wanglab/gogpt-training-data huggingface dataset:
Protein: Putative acyltransferase Rv0859 (EC 2.3.1.-) (O53871)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable fatty oxidation protein FadB
- 3-hydroxybutyryl-CoA dehydrogenase
- Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3
- Acetyl-coenzyme A synthetase
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B
- Phosphate acetyltransferase
- Probable acetyl-CoA acetyltransferase
- Malate synthase G
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit A
- 2-isopropylmalate synthase
Sequence:
MSEEAFIYEAIRTPRGKQKNGSLHEVKPLSLVVGLIDELRKRHPDLDENLISDVILGCVSPVGDQGGDIARAAVLASGMPVTSGGVQLNRFCASGLEAVNTAAQKVRSGWDDLVLAGGVESMSRVPMGSDGGAMGLDPATNYDVMFVPQSIGADLIATIEGFSREDVDAYALRSQQKAAEAWSGGYFAKSVVPVRDQNGLLILDHDEHMRPDTTKEGLAKLKPAFEGLAALGGFDDVALQKYHWVEKINHVHTGGNSSGIVDGAALVMIGSAAAGKLQGLTPRARIVATATSGADPVIMLTGPTPATRKVLDRAGLTVDDIDLFELNEAFASVVLKFQKDLNIPDEKLNVNGGAIAMGHPLGATGAMILGTMVDELERRNARRALITLCIGGGMGVATIIERV
Protein: Anon1A3 (Q7KLV0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GVENLPSVAEAKQNHVDEVKPISEEPGNSSEEVPKAEEPLKSSGETSENGAATETAAAPKEPASVMDVDEDETLVENTPSANKEKALDDEKEPEQKSEEHAAAVLESKEQNEPAKEPTPEPMEVDGSSKGSSDTAQVDTPAIENVSAAPETEAAAKTTESSNDVVEVATEGKETVLEVPAAEPKEAESTVESAEELTETSTVVVTEPKEAASSEEEPSKVVDSAEPKEAESNTDESATPVPIDVSTAPASNDVSKPLEIDTTLVKTADSPAKEPQEICEVKKAEINVNGEPKIVNSSAEVGENAAPKVCN
Protein: Argininosuccinate lyase (ASAL) (EC 4.3.2.1) (Arginosuccinase) (P9WPY7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
Interaction partners:
- Argininosuccinate synthase
- Acetylglutamate kinase
- Ornithine carbamoyltransferase
- N-acetyl-gamma-glutamyl-phosphate reductase
- Acetylornithine aminotransferase
- Arginine repressor
- Arginine biosynthesis bifunctional protein ArgJ
- Adenylosuccinate lyase
- Arginine deiminase
- Malate dehydrogenase
Sequence:
MSTNEGSLWGGRFAGGPSDALAALSKSTHFDWVLAPYDLTASRAHTMVLFRAGLLTEEQRDGLLAGLDSLAQDVADGSFGPLVTDEDVHAALERGLIDRVGPDLGGRLRAGRSRNDQVAALFRMWLRDAVRRVATGVLDVVGALAEQAAAHPSAIMPGKTHLQSAQPILLAHHLLAHAHPLLRDLDRIVDFDKRAAVSPYGSGALAGSSLGLDPDAIAADLGFSAAADNSVDATAARDFAAEAAFVFAMIAVDLSRLAEDIIVWSSTEFGYVTLHDSWSTGSSIMPQKKNPDIAELARGKSGRLIGNLAGLLATLKAQPLAYNRDLQEDKEPVFDSVAQLELLLPAMAGLVASLTFNVQRMAELAPAGYTLATDLAEWLVRQGVPFRSAHEAAGAAVRAAEQRGVGLQELTDDELAAISPELTPQVREVLTIEGSVSARDCRGGTAPGRVAEQLNAIGEAAERLRRQLVR
Protein: Beta-glucosidase 14 (AtBGLU14) (EC 3.2.1.21) (Q9SLA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F2J10.10 protein
- 16S rRNA
- V-type proton ATPase subunit c''1
- V-type proton ATPase subunit c3
- V-type proton ATPase subunit c4
- V-type proton ATPase subunit c1
- V-type proton ATPase subunit c2
- V-type proton ATPase subunit e1
- Probable serine/threonine-protein kinase PBL19
- V-type proton ATPase subunit e2
Sequence:
MTSKYFSVLVFIILASNEVVAKRHSSTPKLRKTDFPEDFIFGAATSAYQVEGAAQEDGRGPSIWDTFSEKYPEKIKDGSNGSIADDSYHLYKEDVGLLHQIGFNAYRFSISWSRILPRGNLKGGINQAGIDYYNNLINELLSKGIKPFATIFHWDTPQDLEDAYGGFRGAEIVNDFRDYADICFKSFGDRVKHWITLNEPLTVVQQGYVAGVMAPGRCSKFTNPNCTAGNGATEPYIVGHNLILAHGEAIKVYRKKYKASQKGQVGIALNAGWNLPYTESAEDRLAAARAMAFTFDYFMEPLVTGKYPVDMVNNVKGGRLPTFTSKQSNMLKGSYDFIGINYYSSSYAKDVPCSSENVTMFSDPCASVTGERDGGIRDLILYAKYKFKDPVMYITENGRDEASTGKILLKDGDRIDYYARHLKMVQDAILIGANVKGFFAWSLLDNFEWASGYTVRFGLVYVDFNDRRKRYLKKSAHWFRHLLNGKKEN
Protein: Proline rich 13 (F8VRX0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWNPNAGPCPPPPGAPHGNPAFPPGGPPHPVPQPGYPGCQPLGPYPPPYPPPAPGIPPVNPLAPGMVGPAVIVDKKMQKKMKKAHKKMHKHQKHHKYHKHGKHSSSSSSSSSSDSD
Protein: 3',5'-cyclic-AMP phosphodiesterase 7B (EC 3.1.4.53) (cAMP-specific phosphodiesterase 7B) (Q9NP56)
Organism: Homo sapiens (Human)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain.
Interaction partners:
- Adenosine kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Adenine phosphoribosyltransferase
- GTP:AMP phosphotransferase AK3, mitochondrial
- Deoxycytidine kinase
- Adenylosuccinate lyase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Adenylate cyclase type 7
- Adenylate cyclase type 8
Sequence:
MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYSGEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIFLFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMSVLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHNKDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEISPLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQHRSRGSSGSGPDHDHAGQGTESEEQEGDSP
Protein: Orphan toxin OrtT (P64453)
Organism: Escherichia coli (strain K12)
Function: Acts as an orphan toxin which is important for maintaining cell fitness during stress related to the stringent response (decreased amino acid, purine and thymidine availability). Overexpression inhibits cell growth and increases the formation of persister cells. Causes 99.9% of cells to undergo bacterial lysis within 2 hours after induction; nucleoids condense, the cytoplasm seems empty and the periplasmic space enlarges. The intracellular ATP level decreases about 27-fold suggesting the membrane potential may be disrupted.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:25643179}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YgeI
- Uncharacterized protein YdcY
- Uncharacterized protein YncL
Sequence:
MSLYQHMLVFYAVMAAIAFLITWFLSHDKKRIRFLSAFLVGATWPMSFPVALLFSLF
Protein: T. brucei spp.-specific protein (Q580J7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRCSPQYNEANPPPTSQLTRLKYTPVELTETIVNCQAIPMSPVLLRMKCVVTNVSPDSLLLPDLLHSRPRKTIKVETRVSDDMEVPLFYGAVCGIYTGPNGKEVAAKQWFVDLARICTQGNAMLRDKKTGVLFPTQPLVTQRKRCREREGVSRNDKANDGCNDGSANMCSETSRSRRIVVLHNPLHRYQLVALRTEEISRNS
Protein: Suppressor of kinetochore protein 1 (Centromere DNA-binding protein complex CBF3 subunit D) (E3 ubiquitin ligase complex SCF subunit SKP1) (P52286)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Centromere DNA-binding protein complex CBF3 subunit C
- Centromere DNA-binding protein complex CBF3 subunit A
- Centromere DNA-binding protein complex CBF3 subunit B
- RING-box protein HRT1
- Cell division control protein 4
- Regulator of V-ATPase in vacuolar membrane protein 1
- Ubiquitin-conjugating enzyme E2-34 kDa
- F-box protein MET30 subunit MET30)
- SCF E3 ubiquitin ligase complex F-box protein GRR1
- Cell division control protein 53
Sequence:
MVTSNVVLVSGEGERFTVDKKIAERSLLLKNYLNDMHDSNLQNNSDSESDSDSETNHKSKDNNNGDDDDEDDDEIVMPVPNVRSSVLQKVIEWAEHHRDSNFPDEDDDDSRKSAPVDSWDREFLKVDQEMLYEIILAANYLNIKPLLDAGCKVVAEMIRGRSPEEIRRTFNIVNDFTPEEEAAIRRENEWAEDR
Protein: Oxalyl-CoA decarboxylase (EC 4.1.1.8) (P40149)
Organism: Oxalobacter formigenes
Function: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA.
Interaction partners:
Sequence:
MSNDDNVELTDGFHVLIDALKMNDIDTMYGVVGIPITNLARMWQDDGQRFYSFRHEQHAGYAASIAGYIEGKPGVCLTVSAPGFLNGVTSLAHATTNCFPMILLSGSSEREIVDLQQGDYEEMDQMNVARPHCKASFRINSIKDIPIGIARAVRTAVSGRPGGVYVDLPAKLFGQTISVEEANKLLFKPIDPAPAQIPAEDAIARAADLIKNAKRPVIMLGKGAAYAQCDDEIRALVEETGIPFLPMGMAKGLLPDNHPQSAAATRAFALAQCDVCVLIGARLNWLMQHGKGKTWGDELKKYVQIDIQANEMDSNQPIAAPVVGDIKSAVSLLRKALKGAPKADAEWTGALKAKVDGNKAKLAGKMTAETPSGMMNYSNSLGVVRDFMLANPDISLVNEGANALDNTRMIVDMLKPRKRLDSGTWGVMGIGMGYCVAAAAVTGKPVIAVEGDSAFGFSGMELETICRYNLPVTVIIMNNGGIYKGNEADPQPGVISCTRLTRGRYDMMMEAFGGKGYVANTPAELKAALEEAVASGKPCLINAMIDPDAGVESGRIKSLNVVSKVGKK
Protein: Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain] (P00740)
Organism: Homo sapiens (Human)
Function: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
Subcellular location: Secreted {ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:3857619, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.
Interaction partners:
- Antithrombin-III
- Coagulation factor VIII
- Tissue factor
- Coagulation factor VII
- Vitamin K-dependent gamma-carboxylase
- Coagulation factor XI
- Immunoglobulin lambda-like polypeptide 5
- Coagulation factor X
- Prothrombin
- von Willebrand factor
Sequence:
MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Protein: Follistatin-related protein 5 (Follistatin-like protein 5) (Q8N475)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MFKCWSVVLVLGFIFLESEGRPTKEGGYGLKSYQPLMRLRHKQEKNQESSRVKGFMIQDGPFGSCENKYCGLGRHCVTSRETGQAECACMDLCKRHYKPVCGSDGEFYENHCEVHRAACLKKQKITIVHNEDCFFKGDKCKTTEYSKMKNMLLDLQNQKYIMQENENPNGDDISRKKLLVDQMFKYFDADSNGLVDINELTQVIKQEELGKDLFDCTLYVLLKYDDFNADKHLALEEFYRAFQVIQLSLPEDQKLSITAATVGQSAVLSCAIQGTLRPPIIWKRNNIILNNLDLEDINDFGDDGSLYITKVTTTHVGNYTCYADGYEQVYQTHIFQVNVPPVIRVYPESQAREPGVTASLRCHAEGIPKPQLGWLKNGIDITPKLSKQLTLQANGSEVHISNVRYEDTGAYTCIAKNEAGVDEDISSLFVEDSARKTLANILWREEGLGIGNMFYVFYEDGIKVIQPIECEFQRHIKPSEKLLGFQDEVCPKAEGDEVQRCVWASAVNVKDKFIYVAQPTLDRVLIVDVQSQKVVQAVSTDPVPVKLHYDKSHDQVWVLSWGTLEKTSPTLQVITLASGNVPHHTIHTQPVGKQFDRVDDFFIPTTTLIITHMRFGFILHKDEAALQKIDLETMSYIKTINLKDYKCVPQSLAYTHLGGYYFIGCKPDSTGAVSPQVMVDGVTDSVIGFNSDVTGTPYVSPDGHYLVSINDVKGLVRVQYITIRGEIQEAFDIYTNLHISDLAFQPSFTEAHQYNIYGSSSTQTDVLFVELSSGKVKMIKSLKEPLKAEEWPWNRKNRQIQDSGLFGQYLMTPSKDSLFILDGRLNKLNCEITEVEKGNTVIWVGDA
Protein: Glucocorticoid modulatory element-binding protein 1 (GMEB-1) (Q9JL60)
Organism: Mus musculus (Mouse)
Function: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter (By similarity).
Subcellular location: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
Interaction partners:
- Glucocorticoid modulatory element-binding protein 2
Sequence:
MANAEVSVPVGDVVVVPTEGNEGENPEDTKTQVILQLQPVQQGIYEAGSENSAAVVAVETHSIHKIEEGIDASSIEGNEDMEIAYPITCGESKAVLLWKKFVCPGINVKCVKFNDQLISPKHFVHLAGKSTLKDWKRAIRLGGIMLRKMMDSGQIDFYQHDKVCSNTCRSTKFDLLISSARAPVPGQQTSVVQTPTSADGNITQIAISEESMEEAGLEWNSALTAAVTMATEEGIKKESEEISEDTLMFWKGIADVGLMEEVVCNIQKEMEELLRGVQQRLIQAPFQVTDAAVLNNVANTFGLMDAVKRVLDNRRKQVEQGEEQFLYTLADLERQLEEQKKQAQDPRLKSQTVQNVVLMPVSTPKPPKRPRLQRPASTTVLSPSPVQQPQFTVISPITITPVGQSFSMGNIPVATLSQGSSPVTVHTLPSGPQLFRYATVVSSAKSNSPDTVTIHPSSSLALLSSTSMQDGSSLGNMATMVSPMELVAMESGLTSAIQAVESTSEDGQTIIEIDPAPDSEADDTEGKAVILETGLRTEEKVVAEMEEHQHQVHNVEIVVLED
Protein: 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial (EC 3.6.1.-) (GTP-binding protein 3) (tRNA modification GTPase GTPBP3, mitochondrial) (Q923K4)
Organism: Mus musculus (Mouse)
Function: GTPase involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14680828}.
Interaction partners:
- 5-taurinomethyluridine-[tRNA] synthase subunit MTO1, mitochondrial
- Large ribosomal subunit protein uL11m
- GTP-binding protein 8
- rRNA methyltransferase 3, mitochondrial
- Mitochondrial tRNA-specific 2-thiouridylase 1
- Large ribosomal subunit protein bL21m
- Mitochondrial ribosome-associated GTPase 1
- Large ribosomal subunit protein uL13m
- Endoplasmic reticulum-Golgi intermediate compartment protein 1
- Endoplasmic reticulum-Golgi intermediate compartment protein 2
Sequence:
MWRGLSALVTQAAWAPLRLCARCSTSAESLVPSSTIFALSSGQGRCAIAVIRTSGPASGLALRSLTALQEPPPARRACLRLLRHPCSGEPLDRSLVLWFPGPQSFTGEDCVEFHVHGGPAVVSGVLQALGSVPGLRPAEAGEFTRRAFAHGKLSLTEVEGLADLIRAETEAQRRQALRQLDGELSQLCQGWAKTLTKALAYVEAYIDFGEDDNLEEGVLEQADREVRALEVALGSHLRDARRGQRLLSGANVVVTGPPNAGKSSLVNLLSQKPVSIVSPEPGTTRDVLETPVDLAGFPVLLSDTAGLREGVGAVEQEGVRRARHRLEQADIILGVLDASDLASSSSCSFLDTVVTPLLAQSQDSGGQRLLLLLNKSDLLSANAPACDIALPPHLLLSCHTGAGMDSLLQALKTELAAVCGDPSTGPPLLTRVRHQYHLQGCLDALGHYQLATDLALAAEALRQARRQLNHLTGGGGTEEILDLIFQDFCVGK
Protein: UPF0665 family protein C23C4.06c (O13926)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein-lysine N-methyltransferase efm4
- Protein N-terminal and lysine N-methyltransferase efm7
- Cell division cycle protein 48
- Probable heat shock protein ssa1
Sequence:
MTFYYIRILRLQEKLEESFKYALRVVFTITSDLGEVSYPQDATVRVEALDRQQSHSRITISKQCVSWIGNGHAAETTLYFPASHQQIQLTLHLENQNSIVDSIHINADTVLPVWSEAFSPKSTLPNMVWRYIQGPEKKSPNDGLWFLEQMGNSIAKHLWDAGVVFSKKILSDDWHYSFSNRKDINVLELGSGCGIVGISIASKYPRALVSMTDTEDAIEFMEKNVEKNKSAMSNNITSDILVWGHDIPRKFRRHWDYIVMSDVMYNESSFSDLEASLQELMDKNTKLYIAYKKRHDNEKTFMSNILGWLDLVYEERGPITIYILQKK
Protein: aldehyde dehydrogenase (NAD(+)) (EC 1.2.1.3) (A0A1B0GTJ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
Protein: Trehalose-6-phosphate synthase (TPS) (EC 2.4.1.15) (EC 2.4.1.347) (Alpha,alpha-trehalose-phosphate synthase [UDP-forming]) (Osmoregulatory trehalose synthesis protein A) (OtsA) (P9WN11)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose. Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Is specific for the glucosyl acceptor (Glc-6-P cannot be replaced by either mannose-6-P, fructose-6-P or glucosamine-6-P), but any of the glucose sugar nucleotides can be used as glucosyl donors. It is more active with the purine sugar nucleotides than with the pyrimidine sugar nucleotides.
Interaction partners:
- Trehalose-phosphate phosphatase
- UTP--glucose-1-phosphate uridylyltransferase
- Glucose-1-phosphate adenylyltransferase
- Uncharacterized glycosyl hydrolase Rv2006
- Putative maltooligosyl trehalose synthase
- Malto-oligosyltrehalose trehalohydrolase
- Trehalose synthase/amylase TreS
- Glycogen synthase
- Trehalase
- Maltokinase
Sequence:
MAPSGGQEAQICDSETFGDSDFVVVANRLPVDLERLPDGSTTWKRSPGGLVTALEPVLRRRRGAWVGWPGVNDDGAEPDLHVLDGPIIQDELELHPVRLSTTDIAQYYEGFSNATLWPLYHDVIVKPLYHREWWDRYVDVNQRFAEAASRAAAHGATVWVQDYQLQLVPKMLRMLRPDLTIGFFLHIPFPPVELFMQMPWRTEIIQGLLGADLVGFHLPGGAQNFLILSRRLVGTDTSRGTVGVRSRFGAAVLGSRTIRVGAFPISVDSGALDHAARDRNIRRRAREIRTELGNPRKILLGVDRLDYTKGIDVRLKAFSELLAEGRVKRDDTVVVQLATPSRERVESYQTLRNDIERQVGHINGEYGEVGHPVVHYLHRPAPRDELIAFFVASDVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELRHAYLVNPHDLEGVKDGIEEALNQTEEAGRRRMRSLRRQVLAHDVDRWAQSFLDALAGAHPRGQG
Protein: Probable V-type proton ATPase subunit G (V-ATPase subunit G) (Vacuolar proton pump subunit G) (P91303)
Organism: Caenorhabditis elegans
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In neurons, required for necrotic cell death by promoting intracellular acidification.
Interaction partners:
- V-type proton ATPase subunit C
- V-type proton ATPase catalytic subunit A
- Probable V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit E
- V-type proton ATPase subunit S1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- Probable V-type proton ATPase subunit H 2
- V-type proton ATPase subunit e
- V-type proton ATPase subunit B 1
Sequence:
MASQTQGIQQLLAAEKRAAEKINEARKRKLQRTKQAKQEAQAEVEKYKQQREAEFKAFEQQYLGTKEDIESKIRRDTEDQISGMKQSVAGNKQAVIVRLLQLVCDIKPELHHNLTLQKKLHGQFAA
Protein: Rhino (Q49BK9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRNHQRPNLGLVDAPPNDHVEEYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESEVFRLHRKAAAKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMDQKKGKNIKKTAGKIKDIENYPKTQMPSTSQVSTDSTEVFDGNPSATTTNMIKSPRIQSLFSDLNLIEPTKDKDVGDTSLKTPPKSRRLIKFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPRRKRKKTYPNWKFPEITKPFGVNRGLDLDEILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK
Protein: LIM domain-binding protein 2a (LIM-domain binding factor 2) (O73713)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSNPPHDPFYSSPFGPFYRRHSPYMVQPEYRIYEMNKRLQSRTEESDSLWWDAFATEFFEEDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESFHNSCITVDCDQCTMVTQHGKPMFTKVCTEGRLILEFAFDDLMRIKTWHFNIRQYRELIPRSILAMHAQDPGVLEQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAGHPQNFKTEIFPTNHKKEPTRQTTTKRRKRKNSASSASNSSLGNSAGGKKRSPANNFSLASQDVMVVGEPTLMGGEFGDEDERLITRLENTQYDATNGLDDDDDFTSSPALANNSPWNSKPPTGQDSKPESTASQPSQ
Protein: Retinoic acid receptor RXR-beta (Nuclear receptor coregulator 1) (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta) (P49743)
Organism: Rattus norvegicus (Rat)
Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE).
Subcellular location: Nucleus {ECO:0000269|PubMed:28267642}. Cytoplasm {ECO:0000269|PubMed:28267642}.
Interaction partners:
- Oxysterols receptor LXR-beta
- Oxysterols receptor LXR-alpha
- Retinoic acid receptor, alpha
- Peroxisome proliferator-activated receptor gamma
- Retinoic acid receptor beta
- Nuclear receptor corepressor 1
- Peroxisome proliferator-activated receptor alpha
- Peroxisome proliferator activated receptor delta, isoform CRA_b.
- Thyroid hormone receptor alpha
- Retinoic acid receptor RXR-alpha
Sequence:
GEAGRDGMGDTGRDSRSPDSSSPNPLSQGIPPSSPPGPPHTPSAPPPPMPPPPLGSPFPVISSSMGSPGLPPPAPPGFSGPVSSPQINSTVSLPGGGSGPPEDVKPPVLGVRGLHCPPPPGGPGAGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYSCRDNKDCTVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGDGAGGAPEEMPVDRILEAELAVEQKSDQGVEGPGATGGGGSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSSLPLDDQVILLRAGWNELLIASFSHRSIDVRDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPGEVEILREKVYASLETYCKQKYPEQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQLA
Protein: DNA (cytosine-5)-methyltransferase 3B (Dnmt3b) (EC 2.1.1.37) (DNA methyltransferase MmuIIIB) (DNA MTase MmuIIIB) (M.MmuIIIB) (O88509)
Organism: Mus musculus (Mouse)
Function: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Functions as a transcriptional corepressor by associating with ZHX1 (By similarity). Required for DUX4 silencing in somatic cells (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15456878}. Note=Accumulates in the major satellite repeats at pericentric heterochromatin.
Interaction partners:
- DNA
- DNA
- Histone deacetylase 1
- Histone-lysine N-methyltransferase EZH2
- DNA
- Histone deacetylase 2
- Histone-lysine N-methyltransferase SUV39H1
- E3 ubiquitin-protein ligase UHRF1
- Histone H3.2
- Histone H3.1
Sequence:
MKGDSRHLNEEEGASGYEECIIVNGNFSDQSSDTKDAPSPPVLEAICTEPVCTPETRGRRSSSRLSKREVSSLLNYTQDMTGDGDRDDEVDDGNGSDILMPKLTRETKDTRTRSESPAVRTRHSNGTSSLERQRASPRITRGRQGRHHVQEYPVEFPATRSRRRRASSSASTPWSSPASVDFMEEVTPKSVSTPSVDLSQDGDQEGMDTTQVDAESRDGDSTEYQDDKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMPGMRWVQWFGDGKFSEISADKLVALGLFSQHFNLATFNKLVSYRKAMYHTLEKARVRAGKTFSSSPGESLEDQLKPMLEWAHGGFKPTGIEGLKPNKKQPVVNKSKVRRSDSRNLEPRRRENKSRRRTTNDSAASESPPPKRLKTNSYGGKDRGEDEESRERMASEVTNNKGNLEDRCLSCGKKNPVSFHPLFEGGLCQSCRDRFLELFYMYDEDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGAGTAEDAKLQEPWSCYMCLPQRCHGVLRRRKDWNMRLQDFFTTDPDLEEFEPPKLYPAIPAAKRRPIRVLSLFDGIATGYLVLKELGIKVEKYIASEVCAESIAVGTVKHEGQIKYVNDVRKITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYTRPKEGDNRPFFWMFENVVAMKVNDKKDISRFLACNPVMIDAIKVSAAHRARYFWGNLPGMNRPVMASKNDKLELQDCLEFSRTAKLKKVQTITTKSNSIRQGKNQLFPVVMNGKDDVLWCTELERIFGFPAHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE
Protein: FOXL2 neighbor protein (Q6ZUU3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTRTPVGSARTRPKPRKLGPQRGKALQASSRLSESPALVKKRMPDACTLGRAGIGLPKMCLHMAVRHSKAQKTGPGILQQRQKPPAPRASGGPALLGKRRGCSEAGSASLEPLSSSRAAAGCLNQVPLSPFLAGPRNTRRLPAPERERIELAATLCLEGWPLRCLASKGKLHCVY
Protein: Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14) (Q63396)
Organism: Rattus norvegicus (Rat)
Function: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA) (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Symplekin
Sequence:
MPKSKELVSSSSSGSDSDSEVEKKLKRKKQVVPEKPVKKQKPGESSRALASSKQSSSSRDDNMFQIGKMRYVSVRDFKGKILIDIREYWMDSEGEMKPGRKGISLNMEQWSQLKEQISDIDDAVRKL