wanglab/gogpt-training-data huggingface dataset:
Protein: Ankyrin-repeat protein, putative (Q38CX0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPSKDSATPLDAAILCHIRTPYLSGSGLVGTVQTRLSATLADVRRLLESLASLARQGNDRNVGNAIGSSEAPVNVSKEEMRKIMSHALHPFDLSADFSFVRGGCGAMVPREREKSTRLVDLFPLLPQLFSVNKKNYHIGWAMEPPAPLVRILARLEDMEVCRNAVAVLFVSMQTPDEMLKDRLTLYQSAANVGFSSKSAQLNSFKKSLNLWNCNVRDCFGRTVLHESVYHGNKEVVAHLLSLPFIHTNEQDAQGLTPLHIAVRKGDERIVSQLLMRGVDVLLQDASGDTALHTALRLRDSRLVELLCQCLREAGIGAEKLSQYRNKRGLSPSDVFKLRWPTFFQLCAVGDVQAIHTLYNHYLFKCDLAHAPDNLLHQSVVHVAAAAGHADVVRYLLDEVGFGRARAECFINSRLQTPLHVAAERGEFATVKFLYERYPKWLAARDITGATPLVAVLRNRRRWGTAIAEYFITVASSETIAPNTCDNGGNGALHLLCELGLFHLARLLVESHGADVNLAHTGTVNTHHFLRVTRRSKSLMEQMKWKLKHQKTGKQAKMTPILCAIRGGRCGIDIIEMLLSHGAATREDEIVELLFYLVSNEHYEVAERVLARENVKPPGHNELLCRFCREKHVVGISWCSKQGFRQLNVMQESHHPLAVSSALGDAAAVAILLEHGANANIGKSVLHTPLALAINGGHDDVVRCLVRAGACLLSADGSWSALRAAVKRGEEFIMAGLLAEPSLPPSEVVHAMVFALQDARGRGVEIRERLCVRLARALNLAECGGVHPTELLHLAASRSCFAVVRVLVDKLLALPREELENILKDAPAAPSLAYALIEPKAVPLPKGVPSRLYALHPSPAPFKRLITLRTWQEGLHHRLHLRDAFSYCASAREESLLETLLFDVGLKPWEGPDFRGWNAADYAVASGLYNSVRILLVSGLAPLRHHHVRSGTWLGILCRSMVTPAARPSETNLLYFTLKRLVCAGETLLIRHILWDVCRRCDVSDMRDASVWLTDVLLCCARSRSLEILHILTREFRVTWGRKFFPTAEPLLMAVLNSDAEMALFLMTHGAVPTAFGPIPKMHDNVKASFLREERRAVSPLWLAARLGETAILQQLLQSTDLLCHEATLDNSTQCGDILQALIDGATRRVTKERDAGMARTIFMLKRAGYLALTPDVVRCAARKGLVQVVNALVDCYGPDPFVEDLKCGGLCAIHFMVANPELCGTLRSLLVAGRSTATETVGGSVSLASAMLATPFRVNPVDYALRHGCAEGALLLLCLGLYGSGTVFAKRARTLSVVIRLAVQRRCTTGWSGYTALHAAIEMQCHSLAKTMACEMAAIHGPNSGPYAEMTIKNDDAPSLHAFMAFHLREAHFGTLLSSGVPPVVDISSPCDIPYIVWSPHASEGRFREAVRESATREGLEQPLDLMKESLRVEVRQHMLSYNENIFFRSRSFAVTALTPMACAVAAGKLSWVQLFSSCGVSLTNDSSIIAAKYSAVSTQGRIKAPPVYKLVDMRDSRKRKAPKSVRRKHVCSKDTGAWLLTAYVHNRCHISPIMLSMAIVVECVRSGAVEQRLLQQLQIIRYLLGSDECPLREEVNLLAIVAAELQLWGLLEDTVVTLERCRAVFDPISEGDIPPFMHNVVGSAHHVMHKVARVAPREIILLVARNSSFVHVEELCDAKGRTALYHALYHPTPAAVDTLLSLNVSVSKRCCSGTGRTPLMVASKLGKLGHAERLMRKEVLDLEDNYGNTALLLAAEGGHKQVVEYLLAQGSSPSTKNAKGMTAVMVAALAGHDSLAVPMVERFSGISDLFTPHTTILHCAAVGGAWGVATTVVSCLAQADPLAVDHFGYTALFLAHAFGNARVLRTLLGAVLHKGITVPSSFVRERQIISRSSELVPRGWLKGTLYLAEAVLGNGRKGSSSSLSSSHYGPMRSSETLYGHRTSIRRNDVPLLLWCVRNNNTLGVRVLGEINVGDNCYALHEAARSGNVEMVKLLLKLEVSSPDVLNESGMLPFEVAAVHKHVECASLILLHTKLDPVRLRVHIDHGDDPDTTANSTDSNTHNPMQLLASSENAEVFADVVDSVQRMSGDTWPSVAQQLFDTLSTPGPDGMTALELQLALGRAAGALRLVKILQRLSLDVAGNCAFAVSSSILHHLTNVSPAVRVLLHDMFGLTDVAKGYGMRRRRFGRLSFADVRLIGISALQSDAYCAAATSSIFTFGNEVGATSSLLERLPFEVRFVPRPFERRSAAERAKLIRWLGSSLILSSYKQLRTCAQFDAVEVEIVSHPAEEFAELVGDHLHHSIYVDGDCQLVVPDLNIILGFATRREKQRLLDEVEHLCGVLTDTMQSLPHPALSKGEVKVDWRNCNIDDVEQEAIECLIENGLKKLRVFLEGNLRDCLCGVNMTDILSVKCTAEPVTEKVHITFQYTREALKKFKPSATELGSTVDGLLCVVRFSDAGMGGLDFVMRSVLYPATLSDVNLVGVSRIRDAWVADVSRRVGQRMGGETIAFKLQLEGSELHELPLHLLKRMMADVTDAIAMLMSRPSAKKHRFLVSHIVGESLASSLRAVFVLFSTSRQPTARRAQGNLLICFNATMTPTMSDIYQCLRRSALKDEAERLKGMLMSIVSTMGLQLSVALPAVPLLMDVLGSLRHQDTENVVSFLSVLCHNDGSLVLKPLIEGVSIGWKTELGRVVRRHVRQISVALEVNGGASCELKENGTFVYKCPLNCAHAGSYAAHSKGLLSAQQIASLLLIQIDAMDPTMRSLISTTKAMACWSRACGTCTRLLDAGSQRCSIVIKRRNILDQPVGQSASDAFSFRGGWSGVKVKGSTGVVRFTAPTKAGYYLQHILLNDQPLFNSPLRIRVRPLGPHLPNTKILSTFNAVVVKRPFHIQLLLHDRYLNRVAHICPLRIEAVDGGAVHVAGWKRLHVDTVEVEVVVKEICEQCSLRFRLLAPGGAGNFVVDYTVASVTPDTYRQQFGPVKSRLMAKGLQGKTGRPQRPPPPPVGIMSKRQKNESRTPRYIFPPLRAVAKGEKNTKRKSKPPST
Protein: Sharpin (Shank-associated RH domain-interacting protein) (Shank-interacting protein-like 1) (mSIPL1) (Q91WA6)
Organism: Mus musculus (Mouse)
Function: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9H0F6}. Synapse {ECO:0000250|UniProtKB:Q9EQL9}. Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1. {ECO:0000250|UniProtKB:Q9EQL9}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF31
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Tumor necrosis factor receptor superfamily member 1A
- NF-kappa-B essential modulator
- Tumor necrosis factor
- Baculoviral IAP repeat-containing protein 3
- Baculoviral IAP repeat-containing protein 2
- Receptor-interacting serine/threonine-protein kinase 1
- Spermatogenesis-associated protein 2
- TNF receptor-associated factor 2
Sequence:
MSPPAGGAAVAADPASPVVLLAVHAAVRPLGAGQDAEAQPRKLQLIADPERPGRFRLGLLGTEPGAVSLEWPLEAICYTVRGPNQHELQPPPGGPGTFSVHFLDPEEAQQWAALVRDATAEGQNGSGSPAPAPAPAMCPISPPCSSMAQIPKATQPEVDLPQSSGNFKKEELATRLSQAIAGGDEKAAAQVAAVLAQHHVALNVQLMEAWFPPGPIRLQVTVEDATSVLSSSSSAHVSLKIHPHCSIAALQDQVFSEFGFPPAVQRWVIGRCLCMPERSLASYGVSQDGDPAFLYLLSAPREVSGQSLQNSKMDRKLGLFPQSLGLPHDLQPSSSSLPSPSQPGWSCPSCTFINASNRPGCEMCSTQRPCAWDPLAAAST
Protein: Protein YIP4b (YPT/RAB GTPase-interacting protein 4b) (YIP4b) (Q93VH1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with YIP4A, involved in the regulation of cell elongation during root and hypocotyl growth. YIP4A and YIP4B are central trafficking components in Rho-of-plant (ROPs, e.g. ARAC4/ROP2, ARAC5/ROP4 and ARAC3/ROP6) small GTPases-dependent root hair formation, thus contributing to activation and plasma membrane accumulation of ROPs during hair initiation. The ECH/YIP4 complex is involved in the modulation of the trans-Golgi network (TGN)-mediated trafficking of some proteins and cell wall components (e.g. pectin and hemicellulose) to the cell wall in dark-grown hypocotyls and in secretory cells of the seed coat.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23832588}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSHNDTIPLYQSSQSDIDEIENMMNDSFQSGPGTVLPARPPSPIRPSIPVSSSPFVQSNLPPLPPSSSSSTQKVMPVPAPPPLPSAGNEGNKSIGGSGFGSPPNTLTEPVWDTVKRDLSRIVSNLKLVVFPNPYREDPGKALRDWDLWGPFFFIVFLGLTLSWSASVKKSEVFAVAFALLAAGAVILTLNVLLLGGHIIFFQSLSLLGYCLFPLDVGAVICMLKDNVILKMVVVSVTLAWSSWAAYPFMSAAVNPRRKALALYPVFLMYVSVGFLIIAIN
Protein: LD16736p (Q8MSX0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSETYDYLFKFLIIGSAGSGKSCLLHHFIESKFKDDSSHTIGVEFRLADCERGRQVGKATDMGHSRSGEIPIGDKIVLSRSSRSSPGLRCHFAGLFQCFDKLAE
Protein: Phosphopentomutase (EC 5.4.2.7) (Glucose phosphomutase 2) (Phosphodeoxyribomutase) (Phosphoglucomutase-2) (EC 5.4.2.2) (Q96G03)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. Catalyzes the interconversion of glucose-1-phosphate into glucose-6-phosphate but with a lower catalytic efficiency. In vitro, has also a low glucose 1,6-bisphosphate synthase activity which is most probably not physiologically relevant.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17804405}.
Interaction partners:
- Phosphoglucomutase-1
- Glucose-6-phosphate isomerase
- Deoxyribose-phosphate aldolase
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, muscle form
- Glycogen phosphorylase, brain form
- Ribokinase
- Phosphoglucomutase-like protein 5
- ADP-dependent glucokinase
Sequence:
MAAPEGSGLGEDARLDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTAGLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHPSSGGSSRRFARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCFHRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDRSALKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKASYFICHDQETIKKLFENLRNYDGKNNYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEQLKKELNELVSAIEEHFFQPQKYNLQPKAD
Protein: Magnetosome protein MamI (Q2W8Q9)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Essential for magnetosome formation. May bind magnetite (Probable). May be involved in an early stage of magnetosome nucleation (By similarity).
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:28790202, ECO:0000305|PubMed:20212111}; Multi-pass membrane protein {ECO:0000255}. Note=Tagged protein forms straight lines extending along most of the cell associated with its inner curvature, in the correct position to be associated with magnetosomes (PubMed:20212111, PubMed:21414040, PubMed:21883528, PubMed:28790202). In a mamK deletion MamI forms a linear punctate pattern, suggesting it is associated with magnetosomes (PubMed:20212111). In a mamE deletion MamI forms a linear punctate pattern (PubMed:21414040). In double mamJ/limJ deletion MamI forms a linear punctate pattern (PubMed:21883528). {ECO:0000269|PubMed:20212111, ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:21883528, ECO:0000269|PubMed:28790202}.
Interaction partners:
- Magnetosome formation protease MamE
- Magnetosome protein MamH
- Actin-like protein MamK
- Magnetosome-associated protein MamJ
- Magnetosome protein MamL
- Magnetosome protein MamM
- Magnetosome protein MamN
- Multi-heme protein MamP
- Magnetosome protein MamB
- Probable membrane transporter protein MamO
Sequence:
MPSVIFGLLALALGLLGVTAWWWSVTEFLRGAVPVALLILGLVALASGVQSVRLPRSNKGTASDPDIDG
Protein: Tricalbin-1 (Q12466)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in membrane trafficking.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22250200}; Multi-pass membrane protein {ECO:0000255}. Note=More enriched in the cortical endoplasmic reticulum (ER) that is closely apposed to the cell membrane than in the perinuclear ER or internal ER tubules that connect the nucleus to the cortical ER. {ECO:0000269|PubMed:22250200}.
Interaction partners:
- Increased sodium tolerance protein 2
- Vesicle-associated membrane protein-associated protein SCS22
- Vesicle-associated membrane protein-associated protein SCS2
- Tricalbin-3
- Phosphatidylinositol-3-phosphatase SAC1
- Nucleus-vacuole junction protein 2
- Protein ICE2
- ATP synthase subunit 9, mitochondrial
Sequence:
MAKEDTGVTAPKKPETAQVANINGIDKLEPPKTKEETESSKSVSSEKAAHASDESFKRSIHEASYVGWKQIGGWEDKDELTLDDELMDMTRETFLDNIIPDSLYGDWYHSVAIFFIGGVASFALGHYKFSMGSAFFVIVITSLLYRTSAKKYRGSIRELVQKEFTVQKVENDYESLEWLNAFLDKYWPILEPSVSQLIVQQANEQMATNEAIPKFITQLWIDELTLGVKPPRVDLVKTFQNTASDVVVMDWGISFTPHDLCDMSAKQVRNYVNELAVVKAKIFGITIPVSVSDIAFKAHARVKFKLMTPFPHVETVNIQLLKVPDFDFVATLFGRSIFNWEILAIPGLMTLIQKMAKKYMGPILLPPFSLQLNIPQLLSGSNLSIGILEITVKNAKGLKRTSSILNESIDPYLSFEFNDISIAKTRTVRDTLNPVWDETLYVLLNSFTDPLTISVYDKRAKLKDKVLGRIQYNLNTLHDKTTQRNLKAQFLRNSKPVGELTFDLRFFPTLEEKKLPDGSVEELPDLNTGIAKVVVEEGSRFAEEEQKVTAYVEVYLNAKLVLTTGKATDTGTLKWNSDYEAVIADRRKTRYKFVVKDGKGEEIGSTIQTLNDLIDRSQVNKNLIPLKNQKGDIKITTYWRPVRLEIGSNSVAYTPPIGAIRVFIEKANDLRNLEKFGTIDPYCKVLVNGLSKGRTDFKSQTLNPVWNQVIYVAVTSPNQRITLQCMDVETVNKDRSLGEFNVNVQDLFKKDENDKYEETIDEKAKVGRLVMPKKKPKGTITYYTSFYPALPVLTLEEIQDLDKVNKKKKALELRKSAIDEKKISKEDKAKFDQEWNEVKELEDMYSNRQKLDLPELLQYNQGVLAVTVLNGELPDSGLYVQAFFDDNGHPRFVSPRIPSRIVKNGWSGDVIIKELDKSITTFRVAKNKNYNRVEKCVCEVELPTQELVKNCYYKPSILHLSGEGSAKLMLQISWFPIDTKQLPANDLITNSGDLTIMSRSAENLIASDLNGYSDPYLKYYINNEEDCAYKTKVVKKTLNPKWNDEGTIQINNRLNDVLRIKVMDWDSTSADDTIGTAEIPLNKVKVEGTTELDVPVEGLENAGQDGGMLHLAFSFKPRYTISVSKREKKVGDIASKGLGTGLKAGTTVIGGGVGAIGKIKKGVFGGLGSLTNHKKNHEMGEEETKF
Protein: 4-aminobutyrate aminotransferase, mitochondrial (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (GABA-T) (L-AIBAT) (Q9BGI0)
Organism: Bos taurus (Bovine)
Function: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Succinate-semialdehyde dehydrogenase
- Uncharacterized protein.
- Glutamate decarboxylase 1
- Glutamate decarboxylase 2
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase, dimeric NADP-preferring
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase family 3 member B1
Sequence:
MASMLVAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGRLMKTEVPGLRCQELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPGLLKLIQQPQNASMFVNRPALGILLPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENGLKTIFMWYRSKERGQRGFPQEELETCMINQAPWCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDIPRKQCCAFLVDVVQTGGGCTGKFWAHEHWARDDPEDVMTSSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLLDLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSDILADFK
Protein: Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 5) (LACS 5) (Q8JZR0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity). ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL (By similarity). May have a role in the survival of glioma cells (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9ULC5}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9ULC5}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q9ULC5}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Lipoprotein lipase
- Monoglyceride lipase
- Palmitoyl-protein thioesterase 1
- Lysosomal thioesterase PPT2
- Palmitoyl thioesterase CPT1C
- Endothelial lipase
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MLFIFNFLFSPLPTPALICLLTFGTAIFLWLINRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYENFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKATMLVENVEKGLTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVKNGIIRRDSLWDKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE
Protein: AP-3 complex subunit beta (O77290)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004145}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004145}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004145}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MQQNSASNPFAMSTYVERPQMGLDVEFGADPASGAAFFQSDGRKHDDLKQMLDSNKDGLKLEAMKRIIGMIARGRDASDLFPAVVKNVVSKNIEVKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVSMIVPIVMLAIRDSAADLSPYVRKTAAHAIPKLYSLDADQKDELVMVIEKLLSDRTTLVVGSAVMAFDEVCPERVDLIHKNYRKLCNFLLDVDEWGQVIIINMLTRYARTQFVDPNADDEDLVNDGLGETPVSERFYDESSHSSSHSDDGSSDDEKNKSSTNNKNNGGGNGSRTPSSPSNSYHIDVDHRLLLRQTKPLLQSRNASVVMAVAQLYHHVAPKNEVQLIAKALIRLLRSHKEVQSVVLNCIASMSTKRKAIFEPHLKSFFVRTSDPTHIKLLKLDILTNLASAGSISLILREFQTYISSSDRSFVAATIQAIGRCASSIKEVTETCLSGLVHLLSNHDEHVVAESVVVIKRLLQTKAAEHFEIITQMAKLIDYINVPAARAAIIWLIGEYNEKVPLIAPDVLRKMAKSFVDEQDVVKLQVLNLGVKLYLTNPEQTSLLCQYVFTLARYDPNYDVRDRARFLRQIIFPASGTSSVLSQHARQVFLASKPAPVPESKYRDGNNFQLGSLSHYLNMPAAGYKELPAFPVIPPDSSVRNIAGFMQDKLPGEDSPSGHSKDKSGREGGKEKGAGGEKGFLSESDDKSSAYSESGSSSGSGTSDSESDSDGSGSSDEEEEEVQKQQPTKVSSVKERLIDAGSNELAATSSPVKATINTNNNARGSSGTSDSEDSSAYSGSSSDDSASGSDNEVKKNETKTDTGTKPEKLKEKHEKQPEQTAVKSNLDLLLDLDDIPPIGPVMTPSLGGFLTPGTPMMAGQAAPLQPQHARNRVELVGPSHIEFKHKELLNKVSGHGLHLAYRFTRSPHLYSSSMCSIELQFQNRGEKEITAIRLGQTTLPAGMQLNEFAPITVLQPQQTASGVLGVDFNDSTHAVDLELLSSAGSSRLQLKPPVGELVRSVQIGESCHREERAKLRGMNEHQCELRGLRQDLIDVVALRQKVFESINVAHTHSSSSGQLHCFAGQTLSSKSLVLLTLDWKTEDALTLLVNCEKMVIGSMVLNELRNALQLSFAM
Protein: Chromosomal serine/threonine-protein kinase JIL-1 (EC 2.7.11.1) (Q9V3I5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Phosphorylates 'Ser-10' of histone H3. May regulate gene expression by establishing or maintaining the structure of more open chromatin regions. Also required for normal polytene chromosome structure, for oogenesis and for viability throughout development. Regulates the structure of polytene chromosomes in salivary glands. May phosphorylate 'Ser-1' of histone H2A.
Subcellular location: Nucleus {ECO:0000269|PubMed:10445035}. Chromosome {ECO:0000269|PubMed:10445035}. Note=Associates with chromosomes throughout the cell cycle. Localizes to interband regions along the polytene chromosomes and is enriched almost two-fold on the male X chromosome compared to the autosome.
Interaction partners:
- Protein male-specific lethal-3
- Protein male-specific lethal-1
- E3 ubiquitin-protein ligase msl-2
- Dosage compensation regulator mle
- Histone-lysine N-methyltransferase Su
- Chromator, isoform A
- Histone acetyltransferase MOF
- Protein suppressor of variegation 3-7
- RINT1-like protein
- Cyclic AMP response element-binding protein B
Sequence:
MSRLQKQNYEILSGTSTSRLKNHQHPRESESLAYEEPDQMVRNHLNGQLVANGNGKTRKNSNSETMTNGKKSKLNTEGSGSGSGKTLNYNNNNNNNNSISATNGQYTNSSSKTTSASARDYTYRETISPPTPPSPPTTNVADIVCISDAESEDGRDPEREYYDQDMEEDEPNGIEIDESSSSLSKAKSNNAAAAAAAAAAAAAAAASKASSSTTPSYAMPTSNSTPLDLDNEAHQRDLEAVTDLKYYVKLYSDEAVSLNDFKIIRVLGTGAYGRVFLVRKLTRHDAGKLYAMKVLNKITVVQKRKTAEHTKTERVVLEAIQRNPFLVSLHYAFQSSSKLYLVLDFANGGELFTHLYHSENFEESRVRVYIAEVVLALEQLHQLGIIYRDIKLENILLDGEGHIVLSDFGLSKILTAENEYRAHSFCGTLEYMAPEIIRTGPPGHDSAVDWWSVGVLTFELLTGASPFATSDGQVQQSEISRRIQKEQPMIPSSFSANARDFVLKMLEKNPKRRLGGNHRDASEIKEHPFFNGINWQELRTKRRKAPYKPTLTAEDDVQNFSNEFTDQVPEDPECDAPPSRIRLFRGYTYVAPEHLEQMRRDNHCEIQYFNTGLQNIPCRPDDLELGTRTSNGAYGTCHFVVDSSTDLVFLAKIIPLSKFRPSEVDALISCALDTTNHKNIVSYHGTFREKCETWIVMEYLSGPELTASIRMDEDSCREIFLQLVMAVRHIHSKHFIHGDLKPENIMFENREDRTVKLIDFGSACYNNRFKSWKDKPRYTLDYAPPEMLADANLVTYSPAVDIYGLGATLYTMLVGHRPYRQNEDDVDHSAAAHHELRKRMRRGTFNQRSMRWESASPAFRHLVSWCLQRDPADRPTLSDILDSEWLQYGSNDPDVDIILPQQMVVDLSEDTMEQPTGGMFDDQQQLEFMHDKSAEDEGITLVSEPMDTTVATHESRRNAAAFSSVVAPTTDDEIVHERFDPAFEVQADFYGFDENAPPLPLPEEYYSELPLPEEDRQYIPPPPALIPVEPETTFRRPRTRQQRRTESQLVQPVSVATYEDSKASLRVLMQQLPPPGDNVVARIPKRTHRVVRTLPPTFGTTKREENFYGFSKTAISWRKTRASWRHFCLLINGVQQVLKVRFKKARRVYCLPHIKEEKLDHAYEKPLTFPRPKAQLKRTKREPKVPRPPTRVQPERARAMRQLYQFQ
Protein: alpha-amylase (EC 3.2.1.1) (Q8MM52)
Organism: Drosophila kikkawai (Fruit fly)
Interaction partners:
Sequence:
MFLTKSIVCLAILALASAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAANGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIAEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGRLKNLNTDHGFSSGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKNQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYRMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFNSDNSCSGGWVCEHRWRQIYNMVAFRNAVGSDAIQNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGTKNGSSCTGKTVTVGSDGRASIYLGNSEDDGVLAIHVNAKL
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g74360 (EC 2.7.11.1) (C0LGJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14671022}; Single-pass type I membrane protein {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Cold-regulated 413 plasma membrane protein 3
- Thioredoxin superfamily protein
- Putative E3 ubiquitin-protein ligase XBAT34
- Oxysterol-binding protein-related protein 1C
- AAA-ATPase At5g17760
- Probable calcium-binding protein CML40
- Phosphatidylinositol 4-kinase gamma 4
- Proteasome subunit beta type-3-B
- Tropinone reductase homolog At1g07440
- U-box domain-containing protein 2
Sequence:
MTMVTRVIMTDDDSQSLCFLCFLLFFFITAIAVAGDSLDSDREVLLSLKSYLESRNPQNRGLYTEWKMENQDVVCQWPGIICTPQRSRVTGINLTDSTISGPLFKNFSALTELTYLDLSRNTIEGEIPDDLSRCHNLKHLNLSHNILEGELSLPGLSNLEVLDLSLNRITGDIQSSFPLFCNSLVVANLSTNNFTGRIDDIFNGCRNLKYVDFSSNRFSGEVWTGFGRLVEFSVADNHLSGNISASMFRGNCTLQMLDLSGNAFGGEFPGQVSNCQNLNVLNLWGNKFTGNIPAEIGSISSLKGLYLGNNTFSRDIPETLLNLTNLVFLDLSRNKFGGDIQEIFGRFTQVKYLVLHANSYVGGINSSNILKLPNLSRLDLGYNNFSGQLPTEISQIQSLKFLILAYNNFSGDIPQEYGNMPGLQALDLSFNKLTGSIPASFGKLTSLLWLMLANNSLSGEIPREIGNCTSLLWFNVANNQLSGRFHPELTRMGSNPSPTFEVNRQNKDKIIAGSGECLAMKRWIPAEFPPFNFVYAILTKKSCRSLWDHVLKGYGLFPVCSAGSTVRTLKISAYLQLSGNKFSGEIPASISQMDRLSTLHLGFNEFEGKLPPEIGQLPLAFLNLTRNNFSGEIPQEIGNLKCLQNLDLSFNNFSGNFPTSLNDLNELSKFNISYNPFISGAIPTTGQVATFDKDSFLGNPLLRFPSFFNQSGNNTRKISNQVLGNRPRTLLLIWISLALALAFIACLVVSGIVLMVVKASREAEIDLLDGSKTRHDMTSSSGGSSPWLSGKIKVIRLDKSTFTYADILKATSNFSEERVVGRGGYGTVYRGVLPDGREVAVKKLQREGTEAEKEFRAEMEVLSANAFGDWAHPNLVRLYGWCLDGSEKILVHEYMGGGSLEELITDKTKLQWKKRIDIATDVARGLVFLHHECYPSIVHRDVKASNVLLDKHGNARVTDFGLARLLNVGDSHVSTVIAGTIGYVAPEYGQTWQATTRGDVYSYGVLTMELATGRRAVDGGEECLVEWARRVMTGNMTAKGSPITLSGTKPGNGAEQMTELLKIGVKCTADHPQARPNMKEVLAMLVKISGKAELFNGLSSQGYIEM
Protein: Thyroid transcriptional factor-1 truncated form (O14956)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPHTAAMQQHAVGHPGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPASK