wanglab/gogpt-training-data huggingface dataset:
Protein: Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)] (P18341)
Organism: Bos taurus (Bovine)
Function: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-2
- TGF-beta receptor type-1
- Decorin
- Latent-transforming growth factor beta-binding protein 1
- Integrin alpha-V
- Mothers against decapentaplegic homolog 2
- SMAD family member 7
- Mothers against decapentaplegic homolog
- Fibromodulin
- CCN family member 2
Sequence:
MPPSGLRLLPLLLPLLWLLMLTPGRPVAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGDVPPGPLPEAILALYNSTRDRVAGESAETEPEPEADYYAKEVTRVLMVEYGNKIYDKMKSSSHSIYMFFNTSELREAVPEPVLLSRADVRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLTRREEIEGFRLSAHCSCDSKDNTLQVDINGFSSGRRGDLATIHGMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
Protein: A-kinase anchor protein 6 (Q3TRB0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
AIVMQAVQWQTRLRKKMGKESETLNVIDPGLMDLNGMSEDALEWDETDISNKLISVHEESNNLDQDLEPMVPTVKLEETHHKDSGYEEEAGDCGGSQYTSNITAPSSPHIYQVYSLHNVEFHEDSHTQFLKSSPKFTGTVQPTVLTKSLSKDSSFSSTKSLPDLLGGSSLVRPYSCQSGDLSQNSGSESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETQHLDPQMGDAANVLEQKFKDEGECIKLSSVSQASVSPVGCVNGKAGDLNSITKHTTDCLGDELQGKHEVFTFYDYSYLQGSKLKFPMIMKQPQSEKAHLEDPLLRGFYFDKKSCKPKHQTSESQPDAPLHEKILASAPHEMGRSSYKSSDIEKALTGIQNARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFSGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKVPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLSREKKRPSVTDEIKVNKDGGSTERANPSDTLDIEALLNCSIKRLSENNGNGKNPPRTHDLGTKG
Protein: CCR4-NOT transcription complex subunit 3 (CCR4-associated factor 3) (Q8K0V4)
Organism: Mus musculus (Mouse)
Function: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of embryonic stem (ES) cell identity; prevents their differentiation towards extraembryonic trophectoderm lineages.
Subcellular location: Nucleus {ECO:0000305|PubMed:20133598}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Note=NANOS2 promotes its localization to P-body.
Interaction partners:
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 4
- CCR4-NOT transcription complex subunit 2
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 10
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 8
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 6-like
Sequence:
MADKRKLQGEIDRCLKKVSEGVEQFEDIWQKLHNAANANQKEKYEADLKKEIKKLQRLRDQIKTWVASNEIKDKRQLIENRKLIETQMERFKVVERETKTKAYSKEGLGLAQKVDPAQKEKEEVGQWLTNTIDTLNMQVDQFESEVESLSVQTRKKKGDKDKQDRIEGLKRHIEKHRYHVRMLETILRMLDNDSILVDAIRKIKDDVEYYVDSSQDPDFEENEFLYDDLDLEDIPQALVATSPPSHSHMEDEIFNQSSSTPTSTTSSSPIPPSPANCTTENSEDDKKRGRSTDSEVSQSPAKNGSKPVHSNQHPQSPAVPPTYPSGPPPTTSALSSTPGNNGASTPAAPTSALGPKASPAPSHNSGTPAPYAQAVAPPNASGPSNAQPRPPSAQPSGGSGGGSGGSSSNSNSGTGGGAGKQNGATSYSSVVADSPAEVTLSSSGGSSASSQALGPTSGPHNPAPSTSKESSTAAPSGAGNVASGSGNNSGGPSLLVPLPVNPPSSPTPSFSEAKAAGTLLNGPPQFSTTPEIKAPEPLSSLKSMAERAAISSGIEDPVPTLHLTDRDIILSSTSAPPTSSQPPLQLSEVNIPLSLGVCPLGPVSLTKEQLYQQAMEEAAWHHMPHPSDSERIRQYLPRNPCPTPPYHHQMPPPHSDTVEFYQRLSTETLFFIFYYLEGTKAQYLAAKALKKQSWRFHTKYMMWFQRHEEPKTITDEFEQGTYIYFDYEKWGQRKKEGFTFEYRYLEDRDLQ
Protein: Malate dehydrogenase (EC 1.1.1.37) (Q95WV4)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MSNTCKRVAVTGAAGQIGYSLLPLIAAGRMLGFDQRVQLQLLDISPALKALEGIRAELMDCSFPLLDGVVITDEPKVAFDKADIAILCGAFPRKPGMERRDLLQTNAKIFSEQGRVLGEVASPNCRVCVVGNPANTNALILLRESKGKLNPRFVTALTRLDHNRATAQVAERARARVEEVKNCIIWGNHSGTQVPDVNSATVGGKPARAAVDNDAFFDNEFITIVQERGAEIMKLRGLSSALSAAKAIVDHVHDWMLGTPSGTHVSMAVYSDGNPYGVPGGLIFSFPVTCSGGEWQIVSGLNVTPAISERIKATTTELEEERREVSTA
Protein: Chaperone protein ClpD, chloroplastic (EC 3.6.1.-) (ATP-dependent Clp protease ATP-binding subunit ClpD homolog) (Casein lytic proteinase D) (ERD1 protein) (Protein EARLY RESPONSIVE TO DEHYDRATION 1) (Protein SENESCENCE ASSOCIATED GENE 15) (P42762)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone that interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast. The ATPase activity of CLPD is stimulated by CLPT1. Has no ADPase activity. Interacts with transit peptides with a positional preference. Localization of the signal sequence at the N-terminal end of a protein seems mandatory for interaction to take place.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:10198079, ECO:0000269|PubMed:10427773, ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:21737456, ECO:0000269|PubMed:9375397}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- ATP-dependent Clp protease adapter protein CLPS1
- ATP-dependent Clp protease proteolytic subunit-related protein 1, chloroplastic
- Chloroplastic ATP-dependent Clp protease proteolytic subunit 1
- ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
- Zinc-finger homeodomain protein 11
- Clp protease adapter protein ClpF
- ATP-dependent Clp protease proteolytic subunit 6, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 3, chloroplastic
Sequence:
MEVLSTSSPLTLHSHRLLSASSSSSHVTSIAASSLSSFASSYLGISLSNRTIHRFSTTPTNLRRFPQRKRKKFTPISAVFERFTERAIRAIIFSQKEAKSLGKDMVYTQHLLLGLIAEDRDPQGFLGSGITIDKAREAVWSIWDEANSDSKQEEASSTSYSKSTDMPFSISTKRVFEAAVEYSRTMDCQYIAPEHIAVGLFTVDDGSAGRVLKRLGANMNLLTAAALTRLKGEIAKDGREPSSSSKGSFESPPSGRIAGSGPGGKKAKNVLEQFCVDLTARASEGLIDPVIGREKEVQRVIQILCRRTKNNPILLGEAGVGKTAIAEGLAISIAEASAPGFLLTKRIMSLDIGLLMAGAKERGELEARVTALISEVKKSGKVILFIDEVHTLIGSGTVGRGNKGSGLDIANLLKPSLGRGELQCIASTTLDEFRSQFEKDKALARRFQPVLINEPSEEDAVKILLGLREKYEAHHNCKYTMEAIDAAVYLSSRYIADRFLPDKAIDLIDEAGSRARIEAFRKKKEDAICILSKPPNDYWQEIKTVQAMHEVVLSSRQKQDDGDAISDESGELVEESSLPPAAGDDEPILVGPDDIAAVASVWSGIPVQQITADERMLLMSLEDQLRGRVVGQDEAVAAISRAVKRSRVGLKDPDRPIAAMLFCGPTGVGKTELTKALAANYFGSEESMLRLDMSEYMERHTVSKLIGSPPGYVGFEEGGMLTEAIRRRPFTVVLFDEIEKAHPDIFNILLQLFEDGHLTDSQGRRVSFKNALIIMTSNVGSLAIAKGRHGSIGFILDDDEEAASYTGMKALVVEELKNYFRPELLNRIDEIVIFRQLEKAQMMEILNLMLQDLKSRLVALGVGLEVSEPVKELICKQGYDPAYGARPLRRTVTEIVEDPLSEAFLAGSFKPGDTAFVVLDDTGNPSVRTKPDSSTIRVTDKTSIA
Protein: Dermokine (Epidermis-specific secreted protein SK30/SK89) (Q6E0U4)
Organism: Homo sapiens (Human)
Function: May act as a soluble regulator of keratinocyte differentiation.
Subcellular location: Secreted {ECO:0000269|PubMed:15234001}.
Interaction partners:
- Suprabasin
- Keratinocyte differentiation-associated protein
Sequence:
MKFQGPLACLLLALCLGSGEAGPLQSGEESTGTNIGEALGHGLGDALSEGVGKAIGKEAGGAAGSKVSEALGQGTREAVGTGVRQVPGFGVADALGNRVGEAAHALGNTGHEIGRQAEDVIRHGADAVRGSWQGVPGHNGAWETSGGHGIFGSQGGLGGQGQGNPGGLGTPWVHGYPGNSAGSFGMNPQGAPWGQGGNGGPPNFGTNTQGAVAQPGYGSVRASNQNEGCTNPPPSGSGGGSSNSGGGSGSQSGSSGSGSNGDNNNGSSSGGSSSGSSSGGSSGGSSGGSSGNSGGSRGDSGSESSWGSSTGSSSGNHGGSGGGNGHKPGCEKPGNEARGSGESGIQNSETSPGMFNFDTFWKNFKSKLGFINWDAINKNQVPPPSTRALLYFSRLWEDFKQNTPFLNWKAIIEGADASSLQKRAGRDDQNYNYNQHAYPTAYGGKYSVKTPAKGGVSPSSSASRVQPGLLQWVKFW
Protein: DNA-directed RNA polymerase subunit (Q9ZQC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005586}.
Interaction partners:
- DNA-directed RNA polymerase subunit
- SIN-like family protein
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit 2
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II and V subunit 8A
Sequence:
MEFCPTCGNLLRYEGGGSSRFFCSTCPYVANIERRVEIKKKQLLVKKSIEPVVTKDDIPTAAETEAPCPRCGHDKAYFKSMQIRSADEPESRFYRCLKCEFTWREE
Protein: Polyamine oxidase (D3Z8W0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Diamine acetyltransferase 1
- S-adenosylmethionine decarboxylase proenzyme
- Spermine synthase
- Ornithine decarboxylase
- Spermidine synthase
- Antizyme inhibitor 2
- Amine oxidase
- Amine oxidase
- Diamine oxidase [copper-containing]
Sequence:
MYAPSWPKILTLIKVRELTSCHYTLGPPIRQDFWCLESGWVCEIKLGLGLSFNPTLTQQDWKGRWSSLEPSAGQGFVRKRSGVVELGAHWIHGPSQGNPVFQLAAEFGLLGEKELSEENQLVETGGHVALPSVSCTSSGTSVSLELVTEMGSLFYGLIDRTREFLNESETPMASVGEFLKKEISQQVANWTEDENTKRLKLAVLNTFFNIECCVSGTHSMDLVALAPFGEYTVLPGLDCTLSGGYQGLTNCILASLPKEVMVFDKPVKTIHWNGSFQEAAFPGETFPVLVECEDGARLPAHHVIVTVPLGFLKEHQDTFFEPPLPAKKAEAIRKLGFGTNNKIFLEFEEPFWEPDCQFIQVVWEDTSPLQDSPLSLQDTWFKKLIGFLVLPSFESSHVLCAFIAGLQSEFMETLSDEEVLLSLTQVLRRVTGNPQLPAAKSVLRSRWHSAPYTRGSYSYVAVGSTGDDLDLMAQPLPADGTGTQLQVLFAGEATHRTFYSTTHGALLSGWREADRLIGLWDSQAEQSRPRL
Protein: Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130) (Q00560)
Organism: Mus musculus (Mouse)
Function: Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating signal transmission. Binding of IL6 to IL6R induces IL6ST homodimerization and formation of a high-affinity receptor complex, which activates the intracellular JAK-MAPK and JAK-STAT3 signaling pathways. That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3. In parallel, the IL6 signaling pathway induces the expression of two cytokine receptor signaling inhibitors, SOCS1 and SOCS3, which inhibit JAK and terminate the activity of the IL6 signaling pathway as a negative feedback loop. Also activates the yes-associated protein 1 (YAP) and NOTCH pathways to control inflammation-induced epithelial regeneration, independently of STAT3. Mediates signals which regulate immune response, hematopoiesis, pain control and bone metabolism. Has a role in embryonic development. Essential for survival of motor and sensory neurons and for differentiation of astrocytes. Required for expression of TRPA1 in nociceptive neurons. Required for the maintenance of PTH1R expression in the osteoblast lineage and for the stimulation of PTH-induced osteoblast differentiation. Required for normal trabecular bone mass and cortical bone composition.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P40189}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Interleukin-6 receptor subunit alpha
- Interleukin-6
- Tyrosine-protein kinase JAK2
- Leukemia inhibitory factor receptor
- Suppressor of cytokine signaling 3
- Oncostatin-M
- Ciliary neurotrophic factor
- Interleukin-27 receptor subunit alpha
- Cardiotrophin-1
- Signal transducer and activator of transcription 3
Sequence:
MSAPRIWLAQALLFFLTTESIGQLLEPCGYIYPEFPVVQRGSNFTAICVLKEACLQHYYVNASYIVWKTNHAAVPREQVTVINRTTSSVTFTDVVLPSVQLTCNILSFGQIEQNVYGVTMLSGFPPDKPTNLTCIVNEGKNMLCQWDPGRETYLETNYTLKSEWATEKFPDCQSKHGTSCMVSYMPTYYVNIEVWVEAENALGKVSSESINFDPVDKVKPTPPYNLSVTNSEELSSILKLSWVSSGLGGLLDLKSDIQYRTKDASTWIQVPLEDTMSPRTSFTVQDLKPFTEYVFRIRSIKDSGKGYWSDWSEEASGTTYEDRPSRPPSFWYKTNPSHGQEYRSVRLIWKALPLSEANGKILDYEVILTQSKSVSQTYTVTGTELTVNLTNDRYVASLAARNKVGKSAAAVLTIPSPHVTAAYSVVNLKAFPKDNLLWVEWTPPPKPVSKYILEWCVLSENAPCVEDWQQEDATVNRTHLRGRLLESKCYQITVTPVFATGPGGSESLKAYLKQAAPARGPTVRTKKVGKNEAVLAWDQIPVDDQNGFIRNYSISYRTSVGKEMVVHVDSSHTEYTLSSLSSDTLYMVRMAAYTDEGGKDGPEFTFTTPKFAQGEIEAIVVPVCLAFLLTTLLGVLFCFNKRDLIKKHIWPNVPDPSKSHIAQWSPHTPPRHNFNSKDQMYSDGNFTDVSVVEIEANNKKPCPDDLKSVDLFKKEKVSTEGHSSGIGGSSCMSSSRPSISSNEENESAQSTASTVQYSTVVHSGYRHQVPSVQVFSRSESTQPLLDSEERPEDLQLVDSVDGGDEILPRQPYFKQNCSQPEACPEISHFERSNQVLSGNEEDFVRLKQQQVSDHISQPYGSEQRRLFQEGSTADALGTGADGQMERFESVGMETTIDEEIPKSYLPQTVRQGGYMPQ
Protein: Ribosome assembly factor mrt4 (Q389X5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364039}. Nucleus, nucleolus {ECO:0000256|RuleBase:RU364039}.
Interaction partners:
- Ribosome biogenesis protein NSA2 homolog
- Nucleolar GTP-binding protein 1
- Nucleolar complex protein 2
- Pescadillo homolog
- Ribosome biogenesis protein BOP1 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Eukaryotic translation initiation factor 6
- NLE domain-containing protein
- Nucleolar protein, putative
- RNA-binding protein, putative
Sequence:
MPKSKRATIVPLTKTRSKTREEKDELINKIRDALDDYTDVYTFELSNIRTNILQQIREERRNDSRLFLGNNKLLMIALGRDDSSSQRPNLHKLSKYLTGSCGLLFTNLPHQDVKEYFKGVSADVFARTGQVATCPLLLRTGPLAQFPHSMFDHLSRLGLPIKLDKGVIVLLRDTTVCEVGDTLTAEAAQLLKLFGIQSAEFKLELTAHWAKGVVKRMSKKKKEEEN
Protein: Phospholipase A and acyltransferase 5 (Ca(2+)-independent N-acyltransferase) (iNAT) (EC 2.3.1.-, EC 3.1.1.32, EC 3.1.1.4) (H-rev107-like protein 5) (HRAS-like suppressor 5) (HRSL5) (Q96KN8)
Organism: Homo sapiens (Human)
Function: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q4KLN5}.
Interaction partners:
- NF-kappa-B inhibitor zeta
Sequence:
MGLSPGAEGEYALRLPRIPPPLPKPASRTASTGPKDQPPALRRSAVPHSGLNSISPLELEESVGFAALVQLPAKQPPPGTLEQGRSIQQGEKAVVSLETTPSQKADWSSIPKPENEGKLIKQAAEGKPRPRPGDLIEIFRIGYEHWAIYVEDDCVVHLAPPSEEFEVGSITSIFSNRAVVKYSRLEDVLHGCSWKVNNKLDGTYLPLPVDKIIQRTKKMVNKIVQYSLIEGNCEHFVNGLRYGVPRSQQVEHALMEGAKAAGAVISAVVDSIKPKPITA
Protein: Plastin-3 (T-fimbrin) (T-plastin) (P13797)
Organism: Homo sapiens (Human)
Function: Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. May play a role in the regulation of bone development.
Subcellular location: Cytoplasm.
Interaction partners:
- Actin, alpha skeletal muscle
- Survival motor neuron protein
- Coronin-1C
- Plastin-2
- Fascin
Sequence:
MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMLDGDRNKDGKISFDEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVLEDLGDGQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMKRV
Protein: Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase subunit alpha) (NAD(+)-specific ICDH subunit alpha) (P56471)
Organism: Sus scrofa (Pig)
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:2252888}.
Interaction partners:
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit gamma, mitochondrial
- Aconitate hydratase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Citrate synthase, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- hydroxymethylglutaryl-CoA lyase
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Sequence:
MAGPAWISKVSRLLGAFHNQKQVTRGFAGGVKTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAAKIETACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD
Protein: CW-type Zinc Finger (F4IZK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEESELEEGEACSYNITNEYAGSIDPDNDLSYIDEKLQHILGHFQKDFEGGVSAENLGAKYGGYGSFLPTYQRSPVWSHPKTPAKPQSSTGTRSPNNLLGESQSGNAASSSVPKKAKSGLASSGNPKKSVKSKKPSSSARMESATKKPCVFSKQNSLKLRIKMVPDGLSTEKNAAAIYSGLGLDVSPSLSLDNNSLSGSEGMNEEPQGYSPTESPTSILNVMTSLPVDHCQFLSPLSEDLIRFIEREKSEKGYKYTSPSRLFTASSSAMAYGLEPQKSGEKPSVEKKKKMVERSSFSAETNVRSKKGLFDSTDAITKESMETNTLYPTFAEKETASSKLFDASKENYNGTVRGEMVGDVDRRLWGLTRHKDLGAHHENPKTISAGSVREDKKAKLGDNEASGYPRKVGKYKGSKASDSVKKESSASKAKSGHKVELEHPLRKQKYDQIEQEPPSSSKFKEQQTSVVFETKLNGQAEKKEVVAVKPQSDSKKAEDTYKDFFGDIGDSEEEEEQDVKDLRISEKGLPPLEDMPEKSSLPLVEPQNVGPEPMLRKLGSDASLPKANPVIIQEHWVACDKCGKWRLLPFGVFPEDLPEKWMCTMLNWLPGVNYCNVPEDETTKALYAMYQIPVPENQASMQSNPSGPKPQFTQGDDNTKKKKKGFKKIDNGMDKEGARTAETNKTIQTSSRNGIQNSQGLGDLAEDERQIHKQKEKGKAVDHLSDESKSLKANNKRKTDLESSMLAKKMKIESFLFPDESEYGNGRPTSSSGVPITSADIKPKPRVSSKMPKEEGGASDTGNSNSTGGIKKRKLRESHGSRIYSENENHERKKARVRKEEKEPSYSQGNGKLEKKNRSHSKIEYANVQNSIAATSSSSKISDSHKPRNSSREAKCSPVESVSSSPMRLSNPEKRISVSKKKEESYDANVFAAGSLKKFSDGEGEDDGGSDRSQSQMKDKHGSHESSVLDIWDNKGSLKAKERADPSLDANFENGGHKTLPRKLDHILGEGKQSSDHHRRSNDSLAKKSGKGSSSRSKEKSQSIRSDSRDGPRHIEKKIYDGSPDSRADMIVRPNIPKPHDSERIPERSNIADLASPSRPPSRGVQGDSSMLSVRKKVDKCSTSAGNNNIQADDVTKATAQIRRKSEPSPSPLRKEITSAQAAHNTLKEAKDLKHTADRLKNSVSNLEHIELYFQACLKFLHGAFLLEMSSNESARQGETMVQSMKIYSSTANLCGFCAHEYEKSKDMGAAALAYKCMEVAYMRVVNSSYTSANRYRNELQTSLQMVPPGESPSSSASDVDNVNHPAAVDRVGTSRGISSPLVAGNHVISAQNRSNLLRLLQFAQDVNLSMDASRKSRVALTACIENSGEAQQQGEGIISIKSALDYNFQDMEGLLRLVKLAMKANNR
Protein: Furaquinocin biosynthesis prenyltransferase (EC 2.5.1.124) (EC 2.5.1.125) (6-linalyl-2-O,3-dimethylflaviolin synthase) (7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase) (Q2L6E3)
Organism: Streptomyces sp. (strain KO-3988)
Function: Involved in the biosynthesis of furaquinocin. Catalyzes the transfer of a geranyl group to 2-methoxy-3-methyl-flaviolin to yield 6-prenyl-2-methoxy-3-methyl-flaviolin and 7-O-geranyl-2-methoxy-3-methyl-flaviolin in a 10:1 ratio. Can also use other substrates such as flaviolin or 1,3-dihydroxy naphthalene, and can also use DMAPP as prenyl donor.
Interaction partners:
Sequence:
MPGTDDVAVDVASVYSAIEKSAGLLDVTAAREVVWPVLTAFEDVLEQAVIAFRVATNARHEGDFDVRFTVPEEVDPYAVALSRSLIAKTDHPVGSLLSDIQQLCSVDTYGVDLGVKSGFKKVWVYFPAGEHETLARLTGLTSMPGSLAGNVDFFTRYGLADKVDVIGIDYRSRTMNVYFAAPSECFERETVLAMHRDIGLPSPSEQMFKFCENSFGLYTTLNWDTMEIERISYGVKTENPMTFFARLGTKVEHFVKNVPYGVDTQKMVYAAVTSSGEEYYKLQSYYRWRSVSRLNAAYIAARDKEST
Protein: RAB11 family interacting protein 2 (A0A8I6A8W0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
Sequence:
MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGNPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSHQINSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHCFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSTNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRSDKLNNGGSDSPCDLKSPSAFNENRQDYFEYESTNPFTAKFRASTIMPSSSFHMNPTSSDDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGMDGKPYTRVFLQEVRSWQNPSRSQEQARNSEAHSPDSGMLIIHEDNLTTS
Protein: Actobindin (P18281)
Organism: Acanthamoeba castellanii (Amoeba)
Function: Is able to bind two actin monomers at high concentrations of G-actin.
Interaction partners:
Sequence:
MNPELQSAIGQGAALKHAETVDKSAPQIENVTVKKVDRSSFLEEVAKPHELKHAETVDKSGPAIPEDVHVKKVDRGAFLSEIEKAAKQ
Protein: NAD-dependent protein deacetylase (EC 2.3.1.286) (F7EYD5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MALDPLGAVSLQSIMALSCRLVLAALRLWGPGGGRRPISLSVGASGGFGCGGHSEKKLSLQDVAELLRTRACSRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDIPYPEAIFELGFFFHNPKPFFTLAKELYPGHYRPNVAHYFLRLLHDKELLLRLYTQNIDGLERASGIPASKLVEAHGSFVSATCTVCRRSFPGEDIRADVMADRVPRCPVCTGVVKPDIVFFGEQLPARFLLHVADFALADLLLILGTSLEVEPFASLSESVQKSVPRLLINRDLVGSFALSPRRKDVVQLGDVVQGVERLVDLLGWTQELQDLIQRENGKLDGQDG
Protein: GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 1) (ARTC1) (Mono(ADP-ribosyl)transferase 1) (CD antigen CD296) (P52961)
Organism: Homo sapiens (Human)
Function: Has ADP-ribosyltransferase activity toward GLP1R.
Subcellular location: Sarcoplasmic reticulum membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Neutrophil defensin 1
- Uncharacterized protein C17orf47
- Poly
Sequence:
MQMPAMMSLLLVSVGLMEALQAQSHPITRRDLFSQEIQLDMALASFDDQYAGCAAAMTAALPDLNHTEFQANQVYADSWTLASSQWQERQARWPEWSLSPTRPSPPPLGFRDEHGVALLAYTANSPLHKEFNAAVREAGRSRAHYLHHFSFKTLHFLLTEALQLLGSGQRPPRCHQVFRGVHGLRFRPAGPRATVRLGGFASASLKHVAAQQFGEDTFFGIWTCLGAPIKGYSFFPGEEEVLIPPFETFQVINASRLAQGPARIYLRALGKHSTYNCEYIKDKKCKSGPCHLDNSAMGQSPLSAVWSLLLLLWFLVVRAFPDGPGLL
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q9W2F3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Mitogen-activated protein kinase ERK-A
- Dual specificity mitogen-activated protein kinase kinase dSOR1
- Dual specificity protein phosphatase Mpk3
- Extracellular signal-regulated kinase 7
Sequence:
MDKLRNNNKENAPIEYPYPQTPRPTHAAPSDTTPLEAGEDAESNKSTPYFTPLEYLQTSFEFPSPTVEVGGGVPGFPEHEDQEEEVFTPRQFTITSPHPAAHVHHPSSSQSPTLGRKFKRLSQYDRRSCSPHINTSSGEERVSGRGIDKENTMPKGGSVDQDLENSLYLSKSEHNSPTILFKDESSTTPGLEASRLSYSPKLLSSINNLNVSGSPLNIINSAGYKNGNFFRFPEIDHVVQDAPMDTVCLEEATRRDRSPALAEPPEQQQQKSEGRKNRKNKNNLTIRITDVPIKNSSQPSPLPKPKTPTIKSTKEKARSLDSAANESELSIVVHNITESHGSCDDMETGQSQPSTSVIHHHLHLQQPASAIHSTSLSRLDSHLSLANQRRTPRRKSPGINTTDWLMYHRKQNPYQVQPTHCSSTTQSSLDSDASLTPSLGDFELKSACSVDGGSKFGIGASLAPRSAHKHNQLLHSSSTNLKTLPECLTLVEFSSSGGGPKESPFKQKSMDLPMPTLQAKTTVSTSSMNLLQRRGSNHSLTLNLHSSCGNLMNSGLSHSNYSLGSILNSKSSCNLDAGTASQIRADQLPQSHLLGSSQGSRQGLFRRRGSNHSITLKTGHTTTSCGDLNSMQQLQQQQAMLSAEKYNRLNMRTNSTGSGSGSGSNVPTPKRGLLERRGSNQSLTLNMGSILGGAAGTEIQMTDIVQPKVTVCSCAAANQAPHQRKFFSTENLNSSKANSQKFFGQVCFGSASDLQPNPQQDSVREDQAIGATCTCAGTVRNIMTRPLSPQTTSEEFKIYLASIQMLQSASNPLNQFDLIRLNYVFDHSYQTNRNIIEQPPVLGSNARDVETPTDMVPPSSEDSELLASYQTVVSRMAQPIPELKENEQKRIFRDLHKEFWDLPLNHQEKPMVFGSQTKNRYKTILPNENSRVLLESESSELTSLLGEIKRTSSVTASEDLPYINANYIKGPDYVSKCYVATQGPLPNTIFEFWLMIYQNTQRYIRRCVDGGSSSSPHVDREQILQQYFQKIVMLTNFTEANRQKCAVYFPIELNEIFAVAAKCEVFQLSAAARDYFDRYLTPTFVPDTVVASSDAIDYEISGRHIGVESVKVTLEGDLLEALPAQGSFFLIKNVGIVRRNGYSVRKLVLLYCIRVPQSASYHLQKIYCYHYWYPDWPDHHSPRDINTLLDTCLHVLNLGKCESEFDIYDDTRSERNAHLAAQRLEIYQQDIFNAVQPLPVIHCSAGIGRTGCFTAILNAVRQLRQSLAYSLTGMLTKSLTSSSTEEYHNPTDSDSSFTCNTIRHISHILDHRDAEAVKTPPSFDRLPKMPDIFVDVLGIVCNLRLQRGGMVQNSEQYELIHRAICLYLKRTLALRRF