wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphorylase b kinase regulatory subunit alpha, liver isoform (Phosphorylase kinase alpha L subunit) (P46019)
Organism: Homo sapiens (Human)
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
- Phosphorylase b kinase regulatory subunit beta
- Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
- Calmodulin-1
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-like protein 6
Sequence:
MRSRSNSGVRLDGYARLVQQTILCYQNPVTGLLSASHEQKDAWVRDNIYSILAVWGLGMAYRKNADRDEDKAKAYELEQNVVKLMRGLLQCMMRQVAKVEKFKHTQSTKDSLHAKYNTATCGTVVGDDQWGHLQVDATSLFLLFLAQMTASGLRIIFTLDEVAFIQNLVFYIEAAYKVADYGMWERGDKTNQGIPELNASSVGMAKAALEAIDELDLFGAHGGRKSVIHVLPDEVEHCQSILFSMLPRASTSKEIDAGLLSIISFPAFAVEDVNLVNVTKNEIISKLQGRYGCCRFLRDGYKTPREDPNRLHYDPAELKLFENIECEWPVFWTYFIIDGVFSGDAVQVQEYREALEGILIRGKNGIRLVPELYAVPPNKVDEEYKNPHTVDRVPMGKVPHLWGQSLYILSSLLAEGFLAAGEIDPLNRRFSTSVKPDVVVQVTVLAENNHIKDLLRKHGVNVQSIADIHPIQVQPGRILSHIYAKLGRNKNMNLSGRPYRHIGVLGTSKLYVIRNQIFTFTPQFTDQHHFYLALDNEMIVEMLRIELAYLCTCWRMTGRPTLTFPISRTMLTNDGSDIHSAVLSTIRKLEDGYFGGARVKLGNLSEFLTTSFYTYLTFLDPDCDEKLFDNASEGTFSPDSDSDLVGYLEDTCNQESQDELDHYINHLLQSTSLRSYLPPLCKNTEDRHVFSAIHSTRDILSVMAKAKGLEVPFVPMTLPTKVLSAHRKSLNLVDSPQPLLEKVPESDFQWPRDDHGDVDCEKLVEQLKDCSNLQDQADILYILYVIKGPSWDTNLSGQHGVTVQNLLGELYGKAGLNQEWGLIRYISGLLRKKVEVLAEACTDLLSHQKQLTVGLPPEPREKIISAPLPPEELTKLIYEASGQDISIAVLTQEIVVYLAMYVRAQPSLFVEMLRLRIGLIIQVMATELARSLNCSGEEASESLMNLSPFDMKNLLHHILSGKEFGVERSVRPIHSSTSSPTISIHEVGHTGVTKTERSGINRLRSEMKQMTRRFSADEQFFSVGQAASSSAHSSKSARSSTPSSPTGTSSSDSGGHHIGWGERQGQWLRRRRLDGAINRVPVGFYQRVWKILQKCHGLSIDGYVLPSSTTREMTPHEIKFAVHVESVLNRVPQPEYRQLLVEAIMVLTLLSDTEMTSIGGIIHVDQIVQMASQLFLQDQVSIGAMDTLEKDQATGICHFFYDSAPSGAYGTMTYLTRAVASYLQELLPNSGCQMQ
Protein: ribose-phosphate diphosphokinase (EC 2.7.6.1) (Q5ALK3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- ribose-phosphate diphosphokinase
- Amidophosphoribosyltransferase
- Ribose-phosphate pyrophosphokinase 1
- Transketolase
- Ribokinase
- Ribose-5-phosphate isomerase
- Phosphoribomutase
- phosphoglucomutase
- ADP-ribose diphosphatase
- ATP phosphoribosyltransferase
Sequence:
MSTNSIKLLASDVHRGLAELVSKRLGLRLTPSELKRESTGEVQFSIGESVRDEDIFIICQIGSGEVNDRVFELMIMINACKTASARRITVILPNFPYARQDRKDKSRAPITAKLMADMLTTAGCDHVITMDLHASQIQGFFDVPVDNLYAEPSVVRYIKETIDYSEAIIISPDAGGAKRAAGLADRLDLNFALIHKERARANEVSRMVLVGDVTDKICVIVDDMADTCGTLAKAAEVLLDNNAKDVIAIVTHGILSGNAIKNINNSKLKKVVCTNTVPFEDKLKLCPKLDTIDISAVIAESIRRLHNGESISYLFKNAPL
Protein: Mannose-1-phosphate guanyltransferase (EC 2.7.7.13) (GDP-mannose pyrophosphorylase) (GTP-mannose-1-phosphate guanylyltransferase) (Q4U3E8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Mannose-1-phosphate guanyltransferase
- Phosphomannomutase
- GDP-mannose 4,6-dehydratase
- Phosphoglucomutase, putative
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- NUDIX family hydrolase, putative
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Eukaryotic translation initiation factor 2 subunit alpha
- Translational initiation factor 2 beta
Sequence:
MKALILVGGFGTRLRPLTLTLPKPLVEFGNRPMILHQVESLAAAGVTDIVLAVNYRPDVMVAALKKYEEQYNVRIEFSVESEPLGTAGPLKLAEKILGKDDSPFFVLNSDIICDYPFKQLAEFHKKHGDEGTIVVTKVDEPSKYGVVVHKPNHPSRIDRFVEKPVEFVGNRINAGIYILNPSVLKRIELRPTSIEQETFPAICSDGQLHSFDLEGFWMDVGQPKDFLTGTCLYLTSLAKRNSKLLAPNSEPYVYGGNVMVDPSAKIGKNCRIGPNVVIGPNVVVGDGVRLQRCVLLENSKVKDHAWIKSTIVGWNSSVGKWARLENVTVLGDDVTIADEVYVNGGSILPHKSIKQNIDVPAIIM
Protein: EF-hand domain-containing protein (Q580J5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Serine/threonine-protein phosphatase
- Serine/threonine protein phosphatase 2a regulatory subunit, putative
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
- EF-hand domain-containing protein
Sequence:
MLALSQGLPTVDPALVKAFKRAANNASTSGDVDDDSRRQEVARINKEAQKAWRAEEKSFIPAIYLRTRDPSAEDVLQHLRVTSKAFELNLRFRDIEQLDEMQVKLWSLLTADKSKQTVTISEFTEIMNKLKVWQGQRFEPTPKTSPCREISVRSAQQECPVDTTPLDEVMYVGVAKRPRPSLQLFLSCPRSHAGGVEVAHIYQRFAKQVSLVKCEAELLMWDTNNDGRLTEDELESYVRDLVSRVDALRDISNDILPFYCCAVSRRIFWALDPGMRGTIRIDALLQSPLMDEWVSLQLMREDLPRNWFSAAITSHLYDKFLLLDTRNQGTLNAANMKLYKKGLPTVRDDGLPRGVGPLSSLFIDRFFETSVMMACSELDFRKFVDFVIAVEFLPACQRPLFFWNILDIEGCGVLRPVHVNSFFRETHSKLVEAGLEMPSRETVVQEVFDLIPTAEPLRITREEFVKAPQAGLFVALLIDCLSFWAYENREQR
Protein: Naphthalene 1,2-dioxygenase system, small oxygenase component (Naphthalene 1,2-dioxygenase ISP beta) (Naphthalene 1,2-dioxygenase subunit beta) (ND subunit beta) (NDO subunit beta) (P0A112)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The beta subunit seems to have a structural role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene.
Interaction partners:
Sequence:
MMINIQEDKLVSAHDAEEILRFFNCHDSALQQEATTLLTQEAHLLDIQAYRAWLEHCVGSEVQYQVISRELRAASERRYKLNEAMNVYNENFQQLKVRVEHQLDPQNWGNSPKLRFTRFITNVQAAMDVNDKELLHIRSNVILHRARRGNQVDVFYAAREDKWKRGEGGVRKLVQRFVDYPERILQTHNLMVFL
Protein: Glycine cleavage system H protein, mitochondrial (Lipoic acid-containing protein) (P20821)
Organism: Bos taurus (Bovine)
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:2211640, ECO:0000269|PubMed:2553401, ECO:0000269|PubMed:3080335}.
Interaction partners:
- Glycine cleavage system P protein
- Aminomethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Dihydrolipoyl dehydrogenase, mitochondrial
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
- Lipoyl synthase, mitochondrial
- Alanine--glyoxylate aminotransferase
- Lipoyl amidotransferase LIPT1, mitochondrial
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Sequence:
MALRAVRSVRAAVGGLRAISAPSAPCLPRPWGLRAGAVRELRTGPALLSVRKFTEKHEWVTTENGVGTVGISNFAQEALGDVVYCSLPEVGTKLNKQEEFGALESVKAASELYSPLSGEVTEINKALAENPGLVNKSCYEDGWLIKMTFSNPSELDELMSEEAYEKYIKSIEE
Protein: Calcipressin-1 (Down syndrome critical region protein 1 homolog) (Myocyte-enriched calcineurin-interacting protein 1) (MCIP1) (Regulator of calcineurin 1) (Q6IN33)
Organism: Rattus norvegicus (Rat)
Function: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development.
Interaction partners:
- Protein phosphatase 3 catalytic subunit alpha
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
- Nuclear factor of activated T-cells 5
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Serine/threonine-protein phosphatase
Sequence:
MHFRDFNYNFSSLIACVANGDVFSESETRAKFESLFRTYDKDITFQYFKSFKRVRINFSNPLSAADARLQLHKTEFLGKEMKLYFAQTLHIGSSHLAPPNPDKQFLISPPASPPVGWKQVEDATPVINYDLLYAISKLGPGEKYELHAATDTTPSVVVHVCESDQEEEEEEEEEMERMKRPKPKIIQTRRPEYTPIHLS
Protein: LD10183p (Q8T0D1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE17222p
- AT19250p
- RT10616p
Sequence:
MNVCRLCLSKEPNFPVFGANGSTALQIMVCTSLEIEPGDGLPQHICTMCRLQLEEMHCFRRRCLAADRKLRRHKALQRQGVKSQLSEVEEERGSGEGCTQTGCAENNAQWRQQAAQLISSEIDAYKKELLSTCKQAVRAEIELELRAELEEVIIPEAKQQLRLSVLDDVFVELERYFVRKRNEATYEMKMNLSSPLPDEQTAGFYETDMGQELREQSDNSVVELLDDEPEASRQPAATPLVAVPMVEINMNDPQLSHLRNDYSKDTFLGANTTALEDVKTPSPCRKKVRFMSPKQTTDNLCRKHSSFKTKCSSSYADFKSCVRCRLRGADKLNNTVT
Protein: Trinucleotide repeat-containing gene 6B protein (Q9UPQ9)
Organism: Homo sapiens (Human)
Function: Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent translational repression and siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins. As scaffolding protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:19167051}. Note=Mammalian P-bodies are also known as GW bodies (GWBs). {ECO:0000269|PubMed:16289642}.
Interaction partners:
- Protein argonaute-2
- Protein argonaute-1
- Helicase MOV-10
- Protein argonaute-3
- Protein argonaute-4
- Endoribonuclease Dicer
- Trinucleotide repeat-containing gene 6A protein
- CCR4-NOT transcription complex subunit 7
- GRB10-interacting GYF protein 2
- Polyhomeotic-like protein 3
Sequence:
MREKEQEREEQLMEDKKRKKEDKKKKEATQKVTEQKTKVPEVTKPSLSQPTAASPIGSSPSPPVNGGNNAKRVAVPNGQPPSAARYMPREVPPRFRCQQDHKVLLKRGQPPPPSCMLLGGGAGPPPCTAPGANPNNAQVTGALLQSESGTAPDSTLGGAAASNYANSTWGSGASSNNGTSPNPIHIWDKVIVDGSDMEEWPCIASKDTESSSENTTDNNSASNPGSEKSTLPGSTTSNKGKGSQCQSASSGNECNLGVWKSDPKAKSVQSSNSTTENNNGLGNWRNVSGQDRIGPGSGFSNFNPNSNPSAWPALVQEGTSRKGALETDNSNSSAQVSTVGQTSREQQSKMENAGVNFVVSGREQAQIHNTDGPKNGNTNSLNLSSPNPMENKGMPFGMGLGNTSRSTDAPSQSTGDRKTGSVGSWGAARGPSGTDTVSGQSNSGNNGNNGKEREDSWKGASVQKSTGSKNDSWDNNNRSTGGSWNFGPQDSNDNKWGEGNKMTSGVSQGEWKQPTGSDELKIGEWSGPNQPNSSTGAWDNQKGHPLPENQGNAQAPCWGRSSSSTGSEVGGQSTGSNHKAGSSDSHNSGRRSYRPTHPDCQAVLQTLLSRTDLDPRVLSNTGWGQTQIKQDTVWDIEEVPRPEGKSDKGTEGWESAATQTKNSGGWGDAPSQSNQMKSGWGELSASTEWKDPKNTGGWNDYKNNNSSNWGGGRPDEKTPSSWNENPSKDQGWGGGRQPNQGWSSGKNGWGEEVDQTKNSNWESSASKPVSGWGEGGQNEIGTWGNGGNASLASKGGWEDCKRSPAWNETGRQPNSWNKQHQQQQPPQQPPPPQPEASGSWGGPPPPPPGNVRPSNSSWSSGPQPATPKDEEPSGWEEPSPQSISRKMDIDDGTSAWGDPNSYNYKNVNLWDKNSQGGPAPREPNLPTPMTSKSASVWSKSTPPAPDNGTSAWGEPNESSPGWGEMDDTGASTTGWGNTPANAPNAMKPNSKSMQDGWGESDGPVTGARHPSWEEEEDGGVWNTTGSQGSASSHNSASWGQGGKKQMKCSLKGGNNDSWMNPLAKQFSNMGLLSQTEDNPSSKMDLSVGSLSDKKFDVDKRAMNLGDFNDIMRKDRSGFRPPNSKDMGTTDSGPYFEKLTLPFSNQDGCLGDEAPCSPFSPSPSYKLSPSGSTLPNVSLGAIGTGLNPQNFAARQGGSHGLFGNSTAQSRGLHTPVQPLNSSPSLRAQVPPQFISPQVSASMLKQFPNSGLSPGLFNVGPQLSPQQIAMLSQLPQIPQFQLACQLLLQQQQQQQLLQNQRKISQAVRQQQEQQLARMVSALQQQQQQQQRQPGMKHSPSHPVGPKPHLDNMVPNALNVGLPDLQTKGPIPGYGSGFSSGGMDYGMVGGKEAGTESRFKQWTSMMEGLPSVATQEANMHKNGAIVAPGKTRGGSPYNQFDIIPGDTLGGHTGPAGDSWLPAKSPPTNKIGSKSSNASWPPEFQPGVPWKGIQNIDPESDPYVTPGSVLGGTATSPIVDTDHQLLRDNTTGSNSSLNTSLPSPGAWPYSASDNSFTNVHSTSAKFPDYKSTWSPDPIGHNPTHLSNKMWKNHISSRNTTPLPRPPPGLTNPKPSSPWSSTAPRSVRGWGTQDSRLASASTWSDGGSVRPSYWLVLHNLTPQIDGSTLRTICMQHGPLLTFHLNLTQGTALIRYSTKQEAAKAQTALHMCVLGNTTILAEFATDDEVSRFLAQAQPPTPAATPSAPAAGWQSLETGQNQSDPVGPALNLFGGSTGLGQWSSSAGGSSGADLAGASLWGPPNYSSSLWGVPTVEDPHRMGSPAPLLPGDLLGGGSDSI
Protein: Protein SEEDLING LETHAL 1, chloroplastic (Mitochondrial transcription termination factor 3) (mTERF 3) (Protein EMBRYO DEFECTIVE 3114) (Transcription termination factor mTERF3) (Q9SJ50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:23087700, ECO:0000269|PubMed:30059532, ECO:0000269|PubMed:33391315}. Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:33391315}.
Interaction partners:
- Mitochondrial transcription termination factor family protein
- FYD
- THO complex subunit 4A
- AT3g62190/T17J13_150
- Mitochondrial transcription termination factor family protein
- Serine/threonine-protein kinase AFC2
- Mitochondrial transcription termination factor family protein
Sequence:
MQQEALSFLSSSLPSLHHNFPSLSRLRFNNFPALSFKPNTSSSSSSFFKSPDIPSLSSTTTTTTTTETLESSIHEKLIYLDSLGIDFLTLINRHPPLLSTALSAVESVVDYMTTPPINFTLQDFRRLVSMCPELLTSPLTSHTIPVITFLLREVGVDSIFDLRQALRRRPRLLACSVDHQLRPTLYFLQRIGILDPHKHTYLLSCSVDNKLVPRIDYFEKLGFSRRSATAMFKRFPQLFNYSIAENYEPKLKYLMVEMGRDVREVLEFPQYFSFSLENRIKPRHEACAAKGVRFPLPVMLKTNEAGFRDTLEVCCDSSPPLKTSRLVTVQKDS
Protein: Calcium-dependent protein kinase 2 (EC 2.7.11.1) (Calmodulin-domain protein kinase CDPK isoform 2) (Q38870)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11891256}; Lipid-anchor {ECO:0000269|PubMed:11891256}.
Interaction partners:
- Respiratory burst oxidase homolog protein D
- S-type anion channel SLAH3
- Respiratory burst oxidase homolog protein B
- Respiratory burst oxidase homolog protein F
- Respiratory burst oxidase homolog protein C
Sequence:
MGNACVGPNISGNGFLQTVTAAMWRPRIGAEQASSSSHGNGQVSKEAASEPATDQVQNKPPEPITMPSSKTNPETKLKPDLEIQPEEKKEKVLAEETKQKVVPEESKQEVPPEESKREVVVQPESAKPETKSESKPETTKPETTSETKPETKAEPQKPKHMRRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCLEKGTGNEYACKSISKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMELCSGGELFDRIIQRGHYTERKAAELARTIVGVLEACHSLGVMHRDLKPENFLFVSREEDSLLKTIDFGLSMFFKPDEVFTDVVGSPYYVAPEVLRKRYGPESDVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDLVRKMLVRDPKRRLTAHQVLCHPWVQIDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVIAESLSEEEIAGLKQMFKMIDADNSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNSGTIDYKEFIAATLHLNKIEREDHLFAAFSYFDKDESGFITPDELQQACEEFGVEDARIEEMMRDVDQDKDGRIDYNEFVAMMQKGSIMGGPVKMGLENSISISLKH
Protein: Nucleolar complex-associated protein 3 (O94288)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Ribosome biogenesis protein erb1
- Uncharacterized NOC2 family protein C1142.04
- Probable nucleolar GTP-binding protein 1
- Protein mak16
- Pescadillo homolog
- Ribosome biogenesis protein ytm1
- Ribosome biogenesis protein brx1
- AdoMet-dependent rRNA methyltransferase spb1
- Uncharacterized RNA-binding protein C1827.05c
- GTPase grn1
Sequence:
MAARKNQKSPKPKVASSKLKNIKKSSKRNNSQSSTEPRKNATSLDSKKTTKKGVALPEIAERELTQEDIEFFNENPSSLKYLSSINPEDLGKKVEKGPRPDIYDLKKSQQFELDTSRLSSDEESVLDYSKDSEDEQDYELRPRVSSSWNNESYNRLPIKTKDGLLQNVVADVNNGEEFLSESESEASLEIDSDIKDEKQKSLEEQKIAPEIPVKQQIKNDKEALGIQAQQLLEEPVENLHLIRNIFEKFDSPYITIKKLSLLTLLAVFRDIIPGYKIRPLSEEEQGTKLSKEVAQRWEYEQTLLKHYAKFLQTLETILKSFSSTLDETQLSLYQVAVRCCTKLIEQASHFNLSEKLFALAVRQISHKTKRPGFDGIINSLKNIFEEDNLGKTSLKCVTILSRMFKQRNYDVLPDVYDLFLSVNILNDMKIKDEAWQDDTTNFKKRKKDLPYLTKKARKNYKETKKITQEMKEADAVITAQDKEKYQSEILKIIFITYFKTLQLKGKLIGNALEGVARLSHLLNIEFLGDLLQVLRELVMDDTVFLPKDKSGVQATREALLTVSTAFEIASAQGVGKLNLDLDLGLFVQRLYKIIFPFSLNPDADLNLKIKRLKDPDAPSKPFVVNATTEMEMLLKCFQVFFFKSKNISSSRLSSFSKRLAIASMQLPEHSASADLALLKKLLSRYSKLSRLLTSEEQIGDGIYNPFIEDPDLSNSSTAVLYEPFLLKNHYSPAVSQSAKELLKSTSL
Protein: sn-1-specific diacylglycerol lipase (EC 3.1.1.116) (X2JDP4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPGLVVFRRRWSVGSDDLVVPGAFLLTIHFICFVIVSVSLVIFEYNTRILSVKLLFYHLIGYLLILFFSICVEIGICVISMRGSILDAEARTSINIWIYLKSLVILFDIAWLAVGSVWLGHYYTTAPIDDPKKVYIAIIICNWALVVITLITIWCTFDAAGRSWVKMKKYQRSMRETESRFNYKRSNSMNRNWRQRKVMRAYQDSWDHRCRLLFCCMGSSERNRNSFTDIARLLSDFFRELDVVPSDVVAGLVLLRKFQRLEREAIVRQRKNGTYEFLSGVPITERTQFLALNDAKNYDFFQTVIHYMYFAQGAYGWPMYVIINRSKMWHLVPELKCFGCCCGTSDDTEVIQDNCCLCNYAALKKTLQLGDIDIVYATYHVDVGETPFFVAIDYTHRAVVISIRGTLSMKDILTDLNAEGEVLPLQPPRDDWLGHKGMVQAAIYIRNKLQEENLIERALQRNPDRQTHTFDLVLVGHSLGAGTAAILAILLKPEHPTLQCFSYSPPGGLLSMPAVEYSKSFITSVVLGKDVVPRIGLNQMEALRADLINAIQRSVDPKWKTISCSVICCGCGPEPTSVVNMSGQDTHINQYQEERGTARSTSAHPTDSSIALTLHQPLYPPGRIIHIVRHHPKPDENVLKNREPVYQAIWADSTDFDEVLISPVMLQDHMPDKVLAALKKVVSCRDRTVKACTTRRRNDNTTITTTTTVTTTTTTTQNTDTRYSRPPSI
Protein: DNA helicase (Q8T145)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA 3'-5' helicase
- RecQ-like DNA helicase BLM
- DNA excision repair protein ERCC-1
- ATP-dependent DNA helicase
- Probable crossover junction endonuclease mus81
- Replication protein A subunit
- RING-type domain-containing protein
- DNA polymerase zeta catalytic subunit
- Nuclear protein localization protein 4 homolog
- DNA topoisomerase 3
Sequence:
MGDKYLNSKKNSSGFSFLNKPVNDNPFVRNESANPFGNGAINQSPLNPFKKASPFKQQQPQPIQRQQQQQQQQQQQQQQPQQQQQQQPFQPFQYQSPKKIQNPNVPISLPQPINNNSTTTTTTSNTPYKSPQTIQQQQQQQQQNVNNIKNTSPYRQQTEQQQSVYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNPIEIELDDFELSFSDDILNKNSGESSSAPKDMEVDSSNSSSSGTTNVNNNSSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKPIIIEDMDFDIDFEFDIDTNVEITGSSNVINSTAAKTSTTTTTTTTTASTTIPSATSILKNSTTSNTSTTTTATTKPPIINLDTISPPLQQQQKLNVTLPILKTPQINKPLQPSLPTKPPIKNNTTLPTTNKSPTTTTTTTKFIDKFKGMKRYTKDLPEGFEISSENQEPYRNEKMIGEFLYPEDNIREYQFKFIQSAFLENTMICLPTGLGKTFIASILMLNYYHWFPKSKLVFLVHTKSLVSQQIEAFHRDTGIPKSDSIQFTGDTTSKLKRQSLWNSKRVFFSTPQILANDIGSGNCDPRSICCIVIDEAHRAQGNYDYCVAIKLILKVNRFFRVLALTATPGSNNAAIQKVINNLLISNMELRSEDSADIKPYIHSKKTDVLSIALSDDYKSIIKDYEFFIVDKLKVLFEFNILNPTTTPDRVSHSFILEKIKSIQFSNSPVYGSGGNKFKLLRALVTLQTLYQGYALLKVHGLESFYDKISNLEDASSKTIKAFSKNENWKQFIIKIKKSIDNGLVHDKLIKLNDVLIEHFQSNNPRSSKVMIFVQFRRSVQEIIDFISNNNNGGGGGGKSLIKVMPFYGQSATDKGVKGIHKKEQQAILNSFVNGDINVLVSTCIGEEGLDIGEVDLVVCYDVQQSSLKNTQRTGRTGRKRDGRCIFLITQGYEEYIYEKSQSNLDSLSNLKESSFVFHYSPKMIDSIPLVKYIKINENNIYSNDDNDIELNDGGGDYYEDDDSLFENNKKSTTSRGVKNSKNYLADDQIRYMQLNHNVVNHKTNFNYKEILSKNSHLNSISTDIEDIKHSDKTNILISISKSIDAIKYSSDYTDLSKMPDIVKKVVSEMPLDNNDNDNDGIGLAYDDSPRDYGYDRYEPFTTSTTTTAIGTSIPTTATTSTTINSTSYSTSTSTSTNTNTKTTLPSTSTINKISPPPQQKQPIISTSSINQSMKTNPIIISNNTVLSNLNNSLGNNFIPFVRKVKQPEHKKVYEIPNLPPDEELIFDFSKILLRENNENEKIITTNDYINTQNQPQPQQPTPTPTPPPPSTPNLTPIKKTISPTPTPTPQISKPFPLSPTPPTPTPPPPIVSNPLPSFQQKQQQQQQQIYISPTPTPPPPQISKPLPLSPVSKPLPLSPVSKPISIQLTPIQPPQKTTPTTPDLTPVKRRKPKNLFDKFDDNDEGDDAVIFENNNLNNIINLKNNNNNNNNNNNNNNNNNNNNNNNNNNNTIVLEKVDKKSIFNLDDIDNNLFTFGLTQQQTQQQFQKKNRDRYRFGDRDKNIDSYGNDKFFEDSEAEEDSEIERRNSQDDDDDDDEEEDGIGENKYDLHDSFINDGDESAENSLSSQSTTPTKKKKKNKRKRKSNNFIYAQSLLSQNSLGFNGGSKRKGGLLSVIEKFEKIGQHEEEFIDENDYTGSEDYDDENENENDYESGSDSIEEIDKSINSSEEKRQKKYHHHNNNNNNPKLSSIHSKPIIDSPKSNNSNNNNSNSKNRKDFSNHDLFSL
Protein: Alpha-aminoadipate reductase (EC 1.2.1.31) (EC 1.2.1.95) (L-aminoadipate-semialdehyde dehydrogenase) (B0Y6V5)
Organism: Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata)
Interaction partners:
Sequence:
MGVETASLQDRLERWAQRLQNLTVSPLTRDYPENQKADLKRAIEAFESLKLPRDVHTGLQKLSGPSSGFITFLAAFVVLVARLTGDEDIAVATSSAEDGRPFVLRVSIDQSETFQQLYSKVENAFNQGAADIVPLGSLRSYIQEKTKSERAPILFRFAAYDAPASSQEYPANTFETTDLVVNVANANGSTSETELGAYYNQRLFSSARIAIILKQLAQIVQNASNNPGEAIGRIDFMTDDQRSLLPDPTSDLHWSNFRGAIHDIFAQNAEKHPDKLCVVETKSEQSPHREFTYRQINEASNILGHHLVRAGIERGDVVMVYAYRGVDLVVAVMGILKAGATFSVIDPAYPPERQCIYLDVARPRALINIAKATKEAGELTQLVRSFIDENLELRTEIPALALQDDGTLVGGSVEGQDVLANQVSLKSTPVGVVVGPDSTPTLSFTSGSEGRPKGVRGRHFSLAYYFPWMSETFKLTPNDRFTMLSGIAHDPIQRDIFTPLFLGAQLLVPAREDIQNEKLAEWMREYSATVTHLTPAMGQILVGGASAQFPALHHAFFVGDILIKRDCRSLQALAPNVNIVNMYGTTETQRAVSYYEIPSYSSQEGFLDTMKDVIPAGRGMVDVQMLVVNRFDPSRICAIGEVGEIYVRAGGLAEGYLSNEELNKKKFLTNWFVDPQKWVEKDKAESQGGNEPWRQFYVGPRDRLYRSGDLGRYTPSGDVECSGRADDQVKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKFEEPTLVSYFVPDMNKWPAWLASKGLKDDDSAEGMVGMLRRFRPLRDDAREHLRSKLPAYAVPTVFIPLKRMPLNPNGKIDKPALPFPDTAELSAAAPRRRSSVLQTLSETEQALAQIWANRISNVTARMIGPDDSFFDLGGHSILAQQMFFDLRRRWRGIDISMNAIFRSPTLRGFAAEIDRLVNFESFASNANEADATADTLATSNEADDEYSKDARKLVETLPRSFPERTEDMLVGEPTVFLTGATGFLGAHILRDLLTRKSPMARVVALVRAKSDEQALDRIRSTCRAYGFWDESWTSRLQCVCGDLGKPRFGLSEALWNDLTERVDAVIHNGALVHWVYPYSTLKPANVLGTIDALKLCASGKPKQFSFVSSTSVLDNDHYVLESERIIAAGGAGISEDDDLEGSSVGLGTGYGQSKWAGEYLVREAGRRGLKGTIVRPGYVLGDSKTGTTNTDDFLIRMMKGCIQLSARPNIHNTVNMVPVDHVARVVIAGAFQPPCTPIGVAQVTGHPRLRFNQFLGALQTYGYDVPQVDYVPWKMSLEHYVNDGKHDDPESQHALMPLYHFVTADLPSNTKAPELDDVHAAASLRADAAWSGIDASAGAGVTEELVGLYASYLVTIGFLPPPSVSTIGVRPLPKVQLSEDQKKALANVGGRGGTS
Protein: unspecific monooxygenase (EC 1.14.14.1) (S5RV20)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Microsome membrane {ECO:0000256|ARBA:ARBA00004524}.
Interaction partners:
Sequence:
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV
Protein: Stress protein DDR48 (DNA damage-responsive protein 48) (DDRP 48) (Q59X49)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cell surface protein involved in the ability to sense and respond to changes in the host environment. Required for stress response and confers partial antifungal drug resistance. Contributes to the DNA damage response. Required for the flocculation response stimulated by 3-aminotriazole-induced amino acid starvation.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:20167299}.
Interaction partners:
- Cell surface Cu-only superoxide dismutase 5
Sequence:
MVFGFGKDDDKDKNDRRDNDSYGSSNRRNNDDSYGSSSFGSSNDDDNSYGSSNKRSNDSYGSSNTDSYGSSNRRDNDSYGSSNNDSYGSSKTDSYGSSNRSGNDSYGSSNNDSYGSSNRKGNDSYGSSNTDSYGSSNTDSYGSSNTDSYGSSNKRGNDSYGSSNDDSYGSSNDDSYGSSNRRGNDSYGSSNDDSYGSSNRRGNSDSYGSSDY
Protein: DNA-binding protein SATB2 (Special AT-rich sequence-binding protein 2) (Q8VI24)
Organism: Mus musculus (Mouse)
Function: Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating Bcl11b expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation.
Subcellular location: Nucleus matrix {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374}.
Interaction partners:
- T-box brain protein 1
- Runt-related transcription factor 2
- B-cell lymphoma/leukemia 11B
- Homeobox protein cut-like 1
- Fez family zinc finger protein 2
- Neurogenic differentiation factor 6
- Histone deacetylase 1
- Paired box protein Pax-6
- Homeobox protein cut-like 2
- Forkhead box protein G1
Sequence:
MERRSESPCLRDSPDRRSGSPDVKGPPPVKVARLEQNGSPMGARGRPNGAVAKAVGGLMIPVFCVVEQLDGSLEYDNREEHAEFVLVRKDVLFSQLVETALLALGYSHSSAAQAQGIIKLGRWNPLPLSYVTDAPDATVADMLQDVYHVVTLKIQLQSCSKLEDLPAEQWNHATVRNALKELLKEMNQSTLAKECPLSQSMISSIVNSTYYANVSATKCQEFGRWYKKYKKIKVERVERENLSDYCVLGQRPMHLPNMNQLASLGKTNEQSPHSQIHHSTPIRNQVPALQPIMSPGLLSPQLSPQLVRQQIAMAHLINQQIAVSRLLAHQHPQAINQQFLNHPPIPRAVKPEPTNSSVEVSPDIYQQVRDELKRASVSQAVFARVAFNRTQGLLSEILRKEEDPRTASQSLLVNLRAMQNFLNLPEVERDRIYQDERERSMNPNVSMVSSASSSPSSSRTPQAKTSTPTTDLPIKVDGANVNITAAIYDEIQQEMKRAKVSQALFAKVAANKSQGWLCELLRWKENPSPENRTLWENLCTIRRFLNLPQHERDVIYEEESRHHHSERMQHVVQLPPEPVQVLHRQQSQPTKESSPPREEAPPPPPPTEDSCAKKPRSRTKISLEALGILQSFIHDVGLYPDQEAIHTLSAQLDLPKHTIIKFFQNQRYHVKHHGKLKEHLGSAVDVAEYKDEELLTESEENDSEEGSEEMYKVEAEEENADKSKAAPAETDQR