wanglab/gogpt-training-data huggingface dataset:
Protein: Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase) (B9E972)
Organism: Macrococcus caseolyticus (strain JCSC5402) (Macrococcoides caseolyticum)
Function: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate. Cannot catalyze the reverse reaction. Is not active with saturated fatty acids and trans-, cis-5-, cis-6-, cis-8-, cis-11-, cis-13-, cis-14-, and cis-15-double bond unsaturated fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of unsaturated fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy fatty acids. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments.
Interaction partners:
- HTH tetR-type domain-containing protein
Sequence:
MYYSNGNYEAFARPKKPEGVDNKSAYLVGSGLASLAAASFLIRDGQMKGENIHILEELDLPGGSLDGILNPERGYIMRGGREMENHFECLWDLFRSVPSLEVEDASVLDEFYWLNKEDPNYSKCRVIENRGQRLESDGKMTLTKKANKEIIQLCLMKEEQLNDVKISDVFSKDFLDSNFWIYWKTMFAFEPWHSAMEMRRYLMRFIHHIGGLADFSALKFTKFNQFESLVMPLIEHLKAKNVTFEYGVTVKNIQVECSKESKVAKAIDIVRRGNEESIPLTENDLVFVTNGSITESTTYGDNDTPAPPTSKPGGAWQLWENLSTQCEEFGNPAKFYKDLPEKSWFVSATATTNNKEVIDYIQKICKRDPLSGRTVTGGIVTVDDSNWQLSFTLNRQQQFKNQPDDQVSVWIYALYSDERGERTNKTIVECSGKEICEEWLYHMGVPEEKISALAAECNTIPSYMPYITAYFMPRKEGDRPLVVPHGSKNIAFIGNFAETERDTVFTTEYSVRTAMEAVYKLLEVDRGVPEVFASVYDVRILLHALSVLNDGKKLDEIDMPFYERLVEKRLLKKASGTFIEELLEEANLI
Protein: Nuclear receptor-binding factor 2 (NRBF-2) (Comodulator of PPAR and RXR) (Q96F24)
Organism: Homo sapiens (Human)
Function: May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasm {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasmic vesicle {ECO:0000269|PubMed:25086043}. Cytoplasmic vesicle, autophagosome {ECO:0000305}.
Interaction partners:
- Beclin-1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Serine/threonine-protein kinase ULK1
- Beclin 1-associated autophagy-related key regulator
- RB1-inducible coiled-coil protein 1
- Phosphoinositide 3-kinase regulatory subunit 4
- Autophagy-related protein 101
- UV radiation resistance-associated gene protein
- Serine/threonine-protein kinase ULK2
- Beclin-2
Sequence:
MEVMEGPLNLAHQQSRRADRLLAAGKYEEAISCHKKAAAYLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAQREERLKAQQNTDKDAAAHLQTSHKPSAEDAEGQSPLSQKYSPSTEKCLPEIQGIFDRDPDTLLYLLQQKSEPAEPCIGSKAPKDDKTIIEEQATKIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGPIEKELDVDADFVETSELWSLPPHAETATASSTWQKFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGFMNN
Protein: Neuronal acetylcholine receptor subunit alpha-7 (nAChR7) (Nicotinic acetylcholine receptor subunit alpha-7) (Q866A2)
Organism: Macaca mulatta (Rhesus macaque)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q05941}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P36544}; Multi-pass membrane protein {ECO:0000255}. Note=TMEM35A/NACHO promotes its trafficking to the cell membrane (By similarity). RIC3 promotes its trafficking to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P36544, ECO:0000250|UniProtKB:Q05941}.
Interaction partners:
- Secreted LY6/PLAUR domain containing 1
- Glutamate receptor
- Glutamate receptor
- Tyrosine-protein kinase
- P2X purinoceptor
- Glutamate receptor
- Glutamate receptor
- P2X purinoceptor
- P2X purinoceptor
- P2X purinoceptor
Sequence:
MRCSQGGVWLALAASLLHVSLQGEFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPSGEWDLVGIPGKRSEKFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFRGLDGMHCAPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA
Protein: Leucine-rich repeats and immunoglobulin-like domains protein 3 (LIG-3) (Q6P1C6)
Organism: Mus musculus (Mouse)
Function: Plays a role in craniofacial and inner ear morphogenesis during embryonic development. Acts within the otic vesicle epithelium to control formation of the lateral semicircular canal in the inner ear, possibly by restricting the expression of NTN1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20126551}; Single-pass type I membrane protein {ECO:0000269|PubMed:20126551}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:20126551}; Single-pass type I membrane protein {ECO:0000269|PubMed:20126551}. Note=Detected in cytoplasmic vesicles when coexpressed with ERBB4.
Interaction partners:
Sequence:
MGAPGLRAATAALGLLLCAGLGRAGPAGSGGHGAPGQLLDDDAQRPCPAACHCLGDLLDCSRRRLVRLPDPLPAWVTRLDLSHNRLSFIQTSSLSHLQSLQEVKLNNNELETIPNLGSISANIRQLSLAGNAIDKILPEQLEAFQSLETLDLSNNNISELRTAFPPLQLKYLYINNNRVSSMEPGYFDNLASTLLVLKLNRNRISAIPPKMFKLPQLQHLELNRNKIKNVDGLTFQGLGALKSLKMQRNGVTKLMDGAFWGLSNMEVLQLDHNNLTEITKGWLYGLLMLRELHLSQNAINRISPDAWEFCQKLSELDLTFNHLSRLDDSSFLGLSLLNALHIGNNKVSYIADCAFRGLTSLKTLDLRNNEISWTIEDMSGAFSGLDRLRQLILQGNRIRSITKKAFAGLDTLEHLDLSGNAIMSLQSNAFSQMKKLQQLHLNTSSLLCDCQLRWLPQWVAENNFQSFVNASCAHPQLLKGRSIFTVSPDGFVCDDFPKPQITVQPETQSAIKGSDVSFTCSAASSSDSPMTFAWKKDNEALQDAEMENYAHLRAQGGELMEYTTILRLRNVEFTSEGKYQCVISNHFGSSYSVKAKLTINMLPSFTKTPMDLTIRAGAMARLECAAVGHPAPQIAWQKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDIGVYSCTAQNSAGSVSANATLTVLETPSFLRPLLDRTVTKGETAVLQCIAGGSPPPRLNWTKDDSPLVVTERHFFAAGNQLLIIVDSDVSDAGKYTCEMSNTLGTERGNVRLSVIPTPTCDSPHMTAPSLDGDGWATVGVVIIAVVCCVVGTSLVWVVIIYHTRRRNEDCSITNTDETNLPADIPSYLSSQGTLADRQDGYISSESGSHHQFVTSSGGGFFLPQHDGAGTCHFDDSSEADVEAASDPFLCPFVGSTGPVYLQGNLYSPDPFEVYLPGCSSDPRTALMDHCESSYVKQDRFSCARPSEEPCERSLKSIPWPHSRKLTDSTYPPNEGHTVQTLCLNKSSVDFSTGPEPGSATSSNSFMGTFGKPLRRPHLDAFSSSAQPPDCQPRPCHGKSLSSPELDSESEENDKERTDFREENHRCTYQQIFHTYRTPDCQPCDSDT
Protein: Repressor of RNA polymerase III transcription MAF1 homolog (Q9H063)
Organism: Homo sapiens (Human)
Function: Plays a role in the repression of RNA polymerase III-mediated transcription in response to changing nutritional, environmental and cellular stress conditions to balance the production of highly abundant tRNAs, 5S rRNA, and other small non-coding RNAs with cell growth and maintenance. Also plays a key role in cell fate determination by promoting mesorderm induction and adipocyte differentiation (By similarity). Mechanistically, associates with the RNA polymerase III clamp and thereby impairs its recruitment to the complex made of the promoter DNA, TBP and the initiation factor TFIIIB. When nutrients are available and mTOR kinase is active, MAF1 is hyperphosphorylated and RNA polymerase III is engaged in transcription. Stress-induced MAF1 dephosphorylation results in nuclear localization, increased targeting of gene-bound RNA polymerase III and a decrease in the transcriptional readout. Additionally, may also regulate RNA polymerase I and RNA polymerase II-dependent transcription through its ability to regulate expression of the central initiation factor TBP.
Subcellular location: Nucleus {ECO:0000269|PubMed:17505538, ECO:0000269|PubMed:20233713}. Cytoplasm {ECO:0000269|PubMed:20233713}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC1
- Transcription factor TFIIIB component B'' homolog
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC4
- DNA polymerase iota
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MKLLENSSFEAINSQLTVETGDAHIIGRIESYSCKMAGDDKHMFKQFCQEGQPHVLEALSPPQTSGLSPSRLSKSQGGEEEGPLSDKCSRKTLFYLIATLNESFRPDYDFSTARSHEFSREPSLSWVVNAVNCSLFSAVREDFKDLKPQLWNAVDEEICLAECDIYSYNPDLDSDPFGEDGSLWSFNYFFYNKRLKRIVFFSCRSISGSTYTPSEAGNELDMELGEEEVEEESRSGGSGAEETSTMEEDRVPVICI
Protein: RIM-binding protein, isoform F (A0A0B4JDC9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Rab3 interacting molecule, isoform F
- Voltage-dependent calcium channel type A subunit alpha-1
- JNK-interacting protein 1
- Liprin-alpha, isoform E
- Unc-13, isoform E
- GH02075p
- Bruchpilot, isoform J
- Ras-related protein Rab-3
- Fife, isoform D
Sequence:
MHLCEFPSANVEEENRRPEKAAAAASKKQKHKQQKSRPRGSHSMPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPVNIHTMKAMPTALSQRGTIQLYNLQSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPDVHNEFLSMPCREAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNVPAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQPDAGSGLLGGLLGGLFSKPTQNQVNQNGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK
Protein: RuBisCO accumulation factor 1 (Q8YLP6)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). Cooperates with RbcX in RbcL folding, plays the major role in assembly of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces Raf1, leading to holoenzyme formation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00856}.
Interaction partners:
- Ribulose bisphosphate carboxylase large chain
- RuBisCO chaperone RbcX
- Ribulose bisphosphate carboxylase small subunit
- Alr4514 protein
- All3677 protein
- All3259 protein
- Asr0773 protein
- Alr4308 protein
- Asl5170 protein
- Alr1713 protein
Sequence:
MTELPPNAPNPENATNELAQELLRKLRQKQGNWVEWGQAIASLQKSGYNPQDIFEATGFEPVQQNQVIVGSQVYNSLEKSGASAATLAHYATRGSDVLYELRLLTHEERAAAGDLTFTHKVDADEAREIAKAIKDFSRFRILPEGFSNHPGDAVAYQAWKLARQYSDLQERSRLIARGLRFAHSETARKQIEQLLVDFTVVSQRPAPIPPFFRFDTEDELPRIVPVVGQLPLKAEELKAVPLVEEIEPFRLVKFSGEQAWVALPGWQVLLAAEDPVTILATSDRFPKQNQTEPGPVLVVVDRSQREWNDFSYFVVDHDGELDFQWFETKPEFPILGKVIILVRPRRILDENVTKDSWQIDE
Protein: VTT domain-containing protein (Q4GYC8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKGAVPSTWASLASVWKKTVGEFELSTLLMAQAVAMLALYKVTNGFQMPFRSLFFFILVIYVILLALHLVGAVPLLFEVYDIIVRNYTSTQEGDSMIHLCRDLHELAETERARVMFVLTLVYVFLQSFCLPGSALINAAIGAVIGLPLGVPYCVLMGTAGASSCYTISHIIAGRCNGHNNRLVQKLRKQVEERTPSDLFAYFLLLRLTPVVPNWLLNMASPVAGVPLPTYAAGTLIGIIPQTYISVRFGEAALTTLSGEELMMTPWDMMWIGILCIVVFAGCMLKRRYGKVDCNT
Protein: GATA transcription factor 12 (P69781)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes (By similarity). Transcription activator involved in xylem formation. Functions upstream of NAC030/VND7, a master switch of xylem vessel differentiation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- Dof zinc finger protein DOF3.2
- At1g32630
- LOB domain-containing protein 15
- Myosin heavy chain, embryonic smooth protein
- RNA exonuclease 4
- LOB domain-containing protein 30
- NAC domain-containing protein 75
Sequence:
MEDEAHEFFHTSDFAVDDLLVDFSNDDDEENDVVADSTTTTTITDSSNFSAADLPSFHGDVQDGTSFSGDLCIPSDDLADELEWLSNIVDESLSPEDVHKLELISGFKSRPDPKSDTGSPENPNSSSPIFTTDVSVPAKARSKRSRAAACNWASRGLLKETFYDSPFTGETILSSQQHLSPPTSPPLLMAPLGKKQAVDGGHRRKKDVSSPESGGAEERRCLHCATDKTPQWRTGPMGPKTLCNACGVRYKSGRLVPEYRPAASPTFVLAKHSNSHRKVMELRRQKEMSRAHHEFIHHHHGTDTAMIFDVSSDGDDYLIHHNVGPDFRQLI
Protein: PRKC apoptosis WT1 regulator protein (PRKC, apoptosis, WT1, regulator) (Pawrl protein) (Q5XJ95)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATGGFKSNSATDFLEEWKAKREKMRAKMLGDIAAATGRTTELNNNGSSSVNCVSSAPSYPVARSSSSSALKDEPKTSEPPGGNLKKTPEKVSAVPQADSPSPAGVDDSDKESPTHSKSKEKKSSGPSARKGKGQIEKRKLREKRRSTGVVSIPSNESLDELDDDDGEEKERKMEENLTQHNTVQNEALTSEHEAAHSVQDNSRSRSHKSDEEGSRHRHRHGRDSSDGAPTALERRVEELERELALEREENERLLKAYQEQDELIMKLKEEIDLLNRDLDDIEDENEQLKQENKTLLKVVGQLTR
Protein: Dipeptidyl peptidase 2 (EC 3.4.14.2) (Dipeptidyl aminopeptidase II) (Dipeptidyl peptidase 7) (Dipeptidyl peptidase II) (DPP II) (Quiescent cell proline dipeptidase) (Q9EPB1)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the degradation of some oligopeptides.
Subcellular location: Lysosome. Cytoplasmic vesicle {ECO:0000250}. Secreted {ECO:0000250}.
Interaction partners:
- dipeptidyl-peptidase IV
- dipeptidyl-peptidase IV
- Dipeptidyl peptidase 4
- Prolyl endopeptidase
Sequence:
MGLHPCSPVDHGVPSWVLVLLLTLGLCSLQATADSVLDPDFRENYFEQYMDHFNFESFSNKTFGQRFLVSDKFWKMGEGPIFFYTGNEGDIWSLANNSGFIVELAAQQEALLVFAEHRYYGKSLPFGVQSTQRGYTQLLTVEQALADFAVLLQALRHNLGVQDAPTIAFGGSYGGMLSAYMRMKYPHLVAGALAASAPVIAVAGLGNPDQFFRDVTADFYGQSPKCAQAVRDAFQQIKDLFLQGAYDTISQNFGTCQSLSSPKDLTQLFGFARNAFTVLAMMDYPYPTNFLGPLPANPVKVGCERLLSEGQRIMGLRALAGLVYNSSGMEPCFDIYQMYQSCADPTGCGTGSNARAWDYQACTEINLTFDSNNVTDMFPEIPFSDELRQQYCLDTWGVWPRPDWLQTSFWGGDLKAASNIIFSNGDLDPWAGGGIQRNLSTSIIAVTIQGGAHHLDLRASNSEDPPSVVEVRKLEATLIREWVAAARLKQPAEAQWPGPK
Protein: Formate-dependent phosphoribosylglycinamide formyltransferase (EC 6.3.1.21) (5'-phosphoribosylglycinamide transformylase 2) (Formate-dependent GAR transformylase) (GAR transformylase 2) (GART 2) (GAR transformylase T) (Non-folate glycinamide ribonucleotide transformylase) (Phosphoribosylglycinamide formyltransferase 2) (P33221)
Organism: Escherichia coli (strain K12)
Function: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. PurT is also able to cleave acetyl phosphate and carbamoyl phosphate to produce ATP with acetate and carbamate, respectively.
Interaction partners:
- Phosphoribosylglycinamide formyltransferase
- Phosphoribosylformylglycinamidine synthase
- Bifunctional purine biosynthesis protein PurH
- Phosphoribosylamine--glycine ligase
- N5-carboxyaminoimidazole ribonucleotide mutase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Formyltetrahydrofolate deformylase
- Amidophosphoribosyltransferase
- Serine hydroxymethyltransferase
- Bifunctional protein FolD
Sequence:
MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIVPEIEAIATDMLIQLEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVADIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWKYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDGVHFCAPVGHRQEDGDYRESWQPQQMSPLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQLTSQNVTFDNVQNAVGADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQG
Protein: cAMP-dependent protein kinase (EC 2.7.11.11) (G5EB66)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Adenylate cyclase
- Ras-like protein
- Ras small monomeric GTPase RasB
- non-specific serine/threonine protein kinase
- mitogen-activated protein kinase
- Cell pattern formation-associated protein stuA
- cAMP-dependent protein kinase
- Lysophospholipase nte1
- Phosphodiesterase
Sequence:
MPTLGGLLKKRRTRDSQDLSKELQAGSTTTGHTTTSPIAAEDSQSQQHHGHHGGHHFFHHNHHNHQPSNNSANSANSQNSHAAKHHQFDQSSATSNQPSDGQTASMQSPAQQPSSTSAHSNSGHHSNAASIHNIIHPSQQNTPQVSRAERTTKGKYTLDDFAIQRTLGTGSFGRVHLVQSKHNHRYYAIKVLKKAQVVKMKQIEHTNDERRMLNRVRHPFLVTLWGTWQDARNLYMVMDFVEGGELFSLLRKSQRFPNPVAKFYAAEVTLALEYLHSLNIIYRDLKPENLLLDRHGHLKITDFGFAKEVPDITWTLCGTPDYLAPEVVASKGYNKSVDWWSLGILIFEMLCGFTPFWDQGSPVKIYQNILAGRIKFPPYLHPDAVDLLSRLITSDLTKRLGNLHGGPDDIKNHPWFAEVTWDRLLRKEIDAPYVPPIRGGQGDASQYENYQEESEPYGQAGEDPHGHLFPDF
Protein: Troponin T, skeletal muscle (Protein intended thorax) (Protein upheld) (P19351)
Organism: Drosophila melanogaster (Fruit fly)
Function: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Tropomyosin-2
- Troponin I
- Myosin light chain alkali
- Paramyosin, long form
- Myosin heavy chain, muscle
- Myosin regulatory light chain 2
- Muscle-specific protein 20
- Alpha-actinin, sarcomeric
- Troponin C, isoform 2
- Trehalose 6-phosphate phosphatase
Sequence:
MSDDEEYTSSEEEEVVEETREETKPPQTPAEGEGDPEFIKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQREIEEKRMRLEEAEKKRQAMLQAMKDKDKKGPNFTIAKKDAGVLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLEERQKRQDYDLKELKERQKQQLRHKALKKGLDPEALTGKYPPKIQVASKYERRVDTRSYDDKKKLFEGGWDEISKDSNEKIWNEKKEQYTGRQKSKLPKWFGERPGKKAGEPETPEGEEDAKADEDIVEDDEEVEEEVVEEEDEEAEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEE
Protein: CCM2 scaffold protein (A0A0A0MT72)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MENEPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA
Protein: Altered inheritance of mitochondria protein 23, mitochondrial (P47015)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Uncharacterized protein YGL159W
- ATP synthase subunit 9, mitochondrial
- Small ribosomal subunit protein uS3m
- Altered inheritance of mitochondria protein 34
Sequence:
MLKVPLSDVLSQKMLFLKSFRYFHCTKYFSRDNASSTTDIFRNAMKRKRELANLKEQSHGNVARNAAFPKEYIKRPKQVPRNATNRKKILITWSTGTDRAKEAANSVVSEIFKKNHKGNIKVVDPTTHRIEASNIRYFAKGIDLDKVGLSIVNVEQIDNENQIPLVKIVESRVALKKYSDFLAKKKEKELMELGVLNKSYKNLVTDKKEDNLKHIKISWQIESDDLKRQKAHEIVSLLKKGNKVTLYLDDKNNINSNNWLENFEELDRSQKGEPPRLPESVFQKRAAVLETLKEIVSEYANDPVLLGNMNSKMIMKLIPKDVKPQNNDKRALKELRKKERQEKLQKRIQRKKMNEM
Protein: FI21816p1 (FI22362p1) (Vitamin D[[3]] up-regulated protein 1, isoform A) (Vitamin D[[3]] up-regulated protein 1, isoform B) (Vitamin D[[3]] up-regulated protein 1, isoform C) (Vitamin D[[3]] up-regulated protein 1, isoform D) (Vitamin D[[3]] up-regulated protein 1, isoform E) (Q0E8K8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein charybde
Sequence:
MPRKLLKFLIIFDNTSLLYFPGQFLSGRVLIELQDETPALGLHFHVVGEGVVRNGRRQERTYDKENYIDFRMRLLGDVDQGGPAILSPGIHSFPFKLGLPLGLPSTFLGRYGWIQFYCKAALRENNGIIHKNHQVFIVMNPIDLNLEKPILAQPFTCEVEHKLGVVCVGGGQIKCRVSLDRGGYVPGENILVTAFISNYSNVSIKRTKASLTETIEYLARGKVVQTEKRELAVLVRGKIRPGAKDEWHNELYVPPLPPTNLHGCHLIKISYDVFFVIEPKSMEKEIKLQLPIVLATYPFRHSGDAVNANTWPESVLKPDTHTHYPSTLPIFRPWLHEKPIEA
Protein: Chromatin structure-remodeling complex subunit rsc1 (RSC complex subunit rsc1) (Remodel the structure of chromatin complex subunit 1) (O74964)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes to centromeric and flanking chromatin. {ECO:0000250}.
Interaction partners:
- Chromatin structure-remodeling complex subunit rsc9
- SWI/SNF and RSC complexes subunit arp42
- Chromatin structure-remodeling complex subunit rsc7
- SWI/SNF and RSC complexes subunit arp9
- Chromatin structure-remodeling complex subunit sfh1
- SWI/SNF and RSC complexes subunit ssr3
- Chromatin structure-remodeling complex subunit rsc4
- Chromatin structure-remodeling complex subunit rsc58
- SWI/SNF and RSC complexes subunit ssr2
- SWI/SNF and RSC complexes subunit ssr1
Sequence:
MSSKIRPSADDKKLQRVLYFFLERVRAAKDVSGQLLSPLIDNASVDTASVSPSSNGRPTTLKSIQSKIDEFQYHDFSEFVSDLAYLFINVKALYEGTQTYSFVQALEEFCIQQLRTFQQQGYIPVITWPNTDSPSATTSSPISRNPEYSVSPPNGSKFVKNEDEAYDSDLYVEEEDSDVKGRSMVGRDGRYKSEDLKRRKLQPSSKPLSSLEARAKVIMRQVRRYRDGSGRQLFAPFERLPDPRMFPEYYQAIEQPMALEVIQKKLSKHRYETIEQFVDDFNLMFDNAKSFNDPSSQVYRDADFLKNYLADVLRLEAGKLDSEFFNYETDSRASPQLPKNDIQPAVSIDGTLLNVGDWVLIRNPADSSKPIVSQIYRIWKSDDDINYVTVCWYLRPEQTVHRADAVFYENEVFKTSLYRDHPVSEIVGRCFVMYITRYIRGRPKGIRSTPVFVCESRYNDDTKQFSKIKSWKACMPQEVSGSEYEMILFDRPITLTKVASPLLHLLASKSQGLPSPATTDSNTHMLPSQGSLLPPSSISETKSFSTKASTPLSTDDIATPLSSAPNPPSVMPTYARKTSSHSERSSHSSYHNSSHVPTAAFNSPIMRTSTKSTSPIPARPFYAQSGSLQSLNTTQHSHQISGGHSGRMNVPYAKLSYTSHNGRHGGSNGNISGAKTPMTNYTINSMPSLPVFPPAFIVPGTHQKLDESSPVPGIDDVTVINTETAKMLDKDEHQNVLWYTVPPLDPIPLENRNGSLTHSVEYVLYKKSKGSQVITEKARSNELSREAKFENLVASLSDALIPP
Protein: Non-specific lethal 1, isoform F (Q0KI68)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPALTAEPLSPKEKLTSTASPSARSSSESGGVGCAVGLVKKPATPTPATATTRITRSSAAAASVTASPHLQQQRSSLAINNKRKSGNAKASNEPMGLSTAPTPHSTTSPNPSTDTAAASTSAVEHNNNDSNSTSAGNSTSADNSSTPKDNSTAQLLADLTINFEETISAEICLRKTLPDVSLGKEPVPPASVLAVATSSTSAGSALSLSAVDEVTKIEIDNIEERLSQLDGNATGRPEEHVAPPSVPVPVQEAPNTPTRPQAPPSAHLESPQPARTQQQSIQQMTPQSTTSSNNFLKDGAAGAVLEDQDIEEVLKALKTFDGGHVNPDTICEFFDEVWEEAAPAAPLPPAPPENVVDVPGAKPSCSGILVSGSNISQPNVIIKQEQRPWQESHAELEQQQHVISRRIEFLLRRMRKLQARAMCRHASEEVVGIMEWSARSSHKAPVPARSSTLTEQEATVLSIVSGRPSSTFWEEQNKHPLPASQMSNVIRHIATAAKHQQICHSASGSSATLAPSSSWYNSCNSSALPMKRPRKNQLDASVATGATPTAPAPGAVTSRQAAGTTGSATGSNTPRADDIVPGYDTYVTNELTHVSGLLHTELREVQNAIDSDATESSSGGESADEMVTYNNNQQLSLPITRRAVWRYSRDRAAIALRWSWLCSQLTDLEMKIRQHSDLYMDLTQSKGEIQLESTAKTSPSLAQPANGIKEEPGSDYLCSRARPLVLSEFRKRKLFQTTNMHTISKKAARPSNIKCGCQWPQVPCTLCTGRTDPTAPRDLVETMMPQNRVALLDAGYHPVLSFASDVSQSVHLEAVARQPDWQYRVMRSQPKAIVKAMWKAERETIASGGVGGQGGSRRSGDAAKRRYIRRKERNNNSNKEAGSGAKAAAVAAGGAGGNGSSSVGGGDSGNAARGKRQPQHPTGANSSSSLWPDSRQRQRQRHHSPSSTSISALSGAKKARKSATNSSSSNSTQQQQNHHGTKINNHHLNGYGDQWGEQSRSRRNSSPSNSHKNERTSERRVRPIYDINNIVIPYSMLAQSKMEIIPYKEIPIPKWRIVDSDNDKGKHSSDESMERKLSNGCVASKSEELAKQQLPPPPDQDQEQPALQPPKVNGLKENQAVKHNNNNNTNNNNNKNGLVNGNAKKDELKAAEDHDTQSKEDDDPKEKVVKPKLNGNLIKNPIDKTAETQDKIAQPAPEPPLPKRPKLETPTSNEVTKANGQLVQQQLESRESEEEPQHVDEDLSDEAFIMRHQRALLEERRRFETFLKFPWSTRSRANRRVDSRAESSGANTPDPASPAPHLGGPGHDNESIPSPLAYPLDAFNESGELLTGGQARQARRRTTSSKLKDQLERRSTTPDLRESYTVMPSPFEPLNFPLSDEVYQRLLAETYAPPRSMTVSKRAKSKSISSNCDGGNTFTGGSGSRRSSKCKIKPNGQLNGQLNGHPAAAKLNGIDAANEGGISEPEEEEMLLEDEDDDYPKHHLAPLDDEEPSTPDVEHELYDSAIDAYLADPEALEEDMGEDPFEDDDPNDPEWKTRTEGVRSRRI