {ECO:0000269|PubMed:22064484}. Nucleus speckle {ECO:0000269|PubMed:12118383}. Cytoplasm, cytosol {ECO:0000269|PubMed:15069192}.
Interaction partners:
- E3 ubiquitin-protein ligase rififylin
- Death effector domain-containing protein
Sequence:
MKAGATSMWASCCGLLNEVMGTGAVRGQQSAFAGATGPFRFTPNPEFSTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLILRNIPIDTCREKEDLVDLVLCHHGLGSEDDMDTSSLNSSRSQTSSFFTRSFFSNYTAPSATMSSFQGELMDGDQTSRSGVPAQVQSEITSANTEDDDDDDDEDDDDEEENAEDRNPGLSKERVRASLSDLSSLDDVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERLQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS
Protein: PX domain-containing protein (Q2UEI4)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- t-SNARE coiled-coil homology domain-containing protein
- Synaptobrevin homolog YKT6
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MSPNLEITIPTTSLSPTSPPYTVYNLTLRLPLRSFTISKRYSDFLNFHKTLLTQTNIPPPAPLPQKTWFKNTVSNASLREDRRQALEAYLQAINDADDPRWRNSPAWRAFLNLPSAANASHTSTRLHAAITDPGSGADNPISDPTLWLDVYRDMKSHLHDARLHLTRRDQETTPQKQHESSARAKSSLVRAGSLVAALEEGLKVMGEAANRAQSPSGKGRGGSLGDGELRRRKDLLINARKEKDGLEDLLNAMAAKSRVDHAVASVQDKEALVGSASRKPARSGRVLGKETERTRELDNQGLLQLQRQTMEDQDQSVEELLKIIRRQKELGIAINEEVEIQNALLSIANEDAERCFCDFSMRSSRGCENFVSLSDGGGMGWSGCIARARMAASIRCKTGEYESSIGKVSTGSLVMSMRRYSESFRHKPTHPHLRRQAPYYSRTCPSHRLQALSAGRKNLRSGVWPGKSDSTFQQECGEQSHTPLGCLLLEKNKAAREISLPCEGLCLLLCNRTQGHRNQFPCLKLAFVSLLSGSKSLT
Protein: B3 domain-containing transcription repressor VAL2 (Protein HIGH-LEVEL EXPRESSION OF SUGAR-INDUCIBLE-LIKE 1) (Protein VP1/ABI3-LIKE 2) (Q5CCK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor of gene expression involved in embryonic pathways, such as LEC1, ABI3, and FUS3. Repressor of the sugar-inducible genes involved in the seed maturation program in seedlings. Plays an essential role in regulating the transition from seed maturation to seedling growth. Functionally redundant with VAL1/HSI2.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone deacetylase 19
- Chromo domain-containing protein LHP1
- Histone-lysine N-methyltransferase EZA1
- Histone deacetylase 6
- Nuclear transcription factor Y subunit B-9
- Agamous-like MADS-box protein AGL15
- CHD3-type chromatin-remodeling factor PICKLE
- Histone deacetylase complex subunit SAP18
- Nuclear transcription factor Y subunit B-6
- Trihelix transcription factor ASIL1
Sequence:
MESIKVCMNALCGAASTSGEWKKGWPMRSGDLASLCDKCGCAYEQSIFCEVFHAKESGWRECNSCDKRLHCGCIASRFMMELLENGGVTCISCAKKSGLISMNVSHESNGKDFPSFASAEHVGSVLERTNLKHLLHFQRIDPTHSSLQMKQEESLLPSSLDALRHKTERKELSAQPNLSISLGPTLMTSPFHDAAVDDRSKTNSIFQLAPRSRQLLPKPANSAPIAAGMEPSGSLVSQIHVARPPPEGRGKTQLLPRYWPRITDQELLQLSGQYPHLSNSKIIPLFEKVLSASDAGRIGRLVLPKACAEAYFPPISLPEGLPLKIQDIKGKEWVFQFRFWPNNNSRMYVLEGVTPCIQSMQLQAGDTVTFSRTEPEGKLVMGYRKATNSTATQMFKGSSEPNLNMFSNSLNPGCGDINWSKLEKSEDMAKDNLFLQSSLTSARKRVRNIGTKSKRLLIDSVDVLELKITWEEAQELLRPPQSTKPSIFTLENQDFEEYDEPPVFGKRTLFVSRQTGEQEQWVQCDACGKWRQLPVDILLPPKWSCSDNLLDPGRSSCSAPDELSPREQDTLVRQSKEFKRRRLASSNEKLNQSQDASALNSLGNAGITTTGEQGEITVAATTKHPRHRAGCSCIVCSQPPSGKGKHKPSCTCTVCEAVKRRFRTLMLRKRNKGEAGQASQQAQSQSECRDETEVESIPAVELAAGENIDLNSDPGASRVSMMRLLQAAAFPLEAYLKQKAISNTAGEQQSSDMVSTEHGSSSAAQETEKDTTNGAHDPVN
Protein: AP-1-like transcription factor YAP2 (Cadmium resistance protein 1) (Transcription factor CAD1) (P24813)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription activator involved in oxidative stress response and cadmium resistance. Regulates the transcription of genes overrepresented for the function of stabilizing proteins including the inducible Hsp90-family protein HSP82. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Activation by alkyl hydroperoxides or cadmium induces nuclear accumulation and as a result CAD1/YAP2 transcriptional activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15341652, ECO:0000269|PubMed:17187783}. Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15341652, ECO:0000269|PubMed:17187783}. Note=Oxidized CAD1/YAP2 is found predominantly in the nucleus, while reduced CAD1/YAP2 is continuously exported to the cytoplasm by CRM1/exportin 1. {ECO:0000269|PubMed:15341652, ECO:0000269|PubMed:17187783}.
Interaction partners:
- AP-1-like transcription factor YAP7
- Serine/threonine-protein kinase RCK1
- AP-1-like transcription factor YAP1
- P-type cation-transporting ATPase
Sequence:
MGNILRKGQQIYLAGDMKKQMLLNKDGTPKRKVGRPGRKRIDSEAKSRRTAQNRAAQRAFRDRKEAKMKSLQERVELLEQKDAQNKTTTDFLLCSLKSLLSEITKYRAKNSDDERILAFLDDLQEQQKRENEKGTSTAVSKAAKELPSPNSDENMTVNTSIEVQPHTQENEKVMWNIGSWNAPSLTNSWDSPPGNRTGAVTIGDESINGSEMPDFSLDLVSNDRQTGLEALDYDIHNYFPQHSERLTAEKIDTSACQCEIDQKYLPYETEDDTLFPSVLPLAVGSQCNNICNRKCIGTKPCSNKEIKCDLITSHLLNQKSLASVLPVAASHTKTIRTQSEAIEHISSAISNGKASCYHILEEISSLPKYSSLDIDDLCSELIIKAKCTDDCKIVVKARDLQSALVRQLL
Protein: Lactamase-like protein aptB (EC 3.1.-.-) (Asperthecin synthesis protein B) (Q5B0C9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster. Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin.
Interaction partners:
Sequence:
MAFRIPFAQDFWNEYLSGRENTIPTLPVVTDITERVIRVLGGNAGPMRLQGTNTYLVGTGRSRILVDTGQGMPSWIRDIAKVLEERDIDISYVLLTHWHGDHTGGVPDLIAYNPALSSRIYKNRPDAGQKDILDGQVFRVEGATLRAVHTPGHAADHMCFLFEEENALFTGDNVLGHGYSVVEDLGQYMNSMVQMANLNLPLGYPAHGAVIDDLPDKMREYIKHREFRVQQVYAILEESRAAGQGRGRGGLTLHEIILAMYGEITDEVEKALAPFLSQVLWKLAEDRKVGFEPGSAAKRRWYVRSRRPN
Protein: DNA-directed RNA polymerase 2, chloroplastic/mitochondrial (EC 2.7.7.6) (NsRpoT-B) (T7 bacteriophage-type single subunit RNA polymerase 2) (Q8VWF8)
Organism: Nicotiana sylvestris (Wood tobacco) (South American tobacco)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast. Mitochondrion.
Interaction partners:
- Protein TPLATE
- rRNA adenine N
- rRNA adenine N
- rRNA adenine N
Sequence:
MSSTKTPISLTIKLNQFTDKPTGLDINPYHNSPIMWRNIIKQLSSRTPQKLLFSSKNRTYSFLGFGQDSIFKDNTKFRSLIPISCSNIVMGFQNLGEYLPGDEFLSRPLIKNQVNNNFCCRKSYASVAEAVAVSSTDAEEDVSVVDEVHELLTELKKEEKKQFAFRRRKQRMLTSGMGHRKYQTLKRRQVKVETEAWEQAAKEYKELLFDMCEQKLAPNLPYVKSLFLGWFEPLRDKIAEEQELCSQGKSKAAYAKYFYQLPADMMAVITMHKLMGLLMTGGDHGTARVVQAALVIGDAIEQEVRIHNFLEKTKKQKAEKDKQKEDGEHVTQEQEKLRKKVTNLMKKQKLRAVGQIVRRQDDSKPWGQDARAKVGSRLIDLLLQTAYIQPPANQLAVDPPDIRPAFVHSVRTVAKETKSASRRYGIIQCDELVFKGLERTARHMVIPYMPMLVPPVKWTGYDKGGHLYLPSYVMRTHGARQQREAVKRASRNQLQPVFEALDTLGNTKWRINKRVLSVVDRIWAGGGRLADLVDRDDAPLPEEPDTEDEALRTKWRWKVKSVKKENRERHSQRCDIELKLAVARKMKDEESFFYPHNVDFRGRAYPMHPHLNHLGSDICRGVLEFAEGRPLGESGLRWLKIHLANLFAGGVEKLSLEGRIGFTENHMDDIFDSSDKPLEGRRWWLNAEDPFQCLAVCINLSEAVRSSSPETSVSHIPVHQDGSCNGLQHYAALGRDKLGAAAVNLVAGEKPADVYSGIAARVLDIMKRDAQRDPAEFPDAVRARVLVNQVDRKLVKQTVMTSVYGVTYIGARDQIKRRLKERGAIADDSELFGAACYAAKVTLTALGEMFEAARSIMTWLGECAKIIASENEPVRWTTPLGLPVVQPYRKIGRHLIKTSLQILTLQRETEKVMVKRQRTAFPPNFIHSLDGSHMMMTAVACRRAGLNFAGVHDSYWTHACDVDKLNRILREKFVELYEAPILEKLLESFQTSYPTLLFPPLPERGDFDMRDVLESPYFFN
Protein: Uncharacterized protein, isoform L (Q7KTI5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNKVEFKNKNKDQGPCARVRKIRPINMGGNVEQRPWTPTVRIGKIAAETTNPGPATVQLPTLIGSKVPDSKKKAAPSYSFGHKLGGKYDTSGPGPAQYNVTGMRAKGRDYPRAATLQSRPKELTRFSNPGPGEYDVVPAAKAVIDATPKYTFGQRPVALKTFQIPAPGAYCPEKVKLNKTPEFSFGIKHHEQRPDYTPAPGTYKPEQVVLEHIPAYSFGLKTKHIQVSDTPAPGAYSPEKSRLHSAPAYSIAGKASQDVVDCTPAPGAYEPEKCVLSRTPAFSFGHRAELAKSSDTPAPGTYNPEKVRLDHTPAFTLSGRPETRSVSETPAPGSYAPEKYRNDRTPAFTFGGKHEQRLESSTPAPGDYCPEKVRHDHNPAFSFAGRHDLHKPSDTPAPGAYDTEKVRQDHNPAFSFAGRHDLHKPSETPAPGAYSPEKVRQDHNPAFSMAGKHSQKVTSDSPAPGDYCPEKVRLDHTPAYSFGVKSDPKVENNTPAPGDYHPEKVRQDHNPAYSFAGRHDLQKPDNTPAPGAYFPEKVRLDHNPAFSMAGKYDAKVTNDTPAPGDYSPEKVRQDTNPAYSFAGRHDLHKPSETPAPGAYSPEKVRLDHNPAFTMAGKHDQKILNGTPAPGDYSPEKCRLDHTPAYSFGGKNDPKVENNTPAPGDYHPEKVRLDHNPAYSFAGRHDLQKPSDTPAPGAYSPEKVRQDHNPAFSMAGKPVEKLTNGTPAPGDYSPEKVRLNHTPAYTFGGKNDPKVENNTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPNDTPAPGAYCPEKVRQDHNPAFSMAGKYTQKVANDTPAPGDYSPEKVRLDHTPAYTFGGKNDPKVESNTPAPGDYHPEKVRQDHNPAFSFAGRHNLQKPSDTPAPGAYSPEKVRQDHNPAFTMAGKHDPKVSNDTPAPGDYSPEKVRLDYTPSFTFAGKNNPKVENDTPAPGDYHPEKVRQDHNPAFSFAGRHDLHKPSDTPAPGAYSPEKVRQDHNPAFSMAGKYIEKITNGTPAPGDYCPEKVRLDHTPAFTFGGKNDPKVENNTPAPGDYHPEKVRQDHVPAFSFAGRHDLHKPNETPAPGAYSPEKVRQDHNPAFTMAGKHDPKVTHDTPAPGDYHPEKVRLDHNPAFSFAGRHDLHKPSETPAPGDYFPEKVRQDFNPAFTFAGKHDPRSLSESPAPGDYSPEKVRLDHAPAFSFGGKHDPKTEHLHPAPCDYAPEKVRLDHTPAYTIAGRPAADHVSQTPAPCDYHPEQCQVDSTPAFTFGMRLGRERISDTPAPSAYEPEKHSLHSTPAYSFGTKSDIRVTTDAPAPGHYHPEQCKLDSSPAYSFGLKTVPTASLPEPRGAYIEDRIVQRRERRLASPVRNNAECTTTTTNHTNNNAGSSTTTTTTTTTTTKTFINGVEQPELQKKETTKQVNGTHKELKSAPQAPLSNGNIVSNGNHSKMVSTTTRIQEVAHGQKESGNLKVVASGKSDASATKAAAVSHQTVVQADGAIVTSGQSSRMQTVKYAVEASSVQEKIISS
Protein: Aryl-hydrocarbon receptor nuclear translocator 2 isoform D (X5DQN9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATPAAVNPPEMASDIPGSVTLPVAPMAATGQVRMAGAMPARGGKRRSGMDFDDEDGEGPSKFSRENHSEIERRRRNKMTQYITELSDMVPTCSALARKPDKLTILRMAVSHMKSMRGTGNKSTDGAYKPSFLTEQELKHLILEAADGFLFVVAAETGRVIYVSDSVTPVLNQPQSEWFGSTLYEQVHPDDVEKLREQLCTSENSMTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGNAPLDHLPLNRITTMRKRFRNGLGPVKEGEAQYAVVHCTGYIKAWPPAGMTIPEEDADVGQGSKYCLVAIGRLQVTSSPVCMDMNGMSVPTEFLSRHNSDGIITFVDPRCISVIGYQPQDLLGKDILEFCHPEDQSHLRESFQQVVKLKGQVLSVMYRFRTKNREWMLIRTSSFTFQNPYSDEIEYIICTNTNVKQLQQQQAELEVHQRDGLSSYDLSQVPVPNLPAGVHEAGKSVEKADAIFSQERDPRFAEMFAGISASEKKMMSSASAAGTQQIYSQGSPFPSGHSGKAFSSSVVHVPGVNDIQSSSSTGQNMSQISRQLNQSQVAWTGSRPPFPGQQIPSQSSKTQSSPFGIGTSHTYPADPSSYSPLSSPATSSPSGNAYSSLANRTPGFAESGQSSGQFQGRPSEVWSQWQSQHHGQQSGEQHSHQQPGQTEVFQDMLPMPGDPTQGTGNYNIEDFADLGMFPPFSE
Protein: Trehalose import ATP-binding protein SugC (EC 7.5.2.-) (MtbSugC) (Nucleotide-binding domain of SugABC transporter) (NBD of SugABC transporter) (SugABC transporter ATPase SugC) (P9WQI3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.tuberculosis. Trehalose uptake is essential for virulence. Probably responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Trehalose-binding lipoprotein LpqY
- Trehalose transport system permease protein SugB
- Trehalose transport system permease protein SugA
- Probable sugar-transport integral membrane protein ABC transporter UspA
- Probable sugar-transport integral membrane protein ABC transporter
- Probable sugar-transport integral membrane protein ABC transporter UspB
- Probable sugar-transport integral membrane protein ABC transporter
- Probable Sn-glycerol-3-phosphate transport integral membrane protein ABC transporter UgpE
- Probable Sn-glycerol-3-phosphate transport integral membrane protein ABC transporter UgpA
- Trehalose import ATP-binding protein SugC
Sequence:
MAEIVLDHVNKSYPDGHTAVRDLNLTIADGEFLILVGPSGCGKTTTLNMIAGLEDISSGELRIAGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKMRKADIAQKVSETAKILDLTNLLDRKPSQLSGGQRQRVAMGRAIVRHPKAFLMDEPLSNLDAKLRVQMRGEIAQLQRRLGTTTVYVTHDQTEAMTLGDRVVVMYGGIAQQIGTPEELYERPANLFVAGFIGSPAMNFFPARLTAIGLTLPFGEVTLAPEVQGVIAAHPKPENVIVGVRPEHIQDAALIDAYQRIRALTFQVKVNLVESLGADKYLYFTTESPAVHSVQLDELAEVEGESALHENQFVARVPAESKVAIGQSVELAFDTARLAVFDADSGANLTIPHRA
Protein: Malate synthase G (EC 2.3.3.9) (P9WK17)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00641}.
Interaction partners:
- Isocitrate lyase
- Putative isocitrate lyase subunit B
- Putative isocitrate lyase subunit A
- Citrate synthase 1
- Fumarate hydratase class II
- Phosphate acetyltransferase
- 2-methylcitrate synthase
- Putative citrate synthase 2
- Acetyl-coenzyme A synthetase
- Probable malate:quinone oxidoreductase
Sequence:
MTDRVSVGNLRIARVLYDFVNNEALPGTDIDPDSFWAGVDKVVADLTPQNQALLNARDELQAQIDKWHRRRVIEPIDMDAYRQFLTEIGYLLPEPDDFTITTSGVDAEITTTAGPQLVVPVLNARFALNAANARWGSLYDALYGTDVIPETDGAEKGPTYNKVRGDKVIAYARKFLDDSVPLSSGSFGDATGFTVQDGQLVVALPDKSTGLANPGQFAGYTGAAESPTSVLLINHGLHIEILIDPESQVGTTDRAGVKDVILESAITTIMDFEDSVAAVDAADKVLGYRNWLGLNKGDLAAAVDKDGTAFLRVLNRDRNYTAPGGGQFTLPGRSLMFVRNVGHLMTNDAIVDTDGSEVFEGIMDALFTGLIAIHGLKASDVNGPLINSRTGSIYIVKPKMHGPAEVAFTCELFSRVEDVLGLPQNTMKIGIMDEERRTTVNLKACIKAAADRVVFINTGFLDRTGDEIHTSMEAGPMVRKGTMKSQPWILAYEDHNVDAGLAAGFSGRAQVGKGMWTMTELMADMVETKIAQPRAGASTAWVPSPTAATLHALHYHQVDVAAVQQGLAGKRRATIEQLLTIPLAKELAWAPDEIREEVDNNCQSILGYVVRWVDQGVGCSKVPDIHDVALMEDRATLRISSQLLANWLRHGVITSADVRASLERMAPLVDRQNAGDVAYRPMAPNFDDSIAFLAAQELILSGAQQPNGYTEPILHRRRREFKARAAEKPAPSDRAGDDAAR
Protein: Pituitary homeobox 1 (Hindlimb-expressed homeobox protein backfoot) (Homeobox protein PITX1) (Paired-like homeodomain transcription factor 1) (P78337)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor that binds gene promoters and activates their transcription. May play a role in the development of anterior structures, and in particular, the brain and facies and in specifying the identity or structure of hindlimb.
Subcellular location: Nucleus.
Interaction partners:
- T-box transcription factor TBX4
- T-box transcription factor TBX19
- Early growth response protein 1
- Pituitary-specific positive transcription factor 1
- T-box transcription factor TBX5
- Steroidogenic factor 1
- Follitropin subunit beta
Sequence:
MDAFKGGMSLERLPEGLRPPPPPPHDMGPAFHLARPADPREPLENSASESSDTELPEKERGGEPKGPEDSGAGGTGCGGADDPAKKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSMREEIAVWTNLTEPRVRVWFKNRRAKWRKRERNQQLDLCKGGYVPQFSGLVQPYEDVYAAGYSYNNWAAKSLAPAPLSTKSFTFFNSMSPLSSQSMFSAPSSISSMTMPSSMGPGAVPGMPNSGLNNINNLTGSSLNSAMSPGACPYGTPASPYSVYRDTCNSSLASLRLKSKQHSSFGYGGLQGPASGLNACQYNS
Protein: ADAMTS-like protein 1 (ADAMTSL-1) (Punctin-1) (Q8N6G6)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11805097, ECO:0000269|PubMed:17395588, ECO:0000269|PubMed:19671700}.
Interaction partners:
- Beta-1,3-glucosyltransferase
- GDP-fucose protein O-fucosyltransferase 2
Sequence:
MECCRRATPGTLLLFLAFLLLSSRTARSEEDRDGLWDAWGPWSECSRTCGGGASYSLRRCLSSKSCEGRNIRYRTCSNVDCPPEAGDFRAQQCSAHNDVKHHGQFYEWLPVSNDPDNPCSLKCQAKGTTLVVELAPKVLDGTRCYTESLDMCISGLCQIVGCDHQLGSTVKEDNCGVCNGDGSTCRLVRGQYKSQLSATKSDDTVVAIPYGSRHIRLVLKGPDHLYLETKTLQGTKGENSLSSTGTFLVDNSSVDFQKFPDKEILRMAGPLTADFIVKIRNSGSADSTVQFIFYQPIIHRWRETDFFPCSATCGGGYQLTSAECYDLRSNRVVADQYCHYYPENIKPKPKLQECNLDPCPASDGYKQIMPYDLYHPLPRWEATPWTACSSSCGGGIQSRAVSCVEEDIQGHVTSVEEWKCMYTPKMPIAQPCNIFDCPKWLAQEWSPCTVTCGQGLRYRVVLCIDHRGMHTGGCSPKTKPHIKEECIVPTPCYKPKEKLPVEAKLPWFKQAQELEEGAAVSEEPSFIPEAWSACTVTCGVGTQVRIVRCQVLLSFSQSVADLPIDECEGPKPASQRACYAGPCSGEIPEFNPDETDGLFGGLQDFDELYDWEYEGFTKCSESCGGGVQEAVVSCLNKQTREPAEENLCVTSRRPPQLLKSCNLDPCPARWEIGKWSPCSLTCGVGLQTRDVFCSHLLSREMNETVILADELCRQPKPSTVQACNRFNCPPAWYPAQWQPCSRTCGGGVQKREVLCKQRMADGSFLELPETFCSASKPACQQACKKDDCPSEWLLSDWTECSTSCGEGTQTRSAICRKMLKTGLSTVVNSTLCPPLPFSSSIRPCMLATCARPGRPSTKHSPHIAAARKVYIQTRRQRKLHFVVGGFAYLLPKTAVVLRCPARRVRKPLITWEKDGQHLISSTHVTVAPFGYLKIHRLKPSDAGVYTCSAGPAREHFVIKLIGGNRKLVARPLSPRSEEEVLAGRKGGPKEALQTHKHQNGIFSNGSKAEKRGLAANPGSRYDDLVSRLLEQGGWPGELLASWEAQDSAERNTTSEEDPGAEQVLLHLPFTMVTEQRRLDDILGNLSQQPEELRDLYSKHLVAQLAQEIFRSHLEHQDTLLKPSERRTSPVTLSPHKHVSGFSSSLRTSSTGDAGGGSRRPHRKPTILRKISAAQQLSASEVVTHLGQTVALASGTLSVLLHCEAIGHPRPTISWARNGEEVQFSDRILLQPDDSLQILAPVEADVGFYTCNATNALGYDSVSIAVTLAGKPLVKTSRMTVINTEKPAVTVDIGSTIKTVQGVNVTINCQVAGVPEAEVTWFRNKSKLGSPHHLHEGSLLLTNVSSSDQGLYSCRAANLHGELTESTQLLILDPPQVPTQLEDIRALLAATGPNLPSVLTSPLGTQLVLDPGNSALLGCPIKGHPVPNITWFHGGQPIVTATGLTHHILAAGQILQVANLSGGSQGEFSCLAQNEAGVLMQKASLVIQDYWWSVDRLATCSASCGNRGVQQPRLRCLLNSTEVNPAHCAGKVRPAVQPIACNRRDCPSRWMVTSWSACTRSCGGGVQTRRVTCQKLKASGISTPVSNDMCTQVAKRPVDTQACNQQLCVEWAFSSWGQCNGPCIGPHLAVQHRQVFCQTRDGITLPSEQCSALPRPVSTQNCWSEACSVHWRVSLWTLCTATCGNYGFQSRRVECVHARTNKAVPEHLCSWGPRPANWQRCNITPCENMECRDTTRYCEKVKQLKLCQLSQFKSRCCGTCGKA
Protein: Small ribosomal subunit protein mS33 (37S ribosomal protein S27, mitochondrial) (O14358)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mitochondrial genome encoded proteins translation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS19m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein bS16m
Sequence:
MASKAILEELNILSSKIFGTQYKSNNSRTGRKFVVQELKGAKLKSYYPATINYRQLRTLLNDKTFPDSDEELRMEIRKGRIRQGKGASKSKKK