wanglab/gogpt-training-data huggingface dataset:
Protein: Cell cycle control protein 50A (P4-ATPase flippase complex beta subunit TMEM30A) (Transmembrane protein 30A) (Q8VEK0)
Organism: Mus musculus (Mouse)
Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF). Can also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations.
Subcellular location: Membrane {ECO:0000269|PubMed:22253360}; Multi-pass membrane protein {ECO:0000269|PubMed:22253360}. Cell membrane {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:22253360}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:22253360}. Apical cell membrane {ECO:0000269|PubMed:22253360}.
Interaction partners:
- Phospholipid-transporting ATPase 11C
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase IH
- Phospholipid-transporting ATPase IC
- Phospholipid-transporting ATPase IF
- Phospholipid-transporting ATPase IB
- Phospholipid-transporting ATPase ID
- Phospholipid-transporting ATPase VA
- Phospholipid-transporting ATPase
- Phospholipid-transporting ATPase VB
Sequence:
MAMNYSAKDEVDGGPAGPPGGAAKTRRPDNTAFKQQRLPAWQPILTAGTVLPTFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPNVTSCACTINFTLKQSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDPSALLNPSKECEPYRRNEDRPIAPCGAIANSMFNDTLELYLVANESDPKPIPIPLKKKGIAWWTDKNVKFRNPPGKESLEEKFKDTIKPVNWHKAVYELDPEDESNNGFINEDFIVWMRTAALPTFRKLYRLIERRDDLHPTLPAGQYFLNITYNYPVHSFDGRKRMILSTISWMGGKNPFLGIAYITIGSISFLLGVVLLVINHKYRNSSNTADITI
Protein: Probable prefoldin subunit 1 (Q17827)
Organism: Caenorhabditis elegans
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). Has a role in gonadogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18062952}.
Interaction partners:
- Probable prefoldin subunit 5
- Probable prefoldin subunit 4
- Probable prefoldin subunit 3
- Prefoldin subunit 2
- Probable prefoldin subunit 6
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- Spindle and kinetochore-associated protein 2
- T-complex protein 1 subunit delta
- Uncharacterized protein D2005.3
Sequence:
MADEEISKAFRDLQFKTNETRMRIVQGEQNKKVNYQKMRISESTKKNLVDLDENLKYYRSVGRMFLLTDKPAEISRHEAEAKQSKEKIEAIEKQKDYLEKGLVEAETNLRELIQSRR
Protein: Beta-defensin 12 (BNBD-12) (BNDB-12) (P46170)
Organism: Bos taurus (Bovine)
Function: Has bactericidal activity. Active against E.coli ML35 and S.aureus 502A.
Subcellular location: Secreted.
Interaction partners:
Sequence:
GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCCRSW
Protein: TTAGGG binding factor (Q4VHG6)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MYCHAGVPSTSPSPTDFSEVHKILCGHIKQGNNFSVAAAVALEPLHGSSEFWRTCGYRSGIVSALLASSLGVQRETDQLSHLEPMTVADVYAMFRHVVDENAHLRQIIARLESGECDPDDGSGGITSSAERLRSLISEGYDALTGRSSPCMGEDDCGQTPGKWKTCSSGAAGTKRRRDSPEVTERAYVRPESPVPASETLSPAANSGDDTVDEAEQNNALDVLEQLPALPGTTRTVSSFDAVGEMVNRGAGGPSLHPTNPSEFRVGSERGSTIETHSSSELSNFANVGVGTSSGKQKRYKFSASEDEAIIKGLARFTKGQQRFQQIYYAYRSVWHPARTVSQLYDHWRGTLRYKVIQQQGYRGKNSVAARSPEKASNMENNE
Protein: Uncharacterized protein C11C11.06c (Q10195)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSAKEGSSHPSYAEIVREHAPEQTAAEKAAPQPPEVEEVLSEEPYQKNEKVVVLDEEDADAFLHPEEAEAKKESEKPSDGEKKGKTEKLEKEAKSVYSKACNFVNAHKVPASAAISINLLSLGAISAYLLKSRQSGTLNNRTLCTCTAIAGIVFTISAVFSKTPKTACCASKKSNKST
Protein: Protein COS8 (P38723)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Putative UPF0377 protein YHL045W
- Uncharacterized protein YHL049C
- DUP240 protein DFP4
- Uncharacterized protein YHL050C
Sequence:
MKENEVKDEKSVDVLSFKQLEFQKTVLPQDVFRNELTWFCYEIYKSLAFRIWMLLWLPLSVWWKLSSNWIHPLIVSLLVLFLGPFFVLVICGLSRKRSLSKQLIQFCKEITEDTPSSDPHDWEVVAANLNSYFYENKTWNTKYFFFNAMSCQKAFKTTLLEPFSLKKDESAKVKSFKDSVPYIEEALQVYAAGFDKEWKLFNTEKEESPFDLEDIQLPKEAYRFKLTWILKRIFNLRCLPLFLYYFLIVYTSGNADLISRFLFPVVMFFIMTRDFQNMRMIVLSVKMEHKMQFLSTIINEQESGANGWDEIAKKMNRYLFEKKVWNNEEFFYDGLDCEWFFRRFFYRLLSLKKPMWFASLNVELWPYIKEAQSARNEKPLK
Protein: Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) (A0A5F9ZHL1)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGKCFLNFRMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
Protein: RE09303p (Q5BIA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METAVVGIHFVVTDQHFDNGKLKLRCSAQLHDVYWKTTEKIILETDLFPKHGNGANGNHVNPDDFYDQYALHEDHLHNKKNSYLTQLQGEEDDGTEGGLGDGGAAWRGAGSSSSRLSPSSSQSCWMVGGSLMAVLSWTLARQLVSPLQAMMTKTGGATCNMSGRCASRRTRAHGMRVSATKQKQKQRQMQQEHRKSCLRVSKSSWKGRGYVCGCGFGRINSRCIRQLT
Protein: Armadillo/beta-catenin-like repeat protein (H2L2I2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRLFSYLDGCGTKNRGIYRSCELPTTMLLHSTNSYSIFTDHEVETRTSRIRSAMFPDWIPPTSAAEATNSTTSIVEMMQMPTQQLKQSVMDLLTYEGSNDMSGLSLPDLVKLMCDHDESVVARAVHRAYMLSREDPNFFNAPGFDHRSFVEALMAASKSSNVNVRRNAIGALSHMSEQRGGPLLIFRSGGLAEIIRMLYDSLESVVHYAVTTLRNLLMHVSDSRAQARALNAVEALTPHLHKTNPKLLAQVADGLYFLLIDDAPSKITFLSLLGPQILVSILREYSDHRKLIYTVVRCIRSLSVCPSNKPALISLGCLPALYVELCTAKDERSQTAILVAMRNLSDSATNEENLTQLIIKLLEIIRVANDGMTACACGTLSNLTCNNTRNKQTVCSHGGIDALVTAIRRLPEVEEVTEPALCALRHCTARHSLAEEAQSELRFCQAFPVILDQLETLRTPVIKAALGVIRNSALLQTNLIELTQEQTANGHTAVSLTMDILRRAITAIEENPDIAVDGVPMWGVIEGAVSALHQLANHPAVAAACCDDIGQVGNPECPPFLDLLHRLLAHPRLGSMDDEVLEREILGLLYQLSKRPDGARAVESTGVSALLMESRGSQYKSVVTYANGVLSNLKRGDSAAIMNMSNSYDYEMSGSAADWQRDGLERELFAEMYPTNDGGHSESINMALNNSQMRPNHNWYDTDL
Protein: Diphosphoinositol polyphosphate phosphohydrolase 2 (DIPP-2) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2) (EC 3.6.1.61) (Nucleoside diphosphate-linked moiety X motif 4) (Nudix motif 4) (Q8R2U6)
Organism: Mus musculus (Mouse)
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). Can also catalyze the hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) but not diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) and the major reaction products are ADP and p4a from Ap6A (By similarity). Also able to hydrolyze 5-phosphoribose 1-diphosphate (By similarity). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NZJ9}.
Interaction partners:
Sequence:
MKFKPNQTRTYDREGFKKRAACLCFRSEQEDEVLLVSSSRYPDQWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGIFENQDRKHRTYVYVLTVTEILEDWEDSVNIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGCSPTNGNSSVPSLPDNNALFVTAAPPSGVPSSIR
Protein: Eukaryotic translation initiation factor 2-alpha kinase 1 (EC 2.7.11.1) (Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase) (Heme-regulated inhibitor 1) (O13889)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates down-regulation of protein synthesis in response to stress conditions by the phosphorylation of the alpha subunit of eIF-2 (tif211) on 'Ser-52'. Protein synthesis is inhibited at the level of initiation. Activity is inhibited in the presence of heme.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit alpha
- eIF-2-alpha kinase GCN2
- Eukaryotic translation initiation factor 2-alpha kinase 2
- Elongation factor 3
- ATP phosphoribosyltransferase
- mRNA export factor elf1
Sequence:
MLGTSTKCSKRDCNYAKENISRIMPTIGLGYKQNFEKKTADTQSSCKLLLVALLESFCKHSDQTPEQSKQMFLYVAHSLQNSGIIDFEFSEELEPIRNAYADSLHNLLSKAFRSTLPMSSTKDSKKSRYSSPDGVLAKTASFLSVLSDGGYEDDVMNVKPSVNVLSNRLNHLPVEALESCFPQTTLESSTFADFCEHKDGTGNLSFSNFDSFPTVQRSRYASDFEELELLGKGGYGSVYKARNKFDGVEYALKKIPLRLRSFSTSSNIFRESRTLARLNHPNVIRFFSSWVELLPSSEKQIEEEPLASADETLSQSADIDNFMFDMDTGLLQHTYPSSVQILFQEDSVADDLTPCYSTKNSTCNLTDLFKKEADQDYAESHDCSSTTSQVDTLGKLAPTKSASEMLLMDSFLSEREEDECSNIPSFDQQPLCLYIQMALCEETLEKHINRRNKHIHGVMSKGLRNCYILLFARILEGVLYLHDAMHLVHRDLKPRNIFLSSGVHSEPCSVCLPNFSDEDNVEVSNAYEPVNQRTLCVVPKIGDFGLVLSQSDNLEEGTNSSAESSFVGTSTYAAPELFSKHMRSVMNNNSSTDIYALGILFFELLYPFNTRMERASAIANLKKGIFPHDFLDSMPEEASLIRSMLSSSNKRPTAAQLLTSNLFHDLVVNELHVYQALLEDAEKRNNNLKAELNILRVLNPNYDC
Protein: Peroxisomal and mitochondrial division factor 1 (Q9LXR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in morphogenesis and proliferation of peroxisomes and mitochondria, independently from the previously defined pathway controlled by the FIS1-DRP3 complex.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:22147290}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:21896887, ECO:0000269|PubMed:22147290}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dynamin-related protein 3A
- Mitochondrial fission 1 protein A
- Dynamin-related protein 3B
- Mitochondrial fission protein ELM1
- Mitochondrial fission 1 protein B
- Mitochondrial Rho GTPase 3
- Mitochondrial Rho GTPase 1
- Small ribosomal subunit protein uS9m
- Dynamin
- Histone-lysine N-methyltransferase MEDEA
Sequence:
MADVEDRAAKGISDYDQGGVKTTELERKIEDMENKNQELTRENRELKERLERLTGEIEEMKDVEAEMNQRFGEMEKEIEEYEEEKKALEAISTRAVELETEVSNLHDDLITSLNGVDKTAEEVAELKKALAEIVEKLEGCEKEAEGLRKDRAEVEKRVRDLERKIGVLEVREMEEKSKKLRSEEEMREIDDEKKREIEELQKTVIVLNLELVKNVEELKKWKSKKKLTEEALSETQKREKELELKKDELLKKVEEGNKTVFALNERTMKPSNGVRDTNGGDQKGSLEAEYQWPVVAAGSVGAAGLVAATFFVCYSKLR
Protein: Putative membrane protein (Q2GJ94)
Organism: Anaplasma phagocytophilum (strain HZ)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Uncharacterized protein
- hydroxymethylpyrimidine kinase
Sequence:
MKYINLLLVALAVVGIGLFLRPVLYACIYALFIAYLLNPIVTKLVLIGMSRAVASFVIICASAGVIGTLIVMLMPVLYSQALGVIKLLIDRVPFLNLEDIKDILSSSGLPSYQEIKSATENPLNLLTSDLFRGDGAEFLKLFKDAPSYFVKAVAGIAHSSLGIGSSIVTILTSLLLSFYILANWPSITKIALELIPRSYVRDFALCFHKIDEVISSYLRGQTLVCLVLACYYSFCFVVIRLEYSLVMGFVSGLLTFLPYIGPSLCCILSVCIAISQGFGITKVVLVALMFLVGQMIESYVVTPGIVGKRLALNQAWLVIGVVVFSSHAGFWGALLSVPFTAILSVLIQFAVKKYKTSNFYLSE
Protein: Fructose-bisphosphate aldolase (FBP aldolase) (EC 4.1.2.13) (G8BI56)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Pyruvate decarboxylase
- Phosphoglycerate mutase
- phosphopyruvate hydratase
- phosphopyruvate hydratase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Pyruvate kinase
- Phosphoglycerate mutase
Sequence:
MAPPAVLKKSGVIYGKDVKDLFDYAQEKGFAIPAINVTSSSTVVAALEAARDNKAPIILQTSQGGAAYFAGKGVDNKNQEASIAGSIAAAHYIRAIAPIYGIPVVLHTDHCAKKLLPWFDGMLKADEEFFAEHGTPLFSSHMLDLSEEADEENIGTCAEYFEKMAKMGQWLEMEIGITGGEEDGVNNEHVQKESLYTLPETVFKVYESLSKISPNFSIAAAFGNVHGVYKPGNVQLKPEILGEHQEYAKKQIGTDNRHPLYLVFHGGSGSSQQEFDTAIKNGVVKVNLDTDCQYAYLEGIRDYILKKQDYLKTPVGNPEGEDKPNKKYFDPRVWVREGEKTMAKRVTEALEIFHTKDQL
Protein: 2,3-diketo-L-gulonate reductase (2,3-DKG reductase) (EC 1.1.1.130) (3-dehydro-L-gulonate 2-dehydrogenase) (P37672)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- L-xylulose/3-keto-L-gulonate kinase
- Protein YiaL
- 2,3-diketo-L-gulonate-binding periplasmic protein YiaO
- DNA-binding transcriptional repressor YiaJ
- Putative L-ribulose-5-phosphate 3-epimerase SgbU
- 2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN
- 3-keto-L-gulonate-6-phosphate decarboxylase SgbH
- L-ribulose-5-phosphate 4-epimerase SgbE
- 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM
- Putative symporter YfeH
Sequence:
MKVTFEQLKAAFNRVLISRGVDSETADACAEMFARTTESGVYSHGVNRFPRFIQQLENGDIIPDAQPKRITSLGAIEQWDAQRSIGNLTAKKMMDRAIELAADHGIGLVALRNANHWMRGGSYGWQAAEKGYIGICWTNSIAVMPPWGAKECRIGTNPLIVAIPSTPITMVDMSMSMFSYGMLEVNRLAGRQLPVDGGFDDEGNLTKEPGVIEKNRRILPMGYWKGSGMSIVLDMIATLLSDGASVAEVTQDNSDEYGISQIFIAIEVDKLIDGPTRDAKLQRIMDYVTSAERADENQAIRLPGHEFTTLLAENRRNGITVDDSVWAKIQAL
Protein: Lipid A 1-diphosphate synthase (EC 2.7.4.29) (Kdo(2)-lipid A phosphotransferase) (Undecaprenyl pyrophosphate:lipid A 1-phosphate phosphotransferase) (P76445)
Organism: Escherichia coli (strain K12)
Function: Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1-diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P). In vitro, has low undecaprenyl-diphosphate phosphatase activity.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:17660416}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000269|PubMed:17660416}. Note=Transferase activity takes place on the periplamic side of the inner membrane. {ECO:0000255|HAMAP-Rule:MF_01945, ECO:0000269|PubMed:18047581}.
Interaction partners:
- Phosphoethanolamine transferase EptA
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Lipid A palmitoyltransferase PagP
- Putative membrane protein PmrR
- Kdo
- Lipid A biosynthesis myristoyltransferase
- Putative undecaprenyl-diphosphatase YbjG
- Phosphatidylglycerophosphatase B
- Undecaprenyl-diphosphatase
- Signal transduction protein PmrD
Sequence:
MIKNLPQIVLLNIVGLALFLSWYIPVNHGFWLPIDADIFYFFNQKLVESKAFLWLVALTNNRAFDGCSLLAMGMLMLSFWLKENAPGRRRIVIIGLVMLLTAVVLNQLGQALIPVKRASPTLTFTDINRVSELLSVPTKDASRDSFPGDHGMMLLIFSAFMWRYFGKVAGLIALIIFVVFAFPRVMIGAHWFTDIIVGSMTVILIGLPWVLLTPLSDRLITFFDKSLPGKNKHFQNK
Protein: Immunoglobulin lambda variable 1-51 (Ig lambda chain V-I region BL2) (Ig lambda chain V-I region EPS) (Ig lambda chain V-I region NEW) (Ig lambda chain V-I region NIG-64) (P01701)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MTCSPLLLTLLIHCTGSWAQSVLTQPPSVSAAPGQKVTISCSGSSSNIGNNYVSWYQQLPGTAPKLLIYDNNKRPSGIPDRFSGSKSGTSATLGITGLQTGDEADYYCGTWDSSLSA
Protein: Pyruvate, phosphate dikinase (EC 2.7.9.1) (Q385E1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- phosphoenolpyruvate carboxykinase
- Pyruvate kinase
- Malic enzyme
- Malic enzyme
- pyruvate dehydrogenase
- Enolase, putative
- phosphopyruvate hydratase
- Pyruvate dehydrogenase E1 component subunit beta
- Transketolase
- Fructose-bisphosphate aldolase
Sequence:
MVAKKWVYYFGGGKADGNKNMKELLGGKGANLAEMVNLGIPVPPGFTITTEACKTYQETETIPQEVADQVRENVSRVEKEMGAKFGDPTNPLLFSVRSGAAASMPGMMDTVLNLGLNKVTVDAWVRRAPRLERFVYDSYRRFITMYADIVMQVGREDFEEALSRMKERRGTKFDTDLTASDLKELCDGYLELFELKTGCSFPQDPVMQLFAAIKAVFRSWGNPRATIYRRMNNITGLLGTAVNVQAMVFGNINDRSATGVAFSRSPSTGENFFFGEYLVNAQGEDVVAGIRTPQQINHSLSLRWAKAHGVGEEERRKRYPSMEEAMPENYRLLCDVRKRLENHYRDMQDLEFTVQDGRLWLLQCRNGKRTIHAAVRIAIDMVNEGLISREEAVLRIDPYQVDHLMHPNLEPGAEKANKPIGRGLAASPGAAVGQVVFDAESAKEWSGRGKKVIMVRLETSPEDLAGMDAACGILTARGGMTSHAAVVARGMGKCCVSGCGDMVIRGKSFKLNGSVFREGDYITIDGSKGLIYAGKLKLRSPDLKGSFQTILQWCQEMKRLGVRTNADTPADAAKARSFGAEGVGLCRTEHMFFEGSRINFIREMILADSASGRKAALDKLLPIQRADFVGILRAMRGLPVTIRLLDPPLHEFVPHDAAAQFELAQKLGMPAEKVRNRVNALHELNPMLGHRGCRLGITYPEIYNMQVRAIIEAAIAVSEEGSSVIPEIMVPLVGKKEELSLIREEVVKTAEAVITKSGKRVHYTVGTMIEVPRAAVTADSIAQKADFFSFGTNDLTQMGCGFSRDDAGPFLRHYGNLGIYAQDPFQSIDQEGIGELVRIAVTKGRRVKPMLKMGICGEHGGDPATIGFCHKVGLDYVSCSPFRVPVAIVAAAHASIKDRRAAMKARKGFAAKL
Protein: TLC domain-containing protein fld-1 (Membrane fluidity homeostasis protein 1) (G5EF48)
Organism: Caenorhabditis elegans
Function: Regulates the composition and fluidity of the plasma membrane. Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity. Does not appear to have any effect on LCPUFA synthesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30509349}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Immunoglobulin domain and leucine-rich repeat-containing protein 2
- Long-chain-fatty-acid--CoA ligase
- Mediator of RNA polymerase II transcription subunit 15
- diacylglycerol cholinephosphotransferase
Sequence:
MRQLAELLTDLLGPVPTMFLWVIVSFAFFRALQFIVRWYLFGKWTWPNFNFFDIRNRIRRRRRGGQEAENTENPPENEAEAGEQVEQEPEPDSRDLSAIPPNKKWRISNECVSLFHSVISGLWAAYALLYYKQLVQDLVNYRCDVAINLVLMSAGYLFHDLVDLLVNEQSARIIELLFHHVVVLSAFAVTMFFNRFLGVVVFGLLMELNSIFLHSRSLLNLYGVDKKSPSFRIIALLNMVTLFAFRLCVSAYLVYFVVVSIPDLEWYVSIINGLVIASLASTNTVLTYRLLAADGLLGSRRTRRTPAATAETQVGDVESGPLRTQVEDEDHHTIGVQTIHGTTEDATQTV
Protein: Integrator complex subunit 3 (SOSS complex subunit A homolog) (Q7PLS8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing. However this subunit is not essential for the 3'-end processing of the snRNA U7 and the spliceosomal snRNAs U1, U2, U4 and U5. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:39032490}. Cytoplasm {ECO:0000250|UniProtKB:Q68E01}.
Interaction partners:
- Integrator complex subunit 11
- Integrator complex subunit 5
- Integrator complex subunit 1
- Integrator complex subunit 4
- Integrator complex subunit 9
- Integrator complex subunit 10
- Protein asunder
- Integrator complex subunit 12
- Integrator complex subunit 7
- Integrator complex subunit 2
Sequence:
MEQQQSKNNAHVSKLFICTAVDCKDDIEEKFERSFVTLQMQISGLSDKEMHDMLSQAVCKEKQHEEISIGFLYIMLTDPSMASKTYRDVTLVSRDGMNGIVTNLTFLVAEKYTKLTEVARRQLIWLLREFVKHQVLSVENVIWNCLRQAGGGDVSSRNLFLIESLLDIFIEFRTWLETNPFLVQSTVYSFVRLIEDHANPALLSLRQKEVKFTISLIRERFHDIIPLGRDFVRLLQNVARIPEFEQLWRDILFNPKMLHQTFNGIWQLLHIRTSRRFLQCRLLPEMERKISFLASSVKFGNQKRYQDWFQDKYFATPESHSLRSDLIRFIINVIHPTNDMLCSDIIPRWAIIGWLISSCTNPIASANAKLSLFYDWLFFDPAKDNIMNIEPGILVMYHSIRNHPFVSSTLLDFLCRITKNFFVKHEDKIRIGVYNSLKLILEKQVIPNLQPLFESPKLDRELRNLIRDNFREFLSPPANHGQLLFTSLHPVQGHILKKESDQRILHCENMDLHETGLINISGTIDEDKKILLVPTDQEIESVFSDETAENLRRVHNIEDNTDDDDDLPLSEVRLKEKPKVELAEAIAESFDAFVTKRNSYTWEAFLKDFRPLPASAFEEFQLNYVISNTVLILRETLPQQNIFSESKTEEKHLAKSISYPLYGLFRFLYENDEKSKKPFQTLLSEICEGIPEIGYLLLYFMKIYCKLQTRKNSQQSYQFKTTIYRQICDAADEKIGNCLLRDLDLLEKENTNIFLWLLPDIYREFKSIATNNTDLLRITLRCIDAKNVRDILYSIAQGKLTIFKQDGLIDCIRQSLEFETYEQFCLWQIVQAHDVPLRCIQDILPELEAGSHPEALSHFLLLLKNEEPTNEIIRLMLSRESKSKGDPFVTSALRFWCQRYEEKLSEIIASLLTSKYPSSSPNKRKRPPKGISVSTSTPSADQVLNHLEHYRRSCRHGTGTGLYVHDMMQRALQSAYSHSNDSTKKQFCDLFALAAEEDTTVGRRGGSGRGRKQPGSKKDVNNHGTSKKNPEMVKTIYSSDDNSSEEDWSKSKILQTAKRRKKANNDSD
Protein: F-actin-capping protein subunit alpha (Aginactin subunit alpha) (CAP34) (P13022)
Organism: Dictyostelium discoideum (Social amoeba)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A0PFK5}.
Interaction partners:
- F-actin-capping protein subunit beta
- Dynactin subunit 2
- Dynactin subunit 4
- Dynactin subunit 5
- Dynactin 150 kDa subunit
- Dynactin subunit 6
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Twinfilin
- Actin-interacting protein 1
- SH3 domain-containing protein
Sequence:
MASNQELVQIATNFLLNAPPCEFMEVVSDVRALLPSESLLNASAGSTFREYNTSQMVSVQTSKGSALITKEGEISNNEYLDPKNKQVITYDHIKQEVTGERSASGEIEQDIEQYRAAFDEEATKYCNEYYPNGVSAVYGTKVSEGIKITVCISTCIYKPNAFYSGRWRSVWTCTFKPGSGNVTSNGKVQVNVHYFEDGNVQLNTVTQKQTTSPSADAQSTAVNAFKAIGKAELNLHTALDNNYSTMGDTTFKALRRALPINRTKINWQKVKNFKIANELNK
Protein: tRNA dimethylallyltransferase 2 (EC 2.5.1.75) (Isopentenyl-diphosphate: tRNA isopentenyltransferase 2) (AtIPT2) (IPP transferase 2) (IPPT 2) (Q9ZUX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). Involved in the cis-type cytokinin biosynthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14726522}.
Interaction partners:
- tRNA dimethylallyltransferase 9
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Isopentenyl-diphosphate Delta-isomerase II, chloroplastic
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Enabled-like protein
- Cytokinin dehydrogenase 7
- Cytokinin dehydrogenase 6
- Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG4
- Cytokinin hydroxylase
- Cytokinin hydroxylase
Sequence:
MMMLNPSNGGIEGEKMKKKAKVVVIMGPTGSGKSKLAVDLASHFPVEIINADAMQIYSGLDVLTNKVTVDEQKGVPHHLLGTVSSDMEFTARDFRDFTVPLIEEIVSRNHIPVLVGGTHYYIQAVVSKFLLDDAAEDTEECCADVASVVDQDMVVESVFGRDDLSHGYELLKELDPVAANRIHPNNHRKINQYLSLHASRGVLPSKLYQGKTAENWGCINASRFDYCLICMDAETAVLDRYVEQRVDAMVDAGLLDEVYDIYKPGADYTRGLRQSIGVREFEDFLKIHLSETCAGHLTSLSNDDKVMKENLRKILNFPKDDKLRIMLEEAIDRVKLNTRRLLRRQKRRVSRLETVFGWNIHYIDATEYILSKSEESWNAQVVKPASEIIRCFLETETESGRDPTSGKSIERDLWTQYVCEACGNKILRGRHEWEHHKQGRTHRKRTTRHKNSQTYKNREVQEAEVN